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Database: PDB
Entry: 5ZT9
LinkDB: 5ZT9
Original site: 5ZT9 
HEADER    BIOSYNTHETIC PROTEIN                    02-MAY-18   5ZT9              
TITLE     SIRB FROM BACILLUS SUBTILIS WITH NI2+                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIROHYDROCHLORIN FERROCHELATASE;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 4.99.1.4;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS (STRAIN 168);                 
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: SIRB, YLNE, BSU15620;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: C41(DE3)                                   
KEYWDS    CHELATASE, BIOSYNTHETIC PROTEIN                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.FUJISHIRO                                                           
REVDAT   1   12-JUN-19 5ZT9    0                                                
JRNL        AUTH   T.FUJISHIRO                                                  
JRNL        TITL   A ROUTE FOR METAL ACQUISITION FOR CHELATASE REACTION         
JRNL        TITL 2 CATALYZED BY SIRB FROM BACILLUS SUBTILIS                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.13_2998                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.43                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 13777                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 690                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 43.4312 -  4.7863    1.00     2687   142  0.1893 0.1992        
REMARK   3     2  4.7863 -  3.7997    1.00     2606   137  0.1909 0.2366        
REMARK   3     3  3.7997 -  3.3196    1.00     2608   138  0.2248 0.2757        
REMARK   3     4  3.3196 -  3.0162    1.00     2579   135  0.2541 0.2958        
REMARK   3     5  3.0162 -  2.8001    1.00     2607   138  0.2646 0.2931        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.680           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.61                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.79                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 31 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8008   5.0903  24.5300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3792 T22:   0.3731                                     
REMARK   3      T33:   0.3085 T12:   0.0248                                     
REMARK   3      T13:   0.0097 T23:   0.1154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2763 L22:   1.5593                                     
REMARK   3      L33:   4.0300 L12:   0.6389                                     
REMARK   3      L13:   1.0222 L23:   1.2386                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0576 S12:   0.5544 S13:   0.3458                       
REMARK   3      S21:  -0.1375 S22:   0.1513 S23:   0.1055                       
REMARK   3      S31:  -0.0970 S32:   0.0573 S33:  -0.2229                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 32 THROUGH 106 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -18.8295   0.9062  31.6654              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3227 T22:   0.4039                                     
REMARK   3      T33:   0.3331 T12:  -0.0438                                     
REMARK   3      T13:   0.0092 T23:   0.1189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3912 L22:   2.6953                                     
REMARK   3      L33:   2.2091 L12:  -0.1387                                     
REMARK   3      L13:   1.8432 L23:  -1.3357                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0548 S12:  -0.6051 S13:  -0.4349                       
REMARK   3      S21:   0.2709 S22:   0.1694 S23:   0.4116                       
REMARK   3      S31:  -0.1027 S32:  -0.3997 S33:  -0.2486                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 107 THROUGH 155 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.5846  -4.6396  35.4180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3686 T22:   0.2235                                     
REMARK   3      T33:   0.3975 T12:   0.0056                                     
REMARK   3      T13:  -0.0511 T23:   0.0718                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2817 L22:   3.1920                                     
REMARK   3      L33:   2.4526 L12:   1.1347                                     
REMARK   3      L13:   1.5114 L23:   0.1660                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2997 S12:  -0.2074 S13:  -0.5494                       
REMARK   3      S21:   0.1542 S22:  -0.1716 S23:  -0.2355                       
REMARK   3      S31:   0.3151 S32:  -0.0709 S33:  -0.1321                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 156 THROUGH 198 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.3630   2.2569  40.6685              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3318 T22:   0.3183                                     
REMARK   3      T33:   0.3812 T12:   0.0371                                     
REMARK   3      T13:  -0.0274 T23:   0.0377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2073 L22:   4.5525                                     
