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Database: PDB
Entry: 5WOR
LinkDB: 5WOR
Original site: 5WOR 
HEADER    PROTEIN FIBRIL                          02-AUG-17   5WOR              
TITLE     CORKSCREW ASSEMBLY OF SOD1 RESIDUES 28-38 WITH FAMILIAL MUTATION G37R 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 FRAGMENT: UNP RESIDUES 29-39;                                        
COMPND   5 SYNONYM: SUPEROXIDE DISMUTASE 1,HSOD1;                               
COMPND   6 EC: 1.15.1.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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;                                                
SOURCE   6 OTHER_DETAILS: SYNTHESIZED                                           
KEYWDS    AMYLOID-RELATED OLIGOMER, PROTEIN FIBRIL                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SANGWAN,M.R.SAWAYA,D.S.EISENBERG                                    
REVDAT   2   18-JUL-18 5WOR    1       JRNL                                     
REVDAT   1   30-MAY-18 5WOR    0                                                
JRNL        AUTH   S.SANGWAN,M.R.SAWAYA,K.A.MURRAY,M.P.HUGHES,D.S.EISENBERG     
JRNL        TITL   ATOMIC STRUCTURES OF CORKSCREW-FORMING SEGMENTS OF SOD1      
JRNL        TITL 2 REVEAL VARIED OLIGOMER CONFORMATIONS.                        
JRNL        REF    PROTEIN SCI.                  V.  27  1231 2018              
JRNL        REFN                   ESSN 1469-896X                               
JRNL        PMID   29453800                                                     
JRNL        DOI    10.1002/PRO.3391                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.77 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.77                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.77                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 5422                           
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)  : 0.214                          
REMARK   3   R VALUE            (WORKING SET)  : 0.211                          
REMARK   3   FREE R VALUE                      : 0.247                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 9.680                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 525                            
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               : 5                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.77                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.10                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 94.30                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 1454                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2489                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 1312                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2468                   
REMARK   3   BIN FREE R VALUE                        : 0.2687                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 9.77                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 142                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 918                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 27                                      
REMARK   3   SOLVENT ATOMS            : 14                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 74.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.57270                                             
REMARK   3    B22 (A**2) : -4.57270                                             
REMARK   3    B33 (A**2) : 9.14540                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.410               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.476               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.289               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.458               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.290               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.913                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.879                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 951    ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 1252   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 358    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 10     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 124    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 951    ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 110    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : 72     ; 1.000  ; HARMONIC            
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 1005   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.20                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.44                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 22.67                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5WOR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229375.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
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) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
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   : 5444                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.770                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.18300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.90700                            
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                                                
REMARK 200 STARTING MODEL: FOUR STRANDS COMPOSED OF RESIDUES VKVWGSI OF PDBID   
REMARK 200  5DLI WERE USED AS INITIAL MODEL                                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR CONTAINED 15% PEG 3350, 0.3M   
REMARK 280  SODIUM MALONATE, PH 7, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
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   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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       32.97567            
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       65.95133            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       65.95133            
