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Database: PDB
Entry: 1Y13
LinkDB: 1Y13
Original site: 1Y13 
HEADER    LYASE, BIOSYNTHETIC PROTEIN             17-NOV-04   1Y13              
TITLE     STRUCTURAL ANALYSIS OF PLASMODIUM FALCIPARUM 6-PYRUVOYL               
TITLE    2 TETRAHYDROPTERIN SYNTHASE (PTPS)                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 6-PYRUVOYL TETRAHYDROPTERIN SYNTHASE;                      
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: PTPS;                                                       
COMPND   5 EC: 4.2.3.12;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;                          
SOURCE   3 ORGANISM_COMMON: MALARIA PARASITE P. FALCIPARUM;                     
SOURCE   4 ORGANISM_TAXID: 5833;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21STAR(DE3);                             
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET14B                                    
KEYWDS    STRUCTURAL GENOMICS OF PATHOGENIC PROTOZOA CONSORTIUM, SGPP,          
KEYWDS   2 STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, LYASE,       
KEYWDS   3 BIOSYNTHETIC PROTEIN                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.BOSCH,W.G.J.HOL,STRUCTURAL GENOMICS OF PATHOGENIC PROTOZOA          
AUTHOR   2 CONSORTIUM (SGPP)                                                    
REVDAT   3   13-JUL-11 1Y13    1       VERSN                                    
REVDAT   2   24-FEB-09 1Y13    1       VERSN                                    
REVDAT   1   04-JAN-05 1Y13    0                                                
JRNL        AUTH   J.BOSCH,W.G.J.HOL,                                           
JRNL        AUTH 2 STRUCTURAL GENOMICS OF PATHOGENIC PROTOZOA CONSORTIUM (SGPP) 
JRNL        TITL   STRUCTURAL ANALYSIS OF PLASMODIUM FALCIPARUM 6-PYRUVOYL      
JRNL        TITL 2 TETRAHYDROPTERIN SYNTHASE (PTPS)                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 34709                          
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1847                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.32                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4905                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2400                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 270                          
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3972                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 126                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 53.55                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.30000                                              
REMARK   3    B22 (A**2) : 0.30000                                              
REMARK   3    B33 (A**2) : -0.60000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.209         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.182         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.138         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.157        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4112 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5552 ; 1.409 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   486 ; 6.478 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   192 ;35.361 ;24.375       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   739 ;15.235 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;21.741 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   615 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3058 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1709 ; 0.208 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2866 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   165 ; 0.162 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.071 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    83 ; 0.217 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.173 ; 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):  2508 ; 2.632 ; 6.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3993 ; 3.132 ;10.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1843 ; 5.093 ;10.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1559 ; 6.397 ;15.000       
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 B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 5                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     11       A      90      2                      
REMARK   3           1     B     11       B      90      2                      
REMARK   3           1     C     11       C      90      2                      
REMARK   3           2     A     91       A      99      4                      
REMARK   3           2     B     91       B      99      4                      
REMARK   3           2     C     91       C      99      4                      
REMARK   3           3     A    100       A     113      2                      
REMARK   3           3     B    100       B     113      2                      
REMARK   3           3     C    100       C     113      2                      
REMARK   3           4     A    114       A     116      4                      