REMARK   3      L33:   2.6248 L12:   1.1724                                     
REMARK   3      L13:   0.8348 L23:   0.7226                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0576 S12:  -0.6581 S13:  -0.2260                       
REMARK   3      S21:   0.3293 S22:   0.0704 S23:  -0.3573                       
REMARK   3      S31:   0.1043 S32:  -0.0324 S33:  -0.1246                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 199 THROUGH 257 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7191   0.4735  33.2002              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3909 T22:   0.2862                                     
REMARK   3      T33:   0.3728 T12:   0.0088                                     
REMARK   3      T13:  -0.0000 T23:   0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6805 L22:   2.3973                                     
REMARK   3      L33:   1.2039 L12:   1.5111                                     
REMARK   3      L13:   1.0005 L23:   0.0810                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4994 S12:  -0.3795 S13:  -0.4368                       
REMARK   3      S21:   0.1741 S22:  -0.2316 S23:  -0.0244                       
REMARK   3      S31:  -0.0227 S32:  -0.1312 S33:  -0.2064                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 106 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  42.2572  14.4989   5.2311              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3854 T22:   0.3854                                     
REMARK   3      T33:   0.2574 T12:   0.0317                                     
REMARK   3      T13:   0.0409 T23:  -0.0190                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1005 L22:   4.2397                                     
REMARK   3      L33:   2.8789 L12:   0.9646                                     
REMARK   3      L13:  -0.1931 L23:  -1.0541                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1179 S12:   0.4608 S13:   0.0892                       
REMARK   3      S21:  -0.0822 S22:   0.0846 S23:  -0.2830                       
REMARK   3      S31:  -0.2433 S32:   0.1737 S33:  -0.1857                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 107 THROUGH 155 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4369   7.8489   9.6264              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5063 T22:   0.5245                                     
REMARK   3      T33:   0.4773 T12:  -0.0378                                     
REMARK   3      T13:  -0.0416 T23:   0.1198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0443 L22:   4.5484                                     
REMARK   3      L33:   3.5477 L12:  -0.2806                                     
REMARK   3      L13:  -2.0348 L23:  -1.0796                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1427 S12:   0.8503 S13:   0.4735                       
REMARK   3      S21:  -0.7034 S22:   0.2249 S23:   0.2749                       
REMARK   3      S31:   0.3535 S32:  -0.5340 S33:  -0.1176                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 156 THROUGH 180 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   9.6280  15.6090   4.6639              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5601 T22:   1.0243                                     
REMARK   3      T33:   0.7685 T12:  -0.0729                                     
REMARK   3      T13:  -0.0897 T23:   0.3394                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3943 L22:   6.6833                                     
REMARK   3      L33:   2.3247 L12:  -1.2770                                     
REMARK   3      L13:   1.5899 L23:  -0.7440                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0954 S12:   1.0221 S13:   0.6729                       
REMARK   3      S21:  -0.2848 S22:   0.2040 S23:   0.0574                       
REMARK   3      S31:  -0.2210 S32:  -0.2601 S33:  -0.3205                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 181 THROUGH 254 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.0874  13.8604  10.7441              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3656 T22:   0.4262                                     
REMARK   3      T33:   0.4654 T12:   0.0110                                     
REMARK   3      T13:  -0.0033 T23:   0.0612                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2487 L22:   1.5825                                     
REMARK   3      L33:   3.8927 L12:   0.7654                                     
REMARK   3      L13:  -1.4668 L23:  -1.2948                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2460 S12:   0.0519 S13:   0.3601                       
REMARK   3      S21:   0.0373 S22:   0.2181 S23:   0.7130                       
REMARK   3      S31:  -0.3641 S32:  -0.4970 S33:  -0.4430                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND RESID 2 THROUGH 254)           
REMARK   3     SELECTION          : (CHAIN B AND RESID 2 THROUGH 254)           
REMARK   3     ATOM PAIRS NUMBER  : 2426                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5ZT9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300007623.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NUMERICAL LINK TYPE SI(111)        
