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Database: PDB
Entry: 5GXO
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HEADER    OXIDOREDUCTASE                          19-SEP-16   5GXO              
TITLE     DISCOVERY OF A COMPOUND THAT ACTIVATES SIRT3 TO DEACETYLATE MANGANESE 
TITLE    2 SUPEROXIDE DISMUTASE                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL;                  
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 GENE: SOD2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: K-12                                       
KEYWDS    SUPEROXIDE DISMUTASE ACETYLATION, OXIDOREDUCTASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LU,J.LI,M.WU,J.WANG,Q.XIA                                           
REVDAT   2   06-DEC-17 5GXO    1       JRNL                                     
REVDAT   1   09-AUG-17 5GXO    0                                                
JRNL        AUTH   J.LU,H.ZHANG,X.CHEN,Y.ZOU,J.LI,L.WANG,M.WU,J.ZANG,Y.YU,      
JRNL        AUTH 2 W.ZHUANG,Q.XIA,J.WANG                                        
JRNL        TITL   A SMALL MOLECULE ACTIVATOR OF SIRT3 PROMOTES DEACETYLATION   
JRNL        TITL 2 AND ACTIVATION OF MANGANESE SUPEROXIDE DISMUTASE.            
JRNL        REF    FREE RADIC. BIOL. MED.        V. 112   287 2017              
JRNL        REFN                   ISSN 1873-4596                               
JRNL        PMID   28711502                                                     
JRNL        DOI    10.1016/J.FREERADBIOMED.2017.07.012                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 20241                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1095                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1481                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.3290                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3090                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 141                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.07000                                              
REMARK   3    B22 (A**2) : 0.07000                                              
REMARK   3    B33 (A**2) : -0.23000                                             
REMARK   3    B12 (A**2) : 0.07000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.332         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.234         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.174         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.338         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3182 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2945 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4331 ; 1.297 ; 1.930       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6755 ; 0.866 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   392 ; 5.296 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   151 ;34.854 ;24.834       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   480 ;16.299 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;15.227 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   450 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3700 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   784 ; 0.007 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1574 ; 2.304 ; 3.009       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1573 ; 2.298 ; 3.008       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1964 ; 3.266 ; 4.507       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1965 ; 3.266 ; 4.508       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1608 ; 2.945 ; 3.224       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1609 ; 2.944 ; 3.225       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2368 ; 4.453 ; 4.714       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 13586 ; 6.010 ;28.458       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 13516 ; 6.008 ;28.436       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5GXO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300001608.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-OCT-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21413                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.740                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 16.10                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 17.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.22000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 10.90                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1SZX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M POTASSIUM PHOSPHATE PH 7.0, VAPOR   
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 289K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.95667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      161.91333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      121.43500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      202.39167            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       40.47833            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       80.95667            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      161.91333            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      202.39167            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      121.43500            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       40.47833            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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  0.500000  0.866025  0.000000       40.06000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      -69.38596            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       40.47833            
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     LYS A   222                                                      
REMARK 465     LYS B   222                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  71    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 114    CG   CD   CE   NZ                                   
REMARK 470     GLU A 119    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 202    CE   NZ                                             
REMARK 470     GLN B  70    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  71    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 119    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 133    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 154    CG   CD   CE   NZ                                   
REMARK 470     GLU B 155    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 221    CG   CD   CE   NZ                                   
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 166     -126.77     60.41                                   
REMARK 500    TYR A 189      -16.19   -150.08                                   
REMARK 500    LYS A 194     -128.68     54.74                                   