REMARK   3           4     B    114       B     116      4                      
REMARK   3           4     C    114       C     116      4                      
REMARK   3           5     A    117       A     175      2                      
REMARK   3           5     B    117       B     175      2                      
REMARK   3           5     C    117       C     175      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    604 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    604 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):    604 ;  0.04 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    729 ;  0.55 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    729 ;  0.46 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    729 ;  0.38 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):    604 ;  0.16 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):    604 ;  0.15 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):    604 ;  0.16 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    729 ;  1.23 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    729 ;  1.18 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):    729 ;  1.24 ;  2.00           
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 :   A    11        A   173                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.3174  15.0529  20.8863              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1681 T22:  -0.0711                                     
REMARK   3      T33:  -0.2554 T12:   0.0527                                     
REMARK   3      T13:  -0.0178 T23:   0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6786 L22:   1.9248                                     
REMARK   3      L33:   1.9237 L12:   2.6050                                     
REMARK   3      L13:  -1.4092 L23:  -1.0725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0518 S12:   0.3761 S13:   0.1379                       
REMARK   3      S21:  -0.0853 S22:   0.1811 S23:   0.0803                       
REMARK   3      S31:  -0.0589 S32:  -0.0676 S33:  -0.2329                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    11        C    81                          
REMARK   3    ORIGIN FOR THE GROUP (A):  91.1914  -0.8526  22.3356              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0300 T22:  -0.0803                                     
REMARK   3      T33:   0.1400 T12:   0.0859                                     
REMARK   3      T13:   0.0239 T23:  -0.0889                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.4113 L22:   0.8895                                     
REMARK   3      L33:   2.4386 L12:  -1.5743                                     
REMARK   3      L13:   3.6803 L23:   0.0270                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0213 S12:  -0.0177 S13:  -0.7114                       
REMARK   3      S21:  -0.1590 S22:   0.0616 S23:  -0.3654                       
REMARK   3      S31:   0.2686 S32:  -0.0417 S33:  -0.0403                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   123        C   173                          
REMARK   3    ORIGIN FOR THE GROUP (A):  92.2576  -1.1593  15.3162              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0454 T22:   0.0066                                     
REMARK   3      T33:   0.1683 T12:   0.1030                                     
REMARK   3      T13:   0.1033 T23:  -0.1973                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6917 L22:   1.7105                                     
REMARK   3      L33:   4.7862 L12:   0.1576                                     
REMARK   3      L13:   3.0091 L23:   0.2394                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2444 S12:   0.2258 S13:  -0.9214                       
REMARK   3      S21:  -0.1706 S22:  -0.0395 S23:  -0.3537                       
REMARK   3      S31:   0.5085 S32:  -0.2358 S33:  -0.2049                       
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   : 1.20                                          
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 1Y13 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030982.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUN-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979029                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36614                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 11.400                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.16200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.50                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.01210                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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   (%): 58.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 1000, HEPES, AMMONIUM CHLORIDE -     
REMARK 280  RESERVOIR: 2.2 M LITHIUM CHLORIDE, PH 6.8, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