REMARK 200                                   DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13781                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.426                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.487                              
REMARK 200  R MERGE                    (I) : 0.17800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.2400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.42                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.99700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.270                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 5ZT7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE, 20 %(W/V) PEG 6000, 10MM   
REMARK 280  NICKEL SULFATE, PH 9.0, VAPOR DIFFUSION, SITTING DROP,              
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       26.85000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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 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   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A   258                                                      
REMARK 465     ALA A   259                                                      
REMARK 465     ALA A   260                                                      
REMARK 465     HIS A   261                                                      
REMARK 465     MET B   -11                                                      
REMARK 465     GLY B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     SER B   255                                                      
REMARK 465     TYR B   256                                                      
REMARK 465     ALA B   257                                                      
REMARK 465     SER B   258                                                      
REMARK 465     ALA B   259                                                      
REMARK 465     ALA B   260                                                      
REMARK 465     HIS B   261                                                      
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    LEU A  44       -5.02     67.44                                   
REMARK 500    ALA A  74     -148.92   -147.40                                   
REMARK 500    HIS A  79      -62.24   -131.35                                   
REMARK 500    ALA A 168      -37.51     76.22                                   
REMARK 500    LYS A 182      -71.09    -49.92                                   
REMARK 500    ASP A 183       85.24     78.85                                   
REMARK 500    ASN A 217       43.00    -90.26                                   
REMARK 500    ASP A 252     -128.20    -90.21                                   
REMARK 500    SER A 255       85.84     57.05                                   
REMARK 500    LEU B  44       -4.34     69.34                                   
REMARK 500    ALA B  74     -147.00   -147.76                                   
REMARK 500    HIS B  79      -59.69   -133.25                                   
REMARK 500    ALA B 168      -37.19     75.97                                   
REMARK 500    ASP B 183       90.52     76.30                                   
REMARK 500    ASN B 217       44.38    -91.37                                   
REMARK 500    ASP B 252       64.28    135.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              NI A 301  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  79   NE2                                                    
REMARK 620 2 GLU A  83   OE2  75.8                                              
REMARK 620 3 HOH A 424   O   163.9  88.8                                        
REMARK 620 4 HOH A 403   O    84.9  61.6  91.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 302  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 115   NE2                                                    
REMARK 620 2 HIS A 229   NE2  90.3                                              
REMARK 620 3 HOH A 425   O    86.0  90.1                                        
REMARK 620 4 HOH A 430   O    86.8 168.7  78.9                                  
REMARK 620 5 HOH A 436   O    93.9 110.6 159.3  80.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 301  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  79   NE2                                                    
REMARK 620 2 GLU B  83   OE1  80.0                                              
REMARK 620 3 HOH B 418   O   100.7  90.1                                        
REMARK 620 4 HOH B 413   O    82.4 145.8 122.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NI B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NI B 302                  
DBREF  5ZT9 A    1   261  UNP    O34632   SIRB_BACSU       1    261             
DBREF  5ZT9 B    1   261  UNP    O34632   SIRB_BACSU       1    261             
