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Database: PDB
Entry: 1T6I
LinkDB: 1T6I
Original site: 1T6I 
HEADER    OXIDOREDUCTASE                          06-MAY-04   1T6I              
TITLE     NICKEL SUPEROXIDE DISMUTASE (NISOD) APO STRUCTURE                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [NI];                                 
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: NISOD, NICKEL- CONTAINING SUPEROXIDE DISMUTASE;             
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR;                        
SOURCE   3 ORGANISM_TAXID: 1902;                                                
SOURCE   4 GENE: SODN, SOD1, SCO5254, 2SC7G11.16C;                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
KEYWDS    NICKEL, 4-HELIX BUNDLE, HEXAMER, SUPEROXIDE DISMUTASE, NISOD, SOD,    
KEYWDS   2 APO, OXIDOREDUCTASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.P.BARONDEAU,C.J.KASSMANN,C.K.BRUNS,J.A.TAINER,E.D.GETZOFF           
REVDAT   3   13-JUL-11 1T6I    1       VERSN                                    
REVDAT   2   24-FEB-09 1T6I    1       VERSN                                    
REVDAT   1   13-JUL-04 1T6I    0                                                
JRNL        AUTH   D.P.BARONDEAU,C.J.KASSMANN,C.K.BRUNS,J.A.TAINER,E.D.GETZOFF  
JRNL        TITL   NICKEL SUPEROXIDE DISMUTASE STRUCTURE AND MECHANISM.         
JRNL        REF    BIOCHEMISTRY                  V.  43  8038 2004              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15209499                                                     
JRNL        DOI    10.1021/BI0496081                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.81 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.81                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 309608.650                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 8940                           
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 SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.292                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.400                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 927                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.81                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1177                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3470                       
REMARK   3   BIN FREE R VALUE                    : 0.4060                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 113                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.038                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2647                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 22                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 63.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -22.36000                                            
REMARK   3    B22 (A**2) : -5.57000                                             
REMARK   3    B33 (A**2) : 27.93000                                             
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) : 0.37                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.41                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.47                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.48                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.130                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.38                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.55                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.180 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.010 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.650 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.520 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.29                                                 
REMARK   3   BSOL        : 10.00                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WAT.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1T6I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022373.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.911656, 0.97912, 0.979311        
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9300                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.4000                            
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.26700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MPEG 2000, HEPES, METHANOL, CALCIUM      
REMARK 280  CHLORIDE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       55.32950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.32950            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       30.21500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.12050            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       30.21500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.12050            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       55.32950            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       30.21500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       55.12050            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       55.32950            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       30.21500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       55.12050            
REMARK 290   SMTRY3   8  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: THE BIOLOGICAL ASSEMBLY IS A HEXAMER GENERATED FROM THE      
REMARK 300 TRIMER IN THE ASYMMETRIC UNIT BY THE OPERATION -X,Y,-Z+1/2           
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10490 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 28720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       55.32950            
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     MSE A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     CYS A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     CYS A     6                                                      
REMARK 465     MSE B     0                                                      
REMARK 465     HIS B     1                                                      
REMARK 465     CYS B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     CYS B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     MSE C     0                                                      
REMARK 465     HIS C     1                                                      
REMARK 465     CYS C     2                                                      
REMARK 465     ASP C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     PRO C     5                                                      
REMARK 465     CYS C     6                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     ALA C   117                                                      
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    ASP A  10      134.15   -170.04                                   
REMARK 500    ASP A  32       -9.96   -145.50                                   
REMARK 500    ASP B  10      126.56   -172.00                                   
REMARK 500    PRO B  11        2.60    -68.88                                   
REMARK 500    TYR B  62      -60.76    -90.84                                   
