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Database: PDB
Entry: 1TYG
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HEADER    BIOSYNTHETIC PROTEIN                    07-JUL-04   1TYG              
TITLE     STRUCTURE OF THE THIAZOLE SYNTHASE/THIS COMPLEX                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: YJBS;                                                      
COMPND   3 CHAIN: B, G;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: THIAZOLE BIOSYNTHESIS PROTEIN THIG;                        
COMPND   7 CHAIN: A, C;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET-16B;                                  
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  10 ORGANISM_TAXID: 1423;                                                
SOURCE  11 GENE: THIG,BSU11690;                                                 
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  15 EXPRESSION_SYSTEM_PLASMID: PET-16B                                   
KEYWDS    ALPHA BETA BARREL, PROTEIN-PROTEIN COMPLEX, THIS, THIG, BIOSYNTHETIC  
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.C.SETTEMBRE,P.C.DORRESTEIN,H.ZHAI,A.CHATTERJEE,F.W.MCLAFFERTY,      
AUTHOR   2 T.P.BEGLEY,S.E.EALICK                                                
REVDAT   3   13-JUL-11 1TYG    1       VERSN                                    
REVDAT   2   24-FEB-09 1TYG    1       VERSN                                    
REVDAT   1   28-SEP-04 1TYG    0                                                
JRNL        AUTH   E.C.SETTEMBRE,P.C.DORRESTEIN,H.ZHAI,A.CHATTERJEE,            
JRNL        AUTH 2 F.W.MCLAFFERTY,T.P.BEGLEY,S.E.EALICK                         
JRNL        TITL   THIAMIN BIOSYNTHESIS IN BACILLUS SUBTILIS: STRUCTURE OF THE  
JRNL        TITL 2 THIAZOLE SYNTHASE/SULFUR CARRIER PROTEIN COMPLEX             
JRNL        REF    BIOCHEMISTRY                  V.  43 11647 2004              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15362849                                                     
JRNL        DOI    10.1021/BI0488911                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 3.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 15975                          
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) : 0.247                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.305                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1261                            
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) : 3.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.23                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1018                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2710                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 66                           
REMARK   3   BIN FREE R VALUE                    : 0.3750                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4540                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 5                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.14000                                              
REMARK   3    B22 (A**2) : 2.14000                                              
REMARK   3    B33 (A**2) : -3.21000                                             
REMARK   3    B12 (A**2) : 1.07000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.534         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.428         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.889        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.890                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.814                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4610 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6247 ; 2.022 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   603 ; 8.555 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   746 ; 0.131 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3381 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2364 ; 0.268 ; 0.200       
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):   141 ; 0.185 ; 0.200       
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):    44 ; 0.234 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.294 ; 0.200       
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):  3012 ; 0.493 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4816 ; 0.927 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1598 ; 1.607 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1431 ; 2.741 ; 4.500       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 5                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    104       A     143      2                      
REMARK   3           1     C    104       C     143      2                      
REMARK   3           2     A    161       A     164      6                      
REMARK   3           2     C    161       C     164      6                      
REMARK   3           3     A    339       A     341      6                      
REMARK   3           3     C    339       C     341      6                      
REMARK   3           4     A    165       A     338      4                      
