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Database: PDB
Entry: 3ZGJ
LinkDB: 3ZGJ
Original site: 3ZGJ 
HEADER    OXIDOREDUCTASE                          18-DEC-12   3ZGJ              
TITLE     S221M V223F Y359A MUTANT OF 4-HYDROXYMANDELATE SYNTHASE FROM          
TITLE    2 STREPTOMYCES COELICOLOR                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 4-HYDROXYPHENYLPYRUVIC ACID DIOXYGENASE;                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: 4-HYDROXYMANDELATE SYNTHASE;                                
COMPND   5 EC: 1.13.11.46;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR;                        
SOURCE   3 ORGANISM_TAXID: 100226;                                              
SOURCE   4 STRAIN: A3(2);                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    OXIDOREDUCTASE, DIOXYGENASE, NON-HEME IRON OXYGENASE, BENZYLIC        
KEYWDS   2 HYDROXYLATION                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.PRATTER,G.STRAGANZ,G.GROGAN                                         
REVDAT   2   20-DEC-23 3ZGJ    1       REMARK LINK                              
REVDAT   1   30-OCT-13 3ZGJ    0                                                
JRNL        AUTH   S.PRATTER,C.KONSTANTINOVICS,C.L.M.DIGIURO,E.LEITNER,D.KUMAR, 
JRNL        AUTH 2 S.P.DE VISSER,G.GROGAN,G.STRAGANZ                            
JRNL        TITL   INVERSION OF ENANTIOSELECTIVITY OF A MONONUCLEAR NON-HEME    
JRNL        TITL 2 IRON(II)-DEPENDENT HYDROXYLASE BY TUNING THE INTERPLAY OF    
JRNL        TITL 3 METAL CENTER GEOMETRY AND PROTEIN STRUCTURE                  
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  52  9677 2013              
JRNL        REFN                   ISSN 1433-7851                               
JRNL        PMID   23881738                                                     
JRNL        DOI    10.1002/ANGE.201304633                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 54.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 57014                          
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) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3049                            
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4191                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 196                          
REMARK   3   BIN FREE R VALUE                    : 0.2730                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5051                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 531                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.68000                                             
REMARK   3    B22 (A**2) : -0.68000                                             
REMARK   3    B33 (A**2) : 1.37000                                              
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): 0.140         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.134         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.094         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.268         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5197 ; 0.021 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7090 ; 2.002 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   665 ; 6.715 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   236 ;33.114 ;22.669       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   727 ;14.576 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    49 ;18.129 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   798 ; 0.156 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4083 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  2675 ; 3.494 ; 3.249       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3332 ; 4.683 ; 4.837       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2522 ; 4.594 ; 3.574       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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.                                                          
REMARK   4                                                                      
REMARK   4 3ZGJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-DEC-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290055174.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 120                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97950                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57014                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 61.440                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49000                            