REMARK 500    TYR C  62      -68.33    -93.69                                   
REMARK 500    PHE C  63      104.07    -57.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR B  62         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1T6I A    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  1T6I B    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  1T6I C    1   117  UNP    P80735   SODN_STRCO      15    131             
SEQADV 1T6I MSE A    0  UNP  P80735              INITIATING METHIONINE          
SEQADV 1T6I MSE A   28  UNP  P80735    MET    42 MODIFIED RESIDUE               
SEQADV 1T6I MSE A   85  UNP  P80735    LEU    99 ENGINEERED                     
SEQADV 1T6I MSE B    0  UNP  P80735              INITIATING METHIONINE          
SEQADV 1T6I MSE B   28  UNP  P80735    MET    42 MODIFIED RESIDUE               
SEQADV 1T6I MSE B   85  UNP  P80735    LEU    99 ENGINEERED                     
SEQADV 1T6I MSE C    0  UNP  P80735              INITIATING METHIONINE          
SEQADV 1T6I MSE C   28  UNP  P80735    MET    42 MODIFIED RESIDUE               
SEQADV 1T6I MSE C   85  UNP  P80735    LEU    99 ENGINEERED                     
SEQRES   1 A  118  MSE HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA          
SEQRES   2 A  118  GLN ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN          
SEQRES   3 A  118  GLU LYS MSE ALA GLY ASN ASP ASP PRO HIS PHE GLN THR          
SEQRES   4 A  118  ARG ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA          
SEQRES   5 A  118  LYS HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS          
SEQRES   6 A  118  PRO PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU          
SEQRES   7 A  118  VAL ASN ASP THR LEU LYS ALA MSE SER ALA ALA LYS GLY          
SEQRES   8 A  118  SER LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR          
SEQRES   9 A  118  ILE ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS          
SEQRES  10 A  118  ALA                                                          
SEQRES   1 B  118  MSE HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA          
SEQRES   2 B  118  GLN ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN          
SEQRES   3 B  118  GLU LYS MSE ALA GLY ASN ASP ASP PRO HIS PHE GLN THR          
SEQRES   4 B  118  ARG ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA          
SEQRES   5 B  118  LYS HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS          
SEQRES   6 B  118  PRO PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU          
SEQRES   7 B  118  VAL ASN ASP THR LEU LYS ALA MSE SER ALA ALA LYS GLY          
SEQRES   8 B  118  SER LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR          
SEQRES   9 B  118  ILE ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS          
SEQRES  10 B  118  ALA                                                          
SEQRES   1 C  118  MSE HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA          
SEQRES   2 C  118  GLN ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN          
SEQRES   3 C  118  GLU LYS MSE ALA GLY ASN ASP ASP PRO HIS PHE GLN THR          
SEQRES   4 C  118  ARG ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA          
SEQRES   5 C  118  LYS HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS          
SEQRES   6 C  118  PRO PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU          
SEQRES   7 C  118  VAL ASN ASP THR LEU LYS ALA MSE SER ALA ALA LYS GLY          
SEQRES   8 C  118  SER LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR          
SEQRES   9 C  118  ILE ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS          
SEQRES  10 C  118  ALA                                                          
MODRES 1T6I MSE A   28  MET  SELENOMETHIONINE                                   
MODRES 1T6I MSE A   85  MET  SELENOMETHIONINE                                   
MODRES 1T6I MSE B   28  MET  SELENOMETHIONINE                                   
MODRES 1T6I MSE B   85  MET  SELENOMETHIONINE                                   
MODRES 1T6I MSE C   28  MET  SELENOMETHIONINE                                   
MODRES 1T6I MSE C   85  MET  SELENOMETHIONINE                                   
HET    MSE  A  28       8                                                       
HET    MSE  A  85       8                                                       
HET    MSE  B  28       8                                                       
HET    MSE  B  85       8                                                       
HET    MSE  C  28       8                                                       
HET    MSE  C  85       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    6(C5 H11 N O2 SE)                                            
FORMUL   4  HOH   *22(H2 O)                                                     
HELIX    1   1 PRO A   11  ASN A   31  1                                  21    
HELIX    2   2 ASP A   33  ASP A   61  1                                  29    
HELIX    3   3 LYS A   64  TYR A   71  1                                   8    
HELIX    4   4 GLU A   73  SER A   91  1                                  19    
HELIX    5   5 ASP A   93  LYS A  115  1                                  23    
HELIX    6   6 PRO B   11  MSE B   28  1                                  18    
HELIX    7   7 ASP B   33  TYR B   62  1                                  30    
HELIX    8   8 LYS B   64  TYR B   71  1                                   8    
HELIX    9   9 GLU B   73  GLY B   90  1                                  18    
HELIX   10  10 ASP B   93  ALA B  117  1                                  25    
HELIX   11  11 PRO C   11  GLY C   30  1                                  20    
HELIX   12  12 ASP C   33  TYR C   62  1                                  30    
HELIX   13  13 LYS C   64  TYR C   71  1                                   8    
HELIX   14  14 GLU C   73  GLY C   90  1                                  18    
HELIX   15  15 ASP C   93  GLU C  113  1                                  21    
LINK         C   LYS A  27                 N   MSE A  28     1555   1555  1.34  
LINK         C   MSE A  28                 N   ALA A  29     1555   1555  1.34  
LINK         C   ALA A  84                 N   MSE A  85     1555   1555  1.34  
LINK         C   MSE A  85                 N   SER A  86     1555   1555  1.34  
LINK         C   LYS B  27                 N   MSE B  28     1555   1555  1.34  
LINK         C   MSE B  28                 N   ALA B  29     1555   1555  1.33  
LINK         C   ALA B  84                 N   MSE B  85     1555   1555  1.34  
LINK         C   MSE B  85                 N   SER B  86     1555   1555  1.34  
LINK         C   LYS C  27                 N   MSE C  28     1555   1555  1.34  
LINK         C   MSE C  28                 N   ALA C  29     1555   1555  1.33  
LINK         C   ALA C  84                 N   MSE C  85     1555   1555  1.34  
LINK         C   MSE C  85                 N   SER C  86     1555   1555  1.34  
CRYST1   60.430  110.241  110.659  90.00  90.00  90.00 C 2 2 21     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      0.016548  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009071  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009037        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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