REMARK   3           4     C    165       C     338      4                      
REMARK   3           5     A    149       A     160      6                      
REMARK   3           5     C    150       C     160      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    152 ;  0.07 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1379 ;  0.43 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    114 ;  0.74 ;  5.00           
REMARK   3   TIGHT THERMAL      1    A (A**2):    152 ;  0.20 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1379 ;  0.91 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):    114 ;  2.08 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    65                          
REMARK   3    ORIGIN FOR THE GROUP (A): -47.7597  -7.2680  35.7806              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0929 T22:   0.2949                                     
REMARK   3      T33:   0.4097 T12:  -0.4687                                     
REMARK   3      T13:   0.0622 T23:   0.0262                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.7906 L22:   9.3717                                     
REMARK   3      L33:   7.7373 L12:   6.8954                                     
REMARK   3      L13:  -3.2008 L23:  -6.8306                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5527 S12:  -0.9781 S13:   0.8766                       
REMARK   3      S21:   1.4122 S22:  -0.1544 S23:   0.9839                       
REMARK   3      S31:   0.1757 S32:  -0.7212 S33:  -0.3983                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   103        A   344                          
REMARK   3    RESIDUE RANGE :   A  1400        A  1400                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.5205   4.4924  16.9759              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4574 T22:   0.0670                                     
REMARK   3      T33:   0.2978 T12:  -0.1029                                     
REMARK   3      T13:  -0.0301 T23:  -0.1071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3397 L22:   1.9213                                     
REMARK   3      L33:   6.4834 L12:   0.6443                                     
REMARK   3      L13:   0.4220 L23:   2.0594                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4465 S12:  -0.1363 S13:  -0.1156                       
REMARK   3      S21:   0.2398 S22:   0.3331 S23:  -0.1727                       
REMARK   3      S31:   0.1868 S32:   0.7520 S33:  -0.7795                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   104        C   143                          
REMARK   3    RESIDUE RANGE :   C  2400        C  2400                          
REMARK   3    RESIDUE RANGE :   C   150        C   345                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.7601  11.7987  12.2642              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4510 T22:   2.2127                                     
REMARK   3      T33:   1.2166 T12:  -0.3433                                     
REMARK   3      T13:   0.2056 T23:  -0.9551                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4528 L22:   1.0938                                     
REMARK   3      L33:   3.7612 L12:  -0.5941                                     
REMARK   3      L13:  -0.3311 L23:   0.5665                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4190 S12:   0.1334 S13:   0.4778                       
REMARK   3      S21:  -0.1696 S22:   0.6486 S23:  -1.1545                       
REMARK   3      S31:  -0.5223 S32:   2.6883 S33:  -1.0677                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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: NULL                                      
REMARK   4                                                                      
REMARK   4 1TYG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023030.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.15                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 8-BM                               
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                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17866                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
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   (%): 62.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG 8K, 200 MM SODIUM CHLORIDE, 100   
REMARK 280  MM SODIUM PHOSPHATE PH 6.1, PH 7.15, VAPOR DIFFUSION, HANGING       
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 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+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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      267.53333            
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      133.76667            
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      200.65000            
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       66.88333            
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      334.41667            
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      267.53333            
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      133.76667            