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: PDB ENTRY 2R5V                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 MICROLITRE 10 MG ML-1 HMS VARIANT,     
REMARK 280  PREINCUBATED WITH 1.25 MM COCL2 AND 2.5 MM R-MANDELATE) PLUS 1      
REMARK 280  MICROLITRE MOTHER LIQUOR. THE BEST CRYSTALS WERE ROUTINELY          
REMARK 280  OBTAINED IN CRYSTAL DROPS CONTAINING 0.05 M TRIS/CL PH 9.0, 0.1     
REMARK 280  M MGCL2, 7.5% (W/V) PEG 4K AND 2.5% (V/V) 2-METHYL-1,4-             
REMARK 280  PENTANEDIOL., PH 8.5                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4                              
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,X,Z                                                  
REMARK 290       4555   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        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     PHE A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     PHE A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     TRP A    10                                                      
REMARK 465     ARG A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     MET A    14                                                      
REMARK 465     PRO A   122                                                      
REMARK 465     SER A   123                                                      
REMARK 465     HIS A   124                                                      
REMARK 465     ARG A   125                                                      
REMARK 465     ALA A   126                                                      
REMARK 465     GLY A   127                                                      
REMARK 465     GLN A   128                                                      
REMARK 465     ASP A   129                                                      
REMARK 465     ALA A   130                                                      
REMARK 465     TRP A   131                                                      
REMARK 465     ALA A   149                                                      
REMARK 465     ASP A   150                                                      
REMARK 465     GLY A   151                                                      
REMARK 465     ASP A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     ALA A   154                                                      
REMARK 465     GLY A   155                                                      
REMARK 465     THR A   295                                                      
REMARK 465     GLU A   296                                                      
REMARK 465     ARG A   297                                                      
REMARK 465     VAL A   298                                                      
REMARK 465     GLY A   299                                                      
REMARK 465     ALA A   300                                                      
REMARK 465     MET A   301                                                      
REMARK 465     ALA A   302                                                      
REMARK 465     ASP A   303                                                      
REMARK 465     VAL A   368                                                      
REMARK 465     ALA A   369                                                      
REMARK 465     GLY A   370                                                      
REMARK 465     ARG A   371                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LEU B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     PHE B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     PHE B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     HIS B     9                                                      
REMARK 465     TRP B    10                                                      
REMARK 465     ARG B    11                                                      
REMARK 465     ALA B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     ALA B   149                                                      
REMARK 465     ASP B   150                                                      
REMARK 465     GLY B   151                                                      
REMARK 465     ASP B   152                                                      
REMARK 465     GLY B   153                                                      
REMARK 465     ALA B   154                                                      
REMARK 465     GLY B   155                                                      