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   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       65.55550            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       51.65950            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       51.65950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       98.33325            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       51.65950            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       51.65950            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       32.77775            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       51.65950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       51.65950            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       98.33325            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       51.65950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       51.65950            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       32.77775            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       65.55550            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 20480 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 36000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -276.0 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  0.000000 -1.000000  0.000000      103.31900            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      103.31900            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       65.55550            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PQS                                                   
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH C 176  LIES ON A SPECIAL POSITION.                          
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 A    -7                                                      
REMARK 465     ALA A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     MET A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     ASN A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     ASP A    10                                                      
REMARK 465     MET B    -7                                                      
REMARK 465     ALA B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     ASN B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     ASP B    10                                                      
REMARK 465     MET C    -7                                                      
REMARK 465     ALA C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     GLU C     4                                                      
REMARK 465     GLU C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     LEU C     7                                                      
REMARK 465     ASN C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     ASP C    10                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  19    OE1  OE2                                            
REMARK 470     GLU A  69    OE1  OE2                                            
REMARK 470     LYS A  72    CD   NZ                                             
REMARK 470     LYS A  77    CD   CE   NZ                                        
REMARK 470     GLU A 105    OE2                                                 
REMARK 470     GLU A 114    OE1  OE2                                            
REMARK 470     GLU B  19    OE1  OE2                                            
REMARK 470     LYS B  77    CE   NZ                                             
REMARK 470     GLU B  94    OE2                                                 
REMARK 470     GLU B 109    OE2                                                 
REMARK 470     GLU B 114    OE2                                                 
REMARK 470     GLU C  19    OE1  OE2                                            
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    LEU A  84   CA  -  CB  -  CG  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    LEU C  84   CA  -  CB  -  CG  ANGL. DEV. =  14.1 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    LYS A  97     -131.13     52.54                                   
REMARK 500    SER A 125       45.44    -82.51                                   
REMARK 500    ASP A 143      111.04     73.01                                   
REMARK 500    LYS B  97     -118.57     55.35                                   
REMARK 500    SER B 125       44.61    -85.25                                   
REMARK 500    ASP B 143      110.74     70.19                                   
REMARK 500    HIS C  80       45.73     72.40                                   
REMARK 500    LYS C  97     -116.51     57.86                                   
REMARK 500    SER C 125       44.20    -85.69                                   
REMARK 500    ASP C 143      108.78     72.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     BIO A  175                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 174  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  41   NE2                                                    
REMARK 620 2 BIO A 175   O9   95.8                                              
