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Database: PDB
Entry: 1ZCO
LinkDB: 1ZCO
Original site: 1ZCO 
HEADER    LYASE                                   12-APR-05   1ZCO              
TITLE     CRYSTAL STRUCTURE OF PYROCOCCUS FURIOSUS 3-DEOXY-D-ARABINO-           
TITLE    2 HEPTULOSONATE 7-PHOSPHATE SYNTHASE                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-DEHYDRO-3-DEOXYPHOSPHOHEPTONATE ALDOLASE;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DAH7PS, 3-DEOXY-D-ARABINO-HEPTULOSONATE 7-PHOSPHATE         
COMPND   5 SYNTHASE;                                                            
COMPND   6 EC: 4.1.2.15;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;                            
SOURCE   3 ORGANISM_TAXID: 2261;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;                   
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PT7-7                                     
KEYWDS    ARABINO-HEPTULOSONATE, SYNTHASE, SHIKIMATE, DAHP, DAH7P, DAHPS,       
KEYWDS   2 DAH7PS, LYASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.R.SCHOFIELD,B.F.ANDERSON,M.L.PATCHETT,G.E.NORRIS,G.B.JAMESON,       
AUTHOR   2 E.J.PARKER                                                           
REVDAT   3   13-JUL-11 1ZCO    1       VERSN                                    
REVDAT   2   24-FEB-09 1ZCO    1       VERSN                                    
REVDAT   1   18-OCT-05 1ZCO    0                                                
JRNL        AUTH   L.R.SCHOFIELD,B.F.ANDERSON,M.L.PATCHETT,G.E.NORRIS,          
JRNL        AUTH 2 G.B.JAMESON,E.J.PARKER                                       
JRNL        TITL   SUBSTRATE AMBIGUITY AND CRYSTAL STRUCTURE OF PYROCOCCUS      
JRNL        TITL 2 FURIOSUS 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-PHOSPHATE         
JRNL        TITL 3 SYNTHASE: AN ANCESTRAL 3-DEOXYALD-2-ULOSONATE-PHOSPHATE      
JRNL        TITL 4 SYNTHASE?(,)                                                 
JRNL        REF    BIOCHEMISTRY                  V.  44 11950 2005              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   16142893                                                     
JRNL        DOI    10.1021/BI050577Z                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.R.SCHOFIELD,M.L.PATCHETT,E.J.PARKER                        
REMARK   1  TITL   EXPRESSION, PURIFICATION, AND CHARACTERISEATION OF           
REMARK   1  TITL 2 3-DEOXY_D_ARABINO_HEPTULOSONATE 7-PHOSPHATE SYNTHASE FROM    
REMARK   1  TITL 3 PYROCOCCUS FURIOSUS                                          
REMARK   1  REF    PROTEIN EXPR.PURIF.           V.  34    17 2004              
REMARK   1  REFN                   ISSN 1046-5928                               
REMARK   1  PMID   14766297                                                     
REMARK   1  DOI    10.1016/J.PEP.2003.11.008                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : SUPPLIED BY CCP4                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 30722                          
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) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2519                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2232                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2760                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 162                          
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4112                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 262                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.45000                                              
REMARK   3    B22 (A**2) : 1.72000                                              
REMARK   3    B33 (A**2) : -2.17000                                             
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): 0.245         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.203         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.163         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.098         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4221 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3934 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5701 ; 1.563 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9171 ; 1.562 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   524 ; 8.654 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   642 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4641 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   813 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   864 ; 0.242 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4666 ; 0.257 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2515 ; 0.085 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   222 ; 0.213 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    21 ; 0.237 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    96 ; 0.253 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.264 ; 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):  2611 ; 1.613 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4213 ; 2.693 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1610 ; 3.680 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1488 ; 5.405 ; 8.000       