SEQADV 5ZT9 MET A  -11  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 GLY A  -10  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 SER A   -9  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 SER A   -8  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 HIS A   -7  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 HIS A   -6  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 HIS A   -5  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 HIS A   -4  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 HIS A   -3  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 HIS A   -2  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 SER A   -1  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 SER A    0  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 MET B  -11  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 GLY B  -10  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 SER B   -9  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 SER B   -8  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 HIS B   -7  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 HIS B   -6  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 HIS B   -5  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 HIS B   -4  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 HIS B   -3  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 HIS B   -2  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 SER B   -1  UNP  O34632              EXPRESSION TAG                 
SEQADV 5ZT9 SER B    0  UNP  O34632              EXPRESSION TAG                 
SEQRES   1 A  273  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER MET          
SEQRES   2 A  273  LYS GLN ALA ILE LEU TYR VAL GLY HIS GLY SER ARG VAL          
SEQRES   3 A  273  LYS LYS ALA GLN GLN GLU ALA ALA ALA PHE LEU GLU GLY          
SEQRES   4 A  273  CYS LYS ALA HIS ILE SER VAL PRO VAL GLN GLU ILE SER          
SEQRES   5 A  273  PHE LEU GLU LEU GLN GLU PRO THR ILE GLU THR GLY PHE          
SEQRES   6 A  273  GLU ALA CYS VAL LYS GLN GLY ALA THR HIS ILE ALA VAL          
SEQRES   7 A  273  VAL PRO LEU LEU LEU LEU THR ALA ALA HIS ALA LYS HIS          
SEQRES   8 A  273  ASP ILE PRO GLU GLU ILE VAL ARG VAL ALA SER ARG TYR          
SEQRES   9 A  273  PRO SER VAL ARG ILE SER TYR GLY LYS PRO ILE GLY ILE          
SEQRES  10 A  273  ASP GLU GLU VAL VAL LYS ALA VAL TYR HIS ARG MET LYS          
SEQRES  11 A  273  ASP ILE GLY VAL PRO TYR GLU ASN ALA ARG VAL VAL LEU          
SEQRES  12 A  273  ILE GLY ARG GLY SER SER ASP PRO ASP VAL LYS ARG ASP          
SEQRES  13 A  273  VAL THR GLY ILE ALA ASN LEU LEU GLN GLU MET VAL PRO          
SEQRES  14 A  273  VAL LYS GLU VAL ILE PRO CYS PHE LEU THR ALA CYS GLY          
SEQRES  15 A  273  PRO ASN TYR LYS GLU VAL PHE SER GLU LEU GLU LYS ASP          
SEQRES  16 A  273  ASP GLY ILE THR THR PHE ILE VAL PRO TYR LEU LEU PHE          
SEQRES  17 A  273  THR GLY MET LEU MET ASN GLU ILE GLU ARG GLU VAL GLN          
SEQRES  18 A  273  LYS LEU LYS ALA HIS ASN PRO ASN VAL TYR LEU SER SER          
SEQRES  19 A  273  TYR ILE GLY PHE HIS PRO HIS VAL LYS ASN ALA PHE LEU          
SEQRES  20 A  273  ASN ARG VAL ARG GLU THR ALA ALA ASN SER GLU GLY GLN          
SEQRES  21 A  273  PHE ASP PHE ASP GLY GLY SER TYR ALA SER ALA ALA HIS          
SEQRES   1 B  273  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER MET          
SEQRES   2 B  273  LYS GLN ALA ILE LEU TYR VAL GLY HIS GLY SER ARG VAL          
SEQRES   3 B  273  LYS LYS ALA GLN GLN GLU ALA ALA ALA PHE LEU GLU GLY          
SEQRES   4 B  273  CYS LYS ALA HIS ILE SER VAL PRO VAL GLN GLU ILE SER          
SEQRES   5 B  273  PHE LEU GLU LEU GLN GLU PRO THR ILE GLU THR GLY PHE          
SEQRES   6 B  273  GLU ALA CYS VAL LYS GLN GLY ALA THR HIS ILE ALA VAL          
SEQRES   7 B  273  VAL PRO LEU LEU LEU LEU THR ALA ALA HIS ALA LYS HIS          
SEQRES   8 B  273  ASP ILE PRO GLU GLU ILE VAL ARG VAL ALA SER ARG TYR          
SEQRES   9 B  273  PRO SER VAL ARG ILE SER TYR GLY LYS PRO ILE GLY ILE          
SEQRES  10 B  273  ASP GLU GLU VAL VAL LYS ALA VAL TYR HIS ARG MET LYS          
SEQRES  11 B  273  ASP ILE GLY VAL PRO TYR GLU ASN ALA ARG VAL VAL LEU          
SEQRES  12 B  273  ILE GLY ARG GLY SER SER ASP PRO ASP VAL LYS ARG ASP          
SEQRES  13 B  273  VAL THR GLY ILE ALA ASN LEU LEU GLN GLU MET VAL PRO          
SEQRES  14 B  273  VAL LYS GLU VAL ILE PRO CYS PHE LEU THR ALA CYS GLY          
SEQRES  15 B  273  PRO ASN TYR LYS GLU VAL PHE SER GLU LEU GLU LYS ASP          
SEQRES  16 B  273  ASP GLY ILE THR THR PHE ILE VAL PRO TYR LEU LEU PHE          
SEQRES  17 B  273  THR GLY MET LEU MET ASN GLU ILE GLU ARG GLU VAL GLN          
SEQRES  18 B  273  LYS LEU LYS ALA HIS ASN PRO ASN VAL TYR LEU SER SER          
SEQRES  19 B  273  TYR ILE GLY PHE HIS PRO HIS VAL LYS ASN ALA PHE LEU          
SEQRES  20 B  273  ASN ARG VAL ARG GLU THR ALA ALA ASN SER GLU GLY GLN          
SEQRES  21 B  273  PHE ASP PHE ASP GLY GLY SER TYR ALA SER ALA ALA HIS          
HET     NI  A 301       1                                                       
HET     NI  A 302       1                                                       
HET     NI  B 301       1                                                       
HET     NI  B 302       1                                                       
HETNAM      NI NICKEL (II) ION                                                  
FORMUL   3   NI    4(NI 2+)                                                     
FORMUL   7  HOH   *62(H2 O)                                                     
