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Database: PDB
Entry: 2C14
LinkDB: 2C14
Original site: 2C14 
HEADER    LYASE                                   11-SEP-05   2C14              
TITLE     5-(4-CARBOXY-2-OXO-BUTYLAMINO)-4-OXO-PENTANOIC ACID ACID BOUND TO     
TITLE    2 PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DELTA-AMINOLEVULINIC ACID DEHYDRATASE;                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PORPHOBILINOGEN SYNTHASE, ALAD, ALADH;                      
COMPND   5 EC: 4.2.1.24;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: PET3A                                      
KEYWDS    ENZYME MECHANISM, METALLOENZYME, PORPHOBILINOGEN SYNTHASE,            
KEYWDS   2 COCRYSTALLIZATION, LYASE, PORPHYRIN BIOSYNTHESIS                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.FRERE,M.NENTWICH,S.GACOND,D.W.HEINZ,R.NEIER,N.FRANKENBERG-DINKEL    
REVDAT   5   13-DEC-23 2C14    1       LINK                                     
REVDAT   4   08-MAY-19 2C14    1       REMARK LINK                              
REVDAT   3   24-FEB-09 2C14    1       VERSN                                    
REVDAT   2   12-JUL-06 2C14    1       JRNL                                     
REVDAT   1   20-JUN-06 2C14    0                                                
JRNL        AUTH   F.FRERE,M.NENTWICH,S.GACOND,D.W.HEINZ,R.NEIER,               
JRNL        AUTH 2 N.FRANKENBERG-DINKEL                                         
JRNL        TITL   PROBING THE ACTIVE SITE OF PSEUDOMONAS AERUGINOSA            
JRNL        TITL 2 PORPHOBILINOGEN SYNTHASE USING NEWLY DEVELOPED INHIBITORS.   
JRNL        REF    BIOCHEMISTRY                  V.  45  8243 2006              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   16819823                                                     
JRNL        DOI    10.1021/BI052611F                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 89.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 52367                          
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) : 0.160                           
REMARK   3   R VALUE            (WORKING SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.201                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2802                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3664                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2420                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 200                          
REMARK   3   BIN FREE R VALUE                    : 0.3090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5149                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 723                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.46000                                              
REMARK   3    B22 (A**2) : 0.46000                                              
REMARK   3    B33 (A**2) : -0.91000                                             
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): 0.148         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.136         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.089         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.982         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5770 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7893 ; 1.525 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   757 ; 5.917 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   284 ;35.899 ;23.239       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   951 ;14.812 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    64 ;18.464 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   858 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4624 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2915 ; 0.231 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4036 ; 0.295 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   575 ; 0.143 ; 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):   136 ; 0.203 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    65 ; 0.162 ; 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):  3737 ; 0.788 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5855 ; 1.207 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2299 ; 2.115 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2038 ; 3.128 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. 5-(4-CARBOXY-2-OXO-BUTYLAMINO)-4-OXO- PENTANOIC ACID     
REMARK   3  WAS INITIALLY BOUND TO K 205 AND K260 VIA SCHIFF BASES. A ALDOLE    
REMARK   3  ADDITION RESULTED IN THE MODIFIED RESIDUE IN POSITION 205 THAT      
REMARK   3  IS ADDITIONALLY BOUND TO THE AMINO MOIETY OF K260 VIA A SINGLE      
REMARK   3  BOND.                                                               
REMARK   4                                                                      
REMARK   4 2C14 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-SEP-05.                  
REMARK 100 THE DEPOSITION ID IS D_1290025607.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-FEB-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98010                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55853                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.130                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 7.800                              
REMARK 200  R MERGE                    (I) : 0.16000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.94                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1B4K                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP IN 24-WELL LIMBRO PLATES.   