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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1ZCO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-APR-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB032573.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAY-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 110.0                              
REMARK 200  PH                             : 7.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC BLUE MIRRORS                 
REMARK 200  OPTICS                         : OSMIC BLUE MIRRORS                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR                       
REMARK 200  DATA SCALING SOFTWARE          : CRYSTALCLEAR                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33241                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.970                              
REMARK 200  R MERGE                    (I) : 0.12600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.97                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
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: CHIMERIC MODEL FROM 1QR7 AND 1FWT                    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 8000, 0.2M AMMONIUM ACETATE,      
REMARK 280  0.1M TRIS-HCL, PH 7.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE   
REMARK 280  295K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       43.61550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.01200            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       72.17500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.61550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.01200            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.17500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.61550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       55.01200            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.17500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.61550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       55.01200            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       72.17500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL TETRAMER CAN BE GENERATED BY THE OPERATION    
REMARK 300 OF THE CRYSTALLOGRAPHIC TWOFOLD AXIS 1-X,Y,-Z ON THE ASYMMETRIC UNIT 
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 13610 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -135.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350   BIOMT1   2 -1.000000  0.000000  0.000000       87.23100            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   903     O    HOH B  1951              1.80            
REMARK 500   O    HOH A   951     O    HOH B  1903              1.80            
REMARK 500   O    HOH B  1933     O    HOH B  1936              2.10            
REMARK 500   NZ   LYS B     2     O    HOH B  1934              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   975     O    HOH B  1978     3655     2.13            
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    ASP A   8      128.41    178.65                                   
REMARK 500    ASN A  16     -125.47     53.99                                   
REMARK 500    ASN A 160       72.96   -102.40                                   
REMARK 500    ARG A 205      120.33    179.22                                   
REMARK 500    ASP B   8      129.72    178.70                                   
REMARK 500    ASN B  16     -119.71     45.88                                   
REMARK 500    PRO B  61      -91.30    -54.14                                   
REMARK 500    ARG B  62      117.71     88.87                                   
REMARK 500    ARG B 205      124.32   -170.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TYR A    7     ASP A    8                 -146.05                    
REMARK 500 GLY B  204     ARG B  205                 -140.12                    
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                              MN B 900  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  31   SG                                                     
REMARK 620 2 GLU B 227   OE2 102.7                                              
REMARK 620 3 ASP B 238   OD2 100.5  77.8                                        
REMARK 620 4 HIS B 201   NE2 158.0  99.2  83.0                                  
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 CL A 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 900                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEP A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEP B 1901                