REMARK 465     ARG B   297                                                      
REMARK 465     VAL B   298                                                      
REMARK 465     GLY B   299                                                      
REMARK 465     ALA B   300                                                      
REMARK 465     VAL B   368                                                      
REMARK 465     ALA B   369                                                      
REMARK 465     GLY B   370                                                      
REMARK 465     ARG B   371                                                      
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     ASP A  78    CG   OD1  OD2                                       
REMARK 470     ARG A 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 118    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 156    CG   CD1  CD2                                       
REMARK 470     ARG A 172    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 196    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 216    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 285    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 306    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 317    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 319    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 366    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 367    CG   CD   OE1  OE2                                  
REMARK 470     MET B  14    CG   SD   CE                                        
REMARK 470     GLU B  86    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 129    CG   OD1  OD2                                       
REMARK 470     GLU B 216    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 296    CG   CD   OE1  OE2                                  
REMARK 470     MET B 301    CG   SD   CE                                        
REMARK 470     ASP B 303    CG   OD1  OD2                                       
REMARK 470     TYR B 322    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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  2079     O    HOH B  2249              2.01            
REMARK 500   O    HOH A  2073     O    HOH A  2079              2.05            
REMARK 500   NH2  ARG B    30     O    HOH B  2023              2.09            
REMARK 500   O    HOH A  2079     O    HOH A  2142              2.11            
REMARK 500   OD1  ASP B    38     O    HOH B  2043              2.13            
REMARK 500   OE2  GLU A   310     O    HOH A  2194              2.16            
REMARK 500   O    HOH A  2079     O    HOH B  2251              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 162   N   -  CA  -  CB  ANGL. DEV. = -20.7 DEGREES          
REMARK 500    LEU A 166   CA  -  CB  -  CG  ANGL. DEV. =  16.8 DEGREES          
REMARK 500    ASP A 240   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP A 240   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    LEU B  24   CA  -  CB  -  CG  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    ASP B  94   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP B 101   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG B 161   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG B 161   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A 112        1.76    -64.47                                   
REMARK 500    PRO A 120       69.59    -52.63                                   
REMARK 500    ARG A 242     -169.99   -122.57                                   
REMARK 500    THR A 336      -87.91   -104.91                                   
REMARK 500    ASN A 345       69.04   -113.58                                   
REMARK 500    TYR B 206      129.90    -39.27                                   
REMARK 500    THR B 295       46.37    120.56                                   
REMARK 500    ASP B 318     -165.08   -112.28                                   
REMARK 500    THR B 336      -91.38   -101.03                                   
REMARK 500    ASN B 345       66.32   -118.45                                   
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 A2035        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH B2069        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH B2165        DISTANCE =  7.13 ANGSTROMS                       
REMARK 525    HOH B2309        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH B2310        DISTANCE =  7.03 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                              CO A1368  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 181   NE2                                                    