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       32.97567            
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: EICOSAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J          
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       59.61500            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       32.97567            
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     ARG B  10    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG I  10    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS E   9      -60.37    -91.01                                   
REMARK 500    TRP H   5      119.29   -162.76                                   
REMARK 500    TRP J   5      119.02   -166.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI B 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL I 101                 
DBREF  5WOR A    1    11  UNP    P00441   SODC_HUMAN      29     39             
DBREF  5WOR B    1    11  UNP    P00441   SODC_HUMAN      29     39             
DBREF  5WOR C    1    11  UNP    P00441   SODC_HUMAN      29     39             
DBREF  5WOR D    1    11  UNP    P00441   SODC_HUMAN      29     39             
DBREF  5WOR E    1    11  UNP    P00441   SODC_HUMAN      29     39             
DBREF  5WOR F    1    11  UNP    P00441   SODC_HUMAN      29     39             
DBREF  5WOR G    1    11  UNP    P00441   SODC_HUMAN      29     39             
DBREF  5WOR H    1    11  UNP    P00441   SODC_HUMAN      29     39             
DBREF  5WOR I    1    11  UNP    P00441   SODC_HUMAN      29     39             
DBREF  5WOR J    1    11  UNP    P00441   SODC_HUMAN      29     39             
SEQADV 5WOR LYS A    1  UNP  P00441    PRO    29 ENGINEERED MUTATION            
SEQADV 5WOR ARG A   10  UNP  P00441    GLY    38 ENGINEERED MUTATION            
SEQADV 5WOR LYS B    1  UNP  P00441    PRO    29 ENGINEERED MUTATION            
SEQADV 5WOR ARG B   10  UNP  P00441    GLY    38 ENGINEERED MUTATION            
SEQADV 5WOR LYS C    1  UNP  P00441    PRO    29 ENGINEERED MUTATION            
SEQADV 5WOR ARG C   10  UNP  P00441    GLY    38 ENGINEERED MUTATION            
SEQADV 5WOR LYS D    1  UNP  P00441    PRO    29 ENGINEERED MUTATION            
SEQADV 5WOR ARG D   10  UNP  P00441    GLY    38 ENGINEERED MUTATION            
SEQADV 5WOR LYS E    1  UNP  P00441    PRO    29 ENGINEERED MUTATION            
SEQADV 5WOR ARG E   10  UNP  P00441    GLY    38 ENGINEERED MUTATION            
SEQADV 5WOR LYS F    1  UNP  P00441    PRO    29 ENGINEERED MUTATION            
SEQADV 5WOR ARG F   10  UNP  P00441    GLY    38 ENGINEERED MUTATION            
SEQADV 5WOR LYS G    1  UNP  P00441    PRO    29 ENGINEERED MUTATION            
SEQADV 5WOR ARG G   10  UNP  P00441    GLY    38 ENGINEERED MUTATION            
SEQADV 5WOR LYS H    1  UNP  P00441    PRO    29 ENGINEERED MUTATION            
SEQADV 5WOR ARG H   10  UNP  P00441    GLY    38 ENGINEERED MUTATION            
SEQADV 5WOR LYS I    1  UNP  P00441    PRO    29 ENGINEERED MUTATION            
SEQADV 5WOR ARG I   10  UNP  P00441    GLY    38 ENGINEERED MUTATION            
SEQADV 5WOR LYS J    1  UNP  P00441    PRO    29 ENGINEERED MUTATION            
SEQADV 5WOR ARG J   10  UNP  P00441    GLY    38 ENGINEERED MUTATION            
SEQRES   1 A   11  LYS VAL LYS VAL TRP GLY SER ILE LYS ARG LEU                  
SEQRES   1 B   11  LYS VAL LYS VAL TRP GLY SER ILE LYS ARG LEU                  
SEQRES   1 C   11  LYS VAL LYS VAL TRP GLY SER ILE LYS ARG LEU                  
SEQRES   1 D   11  LYS VAL LYS VAL TRP GLY SER ILE LYS ARG LEU                  
SEQRES   1 E   11  LYS VAL LYS VAL TRP GLY SER ILE LYS ARG LEU                  
SEQRES   1 F   11  LYS VAL LYS VAL TRP GLY SER ILE LYS ARG LEU                  
SEQRES   1 G   11  LYS VAL LYS VAL TRP GLY SER ILE LYS ARG LEU                  
SEQRES   1 H   11  LYS VAL LYS VAL TRP GLY SER ILE LYS ARG LEU                  
SEQRES   1 I   11  LYS VAL LYS VAL TRP GLY SER ILE LYS ARG LEU                  
SEQRES   1 J   11  LYS VAL LYS VAL TRP GLY SER ILE LYS ARG LEU                  
HET    MLI  A 101       7                                                       
HET    MLI  B 101       7                                                       
HET    MLI  E 101       7                                                       
HET    GOL  I 101       6                                                       
HETNAM     MLI MALONATE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL  11  MLI    3(C3 H2 O4 2-)                                               
FORMUL  14  GOL    C3 H8 O3                                                     
FORMUL  15  HOH   *14(H2 O)                                                     
SHEET    1 AA110 VAL A   2  ILE A   8  0                                        
SHEET    2 AA110 VAL B   2  ILE B   8 -1  O  GLY B   6   N  VAL A   4           
SHEET    3 AA110 VAL C   2  ILE C   8 -1  O  LYS C   3   N  TRP B   5           
SHEET    4 AA110 VAL D   2  ILE D   8 -1  O  ILE D   8   N  VAL C   2           
SHEET    5 AA110 VAL E   2  ILE E   8 -1  O  LYS E   3   N  TRP D   5           
SHEET    6 AA110 VAL F   2  ILE F   8 -1  O  VAL F   4   N  GLY E   6           
SHEET    7 AA110 VAL G   2  ILE G   8 -1  O  LYS G   3   N  TRP F   5           
SHEET    8 AA110 VAL H   2  ILE H   8 -1  O  VAL H   4   N  GLY G   6           
SHEET    9 AA110 VAL I   2  ILE I   8 -1  O  TRP I   5   N  LYS H   3           
SHEET   10 AA110 VAL J   2  ILE J   8 -1  O  GLY J   6   N  VAL I   4           
SITE     1 AC1  6 LYS A   3  TRP A   5  MLI B 101  TRP F   5                    
SITE     2 AC1  6 TRP G   5  TRP J   5                                          
SITE     1 AC2  4 TRP A   5  MLI A 101  TRP B   5  GLY B   6                    
SITE     1 AC3  4 LYS E   3  TRP E   5  TRP F   5  GLY F   6                    
SITE     1 AC4  4 LYS I   3  VAL I   4  TRP J   5  GLY J   6                    
CRYST1   59.615   59.615   98.927  90.00  90.00 120.00 P 31 2 1     60          
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      0.016774  0.009685  0.000000        0.00000                         
SCALE2      0.000000  0.019369  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010108        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system