GenomeNet

Database: PDB
Entry: 4CYU
LinkDB: 4CYU
Original site: 4CYU 
HEADER    TRANSFERASE                             15-APR-14   4CYU              
TITLE     STAPHYLOCOCCUS AUREUS 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-              
TITLE    2 PYROPHOSPHOKINASE IN COMPLEX WITH AMPCPP                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE;       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HPPK;                                                       
COMPND   5 EC: 2.7.6.3;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE;       
COMPND   9 CHAIN: B, C, D;                                                      
COMPND  10 SYNONYM: HPPK;                                                       
COMPND  11 EC: 2.7.6.3;                                                         
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE  11 ORGANISM_TAXID: 1280;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  14 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_VECTOR: PET                                        
KEYWDS    TRANSFERASE, S.AUREUS, FOLATE, STRUCTURE-BASED DRUG DESIGN            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.L.DENNIS,J.D.SWARBRICK,T.S.PEAT                                     
REVDAT   2   08-MAY-19 4CYU    1       REMARK                                   
REVDAT   1   28-JAN-15 4CYU    0                                                
JRNL        AUTH   M.L.DENNIS,S.CHHABRA,Z.WANG,A.DEBONO,O.DOLEZAL,J.NEWMAN,     
JRNL        AUTH 2 N.P.PITCHER,R.RAHMANI,B.CLEARY,N.BARLOW,M.HATTARKI,B.GRAHAM, 
JRNL        AUTH 3 T.S.PEAT,J.B.BAELL,J.D.SWARBRICK                             
JRNL        TITL   STRUCTURE-BASED DESIGN AND DEVELOPMENT OF FUNCTIONALIZED     
JRNL        TITL 2 MERCAPTOGUANINE DERIVATIVES AS INHIBITORS OF THE FOLATE      
JRNL        TITL 3 BIOSYNTHESIS PATHWAY ENZYME                                  
JRNL        TITL 4 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE FROM     
JRNL        TITL 5 STAPHYLOCOCCUS AUREUS.                                       
JRNL        REF    J.MED.CHEM.                   V.  57  9612 2014              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   25357262                                                     
JRNL        DOI    10.1021/JM501417F                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.53                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 17651                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 838                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1303                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 55                           
REMARK   3   BIN FREE R VALUE                    : 0.3830                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4999                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 148                                     
REMARK   3   SOLVENT ATOMS            : 13                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.16000                                              
REMARK   3    B22 (A**2) : 0.06000                                              
REMARK   3    B33 (A**2) : -0.98000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.65000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.361         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5293 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5116 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7224 ; 1.493 ; 2.040       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11796 ; 3.437 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   619 ; 6.304 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   233 ;33.791 ;24.807       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   943 ;14.635 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ;16.655 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   839 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5702 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1094 ; 0.005 ; 0.020       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