DBREF  1ZCO A    1   262  UNP    Q8U0A9   Q8U0A9_PYRFU     1    262             
DBREF  1ZCO B    1   262  UNP    Q8U0A9   Q8U0A9_PYRFU     1    262             
SEQADV 1ZCO ASP A    8  UNP  Q8U0A9    LYS     8 CONFLICT                       
SEQADV 1ZCO GLU A   37  UNP  Q8U0A9    ASP    37 CONFLICT                       
SEQADV 1ZCO ASP B    8  UNP  Q8U0A9    LYS     8 CONFLICT                       
SEQADV 1ZCO GLU B   37  UNP  Q8U0A9    ASP    37 CONFLICT                       
SEQRES   1 A  262  MET LYS TYR SER LYS GLU TYR ASP GLU LYS THR VAL VAL          
SEQRES   2 A  262  LYS ILE ASN ASP VAL LYS PHE GLY GLU GLY PHE THR ILE          
SEQRES   3 A  262  ILE ALA GLY PRO CYS SER ILE GLU SER ARG GLU GLN ILE          
SEQRES   4 A  262  MET LYS VAL ALA GLU PHE LEU ALA GLU VAL GLY ILE LYS          
SEQRES   5 A  262  VAL LEU ARG GLY GLY ALA PHE LYS PRO ARG THR SER PRO          
SEQRES   6 A  262  TYR SER PHE GLN GLY TYR GLY GLU LYS ALA LEU ARG TRP          
SEQRES   7 A  262  MET ARG GLU ALA ALA ASP GLU TYR GLY LEU VAL THR VAL          
SEQRES   8 A  262  THR GLU VAL MET ASP THR ARG HIS VAL GLU LEU VAL ALA          
SEQRES   9 A  262  LYS TYR SER ASP ILE LEU GLN ILE GLY ALA ARG ASN SER          
SEQRES  10 A  262  GLN ASN PHE GLU LEU LEU LYS GLU VAL GLY LYS VAL GLU          
SEQRES  11 A  262  ASN PRO VAL LEU LEU LYS ARG GLY MET GLY ASN THR ILE          
SEQRES  12 A  262  GLN GLU LEU LEU TYR SER ALA GLU TYR ILE MET ALA GLN          
SEQRES  13 A  262  GLY ASN GLU ASN VAL ILE LEU CYS GLU ARG GLY ILE ARG          
SEQRES  14 A  262  THR PHE GLU THR ALA THR ARG PHE THR LEU ASP ILE SER          
SEQRES  15 A  262  ALA VAL PRO VAL VAL LYS GLU LEU SER HIS LEU PRO ILE          
SEQRES  16 A  262  ILE VAL ASP PRO SER HIS PRO ALA GLY ARG ARG SER LEU          
SEQRES  17 A  262  VAL ILE PRO LEU ALA LYS ALA ALA TYR ALA ILE GLY ALA          
SEQRES  18 A  262  ASP GLY ILE MET VAL GLU VAL HIS PRO GLU PRO GLU LYS          
SEQRES  19 A  262  ALA LEU SER ASP SER GLN GLN GLN LEU THR PHE ASP ASP          
SEQRES  20 A  262  PHE LEU GLN LEU LEU LYS GLU LEU GLU ALA LEU GLY TRP          
SEQRES  21 A  262  LYS GLY                                                      
SEQRES   1 B  262  MET LYS TYR SER LYS GLU TYR ASP GLU LYS THR VAL VAL          
SEQRES   2 B  262  LYS ILE ASN ASP VAL LYS PHE GLY GLU GLY PHE THR ILE          
SEQRES   3 B  262  ILE ALA GLY PRO CYS SER ILE GLU SER ARG GLU GLN ILE          
SEQRES   4 B  262  MET LYS VAL ALA GLU PHE LEU ALA GLU VAL GLY ILE LYS          
SEQRES   5 B  262  VAL LEU ARG GLY GLY ALA PHE LYS PRO ARG THR SER PRO          
SEQRES   6 B  262  TYR SER PHE GLN GLY TYR GLY GLU LYS ALA LEU ARG TRP          
SEQRES   7 B  262  MET ARG GLU ALA ALA ASP GLU TYR GLY LEU VAL THR VAL          
SEQRES   8 B  262  THR GLU VAL MET ASP THR ARG HIS VAL GLU LEU VAL ALA          
SEQRES   9 B  262  LYS TYR SER ASP ILE LEU GLN ILE GLY ALA ARG ASN SER          
SEQRES  10 B  262  GLN ASN PHE GLU LEU LEU LYS GLU VAL GLY LYS VAL GLU          
SEQRES  11 B  262  ASN PRO VAL LEU LEU LYS ARG GLY MET GLY ASN THR ILE          
SEQRES  12 B  262  GLN GLU LEU LEU TYR SER ALA GLU TYR ILE MET ALA GLN          
SEQRES  13 B  262  GLY ASN GLU ASN VAL ILE LEU CYS GLU ARG GLY ILE ARG          
SEQRES  14 B  262  THR PHE GLU THR ALA THR ARG PHE THR LEU ASP ILE SER          
SEQRES  15 B  262  ALA VAL PRO VAL VAL LYS GLU LEU SER HIS LEU PRO ILE          
SEQRES  16 B  262  ILE VAL ASP PRO SER HIS PRO ALA GLY ARG ARG SER LEU          
SEQRES  17 B  262  VAL ILE PRO LEU ALA LYS ALA ALA TYR ALA ILE GLY ALA          
SEQRES  18 B  262  ASP GLY ILE MET VAL GLU VAL HIS PRO GLU PRO GLU LYS          
SEQRES  19 B  262  ALA LEU SER ASP SER GLN GLN GLN LEU THR PHE ASP ASP          
SEQRES  20 B  262  PHE LEU GLN LEU LEU LYS GLU LEU GLU ALA LEU GLY TRP          
SEQRES  21 B  262  LYS GLY                                                      
HET     CL  A 902       1                                                       
HET     MN  B 900       1                                                       
HET     CL  B1902       1                                                       
HET    PEP  A 901      10                                                       
HET    PEP  B1901      10                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     PEP PHOSPHOENOLPYRUVATE                                              
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   4   MN    MN 2+                                                        
FORMUL   6  PEP    2(C3 H5 O6 P)                                                
FORMUL   8  HOH   *262(H2 O)                                                    
HELIX    1   1 SER A   35  VAL A   49  1                                  15    
HELIX    2   2 GLY A   72  GLY A   87  1                                  16    
HELIX    3   3 ASP A   96  ARG A   98  5                                   3    