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       66.88333            
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      200.65000            
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      334.41667            
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: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, C, G                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET B   -20                                                      
REMARK 465     GLY B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     ILE B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     ARG B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     GLY B    66                                                      
REMARK 465     GLY A   345                                                      
REMARK 465     THR A   346                                                      
REMARK 465     ALA A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     PRO A   350                                                      
REMARK 465     GLY A   351                                                      
REMARK 465     GLU A   352                                                      
REMARK 465     GLY A   353                                                      
REMARK 465     LEU A   354                                                      
REMARK 465     PRO A   355                                                      
REMARK 465     VAL C   144                                                      
REMARK 465     ARG C   145                                                      
REMARK 465     ARG C   146                                                      
REMARK 465     MET C   147                                                      
REMARK 465     ASN C   148                                                      
REMARK 465     ILE C   149                                                      
REMARK 465     THR C   346                                                      
REMARK 465     ALA C   347                                                      
REMARK 465     SER C   348                                                      
REMARK 465     SER C   349                                                      
REMARK 465     PRO C   350                                                      
REMARK 465     GLY C   351                                                      
REMARK 465     GLU C   352                                                      
REMARK 465     GLY C   353                                                      
REMARK 465     LEU C   354                                                      
REMARK 465     PRO C   355                                                      
REMARK 465     MET G   -20                                                      
REMARK 465     GLY G   -19                                                      
REMARK 465     HIS G   -18                                                      
REMARK 465     HIS G   -17                                                      
REMARK 465     HIS G   -16                                                      
REMARK 465     HIS G   -15                                                      
REMARK 465     HIS G   -14                                                      
REMARK 465     HIS G   -13                                                      
REMARK 465     HIS G   -12                                                      
REMARK 465     HIS G   -11                                                      
REMARK 465     HIS G   -10                                                      
REMARK 465     HIS G    -9                                                      
REMARK 465     SER G    -8                                                      
REMARK 465     SER G    -7                                                      
REMARK 465     GLY G    -6                                                      
REMARK 465     HIS G    -5                                                      
REMARK 465     ILE G    -4                                                      
REMARK 465     GLY G    -3                                                      
REMARK 465     GLY G    -2                                                      
REMARK 465     ARG G    -1                                                      
REMARK 465     HIS G     0                                                      
REMARK 465     GLY G    65                                                      
REMARK 465     GLY G    66                                                      
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     LYS B  13    CG   CD   CE   NZ                                   
REMARK 470     LYS A 129    CG   CD   CE   NZ                                   
REMARK 470     GLU A 151    CG   CD   OE1  OE2                                  
REMARK 470     SER A 153    OG                                                  
REMARK 470     GLN A 154    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 342    CG   CD   CE   NZ                                   
REMARK 470     GLN A 343    CG   CD   OE1  NE2                                  
REMARK 470     MET C 103    CG   SD   CE                                        