REMARK 280  DROPS MADE OF 5 MICROL PROTEIN SOLUTION (10 MG/ML PROTEIN, 50 MM    
REMARK 280  TRIS-HCL, PH 7.5, 5 MM MGCL2, 1MM NACL, 1 MM 5-(4-CARBOXY-2-OXO-    
REMARK 280  BUTYLAMINO)-4-OXO-PENTANOIC ACID MONOSODIUM SALT)) PLUS 5 MICROL    
REMARK 280  RESERVOIR SOLUTION (18.0 % (W/V) PEG-3350, 200 MM LINO3), PH        
REMARK 280  7.50, VAPOR DIFFUSION, HANGING DROP                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 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   -Y+1/2,X+1/2,Z                                          
REMARK 290       4555   Y+1/2,-X+1/2,Z                                          
REMARK 290       5555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       6555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       63.43850            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       63.43850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       63.43850            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       63.43850            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       63.43850            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       63.43850            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       63.43850            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       63.43850            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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  0.000000 -1.000000  0.000000      190.31550            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000      -63.43850            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000       63.43850            
REMARK 350   BIOMT2   3 -1.000000  0.000000  0.000000      190.31550            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000      253.75400            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      126.87700            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2010  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A2015  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B2014  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B2016  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ILE 199 TO VAL                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ILE 199 TO VAL                        
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     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ARG A   337                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B   222                                                      
REMARK 465     ASN B   223                                                      
REMARK 465     LEU B   224                                                      
REMARK 465     GLY B   225                                                      
REMARK 465     LYS B   226                                                      
REMARK 465     GLY B   227                                                      
REMARK 465     ARG B   337                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLY A 336    CA   C    O                                         
REMARK 470     GLY B 336    CA   C    O                                         
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   NH1  ARG A    26     O    HOH A  2062              1.48            
REMARK 500   C8   CYJ B   205     NZ   LYS B   260              1.89            
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   OE1  GLU A   275     OG1  THR B     4     3645     2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A  25   N     ARG A  25   CA      0.229                       
REMARK 500    ALA A 204   C     CYJ A 205   N       0.191                       
REMARK 500    ALA B 204   C     CYJ B 205   N       0.216                       