REMARK 620 3 HIS A  29   NE2  91.2 101.5                                        
REMARK 620 4 BIO A 175   O10  97.0  77.5 171.7                                  
REMARK 620 5 HIS A  43   NE2  94.4 158.2  97.6  82.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 174  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 BIO B 175   O9                                                     
REMARK 620 2 BIO B 175   O10  74.0                                              
REMARK 620 3 HIS B  43   NE2 156.7  84.3                                        
REMARK 620 4 HIS B  29   NE2  96.7 167.7 103.3                                  
REMARK 620 5 HIS B  41   NE2  96.7 102.5  96.4  86.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 174  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 BIO C 175   O9                                                     
REMARK 620 2 HIS C  41   NE2  88.5                                              
REMARK 620 3 BIO C 175   O10  74.2 113.1                                        
REMARK 620 4 HIS C  29   NE2 101.9  81.6 164.3                                  
REMARK 620 5 HIS C  43   NE2 158.2  90.6  86.2  99.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 174                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 174                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 174                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BIO A 175                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BIO B 175                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BIO C 175                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: PFAL004546AAA   RELATED DB: TARGETDB                     
DBREF  1Y13 A    1   173  GB     23612358 NP_703938        1    173             
DBREF  1Y13 B    1   173  GB     23612358 NP_703938        1    173             
DBREF  1Y13 C    1   173  GB     23612358 NP_703938        1    173             
SEQADV 1Y13 MET A   -7  GB   23612358            INITIATING METHIONINE          
SEQADV 1Y13 ALA A   -6  GB   23612358            CLONING ARTIFACT               
SEQADV 1Y13 HIS A   -5  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 HIS A   -4  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 HIS A   -3  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 HIS A   -2  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 HIS A   -1  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 HIS A    0  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 MSE A  142  GB   23612358  MET   142 MODIFIED RESIDUE               
SEQADV 1Y13 MET B   -7  GB   23612358            INITIATING METHIONINE          
SEQADV 1Y13 ALA B   -6  GB   23612358            CLONING ARTIFACT               
SEQADV 1Y13 HIS B   -5  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 HIS B   -4  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 HIS B   -3  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 HIS B   -2  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 HIS B   -1  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 HIS B    0  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 MSE B  142  GB   23612358  MET   142 MODIFIED RESIDUE               
SEQADV 1Y13 MET C   -7  GB   23612358            INITIATING METHIONINE          
SEQADV 1Y13 ALA C   -6  GB   23612358            CLONING ARTIFACT               
SEQADV 1Y13 HIS C   -5  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 HIS C   -4  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 HIS C   -3  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 HIS C   -2  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 HIS C   -1  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 HIS C    0  GB   23612358            EXPRESSION TAG                 
SEQADV 1Y13 MSE C  142  GB   23612358  MET   142 MODIFIED RESIDUE               
SEQRES   1 A  181  MET ALA HIS HIS HIS HIS HIS HIS MET MET LYS GLU GLU          
SEQRES   2 A  181  THR LEU ASN SER ASP ASN SER SER ALA GLU VAL SER VAL          
SEQRES   3 A  181  GLU SER PRO SER PHE SER PHE ASN CYS ALA HIS PHE ILE          
SEQRES   4 A  181  ALA TYR ASN GLY PHE ARG GLU THR LEU HIS GLY HIS ASN          
SEQRES   5 A  181  TYR ASN VAL SER LEU LYS VAL ARG GLY TYR VAL ARG ASP          
SEQRES   6 A  181  ASP GLY TYR VAL ILE ASP PHE SER ILE LEU LYS GLU LYS          
SEQRES   7 A  181  VAL LYS LYS VAL CYS ASN LYS LEU ASP HIS HIS PHE ILE          
SEQRES   8 A  181  LEU PRO ILE TYR SER ASP VAL LEU LYS PHE GLU ASN VAL          
SEQRES   9 A  181  LYS ASN ASN ILE LYS ILE ILE CYS GLU ASP ASN SER GLU          
SEQRES  10 A  181  TYR SER PHE PRO GLU ARG ASP CYS ILE LYS LEU PRO ILE          
SEQRES  11 A  181  LYS HIS SER SER THR GLU GLU ILE GLY GLN TYR ILE LEU          
SEQRES  12 A  181  ASN GLN LEU ILE GLU GLU MSE ASP VAL SER LEU LEU LYS          
SEQRES  13 A  181  SER ARG HIS ILE HIS TYR ILE GLU ILE SER VAL SER GLU          
SEQRES  14 A  181  SER PRO THR GLN LYS ALA ILE VAL HIS LYS TYR ILE              
SEQRES   1 B  181  MET ALA HIS HIS HIS HIS HIS HIS MET MET LYS GLU GLU          
SEQRES   2 B  181  THR LEU ASN SER ASP ASN SER SER ALA GLU VAL SER VAL          
SEQRES   3 B  181  GLU SER PRO SER PHE SER PHE ASN CYS ALA HIS PHE ILE          