REMARK 470     LYS C 109    CG   CD   CE   NZ                                   
REMARK 470     PHE C 150    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU C 151    CG   CD   OE1  OE2                                  
REMARK 470     SER C 153    OG                                                  
REMARK 470     GLN C 154    CG   CD   OE1  NE2                                  
REMARK 470     PHE C 157    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG C 183    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 189    CG   CD   CE   NZ                                   
REMARK 470     LYS G  13    CG   CD   CE   NZ                                   
REMARK 470     LYS G  30    CG   CD   CE   NZ                                   
REMARK 470     LYS G  38    CG   CD   CE   NZ                                   
REMARK 470     LYS G  43    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLN C   221     OE1  GLU C   225              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE C 150   N     PHE C 150   CA      0.144                       
REMARK 500    ASN C 156   CG    ASN C 156   OD1     0.166                       
REMARK 500    GLU C 159   CG    GLU C 159   CD      0.110                       
REMARK 500    GLU C 159   CD    GLU C 159   OE1     0.092                       
REMARK 500    LEU C 163   C     LEU C 163   O       0.125                       
REMARK 500    SER C 164   CB    SER C 164   OG      0.194                       
REMARK 500    ARG C 186   NE    ARG C 186   CZ      0.093                       
REMARK 500    ARG C 186   CZ    ARG C 186   NH1     0.321                       
REMARK 500    ARG C 186   CZ    ARG C 186   NH2     0.095                       
REMARK 500    GLU C 224   CD    GLU C 224   OE1     0.091                       
REMARK 500    GLU C 224   CD    GLU C 224   OE2     0.076                       
REMARK 500    GLU C 225   CB    GLU C 225   CG      0.261                       
REMARK 500    GLU C 225   CG    GLU C 225   CD      0.231                       
REMARK 500    GLU C 225   CD    GLU C 225   OE1     0.088                       
REMARK 500    GLU C 225   CD    GLU C 225   OE2     0.084                       
REMARK 500    PHE C 227   CG    PHE C 227   CD1     0.105                       
REMARK 500    GLU C 245   CD    GLU C 245   OE1     0.073                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B  55   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    LEU A 230   CA  -  CB  -  CG  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    ASP A 236   CB  -  CG  -  OD2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ASP C 138   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG C 186   CD  -  NE  -  CZ  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    ARG C 186   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG C 186   NE  -  CZ  -  NH2 ANGL. DEV. = -11.4 DEGREES          
REMARK 500    ASP C 292   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP G  55   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN B   5       44.84     39.06                                   
REMARK 500    ILE B  18      -36.17    -39.98                                   
REMARK 500    GLN B  26       32.84     73.63                                   
REMARK 500    TYR B  46      -74.49    -49.71                                   
REMARK 500    HIS B  47      -17.18    -33.20                                   
REMARK 500    LEU B  51       83.80    -55.34                                   
REMARK 500    CYS B  52       71.85    -63.20                                   
REMARK 500    ASP B  53     -101.30     -7.01                                   
REMARK 500    ARG B  54       80.04    -67.18                                   
REMARK 500    VAL B  63       66.42   -150.87                                   
REMARK 500    ASP A 138      130.86     32.79                                   
REMARK 500    ILE A 139      108.65     77.53                                   
REMARK 500    GLU A 151     -128.85    -83.58                                   
REMARK 500    SER A 153       97.20    -44.95                                   
REMARK 500    LEU A 161      121.60    -31.80                                   
REMARK 500    ASP A 162       98.61    -63.43                                   
REMARK 500    ASP A 235        1.49     95.62                                   
REMARK 500    ALA A 285      124.72     78.68                                   
REMARK 500    ILE A 287      118.81    -31.81                                   
REMARK 500    LYS A 291      -64.42    -22.33                                   
REMARK 500    ASN A 307      -62.59   -124.81                                   
REMARK 500    ALA A 313        7.63    -69.71                                   
REMARK 500    ASP A 314      -18.65     50.87                                   
REMARK 500    ILE A 339      130.45    -32.72                                   
REMARK 500    PRO A 340     -179.66    -68.71                                   
REMARK 500    ASP C 138      119.69     31.43                                   
REMARK 500    ILE C 139      113.07     94.35                                   
REMARK 500    GLU C 151      -74.70    -80.54                                   