REMARK 500    CYJ B 205   C     TYR B 206   N       0.196                       
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    ALA A 129      144.09    179.89                                   
REMARK 500    ALA A 204       76.12   -118.92                                   
REMARK 500    TYR A 232      -47.50   -138.77                                   
REMARK 500    PRO A 261     -169.95    -63.29                                   
REMARK 500    ALA B 129      142.39   -175.86                                   
REMARK 500    TYR B 232      -39.63   -142.26                                   
REMARK 500    PRO B 261     -164.49    -65.82                                   
REMARK 500    ARG B 335       69.27   -172.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ALA A 204         11.60                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2041        DISTANCE =  7.14 ANGSTROMS                       
REMARK 525    HOH A2046        DISTANCE =  6.84 ANGSTROMS                       
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                              MG A1336  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 245   OE1                                                    
REMARK 620 2 HOH A2245   O   178.2                                              
REMARK 620 3 HOH A2246   O    80.5 100.9                                        
REMARK 620 4 HOH A2303   O    90.3  88.6  91.7                                  
REMARK 620 5 HOH A2304   O    97.7  83.4  88.6 172.0                            
REMARK 620 6 HOH A2306   O    82.9  95.9 161.3  97.0  85.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1336  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 245   OE1                                                    
REMARK 620 2 HOH B2258   O   175.7                                              
REMARK 620 3 HOH B2260   O    81.5 100.4                                        
REMARK 620 4 HOH B2308   O    98.2  85.7  86.7                                  
REMARK 620 5 HOH B2310   O    90.4  85.7  94.5 171.4                            
REMARK 620 6 HOH B2311   O    80.5  98.1 160.0  87.3  94.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN 11-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN 11-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1336                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1336                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1B4K   RELATED DB: PDB                                   
REMARK 900 HIGH RESOLUTION CRYSTAL STRUCTURE OF A MG2- DEPENDENT 5-             
REMARK 900 AMINOLEVULINIC ACID DEHYDRATASE                                      
REMARK 900 RELATED ID: 1GZG   RELATED DB: PDB                                   
REMARK 900 COMPLEX OF A MG2-DEPENDENT PORPHOBILINOGEN SYNTHASE (MUTANT D139N)   
REMARK 900 WITH 5-FLUOROLEVULINIC ACID                                          
REMARK 900 RELATED ID: 1W56   RELATED DB: PDB                                   
REMARK 900 STEPWISE INTRODUCTION OF ZINC BINDING SITE INTO PORPHOBILINOGEN      
REMARK 900 SYNTHASE OF PSEUDOMONAS AERUGINOSA (MUTANTIONS A129C AND D131C)      
REMARK 900 RELATED ID: 1W5M   RELATED DB: PDB                                   
REMARK 900 STEPWISE INTRODUCTION OF ZINC BINDING SITE INTO PORPHOBILINOGEN      
REMARK 900 SYNTHASE OF PSEUDOMONAS AERUGINOSA (MUTANTIONS A129C AND D139C)      
REMARK 900 RELATED ID: 1W5N   RELATED DB: PDB                                   
REMARK 900 STEPWISE INTRODUCTION OF ZINC BINDING SITE INTO PORPHOBILINOGEN      
REMARK 900 SYNTHASE OF PSEUDOMONAS AERUGINOSA (MUTANTIONS D131C AND D139C)      
REMARK 900 RELATED ID: 1W5O   RELATED DB: PDB                                   