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   : 1.10                                          
REMARK   3   ION PROBE RADIUS   : 0.90                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES REFINED INDIVIDUALLY RESIDUES OF LOOP 2 ARE     
REMARK   3  NOT MODELLED IN CHAINS A (RESIDUES 45-48) AND B (RESIDUES 46-48)    
REMARK   3  DUE TO POOR DENSITY.                                                
REMARK   4                                                                      
REMARK   4 4CYU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290060352.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-DEC-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.008000                           
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   : 18506                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.530                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.90000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4AD6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 6.9 MG/ML 1 MM AMPCPP, 2 MM      
REMARK 280  MAGNESIUM CHLORIDE, MAGNESIUM ACETATE 0.119 M, PEG8000 12.6% W/V,   
REMARK 280  TRIS CHLORIDE 0.12 M, SITTING DROP, 281 K, PH 8, VAPOR              
REMARK 280  DIFFUSION, SITTING DROP                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       47.13150            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: D                                     
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     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     PRO A    45                                                      
REMARK 465     VAL A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     TYR A    48                                                      
REMARK 465     LYS A   158                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     VAL B    46                                                      
REMARK 465     GLY B    47                                                      
REMARK 465     TYR B    48                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     LYS C   158                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     LYS D   158                                                      
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   OE2  GLU A    28     NH1  ARG B    88              2.14            
REMARK 500   OE2  GLU C    50     NH2  ARG D   156              2.19            
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 132       33.79   -148.87                                   
REMARK 500    ALA B 132       33.26   -148.11                                   
REMARK 500    LYS C  86      156.07    -42.12                                   
REMARK 500    ALA C 132       33.65   -148.37                                   
REMARK 500    ALA D 132       33.48   -147.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 170  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 APC A1158   O1A                                                    
REMARK 620 2 APC A1158   O1B  91.5                                              
REMARK 620 3 HOH A2002   O    80.4 146.2                                        
REMARK 620 4 ASP A  95   OD1  77.6  82.1  64.2                                  
REMARK 620 5 ASP A  97   OD1 150.2  94.6  78.3  74.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 171  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 APC A1158   O1B                                                    
REMARK 620 2 APC A1158   O1G  71.8                                              
REMARK 620 3 ASP A  97   OD2  73.8  75.8                                        
REMARK 620 4 ASP A  95   OD2  69.7 136.8  75.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 170  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 APC B1159   O1A                                                    
REMARK 620 2 APC B1159   O1A  13.2                                              