REMARK 500    ALA C 152      144.40    156.44                                   
REMARK 500    THR C 172       35.12    -96.95                                   
REMARK 500    GLU C 179      -74.28    -57.77                                   
REMARK 500    ASP C 195       57.02   -169.00                                   
REMARK 500    MET C 196      128.17    176.04                                   
REMARK 500    LEU C 208       34.73     76.98                                   
REMARK 500    GLU C 225       81.28    -68.64                                   
REMARK 500    THR C 233     -162.56   -124.86                                   
REMARK 500    SER C 234      -84.88    -97.87                                   
REMARK 500    ASP C 235        6.07    157.02                                   
REMARK 500    ALA C 250      126.48    168.27                                   
REMARK 500    MET C 252       74.78   -118.97                                   
REMARK 500    ILE C 258      -72.59    -65.43                                   
REMARK 500    PRO C 267     -106.87    -62.37                                   
REMARK 500    LEU C 268      -75.95     10.78                                   
REMARK 500    ASP C 284     -166.63   -125.85                                   
REMARK 500    ALA C 285      114.64     56.79                                   
REMARK 500    ASN C 307      -61.51   -108.81                                   
REMARK 500    ASP C 315       71.74   -151.12                                   
REMARK 500    SER C 333      -74.33    -48.25                                   
REMARK 500    ALA C 336      136.12   -170.92                                   
REMARK 500    ARG C 338      120.12    161.66                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      58 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP B   53     ARG B   54                 -147.20                    
REMARK 500 ASP A  235     ASP A  236                  148.70                    
REMARK 500 SER A  260     GLY A  261                 -146.85                    
REMARK 500 ASP A  314     ASP A  315                  140.48                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL B  56        24.9      L          L   OUTSIDE RANGE           
REMARK 500    SER A 137        21.9      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 213        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 314        24.0      L          L   OUTSIDE RANGE           
REMARK 500    SER C 137        24.6      L          L   OUTSIDE RANGE           
REMARK 500    GLN C 343        21.1      L          L   OUTSIDE RANGE           
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 PO4 A 1400                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 2400                
DBREF  1TYG B    1    66  UNP    O31617   O31617_BACSU     1     66             
DBREF  1TYG A  103   355  UNP    O31618   THIG_BACSU       3    255             
DBREF  1TYG C  103   355  UNP    O31618   THIG_BACSU       3    255             
DBREF  1TYG G    1    66  UNP    O31617   O31617_BACSU     1     66             
SEQADV 1TYG MET B  -20  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG GLY B  -19  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS B  -18  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS B  -17  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS B  -16  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS B  -15  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS B  -14  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS B  -13  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS B  -12  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS B  -11  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS B  -10  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS B   -9  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG SER B   -8  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG SER B   -7  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG GLY B   -6  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS B   -5  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG ILE B   -4  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG GLY B   -3  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG GLY B   -2  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG ARG B   -1  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS B    0  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG MET G  -20  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG GLY G  -19  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS G  -18  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS G  -17  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS G  -16  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS G  -15  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS G  -14  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS G  -13  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS G  -12  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS G  -11  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS G  -10  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS G   -9  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG SER G   -8  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG SER G   -7  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG GLY G   -6  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS G   -5  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG ILE G   -4  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG GLY G   -3  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG GLY G   -2  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG ARG G   -1  UNP  O31617              CLONING ARTIFACT               