REMARK 900 STEPWISE INTRODUCTION OF ZINC BINDING SITE INTO PORPHOBILINOGEN      
REMARK 900 SYNTHASE OF PSEUDOMONAS AERUGINOSA (MUTANTIONS A129C, D131C AND      
REMARK 900 D139C )                                                              
REMARK 900 RELATED ID: 1W5P   RELATED DB: PDB                                   
REMARK 900 STEPWISE INTRODUCTION OF ZINC BINDING SITE INTO PORPHOBILINOGEN      
REMARK 900 SYNTHASE OF PSEUDOMONAS AERUGINOSA (MUTANTIONS A129C, D131C, D139C,  
REMARK 900 P132E)                                                               
REMARK 900 RELATED ID: 1W5Q   RELATED DB: PDB                                   
REMARK 900 STEPWISE INTRODUCTION OF ZINC BINDING SITE INTO PORPHOBILINOGEN      
REMARK 900 SYNTHASE OF PSEUDOMONAS AERUGINOSA (MUTANTIONS A129C, D131C, D139C,  
REMARK 900 P132E, K229R)                                                        
REMARK 900 RELATED ID: 1W54   RELATED DB: PDB                                   
REMARK 900 STEPWISE INTRODUCTION OF A ZINC BINDING SITE INTO PORPHOBILINOGEN    
REMARK 900 SYNTHASE FROM PSEUDOMONAS AERUGINOSA (MUTATION D139C)                
REMARK 900 RELATED ID: 2C13   RELATED DB: PDB                                   
REMARK 900 5-HYDROXY-LEVULINIC ACID BOUND TO PORPHOBILINOGEN SYNTHASE FROM      
REMARK 900 PSEUDOMONAS AERUGINOSA                                               
REMARK 900 RELATED ID: 2C15   RELATED DB: PDB                                   
REMARK 900 5-(4-CARBOXY-2-OXO-BUTOXY)-4-OXO- PENTANOIC ACID ACID BOUND TO       
REMARK 900 PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA                 
REMARK 900 RELATED ID: 2C16   RELATED DB: PDB                                   
REMARK 900 5-(4-CARBOXY-2-OXO-BUTANE-1-SULFINYL)-4 -OXO-PENTANOIC ACID ACID     
REMARK 900 BOUND TO PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA        
REMARK 900 RELATED ID: 2C18   RELATED DB: PDB                                   
REMARK 900 5-(4-CARBOXY-2-OXO-BUTANE-1-SULFONYL)-4 -OXO-PENTANOIC ACID BOUND    
REMARK 900 TO PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA              
REMARK 900 RELATED ID: 2C19   RELATED DB: PDB                                   
REMARK 900 5-(4-CARBOXY-2-OXO-BUTYLSULFANYL)-4-OXO- PENTANOIC ACID ACID BOUND   
REMARK 900 TO PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 I199V EXCHANGE AS CLONING ARTEFACT                                   
DBREF  2C14 A    1   337  UNP    Q59643   HEM2_PSEAE       1    337             
DBREF  2C14 B    1   337  UNP    Q59643   HEM2_PSEAE       1    337             
SEQADV 2C14 VAL A  199  UNP  Q59643    ILE   199 ENGINEERED MUTATION            
SEQADV 2C14 VAL B  199  UNP  Q59643    ILE   199 ENGINEERED MUTATION            
SEQRES   1 A  337  MET SER PHE THR PRO ALA ASN ARG ALA TYR PRO TYR THR          
SEQRES   2 A  337  ARG LEU ARG ARG ASN ARG ARG ASP ASP PHE SER ARG ARG          
SEQRES   3 A  337  LEU VAL ARG GLU ASN VAL LEU THR VAL ASP ASP LEU ILE          
SEQRES   4 A  337  LEU PRO VAL PHE VAL LEU ASP GLY VAL ASN GLN ARG GLU          
SEQRES   5 A  337  SER ILE PRO SER MET PRO GLY VAL GLU ARG LEU SER ILE          
SEQRES   6 A  337  ASP GLN LEU LEU ILE GLU ALA GLU GLU TRP VAL ALA LEU          
SEQRES   7 A  337  GLY ILE PRO ALA LEU ALA LEU PHE PRO VAL THR PRO VAL          
SEQRES   8 A  337  GLU LYS LYS SER LEU ASP ALA ALA GLU ALA TYR ASN PRO          
SEQRES   9 A  337  GLU GLY ILE ALA GLN ARG ALA THR ARG ALA LEU ARG GLU          
SEQRES  10 A  337  ARG PHE PRO GLU LEU GLY ILE ILE THR ASP VAL ALA LEU          
SEQRES  11 A  337  ASP PRO PHE THR THR HIS GLY GLN ASP GLY ILE LEU ASP          
SEQRES  12 A  337  ASP ASP GLY TYR VAL LEU ASN ASP VAL SER ILE ASP VAL          
SEQRES  13 A  337  LEU VAL ARG GLN ALA LEU SER HIS ALA GLU ALA GLY ALA          