SEQRES   4 B  181  ALA TYR ASN GLY PHE ARG GLU THR LEU HIS GLY HIS ASN          
SEQRES   5 B  181  TYR ASN VAL SER LEU LYS VAL ARG GLY TYR VAL ARG ASP          
SEQRES   6 B  181  ASP GLY TYR VAL ILE ASP PHE SER ILE LEU LYS GLU LYS          
SEQRES   7 B  181  VAL LYS LYS VAL CYS ASN LYS LEU ASP HIS HIS PHE ILE          
SEQRES   8 B  181  LEU PRO ILE TYR SER ASP VAL LEU LYS PHE GLU ASN VAL          
SEQRES   9 B  181  LYS ASN ASN ILE LYS ILE ILE CYS GLU ASP ASN SER GLU          
SEQRES  10 B  181  TYR SER PHE PRO GLU ARG ASP CYS ILE LYS LEU PRO ILE          
SEQRES  11 B  181  LYS HIS SER SER THR GLU GLU ILE GLY GLN TYR ILE LEU          
SEQRES  12 B  181  ASN GLN LEU ILE GLU GLU MSE ASP VAL SER LEU LEU LYS          
SEQRES  13 B  181  SER ARG HIS ILE HIS TYR ILE GLU ILE SER VAL SER GLU          
SEQRES  14 B  181  SER PRO THR GLN LYS ALA ILE VAL HIS LYS TYR ILE              
SEQRES   1 C  181  MET ALA HIS HIS HIS HIS HIS HIS MET MET LYS GLU GLU          
SEQRES   2 C  181  THR LEU ASN SER ASP ASN SER SER ALA GLU VAL SER VAL          
SEQRES   3 C  181  GLU SER PRO SER PHE SER PHE ASN CYS ALA HIS PHE ILE          
SEQRES   4 C  181  ALA TYR ASN GLY PHE ARG GLU THR LEU HIS GLY HIS ASN          
SEQRES   5 C  181  TYR ASN VAL SER LEU LYS VAL ARG GLY TYR VAL ARG ASP          
SEQRES   6 C  181  ASP GLY TYR VAL ILE ASP PHE SER ILE LEU LYS GLU LYS          
SEQRES   7 C  181  VAL LYS LYS VAL CYS ASN LYS LEU ASP HIS HIS PHE ILE          
SEQRES   8 C  181  LEU PRO ILE TYR SER ASP VAL LEU LYS PHE GLU ASN VAL          
SEQRES   9 C  181  LYS ASN ASN ILE LYS ILE ILE CYS GLU ASP ASN SER GLU          
SEQRES  10 C  181  TYR SER PHE PRO GLU ARG ASP CYS ILE LYS LEU PRO ILE          
SEQRES  11 C  181  LYS HIS SER SER THR GLU GLU ILE GLY GLN TYR ILE LEU          
SEQRES  12 C  181  ASN GLN LEU ILE GLU GLU MSE ASP VAL SER LEU LEU LYS          
SEQRES  13 C  181  SER ARG HIS ILE HIS TYR ILE GLU ILE SER VAL SER GLU          
SEQRES  14 C  181  SER PRO THR GLN LYS ALA ILE VAL HIS LYS TYR ILE              
MODRES 1Y13 MSE A  142  MET  SELENOMETHIONINE                                   
MODRES 1Y13 MSE B  142  MET  SELENOMETHIONINE                                   
MODRES 1Y13 MSE C  142  MET  SELENOMETHIONINE                                   
HET    MSE  A 142       8                                                       
HET    MSE  B 142       8                                                       
HET    MSE  C 142       8                                                       
HET     ZN  A 174       1                                                       
HET     ZN  B 174       1                                                       
HET     ZN  C 174       1                                                       
HET    BIO  A 175      15                                                       
HET    BIO  B 175      17                                                       
HET    BIO  C 175      17                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      ZN ZINC ION                                                         
HETNAM     BIO BIOPTERIN                                                        
FORMUL   1  MSE    3(C5 H11 N O2 SE)                                            
FORMUL   4   ZN    3(ZN 2+)                                                     
FORMUL   7  BIO    3(C9 H11 N5 O3)                                              
FORMUL  10  HOH   *126(H2 O)                                                    
HELIX    1   1 ASP A   63  ASP A   79  1                                  17    
HELIX    2   2 SER A  126  ASP A  143  1                                  18    
HELIX    3   3 ASP A  143  ARG A  150  1                                   8    
HELIX    4   4 ASP B   63  ASP B   79  1                                  17    
HELIX    5   5 SER B  126  ASP B  143  1                                  18    
HELIX    6   6 ASP B  143  ARG B  150  1                                   8    
HELIX    7   7 ASP C   63  ASP C   79  1                                  17    
HELIX    8   8 SER C  126  ASP C  143  1                                  18    
HELIX    9   9 ASP C  143  ARG C  150  1                                   8    
SHEET    1   A13 ALA A  14  HIS A  29  0                                        
SHEET    2   A13 HIS A  41  GLY A  53 -1  O  VAL A  47   N  PHE A  23           
SHEET    3   A13 TYR A 154  SER A 162 -1  O  GLU A 156   N  LYS A  50           
SHEET    4   A13 GLN A 165  TYR A 172 -1  O  ALA A 167   N  VAL A 159           
SHEET    5   A13 ALA C  14  HIS C  29 -1  O  GLU C  15   N  ILE A 168           
SHEET    6   A13 HIS C  41  GLY C  53 -1  O  VAL C  47   N  PHE C  23           
SHEET    7   A13 TYR C 154  SER C 162 -1  O  GLU C 156   N  LYS C  50           
SHEET    8   A13 GLN C 165  TYR C 172 -1  O  ALA C 167   N  VAL C 159           
SHEET    9   A13 ALA B  14  HIS B  29 -1  N  GLU B  15   O  ILE C 168           
SHEET   10   A13 HIS B  41  GLY B  53 -1  O  VAL B  47   N  PHE B  23           
SHEET   11   A13 TYR B 154  SER B 162 -1  O  GLU B 156   N  LYS B  50           
SHEET   12   A13 GLN B 165  TYR B 172 -1  O  ALA B 167   N  VAL B 159           