REMARK 620 2 HIS A 261   NE2 114.1                                              
REMARK 620 3 GLU A 340   OE1  96.6  89.2                                        
REMARK 620 4 RMN A1369   O8   92.5  87.4 171.0                                  
REMARK 620 5 RMN A1369   O12 112.7 132.4  94.0  82.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO B1368  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 181   NE2                                                    
REMARK 620 2 HIS B 261   NE2 116.7                                              
REMARK 620 3 GLU B 340   OE1 104.0  95.8                                        
REMARK 620 4 RMN B1369   O12 114.0 123.9  93.8                                  
REMARK 620 5 RMN B1369   O8   93.1  87.9 158.4  66.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO B 1368                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 1368                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RMN B 1369                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RMN A 1369                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SER221MET VAL223PHE TYR359ALA MUTATIONS                              
DBREF  3ZGJ A    1   371  UNP    Q9Z4X7   Q9Z4X7_STRCO     1    371             
DBREF  3ZGJ B    1   371  UNP    Q9Z4X7   Q9Z4X7_STRCO     1    371             
SEQADV 3ZGJ MET A  221  UNP  Q9Z4X7    SER   221 ENGINEERED MUTATION            
SEQADV 3ZGJ PHE A  223  UNP  Q9Z4X7    VAL   223 ENGINEERED MUTATION            
SEQADV 3ZGJ ALA A  359  UNP  Q9Z4X7    TYR   359 ENGINEERED MUTATION            
SEQADV 3ZGJ MET B  221  UNP  Q9Z4X7    SER   221 ENGINEERED MUTATION            
SEQADV 3ZGJ PHE B  223  UNP  Q9Z4X7    VAL   223 ENGINEERED MUTATION            
SEQADV 3ZGJ ALA B  359  UNP  Q9Z4X7    TYR   359 ENGINEERED MUTATION            
SEQRES   1 A  371  MET LEU PRO PRO PHE PRO PHE LEU HIS TRP ARG ALA ALA          
SEQRES   2 A  371  MET PRO PRO SER ASP ILE ALA TYR ALA GLU LEU TYR VAL          
SEQRES   3 A  371  ALA ASP ASP ARG GLU ALA SER GLY PHE LEU VAL ASP SER          
SEQRES   4 A  371  LEU GLY PHE VAL PRO LEU ALA VAL ALA GLY PRO ALA THR          
SEQRES   5 A  371  GLY THR HIS ASP ARG ARG SER THR VAL LEU ARG SER GLY          
SEQRES   6 A  371  GLU VAL THR LEU VAL VAL THR GLN ALA LEU ALA PRO ASP          
SEQRES   7 A  371  THR PRO VAL ALA ARG TYR VAL GLU ARG HIS GLY ASP SER          
SEQRES   8 A  371  ILE ALA ASP LEU ALA PHE GLY CYS ASP ASP VAL ARG SER          
SEQRES   9 A  371  CYS PHE ASP ARG ALA VAL LEU ALA GLY ALA GLU ALA LEU          
SEQRES  10 A  371  GLN ALA PRO THR PRO SER HIS ARG ALA GLY GLN ASP ALA          
SEQRES  11 A  371  TRP PHE ALA THR VAL SER GLY PHE GLY ASP ILE ARG HIS          
SEQRES  12 A  371  THR LEU VAL PRO ALA ALA ASP GLY ASP GLY ALA GLY LEU          
SEQRES  13 A  371  LEU PRO PRO ASP ARG ASP TRP ALA LEU LEU PRO ALA ALA          
SEQRES  14 A  371  THR GLY ARG THR GLY PRO ARG PRO LEU LEU ASP HIS VAL          
SEQRES  15 A  371  ALA VAL CYS LEU GLU SER GLY THR LEU ARG SER THR ALA          
SEQRES  16 A  371  GLU PHE TYR GLU ALA ALA PHE ASP MET PRO TYR TYR SER          
SEQRES  17 A  371  SER GLU TYR ILE GLU VAL GLY GLU GLN ALA MET ASP MET          
SEQRES  18 A  371  ILE PHE VAL ARG ASN ALA GLY GLY GLY ILE THR PHE THR          
SEQRES  19 A  371  LEU ILE GLU PRO ASP ASP THR ARG VAL PRO GLY GLN ILE          
SEQRES  20 A  371  ASP GLN PHE LEU SER ALA HIS ASP GLY PRO GLY VAL GLN          
SEQRES  21 A  371  HIS LEU ALA PHE LEU VAL ASP ASP ILE VAL GLY SER VAL          
SEQRES  22 A  371  ARG SER LEU GLY ASP ARG GLY VAL ALA PHE LEU ARG THR          
SEQRES  23 A  371  PRO GLY ALA TYR TYR ASP LEU LEU THR GLU ARG VAL GLY          
SEQRES  24 A  371  ALA MET ALA ASP ALA ILE GLU ASP LEU ARG GLU THR ASN          
SEQRES  25 A  371  VAL LEU ALA ASP ARG ASP GLU TRP GLY TYR LEU LEU GLN          
SEQRES  26 A  371  ILE PHE THR ARG SER PRO TYR PRO ARG GLY THR LEU PHE          
SEQRES  27 A  371  TYR GLU TYR ILE GLN ARG ASN GLY ALA ARG GLY PHE GLY          
SEQRES  28 A  371  SER SER ASN ILE LYS ALA LEU ALA GLU ALA VAL GLU ARG          
SEQRES  29 A  371  GLU ARG GLU VAL ALA GLY ARG                                  
SEQRES   1 B  371  MET LEU PRO PRO PHE PRO PHE LEU HIS TRP ARG ALA ALA          
SEQRES   2 B  371  MET PRO PRO SER ASP ILE ALA TYR ALA GLU LEU TYR VAL          
SEQRES   3 B  371  ALA ASP ASP ARG GLU ALA SER GLY PHE LEU VAL ASP SER          
SEQRES   4 B  371  LEU GLY PHE VAL PRO LEU ALA VAL ALA GLY PRO ALA THR          