REMARK 500    ASN B 166     -121.59     51.62                                   
REMARK 500    TYR B 189      -18.87   -152.02                                   
REMARK 500    LYS B 194     -136.54     50.74                                   
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 481        DISTANCE =  5.90 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 301  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  50   NE2                                                    
REMARK 620 2 HIS A  98   NE2  91.0                                              
REMARK 620 3 ASP A 183   OD2  83.4 108.1                                        
REMARK 620 4 HIS A 187   NE2  89.5 133.2 118.4                                  
REMARK 620 5 HOH A 424   O   170.4  93.9  87.2  93.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 301  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  50   NE2                                                    
REMARK 620 2 HIS B  98   NE2  89.6                                              
REMARK 620 3 ASP B 183   OD2  85.5 101.5                                        
REMARK 620 4 HIS B 187   NE2  86.7 129.0 128.8                                  
REMARK 620 5 HOH B 428   O   171.1  99.3  91.7  88.5                            
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 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 301                  
DBREF  5GXO A   25   222  UNP    P04179   SODM_HUMAN      25    222             
DBREF  5GXO B   25   222  UNP    P04179   SODM_HUMAN      25    222             
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 TYR VAL ASN ASN LEU ASN          
SEQRES   4 A  198  VAL THR GLU GLU ALY 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 TYR VAL ASN ASN LEU ASN          
SEQRES   4 B  198  VAL THR GLU GLU ALY 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                                                  
MODRES 5GXO ALY A   68  LYS  MODIFIED RESIDUE                                   
MODRES 5GXO ALY B   68  LYS  MODIFIED RESIDUE                                   
HET    ALY  A  68      12                                                       
HET    ALY  B  68      12                                                       
HET     MN  A 301       1                                                       
HET     MN  B 301       1                                                       
HETNAM     ALY N(6)-ACETYLLYSINE                                                
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   1  ALY    2(C8 H16 N2 O3)                                              
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  HOH   *141(H2 O)                                                    
HELIX    1 AA1 ASN A   43  LYS A   53  1                                  11    
HELIX    2 AA2 LYS A   53  LYS A   75  1                                  23    
HELIX    3 AA3 ASP A   77  ASN A  104  1                                  28    
HELIX    4 AA4 GLY A  115  GLY A  126  1                                  12    
HELIX    5 AA5 SER A  127  GLY A  141  1                                  15    
HELIX    6 AA6 PRO A  169  GLY A  175  1                                   7    
HELIX    7 AA7 TRP A  185  ALA A  188  5                                   4    
HELIX    8 AA8 TYR A  189  LYS A  194  1                                   6    
HELIX    9 AA9 VAL A  196  TRP A  205  1                                  10    
HELIX   10 AB1 ASN A  206  ILE A  208  5                                   3    
HELIX   11 AB2 ASN A  209  ALA A  219  1                                  11    
HELIX   12 AB3 ASN B   43  LYS B   53  1                                  11    
HELIX   13 AB4 LYS B   53  LYS B   75  1                                  23    
HELIX   14 AB5 ASP B   77  LEU B   84  1                                   8    
HELIX   15 AB6 LEU B   84  LEU B  105  1                                  22    
HELIX   16 AB7 LYS B  114  GLY B  126  1                                  13    
HELIX   17 AB8 SER B  127  VAL B  142  1                                  16    
HELIX   18 AB9 PRO B  169  GLY B  175  1                                   7    
HELIX   19 AC1 TRP B  185  ALA B  188  5                                   4    
HELIX   20 AC2 TYR B  189  LYS B  194  1                                   6    
HELIX   21 AC3 VAL B  196  TRP B  205  1                                  10    
HELIX   22 AC4 ASN B  206  ILE B  208  5                                   3    
HELIX   23 AC5 ASN B  209  LYS B  221  1                                  13    
SHEET    1 AA1 3 HIS A 158  PRO A 165  0                                        
SHEET    2 AA1 3 GLY A 146  ASN A 153 -1  N  ASN A 153   O  HIS A 158           
SHEET    3 AA1 3 ILE A 177  ASP A 183 -1  O  LEU A 180   N  LEU A 150           
SHEET    1 AA2 3 HIS B 158  PRO B 165  0                                        
SHEET    2 AA2 3 GLY B 146  ASN B 153 -1  N  TRP B 149   O  ALA B 162           
SHEET    3 AA2 3 ILE B 177  ASP B 183 -1  O  LEU B 180   N  LEU B 150           
LINK         NE2 HIS A  50                MN    MN A 301     1555   1555  2.25  
LINK         C   GLU A  67                 N   ALY A  68     1555   1555  1.33  
LINK         C   ALY A  68                 N   TYR A  69     1555   1555  1.33  
LINK         NE2 HIS A  98                MN    MN A 301     1555   1555  2.22  
LINK         OD2 ASP A 183                MN    MN A 301     1555   1555  2.01  
LINK         NE2 HIS A 187                MN    MN A 301     1555   1555  2.29  
LINK         NE2 HIS B  50                MN    MN B 301     1555   1555  2.18  
LINK         C   GLU B  67                 N   ALY B  68     1555   1555  1.30  
LINK         C   ALY B  68                 N   TYR B  69     1555   1555  1.32  
LINK         NE2 HIS B  98                MN    MN B 301     1555   1555  2.22  
LINK         OD2 ASP B 183                MN    MN B 301     1555   1555  2.10  
LINK         NE2 HIS B 187                MN    MN B 301     1555   1555  2.23  
LINK        MN    MN A 301                 O   HOH A 424     1555   1555  2.28  
LINK        MN    MN B 301                 O   HOH B 428     1555   1555  2.24  
CISPEP   1 GLU A   39    PRO A   40          0        -4.44                     
CISPEP   2 GLU B   39    PRO B   40          0        -1.46                     
SITE     1 AC1  5 HIS A  50  HIS A  98  ASP A 183  HIS A 187                    
SITE     2 AC1  5 HOH A 424                                                     
SITE     1 AC2  5 HIS B  50  HIS B  98  ASP B 183  HIS B 187                    
SITE     2 AC2  5 HOH B 428                                                     
CRYST1   80.120   80.120  242.870  90.00  90.00 120.00 P 61 2 2     24          
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      0.012481  0.007206  0.000000        0.00000                         
SCALE2      0.000000  0.014412  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004117        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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