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Database: PDB
Entry: 4NIO
LinkDB: 4NIO
Original site: 4NIO 
HEADER    PROTEIN FIBRIL                          06-NOV-13   4NIO              
TITLE     GVTGIAQ SEGMENT 147-153 FROM HUMAN SUPEROXIDE DISMUTASE WITH I149T    
TITLE    2 MUTATION ASSOCIATED WITH A FAMILIAL FORM OF AMYOTROPHIC LATERAL      
TITLE    3 SCLEROSIS                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GVTGIAQ SEGMENT FROM SUPEROXIDE DISMUTASE [CU-ZN];         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 148-154;                                      
COMPND   5 SYNONYM: SUPEROXIDE DISMUTASE 1, HSOD1;                              
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606                                                 
KEYWDS    STERIC ZIPPER, CROSS-BETA SPINE, AMYLOID FIBER, PROTEIN FIBRIL        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.A.SIEVERS,M.R.SAWAYA,D.EISENBERG,M.I.IVANOVA                        
REVDAT   3   22-NOV-17 4NIO    1       REMARK                                   
REVDAT   2   22-JAN-14 4NIO    1       JRNL                                     
REVDAT   1   04-DEC-13 4NIO    0                                                
JRNL        AUTH   M.I.IVANOVA,S.A.SIEVERS,E.L.GUENTHER,L.M.JOHNSON,            
JRNL        AUTH 2 D.D.WINKLER,A.GALALELDEEN,M.R.SAWAYA,P.J.HART,D.S.EISENBERG  
JRNL        TITL   AGGREGATION-TRIGGERING SEGMENTS OF SOD1 FIBRIL FORMATION     
JRNL        TITL 2 SUPPORT A COMMON PATHWAY FOR FAMILIAL AND SPORADIC ALS.      
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 111   197 2014              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24344300                                                     
JRNL        DOI    10.1073/PNAS.1320786110                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 1053                           
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 11.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 116                             
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) : 1.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.34                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 51                           
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.69                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 7                            
REMARK   3   BIN FREE R VALUE                    : 0.5390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 45                                      
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 4                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 9.17                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.09000                                             
REMARK   3    B22 (A**2) : -0.24000                                             
REMARK   3    B33 (A**2) : 0.64000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.46000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.071         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.073         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.052         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.390         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):    44 ; 0.004 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):    24 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):    59 ; 1.064 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    61 ; 0.611 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):     6 ; 5.920 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):     1 ;45.167 ;30.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):     6 ; 3.500 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):     8 ; 0.063 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):    50 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):     6 ; 0.000 ; 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):    33 ; 0.534 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):    15 ; 0.071 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):    51 ; 0.894 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):    11 ; 0.640 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):     8 ; 1.261 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 4NIO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000083251.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : CRYOGENICALLY-COOLED SINGLE        
REMARK 200                                   CRYSTAL SI(220)                    
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 1053                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.12800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26900                            
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: PHASER 2.1.4                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 16.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 4.5, 0.7 M       
REMARK 280  HEXANEDIOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       23.89350            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        2.39350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       23.89350            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000        2.39350            
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 300 REMARK: BIOLOGICAL UNIT IS A PAIR OF BETA-SHEETS. ONE SHEET IS       
REMARK 300 COMPOSED OF SYMMETRY OPERATORS X,Y,Z; X,Y-1,Z; X,Y+1,Z; X,Y-2,Z; X,  
REMARK 300 Y+2,Z, ETC.: THE OPPOSING SHEET IS COMPOSED OF SYMMETRY OPERATORS 1/ 
REMARK 300 2-X,1/2+Y,-Z; 1/2-X,-1/2+Y,-Z; 1/2-X, 3/2+Y,-Z; 1/2-X,-3/2+Y,-Z; 1/  
REMARK 300 2-X, 5/2+Y,-Z, ETC.                                                  
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: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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       -4.78700            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000       -9.57400            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000        4.78700            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000        9.57400            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   6 -1.000000  0.000000  0.000000       23.89350            
REMARK 350   BIOMT2   6  0.000000  1.000000  0.000000        2.39350            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   7 -1.000000  0.000000  0.000000       23.89350            
REMARK 350   BIOMT2   7  0.000000  1.000000  0.000000       -2.39350            
REMARK 350   BIOMT3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   8 -1.000000  0.000000  0.000000       23.89350            
REMARK 350   BIOMT2   8  0.000000  1.000000  0.000000       -7.18050            
REMARK 350   BIOMT3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   9 -1.000000  0.000000  0.000000       23.89350            
REMARK 350   BIOMT2   9  0.000000  1.000000  0.000000        7.18050            
REMARK 350   BIOMT3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1  10 -1.000000  0.000000  0.000000       23.89350            
REMARK 350   BIOMT2  10  0.000000  1.000000  0.000000       11.96750            
REMARK 350   BIOMT3  10  0.000000  0.000000 -1.000000        0.00000            
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4NIN   RELATED DB: PDB                                   
REMARK 900 A DIFFERENT SEGMENT (RESIDUES 101-107) FROM THE SAME PROTEIN, HUMAN  
REMARK 900 SOD.                                                                 
REMARK 900 RELATED ID: 4NIP   RELATED DB: PDB                                   
DBREF  4NIO A    1     7  UNP    P00441   SODC_HUMAN     148    154             
SEQADV 4NIO THR A    3  UNP  P00441    ILE   150 ENGINEERED MUTATION            
SEQRES   1 A    7  GLY VAL THR GLY ILE ALA GLN                                  
FORMUL   2  HOH   *4(H2 O)                                                      
CRYST1   47.787    4.787   17.687  90.00 109.39  90.00 C 1 2 1       4          
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      0.020926  0.000000  0.007366        0.00000                         
SCALE2      0.000000  0.208899  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.059939        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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