SEQRES  14 A  337  GLN VAL VAL ALA PRO SER ASP MET MET ASP GLY ARG ILE          
SEQRES  15 A  337  GLY ALA ILE ARG GLU ALA LEU GLU SER ALA GLY HIS THR          
SEQRES  16 A  337  ASN VAL ARG VAL MET ALA TYR SER ALA CYJ TYR ALA SER          
SEQRES  17 A  337  ALA TYR TYR GLY PRO PHE ARG ASP ALA VAL GLY SER ALA          
SEQRES  18 A  337  SER ASN LEU GLY LYS GLY ASN LYS ALA THR TYR GLN MET          
SEQRES  19 A  337  ASP PRO ALA ASN SER ASP GLU ALA LEU HIS GLU VAL ALA          
SEQRES  20 A  337  ALA ASP LEU ALA GLU GLY ALA ASP MET VAL MET VAL LYS          
SEQRES  21 A  337  PRO GLY MET PRO TYR LEU ASP ILE VAL ARG ARG VAL LYS          
SEQRES  22 A  337  ASP GLU PHE ARG ALA PRO THR PHE VAL TYR GLN VAL SER          
SEQRES  23 A  337  GLY GLU TYR ALA MET HIS MET GLY ALA ILE GLN ASN GLY          
SEQRES  24 A  337  TRP LEU ALA GLU SER VAL ILE LEU GLU SER LEU THR ALA          
SEQRES  25 A  337  PHE LYS ARG ALA GLY ALA ASP GLY ILE LEU THR TYR PHE          
SEQRES  26 A  337  ALA LYS GLN ALA ALA GLU GLN LEU ARG ARG GLY ARG              
SEQRES   1 B  337  MET SER PHE THR PRO ALA ASN ARG ALA TYR PRO TYR THR          
SEQRES   2 B  337  ARG LEU ARG ARG ASN ARG ARG ASP ASP PHE SER ARG ARG          
SEQRES   3 B  337  LEU VAL ARG GLU ASN VAL LEU THR VAL ASP ASP LEU ILE          
SEQRES   4 B  337  LEU PRO VAL PHE VAL LEU ASP GLY VAL ASN GLN ARG GLU          
SEQRES   5 B  337  SER ILE PRO SER MET PRO GLY VAL GLU ARG LEU SER ILE          
SEQRES   6 B  337  ASP GLN LEU LEU ILE GLU ALA GLU GLU TRP VAL ALA LEU          
SEQRES   7 B  337  GLY ILE PRO ALA LEU ALA LEU PHE PRO VAL THR PRO VAL          
SEQRES   8 B  337  GLU LYS LYS SER LEU ASP ALA ALA GLU ALA TYR ASN PRO          
SEQRES   9 B  337  GLU GLY ILE ALA GLN ARG ALA THR ARG ALA LEU ARG GLU          
SEQRES  10 B  337  ARG PHE PRO GLU LEU GLY ILE ILE THR ASP VAL ALA LEU          
SEQRES  11 B  337  ASP PRO PHE THR THR HIS GLY GLN ASP GLY ILE LEU ASP          
SEQRES  12 B  337  ASP ASP GLY TYR VAL LEU ASN ASP VAL SER ILE ASP VAL          
SEQRES  13 B  337  LEU VAL ARG GLN ALA LEU SER HIS ALA GLU ALA GLY ALA          
SEQRES  14 B  337  GLN VAL VAL ALA PRO SER ASP MET MET ASP GLY ARG ILE          
SEQRES  15 B  337  GLY ALA ILE ARG GLU ALA LEU GLU SER ALA GLY HIS THR          
SEQRES  16 B  337  ASN VAL ARG VAL MET ALA TYR SER ALA CYJ TYR ALA SER          
SEQRES  17 B  337  ALA TYR TYR GLY PRO PHE ARG ASP ALA VAL GLY SER ALA          
SEQRES  18 B  337  SER ASN LEU GLY LYS GLY ASN LYS ALA THR TYR GLN MET          
SEQRES  19 B  337  ASP PRO ALA ASN SER ASP GLU ALA LEU HIS GLU VAL ALA          
SEQRES  20 B  337  ALA ASP LEU ALA GLU GLY ALA ASP MET VAL MET VAL LYS          
SEQRES  21 B  337  PRO GLY MET PRO TYR LEU ASP ILE VAL ARG ARG VAL LYS          
SEQRES  22 B  337  ASP GLU PHE ARG ALA PRO THR PHE VAL TYR GLN VAL SER          
SEQRES  23 B  337  GLY GLU TYR ALA MET HIS MET GLY ALA ILE GLN ASN GLY          
SEQRES  24 B  337  TRP LEU ALA GLU SER VAL ILE LEU GLU SER LEU THR ALA          
SEQRES  25 B  337  PHE LYS ARG ALA GLY ALA ASP GLY ILE LEU THR TYR PHE          
SEQRES  26 B  337  ALA LYS GLN ALA ALA GLU GLN LEU ARG ARG GLY ARG              
MODRES 2C14 CYJ A  205  LYS                                                     
MODRES 2C14 CYJ B  205  LYS                                                     
HET    CYJ  A 205      24                                                       
HET    CYJ  B 205      24                                                       
HET     MG  A1336       1                                                       
HET     MG  B1336       1                                                       
HETNAM     CYJ (Z)-N~6~-[(4R,5S)-5-(2-CARBOXYETHYL)-4-(CARBOXYMETHYL)           
HETNAM   2 CYJ  PIPERIDIN-3-YLIDENE]-L-LYSINE                                   