HELIX    1 AA1 VAL A   14  LYS A   29  1                                  16    
HELIX    2 AA2 ALA A   30  ILE A   32  5                                   3    
HELIX    3 AA3 THR A   48  GLN A   59  1                                  12    
HELIX    4 AA4 ALA A   74  HIS A   79  1                                   6    
HELIX    5 AA5 HIS A   79  SER A   90  1                                  12    
HELIX    6 AA6 ASP A  106  ASP A  119  1                                  14    
HELIX    7 AA7 ASP A  138  VAL A  156  1                                  19    
HELIX    8 AA8 ASN A  172  LEU A  180  1                                   9    
HELIX    9 AA9 GLY A  198  ASN A  215  1                                  18    
HELIX   10 AB1 HIS A  227  ASN A  244  1                                  18    
HELIX   11 AB2 VAL B   14  LYS B   29  1                                  16    
HELIX   12 AB3 ALA B   30  ILE B   32  5                                   3    
HELIX   13 AB4 THR B   48  GLN B   59  1                                  12    
HELIX   14 AB5 ALA B   74  HIS B   79  1                                   6    
HELIX   15 AB6 HIS B   79  SER B   90  1                                  12    
HELIX   16 AB7 ASP B  106  ASP B  119  1                                  14    
HELIX   17 AB8 ASP B  138  VAL B  156  1                                  19    
HELIX   18 AB9 ASN B  172  LEU B  180  1                                   9    
HELIX   19 AC1 GLY B  198  ASN B  215  1                                  18    
HELIX   20 AC2 HIS B  227  ASN B  244  1                                  18    
SHEET    1 AA1 5 VAL A  36  PHE A  41  0                                        
SHEET    2 AA1 5 GLN A   3  GLY A   9  1  N  TYR A   7   O  GLU A  38           
SHEET    3 AA1 5 HIS A  63  PRO A  68  1  O  ALA A  65   N  ALA A   4           
SHEET    4 AA1 5 ARG A  96  TYR A  99  1  O  SER A  98   N  VAL A  66           
SHEET    5 AA1 5 ASP A 250  PHE A 251 -1  O  PHE A 251   N  ILE A  97           
SHEET    1 AA2 4 GLU A 160  PHE A 165  0                                        
SHEET    2 AA2 4 ARG A 128  GLY A 133  1  N  VAL A 129   O  ILE A 162           
SHEET    3 AA2 4 THR A 188  TYR A 193  1  O  TYR A 193   N  ILE A 132           
SHEET    4 AA2 4 VAL A 218  LEU A 220  1  O  TYR A 219   N  ILE A 190           
SHEET    1 AA3 5 VAL B  36  PHE B  41  0                                        
SHEET    2 AA3 5 GLN B   3  GLY B   9  1  N  TYR B   7   O  GLU B  38           
SHEET    3 AA3 5 HIS B  63  LEU B  69  1  O  ALA B  65   N  ALA B   4           
SHEET    4 AA3 5 ARG B  96  TYR B  99  1  O  SER B  98   N  VAL B  66           
SHEET    5 AA3 5 ASP B 250  PHE B 251 -1  O  PHE B 251   N  ILE B  97           
SHEET    1 AA4 4 GLU B 160  PHE B 165  0                                        
SHEET    2 AA4 4 ARG B 128  GLY B 133  1  N  VAL B 129   O  ILE B 162           
SHEET    3 AA4 4 THR B 188  PRO B 192  1  O  PHE B 189   N  VAL B 130           
SHEET    4 AA4 4 VAL B 218  LEU B 220  1  O  TYR B 219   N  ILE B 190           
LINK         NE2 HIS A  79                NI    NI A 301     1555   1555  2.78  
LINK         OE2 GLU A  83                NI    NI A 301     1555   1555  2.49  
LINK         NE2 HIS A 115                NI    NI A 302     1555   1555  2.13  
LINK         NE2 HIS A 229                NI    NI A 302     1555   1555  2.34  
LINK         NE2 HIS B  79                NI    NI B 301     1555   1555  2.45  
LINK         OE1 GLU B  83                NI    NI B 301     1555   1555  2.14  
LINK        NI    NI A 301                 O   HOH A 424     1555   1555  1.90  
LINK        NI    NI A 301                 O   HOH A 403     1555   1555  2.57  
LINK        NI    NI A 302                 O   HOH A 425     1555   1555  2.42  
LINK        NI    NI A 302                 O   HOH A 430     1555   1555  2.47  
LINK        NI    NI A 302                 O   HOH A 436     1555   1555  2.55  
LINK        NI    NI B 301                 O   HOH B 418     1555   1555  2.52  
LINK        NI    NI B 301                 O   HOH B 413     1555   1555  2.50  
CISPEP   1 GLU A   46    PRO A   47          0        11.59                     
CISPEP   2 GLY A  170    PRO A  171          0        -3.02                     
CISPEP   3 GLU B   46    PRO B   47          0        -4.02                     
CISPEP   4 GLY B  170    PRO B  171          0        -2.56                     
SITE     1 AC1  5 HIS A  79  GLU A  83  HOH A 403  HOH A 424                    
SITE     2 AC1  5 HOH A 428                                                     
SITE     1 AC2  5 HIS A 115  HIS A 229  HOH A 425  HOH A 430                    
SITE     2 AC2  5 HOH A 436                                                     
SITE     1 AC3  4 HIS B  79  GLU B  83  HOH B 413  HOH B 418                    
SITE     1 AC4  2 HIS B 115  HIS B 229                                          
CRYST1   69.730   53.700   78.020  90.00 107.66  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014341  0.000000  0.004566        0.00000                         
SCALE2      0.000000  0.018622  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013451        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system