REMARK 620 3 GLU B  78   OE2 113.1 101.2                                        
REMARK 620 4 HOH B2001   O    62.6  73.7 172.0                                  
REMARK 620 5 ASP B  95   OD1  75.2  76.4  75.3 108.8                            
REMARK 620 6 ASP B  97   OD1 104.5 116.9 121.5  66.4  73.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 171  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  95   OD2                                                    
REMARK 620 2 APC B1159   O1B 123.3                                              
REMARK 620 3 APC B1159   O2B  69.7  54.1                                        
REMARK 620 4 APC B1159   O1B  72.9  53.1  10.2                                  
REMARK 620 5 ASP B  97   OD2  76.4 104.7  86.6  77.8                            
REMARK 620 6 APC B1159   O1G 140.2  50.9  87.9  80.1  69.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 170  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 APC C1158   O1B                                                    
REMARK 620 2 HOH C2001   O   162.7                                              
REMARK 620 3 APC C1158   O1A  85.0 101.2                                        
REMARK 620 4 ASP C  95   OD1  86.0  78.2  87.9                                  
REMARK 620 5 HOH C2002   O    93.6  98.8 112.1 159.9                            
REMARK 620 6 ASP C  97   OD1  88.7  80.9 163.6  76.5  83.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 171  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 APC C1158   O1G                                                    
REMARK 620 2 APC C1158   O1B  72.7                                              
REMARK 620 3 ASP C  95   OD2 139.6  70.1                                        
REMARK 620 4 ASP C  97   OD2  77.5  75.5  78.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 170  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 APC D1158   O1B                                                    
REMARK 620 2 ASP D  95   OD1  81.5                                              
REMARK 620 3 ASP D  97   OD1  87.7  74.8                                        
REMARK 620 4 HOH D2002   O   166.0  84.8  85.6                                  
REMARK 620 5 APC D1158   O1A  79.1  73.3 146.9 100.1                            
REMARK 620 6 APC D1158   O2B  13.1  71.4  92.9 155.6  68.7                      
REMARK 620 7 APC D1158   O1A  69.3  84.9 151.5 112.8  16.0  61.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 171  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 APC D1158   O1G                                                    
REMARK 620 2 APC D1158   O1B  79.5                                              
REMARK 620 3 APC D1158   O2B  88.5  13.8                                        
REMARK 620 4 ASP D  95   OD2 153.4  76.8  70.7                                  
REMARK 620 5 ASP D  97   OD2  84.8  76.4  87.4  78.0                            
REMARK 620 6 APC D1158   O1B  46.0  56.3  56.6 124.4 113.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 170                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 171                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 170                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 171                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 170                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 171                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 170                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 171                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APC A 1158                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APC B 1159                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APC C 1158                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE APC D 1158                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 1160                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 1159                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 HEXAHISTIDINE-TAG WITH THROMBIN CLEAVAGE AT THE N-TERMINUS           