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     CYJ 2-AMINO-6-(3-CARBOXY-1-[(4-CARBOXY-2-OXO-BUTYLAMINO)-            
HETSYN   2 CYJ  METHYL]-PROPYLIDENEAMINO)-HEXANOIC ACID                         
FORMUL   1  CYJ    2(C16 H27 N3 O6)                                             
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  HOH   *723(H2 O)                                                    
HELIX    1   1 ASP A   21  ARG A   29  1                                   9    
HELIX    2   2 THR A   34  ASP A   36  5                                   3    
HELIX    3   3 ILE A   65  LEU A   78  1                                  14    
HELIX    4   4 PRO A   90  LYS A   94  5                                   5    
HELIX    5   5 ALA A   98  ASN A  103  5                                   6    
HELIX    6   6 GLY A  106  PHE A  119  1                                  14    
HELIX    7   7 LEU A  149  GLY A  168  1                                  20    
HELIX    8   8 GLY A  180  ALA A  192  1                                  13    
HELIX    9   9 TYR A  211  VAL A  218  1                                   8    
HELIX   10  10 SER A  220  GLY A  225  1                                   6    
HELIX   11  11 SER A  239  GLU A  252  1                                  14    
HELIX   12  12 GLY A  262  PRO A  264  5                                   3    
HELIX   13  13 TYR A  265  ARG A  277  1                                  13    
HELIX   14  14 VAL A  285  ASN A  298  1                                  14    
HELIX   15  15 SER A  304  GLY A  317  1                                  14    
HELIX   16  16 PHE A  325  ARG A  335  1                                  11    
HELIX   17  17 ASP B   21  ARG B   29  1                                   9    
HELIX   18  18 THR B   34  ASP B   36  5                                   3    
HELIX   19  19 ILE B   65  GLY B   79  1                                  15    
HELIX   20  20 PRO B   90  LYS B   94  5                                   5    
HELIX   21  21 ALA B   98  ASN B  103  5                                   6    
HELIX   22  22 GLY B  106  PHE B  119  1                                  14    
HELIX   23  23 LEU B  149  GLY B  168  1                                  20    
HELIX   24  24 GLY B  180  ALA B  192  1                                  13    
HELIX   25  25 SER B  208  TYR B  210  5                                   3    
HELIX   26  26 TYR B  211  VAL B  218  1                                   8    
HELIX   27  27 ASN B  228  TYR B  232  5                                   5    
HELIX   28  28 SER B  239  GLU B  252  1                                  14    
HELIX   29  29 GLY B  262  PRO B  264  5                                   3    
HELIX   30  30 TYR B  265  ARG B  277  1                                  13    
HELIX   31  31 VAL B  285  ASN B  298  1                                  14    
HELIX   32  32 SER B  304  GLY B  317  1                                  14    
HELIX   33  33 PHE B  325  ARG B  335  1                                  11    
SHEET    1  AA12 LEU A  38  LEU A  45  0                                        
SHEET    2  AA12 GLY A 320  THR A 323  1  O  ILE A 321   N  ILE A  39           
SHEET    3  AA12 THR A 280  GLN A 284  1  O  VAL A 282   N  LEU A 322           
SHEET    4  AA12 MET A 256  VAL A 259  1  O  VAL A 257   N  PHE A 281           
SHEET    5  AA12 ARG A 198  ALA A 204  1  O  ALA A 201   N  MET A 258           
SHEET    6  AA12 VAL A 171  PRO A 174  1  O  VAL A 172   N  MET A 200           
SHEET    7  AA12 GLY A 123  VAL A 128  1  O  ILE A 124   N  VAL A 171           
SHEET    8  AA12 ALA A  82  PRO A  87  1  O  LEU A  83   N  ILE A 125           
SHEET    9  AA12 LEU A  38  LEU A  45  1  O  LEU A  38   N  ALA A  82           
