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Database: PDB
Entry: 1N0J
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HEADER    OXIDOREDUCTASE                          14-OCT-02   1N0J              
TITLE     THE STRUCTURE OF HUMAN MITOCHONDRIAL MN3+ SUPEROXIDE DISMUTASE REVEALS
TITLE    2 A NOVEL TETRAMERIC INTERFACE OF TWO 4-HELIX BUNDLES                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN];                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: SODASODB                                   
KEYWDS    FOUR-HELIX BUNDLE, METALLOENZYME, MANGANESE, OXIDOREDUCTASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.E.O.BORGSTAHL,H.E.PARGE,J.A.TAINER                                  
REVDAT   4   11-OCT-17 1N0J    1       REMARK HELIX                             
REVDAT   3   13-JUL-11 1N0J    1       VERSN                                    
REVDAT   2   24-FEB-09 1N0J    1       VERSN                                    
REVDAT   1   06-NOV-02 1N0J    0                                                
SPRSDE     06-NOV-02 1N0J      1ABM                                             
JRNL        AUTH   G.E.BORGSTAHL,H.E.PARGE,M.J.HICKEY,W.F.BEYER JR.,            
JRNL        AUTH 2 R.A.HALLEWELL,J.A.TAINER                                     
JRNL        TITL   THE STRUCTURE OF HUMAN MITOCHONDRIAL MN3+ SUPEROXIDE         
JRNL        TITL 2 DISMUTASE REVEALS A NOVEL TETRAMERIC INTERFACE OF TWO        
JRNL        TITL 3 4-HELIX BUNDLES                                              
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V.  71   107 1992              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   1394426                                                      
JRNL        DOI    10.1016/0092-8674(92)90270-M                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 20                                            
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
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             : 19738                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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            : 3146                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 169                                     
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) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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) : 0.018                           
REMARK   3   BOND ANGLES            (DEGREES) : 3.300                           
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  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 1N0J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-02.                  
REMARK 100 THE DEPOSITION ID IS D_1000017367.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 7.5                                
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          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : X-GEN                              
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19738                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.09000                            
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) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 52.0                               
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 600, PH 7.5, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       38.06500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.95000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.06500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.95000            
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,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 8150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     MET B     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    CYS A   196     N    LYS A   197              1.60            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A   2   NE2   HIS A   2   CD2    -0.070                       
REMARK 500    HIS A  26   NE2   HIS A  26   CD2    -0.066                       
REMARK 500    HIS A  27   NE2   HIS A  27   CD2    -0.072                       
REMARK 500    HIS A  30   NE2   HIS A  30   CD2    -0.081                       
REMARK 500    HIS A  31   NE2   HIS A  31   CD2    -0.067                       
REMARK 500    ALA A 195   C     CYS A 196   N      -0.227                       
REMARK 500    CYS A 196   N     CYS A 196   CA     -0.295                       
REMARK 500    CYS A 196   C     CYS A 196   O      -0.172                       
REMARK 500    CYS A 196   C     LYS A 197   N      -0.538                       
REMARK 500    HIS B   2   NE2   HIS B   2   CD2    -0.082                       
REMARK 500    HIS B  31   NE2   HIS B  31   CD2    -0.080                       
REMARK 500    HIS B  71   NE2   HIS B  71   CD2    -0.077                       
REMARK 500    ALA B 195   C     CYS B 196   N      -0.164                       
REMARK 500    CYS B 196   N     CYS B 196   CA     -0.235                       
REMARK 500    CYS B 196   C     CYS B 196   O       0.146                       
REMARK 500    CYS B 196   C     LYS B 197   N       0.144                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    TYR A  45   CB  -  CG  -  CD1 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    TRP A  78   CD1 -  CG  -  CD2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    TRP A  78   CB  -  CG  -  CD1 ANGL. DEV. = -10.0 DEGREES          
REMARK 500    TRP A  78   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    TRP A  78   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    TRP A  78   CG  -  CD2 -  CE3 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG A  99   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    VAL A 116   CG1 -  CB  -  CG2 ANGL. DEV. = -10.0 DEGREES          
REMARK 500    TRP A 123   CD1 -  CG  -  CD2 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    TRP A 125   CD1 -  CG  -  CD2 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    TRP A 125   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG A 132   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    HIS A 134   CA  -  CB  -  CG  ANGL. DEV. =  10.4 DEGREES          