SEQRES   5 B  371  GLY THR HIS ASP ARG ARG SER THR VAL LEU ARG SER GLY          
SEQRES   6 B  371  GLU VAL THR LEU VAL VAL THR GLN ALA LEU ALA PRO ASP          
SEQRES   7 B  371  THR PRO VAL ALA ARG TYR VAL GLU ARG HIS GLY ASP SER          
SEQRES   8 B  371  ILE ALA ASP LEU ALA PHE GLY CYS ASP ASP VAL ARG SER          
SEQRES   9 B  371  CYS PHE ASP ARG ALA VAL LEU ALA GLY ALA GLU ALA LEU          
SEQRES  10 B  371  GLN ALA PRO THR PRO SER HIS ARG ALA GLY GLN ASP ALA          
SEQRES  11 B  371  TRP PHE ALA THR VAL SER GLY PHE GLY ASP ILE ARG HIS          
SEQRES  12 B  371  THR LEU VAL PRO ALA ALA ASP GLY ASP GLY ALA GLY LEU          
SEQRES  13 B  371  LEU PRO PRO ASP ARG ASP TRP ALA LEU LEU PRO ALA ALA          
SEQRES  14 B  371  THR GLY ARG THR GLY PRO ARG PRO LEU LEU ASP HIS VAL          
SEQRES  15 B  371  ALA VAL CYS LEU GLU SER GLY THR LEU ARG SER THR ALA          
SEQRES  16 B  371  GLU PHE TYR GLU ALA ALA PHE ASP MET PRO TYR TYR SER          
SEQRES  17 B  371  SER GLU TYR ILE GLU VAL GLY GLU GLN ALA MET ASP MET          
SEQRES  18 B  371  ILE PHE VAL ARG ASN ALA GLY GLY GLY ILE THR PHE THR          
SEQRES  19 B  371  LEU ILE GLU PRO ASP ASP THR ARG VAL PRO GLY GLN ILE          
SEQRES  20 B  371  ASP GLN PHE LEU SER ALA HIS ASP GLY PRO GLY VAL GLN          
SEQRES  21 B  371  HIS LEU ALA PHE LEU VAL ASP ASP ILE VAL GLY SER VAL          
SEQRES  22 B  371  ARG SER LEU GLY ASP ARG GLY VAL ALA PHE LEU ARG THR          
SEQRES  23 B  371  PRO GLY ALA TYR TYR ASP LEU LEU THR GLU ARG VAL GLY          
SEQRES  24 B  371  ALA MET ALA ASP ALA ILE GLU ASP LEU ARG GLU THR ASN          
SEQRES  25 B  371  VAL LEU ALA ASP ARG ASP GLU TRP GLY TYR LEU LEU GLN          
SEQRES  26 B  371  ILE PHE THR ARG SER PRO TYR PRO ARG GLY THR LEU PHE          
SEQRES  27 B  371  TYR GLU TYR ILE GLN ARG ASN GLY ALA ARG GLY PHE GLY          
SEQRES  28 B  371  SER SER ASN ILE LYS ALA LEU ALA GLU ALA VAL GLU ARG          
SEQRES  29 B  371  GLU ARG GLU VAL ALA GLY ARG                                  
HET     CO  A1368       1                                                       
HET    RMN  A1369      11                                                       
HET     CO  B1368       1                                                       
HET    RMN  B1369      11                                                       
HETNAM      CO COBALT (II) ION                                                  
HETNAM     RMN (R)-MANDELIC ACID                                                
FORMUL   3   CO    2(CO 2+)                                                     
FORMUL   4  RMN    2(C8 H8 O3)                                                  
FORMUL   7  HOH   *531(H2 O)                                                    
HELIX    1   1 ASP A   28  SER A   39  1                                  12    
HELIX    2   2 GLY A   49  GLY A   53  5                                   5    
HELIX    3   3 THR A   79  GLY A   89  1                                  11    
HELIX    4   4 ASP A  101  ALA A  112  1                                  12    
HELIX    5   5 PRO A  167  GLY A  171  5                                   5    
HELIX    6   6 THR A  190  ASP A  203  1                                  14    
HELIX    7   7 GLY A  245  ASP A  255  1                                  11    
HELIX    8   8 ASP A  268  ARG A  279  1                                  12    
HELIX    9   9 PRO A  287  LEU A  294  1                                   8    
HELIX   10  10 ALA A  304  ASN A  312  1                                   9    
HELIX   11  11 GLY A  351  GLU A  367  1                                  17    
HELIX   12  12 ASP B   28  SER B   39  1                                  12    
HELIX   13  13 GLY B   49  GLY B   53  5                                   5    
HELIX   14  14 THR B   79  GLY B   89  1                                  11    
HELIX   15  15 ASP B  101  ALA B  112  1                                  12    
HELIX   16  16 PRO B  167  GLY B  171  5                                   5    
HELIX   17  17 THR B  190  ASP B  203  1                                  14    
HELIX   18  18 GLY B  245  HIS B  254  1                                  10    
HELIX   19  19 ASP B  268  ARG B  279  1                                  12    
HELIX   20  20 PRO B  287  LEU B  294  1                                   8    
HELIX   21  21 MET B  301  ASN B  312  1                                  12    
HELIX   22  22 GLY B  351  GLU B  367  1                                  17    
SHEET    1  AA 9 ALA A 116  GLN A 118  0                                        