SEQADV 1TYG HIS G    0  UNP  O31617              CLONING ARTIFACT               
SEQRES   1 B   87  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 B   87  SER GLY HIS ILE GLY GLY ARG HIS MET LEU GLN LEU ASN          
SEQRES   3 B   87  GLY LYS ASP VAL LYS TRP LYS LYS ASP THR GLY THR ILE          
SEQRES   4 B   87  GLN ASP LEU LEU ALA SER TYR GLN LEU GLU ASN LYS ILE          
SEQRES   5 B   87  VAL ILE VAL GLU ARG ASN LYS GLU ILE ILE GLY LYS GLU          
SEQRES   6 B   87  ARG TYR HIS GLU VAL GLU LEU CYS ASP ARG ASP VAL ILE          
SEQRES   7 B   87  GLU ILE VAL HIS PHE VAL GLY GLY GLY                          
SEQRES   1 A  253  MET LEU THR ILE GLY GLY LYS SER PHE GLN SER ARG LEU          
SEQRES   2 A  253  LEU LEU GLY THR GLY LYS TYR PRO SER PHE ASP ILE GLN          
SEQRES   3 A  253  LYS GLU ALA VAL ALA VAL SER GLU SER ASP ILE LEU THR          
SEQRES   4 A  253  PHE ALA VAL ARG ARG MET ASN ILE PHE GLU ALA SER GLN          
SEQRES   5 A  253  PRO ASN PHE LEU GLU GLN LEU ASP LEU SER LYS TYR THR          
SEQRES   6 A  253  LEU LEU PRO ASN THR ALA GLY ALA SER THR ALA GLU GLU          
SEQRES   7 A  253  ALA VAL ARG ILE ALA ARG LEU ALA LYS ALA SER GLY LEU          
SEQRES   8 A  253  CYS ASP MET ILE LYS VAL GLU VAL ILE GLY CYS SER ARG          
SEQRES   9 A  253  SER LEU LEU PRO ASP PRO VAL GLU THR LEU LYS ALA SER          
SEQRES  10 A  253  GLU GLN LEU LEU GLU GLU GLY PHE ILE VAL LEU PRO TYR          
SEQRES  11 A  253  THR SER ASP ASP VAL VAL LEU ALA ARG LYS LEU GLU GLU          
SEQRES  12 A  253  LEU GLY VAL HIS ALA ILE MET PRO GLY ALA SER PRO ILE          
SEQRES  13 A  253  GLY SER GLY GLN GLY ILE LEU ASN PRO LEU ASN LEU SER          
SEQRES  14 A  253  PHE ILE ILE GLU GLN ALA LYS VAL PRO VAL ILE VAL ASP          
SEQRES  15 A  253  ALA GLY ILE GLY SER PRO LYS ASP ALA ALA TYR ALA MET          
SEQRES  16 A  253  GLU LEU GLY ALA ASP GLY VAL LEU LEU ASN THR ALA VAL          
SEQRES  17 A  253  SER GLY ALA ASP ASP PRO VAL LYS MET ALA ARG ALA MET          
SEQRES  18 A  253  LYS LEU ALA VAL GLU ALA GLY ARG LEU SER TYR GLU ALA          
SEQRES  19 A  253  GLY ARG ILE PRO LEU LYS GLN TYR GLY THR ALA SER SER          
SEQRES  20 A  253  PRO GLY GLU GLY LEU PRO                                      
SEQRES   1 C  253  MET LEU THR ILE GLY GLY LYS SER PHE GLN SER ARG LEU          
SEQRES   2 C  253  LEU LEU GLY THR GLY LYS TYR PRO SER PHE ASP ILE GLN          
SEQRES   3 C  253  LYS GLU ALA VAL ALA VAL SER GLU SER ASP ILE LEU THR          
SEQRES   4 C  253  PHE ALA VAL ARG ARG MET ASN ILE PHE GLU ALA SER GLN          
SEQRES   5 C  253  PRO ASN PHE LEU GLU GLN LEU ASP LEU SER LYS TYR THR          
SEQRES   6 C  253  LEU LEU PRO ASN THR ALA GLY ALA SER THR ALA GLU GLU          
SEQRES   7 C  253  ALA VAL ARG ILE ALA ARG LEU ALA LYS ALA SER GLY LEU          
SEQRES   8 C  253  CYS ASP MET ILE LYS VAL GLU VAL ILE GLY CYS SER ARG          
SEQRES   9 C  253  SER LEU LEU PRO ASP PRO VAL GLU THR LEU LYS ALA SER          
SEQRES  10 C  253  GLU GLN LEU LEU GLU GLU GLY PHE ILE VAL LEU PRO TYR          
SEQRES  11 C  253  THR SER ASP ASP VAL VAL LEU ALA ARG LYS LEU GLU GLU          
SEQRES  12 C  253  LEU GLY VAL HIS ALA ILE MET PRO GLY ALA SER PRO ILE          
SEQRES  13 C  253  GLY SER GLY GLN GLY ILE LEU ASN PRO LEU ASN LEU SER          
SEQRES  14 C  253  PHE ILE ILE GLU GLN ALA LYS VAL PRO VAL ILE VAL ASP          
SEQRES  15 C  253  ALA GLY ILE GLY SER PRO LYS ASP ALA ALA TYR ALA MET          
SEQRES  16 C  253  GLU LEU GLY ALA ASP GLY VAL LEU LEU ASN THR ALA VAL          
SEQRES  17 C  253  SER GLY ALA ASP ASP PRO VAL LYS MET ALA ARG ALA MET          
SEQRES  18 C  253  LYS LEU ALA VAL GLU ALA GLY ARG LEU SER TYR GLU ALA          
SEQRES  19 C  253  GLY ARG ILE PRO LEU LYS GLN TYR GLY THR ALA SER SER          
SEQRES  20 C  253  PRO GLY GLU GLY LEU PRO                                      
SEQRES   1 G   87  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 G   87  SER GLY HIS ILE GLY GLY ARG HIS MET LEU GLN LEU ASN          
SEQRES   3 G   87  GLY LYS ASP VAL LYS TRP LYS LYS ASP THR GLY THR ILE          
SEQRES   4 G   87  GLN ASP LEU LEU ALA SER TYR GLN LEU GLU ASN LYS ILE          
SEQRES   5 G   87  VAL ILE VAL GLU ARG ASN LYS GLU ILE ILE GLY LYS GLU          
SEQRES   6 G   87  ARG TYR HIS GLU VAL GLU LEU CYS ASP ARG ASP VAL ILE          
SEQRES   7 G   87  GLU ILE VAL HIS PHE VAL GLY GLY GLY                          
HET    PO4  A1400       5                                                       
HET    PO4  C2400       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   5  PO4    2(O4 P 3-)                                                   
FORMUL   7  HOH   *5(H2 O)                                                      