REMARK 500    ASP A 144   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    TRP A 161   CD1 -  CG  -  CD2 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    TRP A 161   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    TYR A 169   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    VAL A 172   CG1 -  CB  -  CG2 ANGL. DEV. = -10.7 DEGREES          
REMARK 500    ARG A 173   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    TRP A 181   CD1 -  CG  -  CD2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    TRP A 181   CB  -  CG  -  CD1 ANGL. DEV. =  -8.4 DEGREES          
REMARK 500    TRP A 181   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    TRP A 181   CG  -  CD2 -  CE3 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    TRP A 186   CD1 -  CG  -  CD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    TRP A 186   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    TRP A 186   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ALA A 195   CA  -  C   -  N   ANGL. DEV. =  16.5 DEGREES          
REMARK 500    ALA A 195   O   -  C   -  N   ANGL. DEV. = -15.7 DEGREES          
REMARK 500    CYS A 196   N   -  CA  -  CB  ANGL. DEV. =  20.0 DEGREES          
REMARK 500    CYS A 196   CA  -  C   -  N   ANGL. DEV. =  14.5 DEGREES          
REMARK 500    TYR B   9   CB  -  CG  -  CD1 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    MET B  23   CG  -  SD  -  CE  ANGL. DEV. = -21.4 DEGREES          
REMARK 500    TYR B  45   CB  -  CG  -  CD1 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    VAL B  54   CG1 -  CB  -  CG2 ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    TRP B  78   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    TRP B  78   CB  -  CG  -  CD1 ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    TRP B  78   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    TRP B  78   CG  -  CD2 -  CE3 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    TRP B 123   CD1 -  CG  -  CD2 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    TRP B 125   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TRP B 125   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    TRP B 161   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TRP B 161   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    TRP B 161   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    TYR B 169   CB  -  CG  -  CD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    TRP B 181   CD1 -  CG  -  CD2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    TRP B 181   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    TRP B 186   CD1 -  CG  -  CD2 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    TRP B 186   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ALA B 195   CA  -  C   -  N   ANGL. DEV. =  27.1 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      53 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 142     -128.50     48.57                                   
REMARK 500    TYR A 165      -16.18   -140.74                                   
REMARK 500    GLN A 168      -61.10    -94.42                                   
REMARK 500    LYS A 170     -135.39     46.29                                   
REMARK 500    ASN B 142     -113.30     52.18                                   
REMARK 500    TYR B 165      -20.11   -140.91                                   
REMARK 500    LYS B 170     -140.10     43.36                                   
REMARK 500    ASN B 171        2.50    -67.60                                   
REMARK 500    CYS B 196       38.20    -83.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA B  195     CYS B  196                  140.77                    
REMARK 500 CYS B  196     LYS B  197                  135.34                    
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 166         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 199  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 159   OD1                                                    
REMARK 620 2 HOH A 400   O    86.0                                              
REMARK 620 3 HIS A 163   NE2 117.6  92.2                                        
REMARK 620 4 HIS A  74   NE2 102.5  91.7 139.9                                  
REMARK 620 5 HIS A  26   NE2  92.9 178.6  87.6  89.3                            
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   OD1                                                    
REMARK 620 2 HOH B 401   O    92.4                                              
REMARK 620 3 HIS B  74   NE2 100.7  95.0                                        
REMARK 620 4 HIS B 163   NE2 131.0  87.2 128.2                                  
REMARK 620 5 HIS B  26   NE2  93.4 172.9  79.9  92.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: MNA                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: active site, trigonal bipyramidal manganese        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MNB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: active site, trigonal bipyramidal manganese        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 199                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 199                  
DBREF  1N0J A    1   198  UNP    P04179   SODM_HUMAN      25    222             
DBREF  1N0J B    1   198  UNP    P04179   SODM_HUMAN      25    222             
SEQADV 1N0J MET A    0  UNP  P04179              EXPRESSION TAG                 
SEQADV 1N0J MET B    0  UNP  P04179              EXPRESSION TAG                 
SEQRES   1 A  199  MET LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY          
SEQRES   2 A  199  ALA LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU          
SEQRES   3 A  199  HIS HIS SER LYS HIS HIS ALA ALA TYR VAL ASN ASN LEU          
SEQRES   4 A  199  ASN VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS          
SEQRES   5 A  199  GLY ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU          
SEQRES   6 A  199  LYS PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE          
SEQRES   7 A  199  TRP THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS          
SEQRES   8 A  199  GLY GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER          
SEQRES   9 A  199  PHE ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL          
SEQRES  10 A  199  GLY VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN          