DBREF  4CYU A    1   158  UNP    C8MLE4   C8MLE4_STAAU     1    158             
DBREF  4CYU B    1   158  UNP    C8MLE4   C8MLE4_STAAU     1    158             
DBREF  4CYU C    1   158  UNP    C8MLE4   C8MLE4_STAAU     1    158             
DBREF  4CYU D    1   158  UNP    C8MLE4   C8MLE4_STAAU     1    158             
SEQADV 4CYU GLY A   -2  UNP  C8MLE4              EXPRESSION TAG                 
SEQADV 4CYU SER A   -1  UNP  C8MLE4              EXPRESSION TAG                 
SEQADV 4CYU HIS A    0  UNP  C8MLE4              EXPRESSION TAG                 
SEQADV 4CYU ASN A  151  UNP  C8MLE4    ASP   151 CONFLICT                       
SEQADV 4CYU GLY B   -2  UNP  C8MLE4              EXPRESSION TAG                 
SEQADV 4CYU SER B   -1  UNP  C8MLE4              EXPRESSION TAG                 
SEQADV 4CYU HIS B    0  UNP  C8MLE4              EXPRESSION TAG                 
SEQADV 4CYU GLY C   -2  UNP  C8MLE4              EXPRESSION TAG                 
SEQADV 4CYU SER C   -1  UNP  C8MLE4              EXPRESSION TAG                 
SEQADV 4CYU HIS C    0  UNP  C8MLE4              EXPRESSION TAG                 
SEQADV 4CYU GLY D   -2  UNP  C8MLE4              EXPRESSION TAG                 
SEQADV 4CYU SER D   -1  UNP  C8MLE4              EXPRESSION TAG                 
SEQADV 4CYU HIS D    0  UNP  C8MLE4              EXPRESSION TAG                 
SEQRES   1 A  161  GLY SER HIS MET ILE GLN ALA TYR LEU GLY LEU GLY SER          
SEQRES   2 A  161  ASN ILE GLY ASP ARG GLU SER GLN LEU ASN ASP ALA ILE          
SEQRES   3 A  161  LYS ILE LEU ASN GLU TYR ASP GLY ILE SER VAL SER ASN          
SEQRES   4 A  161  ILE SER PRO ILE TYR GLU THR ALA PRO VAL GLY TYR THR          
SEQRES   5 A  161  GLU GLN PRO ASN PHE LEU ASN LEU CYS VAL GLU ILE GLN          
SEQRES   6 A  161  THR THR LEU THR VAL LEU GLN LEU LEU GLU CYS CYS LEU          
SEQRES   7 A  161  LYS THR GLU GLU CYS LEU HIS ARG ILE ARG LYS GLU ARG          
SEQRES   8 A  161  TRP GLY PRO ARG THR LEU ASP VAL ASP ILE LEU LEU TYR          
SEQRES   9 A  161  GLY GLU GLU MET ILE ASP LEU PRO LYS LEU SER VAL PRO          
SEQRES  10 A  161  HIS PRO ARG MET ASN GLU ARG ALA PHE VAL LEU ILE PRO          
SEQRES  11 A  161  LEU ASN ASP ILE ALA ALA ASN VAL VAL GLU PRO ARG SER          
SEQRES  12 A  161  LYS LEU LYS VAL LYS ASP LEU VAL PHE VAL ASN ASP SER          
SEQRES  13 A  161  VAL LYS ARG TYR LYS                                          
SEQRES   1 B  161  GLY SER HIS MET ILE GLN ALA TYR LEU GLY LEU GLY SER          
SEQRES   2 B  161  ASN ILE GLY ASP ARG GLU SER GLN LEU ASN ASP ALA ILE          
SEQRES   3 B  161  LYS ILE LEU ASN GLU TYR ASP GLY ILE SER VAL SER ASN          
SEQRES   4 B  161  ILE SER PRO ILE TYR GLU THR ALA PRO VAL GLY TYR THR          
SEQRES   5 B  161  GLU GLN PRO ASN PHE LEU ASN LEU CYS VAL GLU ILE GLN          
SEQRES   6 B  161  THR THR LEU THR VAL LEU GLN LEU LEU GLU CYS CYS LEU          
SEQRES   7 B  161  LYS THR GLU GLU CYS LEU HIS ARG ILE ARG LYS GLU ARG          
SEQRES   8 B  161  TRP GLY PRO ARG THR LEU ASP VAL ASP ILE LEU LEU TYR          
SEQRES   9 B  161  GLY GLU GLU MET ILE ASP LEU PRO LYS LEU SER VAL PRO          
SEQRES  10 B  161  HIS PRO ARG MET ASN GLU ARG ALA PHE VAL LEU ILE PRO          
SEQRES  11 B  161  LEU ASN ASP ILE ALA ALA ASN VAL VAL GLU PRO ARG SER          
SEQRES  12 B  161  LYS LEU LYS VAL LYS ASP LEU VAL PHE VAL ASP ASP SER          
SEQRES  13 B  161  VAL LYS ARG TYR LYS                                          
SEQRES   1 C  161  GLY SER HIS MET ILE GLN ALA TYR LEU GLY LEU GLY SER          
SEQRES   2 C  161  ASN ILE GLY ASP ARG GLU SER GLN LEU ASN ASP ALA ILE          
SEQRES   3 C  161  LYS ILE LEU ASN GLU TYR ASP GLY ILE SER VAL SER ASN          
SEQRES   4 C  161  ILE SER PRO ILE TYR GLU THR ALA PRO VAL GLY TYR THR          
SEQRES   5 C  161  GLU GLN PRO ASN PHE LEU ASN LEU CYS VAL GLU ILE GLN          
SEQRES   6 C  161  THR THR LEU THR VAL LEU GLN LEU LEU GLU CYS CYS LEU          