HELIX    1   1 THR B   17  TYR B   25  1                                   9    
HELIX    2   2 GLY B   42  TYR B   46  5                                   5    
HELIX    3   3 SER A  124  GLU A  136  1                                  13    
HELIX    4   4 ASN A  156  LEU A  161  1                                   6    
HELIX    5   5 ASP A  162  TYR A  166  5                                   5    
HELIX    6   6 THR A  177  SER A  191  1                                  15    
HELIX    7   7 ASP A  211  GLU A  225  1                                  15    
HELIX    8   8 ASP A  236  GLU A  245  1                                  10    
HELIX    9   9 ASN A  266  ALA A  277  1                                  12    
HELIX   10  10 SER A  289  LEU A  299  1                                  11    
HELIX   11  11 ASN A  307  GLY A  312  1                                   6    
HELIX   12  12 ASP A  315  ALA A  336  1                                  22    
HELIX   13  13 SER C  124  GLU C  136  1                                  13    
HELIX   14  14 ASN C  156  LEU C  161  5                                   6    
HELIX   15  15 THR C  177  GLY C  192  1                                  16    
HELIX   16  16 ASP C  211  GLU C  225  1                                  15    
HELIX   17  17 ASP C  236  GLU C  245  1                                  10    
HELIX   18  18 LEU C  268  ALA C  277  1                                  10    
HELIX   19  19 SER C  289  LEU C  299  1                                  11    
HELIX   20  20 ASN C  307  GLY C  312  1                                   6    
HELIX   21  21 ASP C  315  ALA C  336  1                                  22    
HELIX   22  22 THR G   17  SER G   24  1                                   8    
HELIX   23  23 GLY G   42  TYR G   46  5                                   5    
SHEET    1   A 5 LYS B   7  VAL B   9  0                                        
SHEET    2   A 5 LEU B   2  LEU B   4 -1  N  LEU B   2   O  VAL B   9           
SHEET    3   A 5 VAL B  56  PHE B  62  1  O  ILE B  57   N  GLN B   3           
SHEET    4   A 5 ILE B  33  ARG B  36 -1  N  ILE B  33   O  VAL B  60           
SHEET    5   A 5 GLU B  39  ILE B  41 -1  O  ILE B  41   N  VAL B  34           
SHEET    1   B 4 LYS B   7  VAL B   9  0                                        
SHEET    2   B 4 LEU B   2  LEU B   4 -1  N  LEU B   2   O  VAL B   9           
SHEET    3   B 4 VAL B  56  PHE B  62  1  O  ILE B  57   N  GLN B   3           
SHEET    4   B 4 VAL A 144  ARG A 146 -1  O  ARG A 145   N  HIS B  61           
SHEET    1   C 2 THR A 105  ILE A 106  0                                        
SHEET    2   C 2 LYS A 109  SER A 110 -1  O  LYS A 109   N  ILE A 106           
SHEET    1   D 5 LEU A 168  PRO A 170  0                                        
SHEET    2   D 5 LEU A 140  PHE A 142  1  N  LEU A 140   O  LEU A 169           
SHEET    3   D 5 LEU A 115  GLY A 118  1  N  LEU A 117   O  THR A 141           
SHEET    4   D 5 GLY A 303  LEU A 306  1  O  VAL A 304   N  LEU A 116           
SHEET    5   D 5 ILE A 282  ASP A 284  1  N  VAL A 283   O  GLY A 303           
SHEET    1   E 3 MET A 196  VAL A 199  0                                        
SHEET    2   E 3 ILE A 228  THR A 233  1  O  TYR A 232   N  VAL A 199           
SHEET    3   E 3 MET A 252  PRO A 253  1  O  MET A 252   N  THR A 233           
SHEET    1   F 2 LEU C 104  ILE C 106  0                                        
SHEET    2   F 2 LYS C 109  PHE C 111 -1  O  PHE C 111   N  LEU C 104           
SHEET    1   G 5 LEU C 169  PRO C 170  0                                        
SHEET    2   G 5 LEU C 140  PHE C 142  1  N  LEU C 140   O  LEU C 169           
SHEET    3   G 5 LEU C 115  GLY C 118  1  N  LEU C 117   O  THR C 141           
SHEET    4   G 5 GLY C 303  LEU C 306  1  O  VAL C 304   N  LEU C 116           
SHEET    5   G 5 ILE C 282  VAL C 283  1  N  VAL C 283   O  LEU C 305           
SHEET    1   H 3 ILE C 197  VAL C 199  0                                        
SHEET    2   H 3 VAL C 229  THR C 233  1  O  TYR C 232   N  VAL C 199           
SHEET    3   H 3 MET C 252  PRO C 253  1  O  MET C 252   N  THR C 233           
SHEET    1   I 3 LYS G   7  VAL G   9  0                                        
SHEET    2   I 3 LEU G   2  LEU G   4 -1  N  LEU G   4   O  LYS G   7           
SHEET    3   I 3 VAL G  56  ILE G  57  1  O  ILE G  57   N  GLN G   3           
SHEET    1   J 2 VAL G  34  GLU G  35  0                                        
SHEET    2   J 2 ILE G  40  ILE G  41 -1  O  ILE G  41   N  VAL G  34           
SITE     1 AC1  6 ILE A 258  GLY A 259  ALA A 285  GLY A 286                    
SITE     2 AC1  6 ASN A 307  THR A 308                                          
SITE     1 AC2  7 ILE C 258  ALA C 285  GLY C 286  ILE C 287                    
SITE     2 AC2  7 LEU C 306  ASN C 307  THR C 308                               
CRYST1   91.654   91.654  401.300  90.00  90.00 120.00 P 65 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      0.010911  0.006299  0.000000        0.00000                         
SCALE2      0.000000  0.012598  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002492        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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