SEQRES  11 A  199  LYS GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN          
SEQRES  12 A  199  GLN ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU          
SEQRES  13 A  199  LEU GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN          
SEQRES  14 A  199  TYR LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP          
SEQRES  15 A  199  ASN VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET          
SEQRES  16 A  199  ALA CYS LYS LYS                                              
SEQRES   1 B  199  MET LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY          
SEQRES   2 B  199  ALA LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU          
SEQRES   3 B  199  HIS HIS SER LYS HIS HIS ALA ALA TYR VAL ASN ASN LEU          
SEQRES   4 B  199  ASN VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS          
SEQRES   5 B  199  GLY ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU          
SEQRES   6 B  199  LYS PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE          
SEQRES   7 B  199  TRP THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS          
SEQRES   8 B  199  GLY GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER          
SEQRES   9 B  199  PHE ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL          
SEQRES  10 B  199  GLY VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN          
SEQRES  11 B  199  LYS GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN          
SEQRES  12 B  199  GLN ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU          
SEQRES  13 B  199  LEU GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN          
SEQRES  14 B  199  TYR LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP          
SEQRES  15 B  199  ASN VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET          
SEQRES  16 B  199  ALA CYS LYS LYS                                              
HET     MN  A 199       1                                                       
HET     MN  B 199       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  HOH   *169(H2 O)                                                    
HELIX    1   1 ASP A   10  GLU A   15  5                                   6    
HELIX    2   2 ASN A   19  LYS A   29  1                                  11    
HELIX    3   3 LYS A   29  LYS A   51  1                                  23    
HELIX    4   4 ASP A   53  LEU A   81  1                                  29    
HELIX    5   5 GLY A   91  GLY A  102  1                                  12    
HELIX    6   6 SER A  103  GLY A  117  1                                  15    
HELIX    7   7 PRO A  145  GLY A  151  1                                   7    
HELIX    8   8 TRP A  161  ALA A  164  5                                   4    
HELIX    9   9 TYR A  165  LYS A  170  1                                   6    
HELIX   10  10 VAL A  172  TRP A  181  1                                  10    
HELIX   11  11 ASN A  182  ILE A  184  5                                   3    
HELIX   12  12 ASN A  185  LYS A  197  1                                  13    
HELIX   13  13 ASP B   10  GLU B   15  5                                   6    
HELIX   14  14 ASN B   19  LYS B   29  1                                  11    
HELIX   15  15 LYS B   29  LYS B   51  1                                  23    
HELIX   16  16 ASP B   53  LEU B   60  1                                   8    
HELIX   17  17 LEU B   60  LEU B   81  1                                  22    
HELIX   18  18 GLY B   91  GLY B  102  1                                  12    
HELIX   19  19 SER B  103  GLY B  117  1                                  15    
HELIX   20  20 PRO B  145  GLY B  151  1                                   7    
HELIX   21  21 TRP B  161  ALA B  164  5                                   4    
HELIX   22  22 TYR B  165  LYS B  170  1                                   6    
HELIX   23  23 VAL B  172  TRP B  181  1                                  10    
HELIX   24  24 ASN B  185  CYS B  196  1                                  12    
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  TRP B 125   O  ALA B 138           
SHEET    3   B 3 ILE B 153  ASP B 159 -1  O  LEU B 156   N  LEU B 126           
LINK         OD1 ASP A 159                MN    MN A 199     1555   1555  1.94  
LINK         OD1 ASP B 159                MN    MN B 199     1555   1555  1.94  
LINK        MN    MN A 199                 O   HOH A 400     1555   1555  2.02  
LINK        MN    MN B 199                 O   HOH B 401     1555   1555  2.01  
LINK        MN    MN A 199                 NE2 HIS A 163     1555   1555  2.10  
LINK        MN    MN A 199                 NE2 HIS A  74     1555   1555  2.08  
LINK        MN    MN A 199                 NE2 HIS A  26     1555   1555  2.10  
LINK        MN    MN B 199                 NE2 HIS B  74     1555   1555  2.11  
LINK        MN    MN B 199                 NE2 HIS B 163     1555   1555  2.10  
LINK        MN    MN B 199                 NE2 HIS B  26     1555   1555  2.09  
CISPEP   1 GLU A   15    PRO A   16          0         3.86                     
CISPEP   2 GLU B   15    PRO B   16          0       -10.53                     
SITE     1 MNA  5 HIS A  26  HIS A  74  ASP A 159  HIS A 163                    
SITE     2 MNA  5 HOH A 400                                                     
SITE     1 MNB  5 HIS B  26  HIS B  74  ASP B 159  HIS B 163                    
SITE     2 MNB  5 HOH B 401                                                     
SITE     1 AC1  5 HIS A  26  HIS A  74  ASP A 159  HIS A 163                    
SITE     2 AC1  5 HOH A 400                                                     
SITE     1 AC2  5 HIS B  26  HIS B  74  ASP B 159  HIS B 163                    
SITE     2 AC2  5 HOH B 401                                                     
CRYST1   76.130   79.900   68.050  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013135  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012516  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014695        0.00000                         
MTRIX1   1  0.886100 -0.463500  0.006700       -0.32100    1                    
MTRIX2   1 -0.463500 -0.886100  0.002200       -0.26000    1                    
MTRIX3   1  0.004900 -0.005100 -1.000000      101.43300    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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