SEQRES   7 C  161  LYS THR GLU GLU CYS LEU HIS ARG ILE ARG LYS GLU ARG          
SEQRES   8 C  161  TRP GLY PRO ARG THR LEU ASP VAL ASP ILE LEU LEU TYR          
SEQRES   9 C  161  GLY GLU GLU MET ILE ASP LEU PRO LYS LEU SER VAL PRO          
SEQRES  10 C  161  HIS PRO ARG MET ASN GLU ARG ALA PHE VAL LEU ILE PRO          
SEQRES  11 C  161  LEU ASN ASP ILE ALA ALA ASN VAL VAL GLU PRO ARG SER          
SEQRES  12 C  161  LYS LEU LYS VAL LYS ASP LEU VAL PHE VAL ASP ASP SER          
SEQRES  13 C  161  VAL LYS ARG TYR LYS                                          
SEQRES   1 D  161  GLY SER HIS MET ILE GLN ALA TYR LEU GLY LEU GLY SER          
SEQRES   2 D  161  ASN ILE GLY ASP ARG GLU SER GLN LEU ASN ASP ALA ILE          
SEQRES   3 D  161  LYS ILE LEU ASN GLU TYR ASP GLY ILE SER VAL SER ASN          
SEQRES   4 D  161  ILE SER PRO ILE TYR GLU THR ALA PRO VAL GLY TYR THR          
SEQRES   5 D  161  GLU GLN PRO ASN PHE LEU ASN LEU CYS VAL GLU ILE GLN          
SEQRES   6 D  161  THR THR LEU THR VAL LEU GLN LEU LEU GLU CYS CYS LEU          
SEQRES   7 D  161  LYS THR GLU GLU CYS LEU HIS ARG ILE ARG LYS GLU ARG          
SEQRES   8 D  161  TRP GLY PRO ARG THR LEU ASP VAL ASP ILE LEU LEU TYR          
SEQRES   9 D  161  GLY GLU GLU MET ILE ASP LEU PRO LYS LEU SER VAL PRO          
SEQRES  10 D  161  HIS PRO ARG MET ASN GLU ARG ALA PHE VAL LEU ILE PRO          
SEQRES  11 D  161  LEU ASN ASP ILE ALA ALA ASN VAL VAL GLU PRO ARG SER          
SEQRES  12 D  161  LYS LEU LYS VAL LYS ASP LEU VAL PHE VAL ASP ASP SER          
SEQRES  13 D  161  VAL LYS ARG TYR LYS                                          
HET     MG  A 170       1                                                       
HET     MG  A 171       1                                                       
HET    APC  A1158      31                                                       
HET    TRS  A1159       8                                                       
HET     MG  B 170       1                                                       
HET     MG  B 171       1                                                       
HET    APC  B1159      62                                                       
HET    TRS  B1160       8                                                       
HET     MG  C 170       1                                                       
HET     MG  C 171       1                                                       
HET    APC  C1158      31                                                       
HET     MG  D 170       1                                                       
HET     MG  D 171       1                                                       
HET    APC  D1158      62                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER                    
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     APC ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE                    
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   5   MG    8(MG 2+)                                                     
FORMUL   7  APC    4(C11 H18 N5 O12 P3)                                         
FORMUL   8  TRS    2(C4 H12 N O3 1+)                                            
FORMUL  19  HOH   *13(H2 O)                                                     
HELIX    1   1 ASP A   14  GLU A   28  1                                  15    
HELIX    2   2 THR A   66  ILE A   84  1                                  19    
HELIX    3   3 ARG A  117  GLU A  120  5                                   4    
HELIX    4   4 ARG A  121  ALA A  133  1                                  13    
HELIX    5   5 VAL A  144  VAL A  148  1                                   5    
HELIX    6   6 ASP B   14  GLU B   28  1                                  15    
HELIX    7   7 THR B   66  ILE B   84  1                                  19    
HELIX    8   8 ARG B  117  GLU B  120  5                                   4    
HELIX    9   9 ARG B  121  ALA B  133  1                                  13    