SHEET   13   A13 ALA A  14  HIS A  29 -1  N  GLU A  15   O  ILE B 168           
SHEET    1   B 2 ALA A  32  TYR A  33  0                                        
SHEET    2   B 2 PHE A  36  ARG A  37 -1  O  PHE A  36   N  TYR A  33           
SHEET    1   C 2 PHE A  82  PRO A  85  0                                        
SHEET    2   C 2 CYS A 117  LEU A 120  1  O  ILE A 118   N  PHE A  82           
SHEET    1   D 3 LEU A  91  VAL A  96  0                                        
SHEET    2   D 3 ASN A  99  CYS A 104 -1  O  ILE A 103   N  LYS A  92           
SHEET    3   D 3 GLU A 109  PRO A 113 -1  O  TYR A 110   N  ILE A 102           
SHEET    1   E 2 ALA B  32  TYR B  33  0                                        
SHEET    2   E 2 PHE B  36  ARG B  37 -1  O  PHE B  36   N  TYR B  33           
SHEET    1   F 2 PHE B  82  PRO B  85  0                                        
SHEET    2   F 2 CYS B 117  LEU B 120  1  O  ILE B 118   N  LEU B  84           
SHEET    1   G 3 LEU B  91  VAL B  96  0                                        
SHEET    2   G 3 ASN B  99  CYS B 104 -1  O  LYS B 101   N  GLU B  94           
SHEET    3   G 3 GLU B 109  PRO B 113 -1  O  PHE B 112   N  ILE B 100           
SHEET    1   H 2 ALA C  32  TYR C  33  0                                        
SHEET    2   H 2 PHE C  36  ARG C  37 -1  O  PHE C  36   N  TYR C  33           
SHEET    1   I 2 PHE C  82  PRO C  85  0                                        
SHEET    2   I 2 CYS C 117  LEU C 120  1  O  ILE C 118   N  PHE C  82           
SHEET    1   J 3 LEU C  91  VAL C  96  0                                        
SHEET    2   J 3 ASN C  99  CYS C 104 -1  O  LYS C 101   N  GLU C  94           
SHEET    3   J 3 GLU C 109  PRO C 113 -1  O  PHE C 112   N  ILE C 100           
LINK         C   GLU A 141                 N   MSE A 142     1555   1555  1.33  
LINK         C   MSE A 142                 N   ASP A 143     1555   1555  1.33  
LINK        ZN    ZN A 174                 NE2 HIS A  41     1555   1555  2.13  
LINK        ZN    ZN A 174                 O9  BIO A 175     1555   1555  2.34  
LINK        ZN    ZN A 174                 NE2 HIS A  29     1555   1555  2.29  
LINK        ZN    ZN A 174                 O10 BIO A 175     1555   1555  1.95  
LINK        ZN    ZN A 174                 NE2 HIS A  43     1555   1555  2.25  
LINK         C   GLU B 141                 N   MSE B 142     1555   1555  1.33  
LINK         C   MSE B 142                 N   ASP B 143     1555   1555  1.34  
LINK        ZN    ZN B 174                 O9  BIO B 175     1555   1555  2.35  
LINK        ZN    ZN B 174                 O10 BIO B 175     1555   1555  2.39  
LINK        ZN    ZN B 174                 NE2 HIS B  43     1555   1555  2.23  
LINK        ZN    ZN B 174                 NE2 HIS B  29     1555   1555  2.26  
LINK        ZN    ZN B 174                 NE2 HIS B  41     1555   1555  2.11  
LINK         C   GLU C 141                 N   MSE C 142     1555   1555  1.33  
LINK         C   MSE C 142                 N   ASP C 143     1555   1555  1.34  
LINK        ZN    ZN C 174                 O9  BIO C 175     1555   1555  2.48  
LINK        ZN    ZN C 174                 NE2 HIS C  41     1555   1555  2.40  
LINK        ZN    ZN C 174                 O10 BIO C 175     1555   1555  2.61  
LINK        ZN    ZN C 174                 NE2 HIS C  29     1555   1555  2.33  
LINK        ZN    ZN C 174                 NE2 HIS C  43     1555   1555  2.24  
SITE     1 AC1  4 HIS A  29  HIS A  41  HIS A  43  BIO A 175                    
SITE     1 AC2  5 HIS B  29  HIS B  41  HIS B  43  GLU B 161                    
SITE     2 AC2  5 BIO B 175                                                     
SITE     1 AC3  5 HIS C  29  HIS C  41  HIS C  43  GLU C 161                    
SITE     2 AC3  5 BIO C 175                                                     
SITE     1 AC4 13 HIS A  29  ILE A  31  GLU A  38  HIS A  41                    
SITE     2 AC4 13 HIS A  43  GLU A 128  GLU A 161   ZN A 174                    
SITE     3 AC4 13 HIS B  80  TYR C  60  ILE C  62  ASP C  63                    
SITE     4 AC4 13 PHE C  64                                                     
SITE     1 AC5 15 TYR A  60  ILE A  62  ASP A  63  PHE A  64                    
SITE     2 AC5 15 HIS A  80  HIS B  29  ILE B  31  GLU B  38                    
SITE     3 AC5 15 HIS B  41  HIS B  43  SER B 126  THR B 127                    
SITE     4 AC5 15 GLU B 128  GLU B 161   ZN B 174                               
SITE     1 AC6 14 TYR B  60  ILE B  62  ASP B  63  PHE B  64                    
SITE     2 AC6 14 ILE C  31  GLU C  38  HIS C  41  HIS C  43                    
SITE     3 AC6 14 HIS C  80  SER C 126  THR C 127  GLU C 128                    
SITE     4 AC6 14 GLU C 161   ZN C 174                                          
CRYST1  103.319  103.319  131.111  90.00  90.00  90.00 P 43 21 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      0.009679  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009679  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007627        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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