HELIX    4   4 HIS A   99  SER A  107  1                                   9    
HELIX    5   5 GLY A  113  SER A  117  5                                   5    
HELIX    6   6 ASN A  119  GLY A  127  1                                   9    
HELIX    7   7 THR A  142  ALA A  155  1                                  14    
HELIX    8   8 SER A  182  SER A  191  1                                  10    
HELIX    9   9 ARG A  205  SER A  207  5                                   3    
HELIX   10  10 LEU A  208  ILE A  219  1                                  12    
HELIX   11  11 GLU A  231  ALA A  235  5                                   5    
HELIX   12  12 THR A  244  LEU A  258  1                                  15    
HELIX   13  13 SER B   35  GLY B   50  1                                  16    
HELIX   14  14 GLY B   72  GLY B   87  1                                  16    
HELIX   15  15 ASP B   96  ARG B   98  5                                   3    
HELIX   16  16 HIS B   99  SER B  107  1                                   9    
HELIX   17  17 GLY B  113  SER B  117  5                                   5    
HELIX   18  18 ASN B  119  GLY B  127  1                                   9    
HELIX   19  19 THR B  142  GLN B  156  1                                  15    
HELIX   20  20 SER B  182  SER B  191  1                                  10    
HELIX   21  21 PRO B  199  GLY B  204  1                                   6    
HELIX   22  22 ARG B  205  SER B  207  5                                   3    
HELIX   23  23 LEU B  208  GLY B  220  1                                  13    
HELIX   24  24 GLU B  231  ALA B  235  5                                   5    
HELIX   25  25 THR B  244  ALA B  257  1                                  14    
SHEET    1   A 2 VAL A  13  ILE A  15  0                                        
SHEET    2   A 2 VAL A  18  PHE A  20 -1  O  PHE A  20   N  VAL A  13           
SHEET    1   B 9 THR A  25  GLY A  29  0                                        
SHEET    2   B 9 VAL A  53  ARG A  55  1  O  ARG A  55   N  ALA A  28           
SHEET    3   B 9 VAL A  89  GLU A  93  1  O  VAL A  89   N  LEU A  54           
SHEET    4   B 9 ILE A 109  ILE A 112  1  O  ILE A 109   N  THR A  90           
SHEET    5   B 9 VAL A 133  LYS A 136  1  O  LEU A 134   N  LEU A 110           
SHEET    6   B 9 VAL A 161  GLU A 165  1  O  ILE A 162   N  LEU A 135           
SHEET    7   B 9 ILE A 195  VAL A 197  1  O  ILE A 196   N  LEU A 163           
SHEET    8   B 9 GLY A 223  GLU A 227  1  O  MET A 225   N  VAL A 197           
SHEET    9   B 9 THR A  25  GLY A  29  1  N  ILE A  27   O  ILE A 224           
SHEET    1   C 2 VAL B  13  ILE B  15  0                                        
SHEET    2   C 2 VAL B  18  PHE B  20 -1  O  VAL B  18   N  ILE B  15           
SHEET    1   D 9 THR B  25  GLY B  29  0                                        
SHEET    2   D 9 VAL B  53  ARG B  55  1  O  VAL B  53   N  ALA B  28           
SHEET    3   D 9 VAL B  89  GLU B  93  1  O  VAL B  89   N  LEU B  54           
SHEET    4   D 9 ILE B 109  ILE B 112  1  O  ILE B 109   N  THR B  90           
SHEET    5   D 9 VAL B 133  LYS B 136  1  O  LEU B 134   N  ILE B 112           
SHEET    6   D 9 VAL B 161  GLU B 165  1  O  ILE B 162   N  VAL B 133           
SHEET    7   D 9 ILE B 195  VAL B 197  1  O  ILE B 196   N  LEU B 163           
SHEET    8   D 9 GLY B 223  GLU B 227  1  O  MET B 225   N  VAL B 197           
SHEET    9   D 9 THR B  25  GLY B  29  1  N  ILE B  27   O  ILE B 224           
LINK        MN    MN B 900                 SG  CYS B  31     1555   1555  2.12  
LINK        MN    MN B 900                 OE2 GLU B 227     1555   1555  2.03  
LINK        MN    MN B 900                 OD2 ASP B 238     1555   1555  2.69  
LINK        MN    MN B 900                 NE2 HIS B 201     1555   1555  2.66  
SITE     1 AC1  3 ALA A 114  ARG A 115  PEP A 901                               
SITE     1 AC2  4 CYS B  31  HIS B 201  GLU B 227  ASP B 238                    
SITE     1 AC3  4 GLY B 113  ALA B 114  ARG B 115  PEP B1901                    
SITE     1 AC4 11 ARG A  55  GLN A 111  GLY A 113  ALA A 114                    
SITE     2 AC4 11 ARG A 115  LYS A 136  ARG A 166  ASP A 198                    
SITE     3 AC4 11 HIS A 201   CL A 902  HOH A 904                               
SITE     1 AC5 10 ARG B  55  LYS B  60  GLN B 111  ALA B 114                    
SITE     2 AC5 10 ARG B 115  LYS B 136  ARG B 166  HIS B 201                    
SITE     3 AC5 10  CL B1902  HOH B1904                                          
CRYST1   87.231  110.024  144.350  90.00  90.00  90.00 I 2 2 2      16          
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      0.011464  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009089  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006928        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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