HELIX   10  10 VAL B  144  VAL B  148  1                                   5    
HELIX   11  11 ASP C   14  ASN C   27  1                                  14    
HELIX   12  12 THR C   66  LYS C   86  1                                  21    
HELIX   13  13 ARG C  117  GLU C  120  5                                   4    
HELIX   14  14 ARG C  121  ALA C  133  1                                  13    
HELIX   15  15 VAL C  144  VAL C  148  1                                   5    
HELIX   16  16 ASP D   14  GLU D   28  1                                  15    
HELIX   17  17 THR D   66  ARG D   85  1                                  20    
HELIX   18  18 ARG D  117  GLU D  120  5                                   4    
HELIX   19  19 ARG D  121  ALA D  133  1                                  13    
HELIX   20  20 VAL D  144  VAL D  148  1                                   5    
SHEET    1  AA 2 ILE A  32  ILE A  37  0                                        
SHEET    2  AA 2 PHE A  54  THR A  63 -1  O  GLU A  60   N  SER A  35           
SHEET    1  AB 5 ASP A  95  TYR A 101  0                                        
SHEET    2  AB 5 ILE A   2  SER A  10 -1  O  TYR A   5   N  LEU A  99           
SHEET    3  AB 5 PHE A  54  THR A  63 -1  O  LEU A  55   N  SER A  10           
SHEET    4  AB 5 TYR A  41  THR A  43 -1  O  TYR A  41   N  ASN A  56           
SHEET    5  AB 5 VAL A 154  ARG A 156 -1  O  LYS A 155   N  GLU A  42           
SHEET    1  AC 4 ASP A  95  TYR A 101  0                                        
SHEET    2  AC 4 ILE A   2  SER A  10 -1  O  TYR A   5   N  LEU A  99           
SHEET    3  AC 4 PHE A  54  THR A  63 -1  O  LEU A  55   N  SER A  10           
SHEET    4  AC 4 ILE A  32  ILE A  37 -1  O  SER A  33   N  GLN A  62           
SHEET    1  AD 2 ILE A 106  LEU A 108  0                                        
SHEET    2  AD 2 LEU A 111  VAL A 113 -1  O  LEU A 111   N  LEU A 108           
SHEET    1  AE 2 VAL A 136  GLU A 137  0                                        
SHEET    2  AE 2 LEU A 142  LYS A 143 -1  O  LEU A 142   N  GLU A 137           
SHEET    1  BA 2 ILE B  32  ILE B  37  0                                        
SHEET    2  BA 2 PHE B  54  THR B  63 -1  O  GLU B  60   N  SER B  35           
SHEET    1  BB 5 ASP B  95  TYR B 101  0                                        
SHEET    2  BB 5 ILE B   2  SER B  10 -1  O  TYR B   5   N  LEU B  99           
SHEET    3  BB 5 PHE B  54  THR B  63 -1  O  LEU B  55   N  SER B  10           
SHEET    4  BB 5 TYR B  41  THR B  43 -1  O  TYR B  41   N  ASN B  56           
SHEET    5  BB 5 VAL B 154  ARG B 156 -1  O  LYS B 155   N  GLU B  42           
SHEET    1  BC 4 ASP B  95  TYR B 101  0                                        
SHEET    2  BC 4 ILE B   2  SER B  10 -1  O  TYR B   5   N  LEU B  99           
SHEET    3  BC 4 PHE B  54  THR B  63 -1  O  LEU B  55   N  SER B  10           
SHEET    4  BC 4 ILE B  32  ILE B  37 -1  O  SER B  33   N  GLN B  62           
SHEET    1  BD 2 ILE B 106  LEU B 108  0                                        
SHEET    2  BD 2 LEU B 111  VAL B 113 -1  O  LEU B 111   N  LEU B 108           
SHEET    1  BE 2 VAL B 136  GLU B 137  0                                        
SHEET    2  BE 2 LEU B 142  LYS B 143 -1  O  LEU B 142   N  GLU B 137           
SHEET    1  CA 2 ILE C  32  ILE C  37  0                                        
SHEET    2  CA 2 PHE C  54  THR C  63 -1  O  GLU C  60   N  SER C  35           
SHEET    1  CB 5 ASP C  95  TYR C 101  0                                        
SHEET    2  CB 5 ILE C   2  SER C  10 -1  O  TYR C   5   N  LEU C  99           
SHEET    3  CB 5 PHE C  54  THR C  63 -1  O  LEU C  55   N  SER C  10           
SHEET    4  CB 5 TYR C  41  THR C  43 -1  O  TYR C  41   N  ASN C  56           
SHEET    5  CB 5 VAL C 154  ARG C 156 -1  O  LYS C 155   N  GLU C  42           
SHEET    1  CC 4 ASP C  95  TYR C 101  0                                        
SHEET    2  CC 4 ILE C   2  SER C  10 -1  O  TYR C   5   N  LEU C  99           
SHEET    3  CC 4 PHE C  54  THR C  63 -1  O  LEU C  55   N  SER C  10           