SHEET   10  AA12 GLY A 320  THR A 323  1  O  ILE A 321   N  ILE A  39           
SHEET   11  AA12 THR A 280  GLN A 284  1  O  VAL A 282   N  LEU A 322           
SHEET   12  AA12 LEU A  38  LEU A  45  0                                        
SHEET    1  BA12 LEU B  38  LEU B  45  0                                        
SHEET    2  BA12 GLY B 320  THR B 323  1  O  ILE B 321   N  ILE B  39           
SHEET    3  BA12 THR B 280  GLN B 284  1  O  VAL B 282   N  LEU B 322           
SHEET    4  BA12 MET B 256  VAL B 259  1  O  VAL B 257   N  PHE B 281           
SHEET    5  BA12 ARG B 198  ALA B 204  1  O  ALA B 201   N  MET B 258           
SHEET    6  BA12 VAL B 171  PRO B 174  1  O  VAL B 172   N  MET B 200           
SHEET    7  BA12 GLY B 123  VAL B 128  1  O  ILE B 124   N  VAL B 171           
SHEET    8  BA12 ALA B  82  PRO B  87  1  O  LEU B  83   N  ILE B 125           
SHEET    9  BA12 LEU B  38  LEU B  45  1  O  LEU B  38   N  ALA B  82           
SHEET   10  BA12 GLY B 320  THR B 323  1  O  ILE B 321   N  ILE B  39           
SHEET   11  BA12 THR B 280  GLN B 284  1  O  VAL B 282   N  LEU B 322           
SHEET   12  BA12 LEU B  38  LEU B  45  0                                        
LINK         C   ALA A 204                 N   CYJ A 205     1555   1555  1.53  
LINK         C   CYJ A 205                 N   TYR A 206     1555   1555  1.43  
LINK         C8  CYJ A 205                 NZ  LYS A 260     1555   1555  1.77  
LINK         C   ALA B 204                 N   CYJ B 205     1555   1555  1.55  
LINK         C   CYJ B 205                 N   TYR B 206     1555   1555  1.53  
LINK         OE1 GLU A 245                MG    MG A1336     1555   1555  2.02  
LINK        MG    MG A1336                 O   HOH A2245     1555   1555  2.19  
LINK        MG    MG A1336                 O   HOH A2246     1555   1555  2.17  
LINK        MG    MG A1336                 O   HOH A2303     1555   1555  2.06  
LINK        MG    MG A1336                 O   HOH A2304     1555   1555  2.20  
LINK        MG    MG A1336                 O   HOH A2306     1555   1555  2.22  
LINK         OE1 GLU B 245                MG    MG B1336     1555   1555  2.05  
LINK        MG    MG B1336                 O   HOH B2258     1555   1555  2.19  
LINK        MG    MG B1336                 O   HOH B2260     1555   1555  2.18  
LINK        MG    MG B1336                 O   HOH B2308     1555   1555  2.07  
LINK        MG    MG B1336                 O   HOH B2310     1555   1555  2.25  
LINK        MG    MG B1336                 O   HOH B2311     1555   1555  2.21  
CISPEP   1 TYR A   10    PRO A   11          0         1.94                     
CISPEP   2 LYS A  260    PRO A  261          0        -7.59                     
CISPEP   3 TYR B   10    PRO B   11          0        -0.72                     
CISPEP   4 LYS B  260    PRO B  261          0        -6.00                     
SITE     1 AC1  6 GLU A 245  HOH A2245  HOH A2246  HOH A2303                    
SITE     2 AC1  6 HOH A2304  HOH A2306                                          
SITE     1 AC2  6 GLU B 245  HOH B2258  HOH B2260  HOH B2308                    
SITE     2 AC2  6 HOH B2310  HOH B2311                                          
CRYST1  126.877  126.877   86.098  90.00  90.00  90.00 P 4 21 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      0.007882  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007882  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011615        0.00000                         
MTRIX1   1 -0.836420  0.548070 -0.004240      198.32870    1                    
MTRIX2   1  0.548070  0.836430 -0.000330      -59.24349    1                    
MTRIX3   1  0.003370 -0.002600 -0.999990      -17.45602    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system