SHEET    2  AA 9 ALA A 133  SER A 136 -1  O  THR A 134   N  LEU A 117           
SHEET    3  AA 9 ARG A 142  PRO A 147 -1  O  HIS A 143   N  VAL A 135           
SHEET    4  AA 9 SER A  91  CYS A  99  1  O  ALA A  93   N  ARG A 142           
SHEET    5  AA 9 ASP A  18  VAL A  26 -1  O  ASP A  18   N  GLY A  98           
SHEET    6  AA 9 VAL A  67  ALA A  74  1  O  THR A  68   N  ALA A  22           
SHEET    7  AA 9 ARG A  57  SER A  64 -1  O  ARG A  58   N  GLN A  73           
SHEET    8  AA 9 VAL A  43  ALA A  48 -1  O  VAL A  43   N  ARG A  63           
SHEET    9  AA 9 ALA A 164  LEU A 165 -1  O  ALA A 164   N  VAL A  47           
SHEET    1  AB 8 TYR A 206  VAL A 214  0                                        
SHEET    2  AB 8 GLN A 217  ARG A 225 -1  O  GLN A 217   N  VAL A 214           
SHEET    3  AB 8 THR A 232  PRO A 238 -1  O  PHE A 233   N  VAL A 224           
SHEET    4  AB 8 LEU A 178  CYS A 185  1  O  VAL A 182   N  THR A 234           
SHEET    5  AB 8 GLY A 258  LEU A 265 -1  O  GLY A 258   N  CYS A 185           
SHEET    6  AB 8 PHE A 338  ARG A 344  1  O  PHE A 338   N  LEU A 262           
SHEET    7  AB 8 GLY A 321  PHE A 327 -1  O  LEU A 324   N  GLN A 343           
SHEET    8  AB 8 LEU A 314  ASP A 318 -1  O  LEU A 314   N  GLN A 325           
SHEET    1  BA 9 ALA B 116  PRO B 122  0                                        
SHEET    2  BA 9 TRP B 131  SER B 136 -1  O  PHE B 132   N  THR B 121           
SHEET    3  BA 9 ARG B 142  PRO B 147 -1  O  HIS B 143   N  VAL B 135           
SHEET    4  BA 9 SER B  91  CYS B  99  1  O  ALA B  93   N  ARG B 142           
SHEET    5  BA 9 ASP B  18  VAL B  26 -1  O  ASP B  18   N  GLY B  98           
SHEET    6  BA 9 VAL B  67  ALA B  74  1  O  THR B  68   N  ALA B  22           
SHEET    7  BA 9 ARG B  57  SER B  64 -1  O  ARG B  58   N  GLN B  73           
SHEET    8  BA 9 VAL B  43  ALA B  48 -1  O  VAL B  43   N  ARG B  63           
SHEET    9  BA 9 ALA B 164  LEU B 165 -1  O  ALA B 164   N  VAL B  47           
SHEET    1  BB 8 TYR B 206  VAL B 214  0                                        
SHEET    2  BB 8 GLN B 217  ARG B 225 -1  O  GLN B 217   N  VAL B 214           
SHEET    3  BB 8 THR B 232  PRO B 238 -1  O  PHE B 233   N  VAL B 224           
SHEET    4  BB 8 LEU B 178  CYS B 185  1  O  VAL B 182   N  THR B 234           
SHEET    5  BB 8 GLY B 258  LEU B 265 -1  O  GLY B 258   N  CYS B 185           
SHEET    6  BB 8 PHE B 338  ARG B 344  1  O  PHE B 338   N  LEU B 262           
SHEET    7  BB 8 GLY B 321  PHE B 327 -1  O  LEU B 324   N  GLN B 343           
SHEET    8  BB 8 LEU B 314  ASP B 318 -1  O  LEU B 314   N  GLN B 325           
SSBOND   1 CYS B   99    CYS B  105                          1555   1555  2.29  
LINK         NE2 HIS A 181                CO    CO A1368     1555   1555  2.08  
LINK         NE2 HIS A 261                CO    CO A1368     1555   1555  2.11  
LINK         OE1 GLU A 340                CO    CO A1368     1555   1555  2.06  
LINK        CO    CO A1368                 O8  RMN A1369     1555   1555  2.34  
LINK        CO    CO A1368                 O12 RMN A1369     1555   1555  2.06  
LINK         NE2 HIS B 181                CO    CO B1368     1555   1555  2.05  
LINK         NE2 HIS B 261                CO    CO B1368     1555   1555  2.07  
LINK         OE1 GLU B 340                CO    CO B1368     1555   1555  1.77  
LINK        CO    CO B1368                 O12 RMN B1369     1555   1555  2.10  
LINK        CO    CO B1368                 O8  RMN B1369     1555   1555  2.33  
CISPEP   1 ARG A  176    PRO A  177          0        -5.99                     
CISPEP   2 ARG B  176    PRO B  177          0        -2.46                     
SITE     1 AC1  4 HIS B 181  HIS B 261  GLU B 340  RMN B1369                    
SITE     1 AC2  4 HIS A 181  HIS A 261  GLU A 340  RMN A1369                    
SITE     1 AC3 10 HIS B 181  THR B 234  ILE B 236  HIS B 261                    
SITE     2 AC3 10 GLN B 325  GLU B 340  PHE B 350  ILE B 355                    
SITE     3 AC3 10  CO B1368  HOH B2232                                          
SITE     1 AC4  8 HIS A 181  THR A 234  HIS A 261  GLN A 325                    
SITE     2 AC4  8 GLU A 340  PHE A 350  ILE A 355   CO A1368                    
CRYST1  122.870  122.870   54.860  90.00  90.00  90.00 P 4           8          
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      0.008139  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008139  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018228        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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