SHEET    4  CC 4 ILE C  32  ILE C  37 -1  O  SER C  33   N  GLN C  62           
SHEET    1  CD 2 ILE C 106  LEU C 108  0                                        
SHEET    2  CD 2 LEU C 111  VAL C 113 -1  O  LEU C 111   N  LEU C 108           
SHEET    1  CE 2 VAL C 136  GLU C 137  0                                        
SHEET    2  CE 2 LEU C 142  LYS C 143 -1  O  LEU C 142   N  GLU C 137           
SHEET    1  DA 2 ILE D  32  ILE D  37  0                                        
SHEET    2  DA 2 PHE D  54  THR D  63 -1  O  GLU D  60   N  SER D  35           
SHEET    1  DB 5 ASP D  95  TYR D 101  0                                        
SHEET    2  DB 5 ILE D   2  SER D  10 -1  O  TYR D   5   N  LEU D  99           
SHEET    3  DB 5 PHE D  54  THR D  63 -1  O  LEU D  55   N  SER D  10           
SHEET    4  DB 5 TYR D  41  THR D  43 -1  O  TYR D  41   N  ASN D  56           
SHEET    5  DB 5 VAL D 154  ARG D 156 -1  O  LYS D 155   N  GLU D  42           
SHEET    1  DC 4 ASP D  95  TYR D 101  0                                        
SHEET    2  DC 4 ILE D   2  SER D  10 -1  O  TYR D   5   N  LEU D  99           
SHEET    3  DC 4 PHE D  54  THR D  63 -1  O  LEU D  55   N  SER D  10           
SHEET    4  DC 4 ILE D  32  ILE D  37 -1  O  SER D  33   N  GLN D  62           
SHEET    1  DD 2 ILE D 106  LEU D 108  0                                        
SHEET    2  DD 2 LEU D 111  VAL D 113 -1  O  LEU D 111   N  LEU D 108           
SHEET    1  DE 2 VAL D 136  GLU D 137  0                                        
SHEET    2  DE 2 LEU D 142  LYS D 143 -1  O  LEU D 142   N  GLU D 137           
SSBOND   1 CYS B   80    CYS D   80                          1555   2746  1.96  
LINK        MG    MG A 170                 O1A APC A1158     1555   1555  2.00  
LINK        MG    MG A 170                 O1B APC A1158     1555   1555  2.15  
LINK        MG    MG A 170                 O   HOH A2002     1555   1555  2.32  
LINK        MG    MG A 170                 OD1 ASP A  95     1555   1555  2.45  
LINK        MG    MG A 170                 OD1 ASP A  97     1555   1555  2.01  
LINK        MG    MG A 171                 O1B APC A1158     1555   1555  2.45  
LINK        MG    MG A 171                 O1G APC A1158     1555   1555  2.06  
LINK        MG    MG A 171                 OD2 ASP A  97     1555   1555  2.38  
LINK        MG    MG A 171                 OD2 ASP A  95     1555   1555  2.05  
LINK        MG    MG B 170                 O1AAAPC B1159     1555   1555  2.30  
LINK        MG    MG B 170                 O1ABAPC B1159     1555   1555  2.60  
LINK        MG    MG B 170                 OE2 GLU B  78     1555   1555  2.82  
LINK        MG    MG B 170                 O   HOH B2001     1555   1555  2.07  
LINK        MG    MG B 170                 OD1 ASP B  95     1555   1555  2.19  
LINK        MG    MG B 170                 OD1 ASP B  97     1555   1555  2.42  
LINK        MG    MG B 171                 OD2 ASP B  95     1555   1555  2.05  
LINK        MG    MG B 171                 O1BAAPC B1159     1555   1555  2.81  
LINK        MG    MG B 171                 O2BAAPC B1159     1555   1555  2.64  
LINK        MG    MG B 171                 O1BBAPC B1159     1555   1555  2.47  
LINK        MG    MG B 171                 OD2 ASP B  97     1555   1555  2.43  
LINK        MG    MG B 171                 O1GBAPC B1159     1555   1555  1.86  
LINK        MG    MG C 170                 O1B APC C1158     1555   1555  2.16  
LINK        MG    MG C 170                 O   HOH C2001     1555   1555  2.15  
LINK        MG    MG C 170                 O1A APC C1158     1555   1555  1.93  
LINK        MG    MG C 170                 OD1 ASP C  95     1555   1555  2.23  
LINK        MG    MG C 170                 O   HOH C2002     1555   1555  2.10  
LINK        MG    MG C 170                 OD1 ASP C  97     1555   1555  2.14  
LINK        MG    MG C 171                 O1G APC C1158     1555   1555  2.01  
LINK        MG    MG C 171                 O1B APC C1158     1555   1555  2.54  
LINK        MG    MG C 171                 OD2 ASP C  95     1555   1555  2.02  
LINK        MG    MG C 171                 OD2 ASP C  97     1555   1555  2.26  
LINK        MG    MG D 170                 O1BBAPC D1158     1555   1555  2.21  
LINK        MG    MG D 170                 OD1 ASP D  95     1555   1555  2.49  
LINK        MG    MG D 170                 OD1 ASP D  97     1555   1555  1.97  
LINK        MG    MG D 170                 O   HOH D2002     1555   1555  2.06  
LINK        MG    MG D 170                 O1ABAPC D1158     1555   1555  2.07  
LINK        MG    MG D 170                 O2BAAPC D1158     1555   1555  2.44  
LINK        MG    MG D 170                 O1AAAPC D1158     1555   1555  1.88  
LINK        MG    MG D 171                 O1GBAPC D1158     1555   1555  1.84  
LINK        MG    MG D 171                 O1BBAPC D1158     1555   1555  2.42  
LINK        MG    MG D 171                 O2BAAPC D1158     1555   1555  2.39  
LINK        MG    MG D 171                 OD2 ASP D  95     1555   1555  2.10  
LINK        MG    MG D 171                 OD2 ASP D  97     1555   1555  2.27  
LINK        MG    MG D 171                 O1BAAPC D1158     1555   1555  2.85  
CISPEP   1 VAL A  113    PRO A  114          0        -0.48                     
CISPEP   2 VAL B  113    PRO B  114          0        -1.87                     
CISPEP   3 VAL C  113    PRO C  114          0        -1.08                     
CISPEP   4 VAL D  113    PRO D  114          0        -1.86                     
SITE     1 AC1  4 ASP A  95  ASP A  97  APC A1158  HOH A2002                    
SITE     1 AC2  3 ASP A  95  ASP A  97  APC A1158                               
SITE     1 AC3  6 GLU B  78  ASP B  95  VAL B  96  ASP B  97                    
SITE     2 AC3  6 APC B1159  HOH B2001                                          
SITE     1 AC4  3 ASP B  95  ASP B  97  APC B1159                               
SITE     1 AC5  5 ASP C  95  ASP C  97  APC C1158  HOH C2001                    
SITE     2 AC5  5 HOH C2002                                                     
SITE     1 AC6  3 ASP C  95  ASP C  97  APC C1158                               
SITE     1 AC7  4 ASP D  95  ASP D  97  APC D1158  HOH D2002                    
SITE     1 AC8  3 ASP D  95  ASP D  97  APC D1158                               
SITE     1 AC9 14 ARG A  92  ASP A  95  ASP A  97  ILE A  98                    
SITE     2 AC9 14 LYS A 110  LEU A 111  SER A 112  HIS A 115                    
SITE     3 AC9 14 ARG A 117  ARG A 121   MG A 170   MG A 171                    
SITE     4 AC9 14 HOH A2002  HOH A2005                                          
SITE     1 BC1 11 GLN A   3  ARG B  92  ASP B  95  ASP B  97                    
SITE     2 BC1 11 ILE B  98  LYS B 110  LEU B 111  SER B 112                    
SITE     3 BC1 11  MG B 170   MG B 171  HOH B2001                               
SITE     1 BC2 14 LEU C  71  ARG C  92  ASP C  95  ASP C  97                    
SITE     2 BC2 14 ILE C  98  LYS C 110  LEU C 111  SER C 112                    
SITE     3 BC2 14 HIS C 115  ARG C 117  ARG C 121   MG C 170                    
SITE     4 BC2 14  MG C 171  HOH C2002                                          
SITE     1 BC3 11 GLN C   3  LEU D  71  ARG D  92  ASP D  95                    
SITE     2 BC3 11 ASP D  97  ILE D  98  LYS D 110  LEU D 111                    
SITE     3 BC3 11 SER D 112   MG D 170   MG D 171                               
SITE     1 BC4  4 ASN B  27  GLU B  28  TYR B  29  ASP B  30                    
SITE     1 BC5  5 ASN A  27  GLU A  28  TYR A  29  ASP A  30                    
SITE     2 BC5  5 ILE A  32                                                     
CRYST1   62.002   94.263   62.989  90.00 112.44  90.00 P 1 21 1      6          
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      0.016129  0.000000  0.006661        0.00000                         
SCALE2      0.000000  0.010609  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017176        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system