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Database: PDB
Entry: 3PY9
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Original site: 3PY9 
HEADER    TRANSFERASE                             12-DEC-10   3PY9              
TITLE     X-RAY STRUCTURAL STUDIES OF THE ENTIRE EXTRA-CELLULAR REGION OF THE   
TITLE    2 SER/THR KINASE PRKC FROM STAPHYLOCOCCUS AUREUS                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN KINASE;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRA-CELLULAR DOMAIN (UNP RESIDUES 378-664);              
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS MU50;       
SOURCE   3 ORGANISM_TAXID: 158878;                                              
SOURCE   4 STRAIN: MU50 / ATCC 700699;                                          
SOURCE   5 GENE: SAV1220;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PBAD24                                    
KEYWDS    PASTA, KINASE, MUROPEPTIDE BINDING, PHOSPHORYLATION, MEMBRANE,        
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.RUGGIERO,F.SQUEGLIA,D.MARASCO,R.MARCHETTI,A.MOLINARO,R.BERISIO      
REVDAT   2   30-MAR-11 3PY9    1       JRNL                                     
REVDAT   1   19-JAN-11 3PY9    0                                                
JRNL        AUTH   A.RUGGIERO,F.SQUEGLIA,D.MARASCO,R.MARCHETTI,A.MOLINARO,      
JRNL        AUTH 2 R.BERISIO                                                    
JRNL        TITL   X-RAY STRUCTURAL STUDIES OF THE ENTIRE EXTRACELLULAR REGION  
JRNL        TITL 2 OF THE SERINE/THREONINE KINASE PRKC FROM STAPHYLOCOCCUS      
JRNL        TITL 3 AUREUS.                                                      
JRNL        REF    BIOCHEM.J.                    V. 435    33 2011              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   21208192                                                     
JRNL        DOI    10.1042/BJ20101643                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 9.97                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 15327                          
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) : 0.247                           
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.293                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 829                             
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.25                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1031                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.80                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 63                           
REMARK   3   BIN FREE R VALUE                    : 0.3510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2180                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 124                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : -0.04000                                             
REMARK   3    B33 (A**2) : 0.03000                                              
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): 0.347         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.263         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.210         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.385         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.925                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2206 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2960 ; 1.286 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   277 ; 6.427 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    93 ;40.673 ;26.882       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   446 ;17.809 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     5 ;15.275 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   337 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1591 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1001 ; 0.235 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1491 ; 0.300 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   153 ; 0.200 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    42 ; 0.234 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.175 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1421 ; 0.762 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2258 ; 1.327 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   872 ; 1.702 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   702 ; 2.771 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 3PY9 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062960.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC BLUE CONFOCAL (RIGAKU)       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 92                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18045                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: AUTO-RICKSHAW                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5 MG/ML PROTEIN SOLUTION, 21% (W/V)      
REMARK 280  MPEG2000, 3% W/V D-(+)-GALACTOSE, 160 MM AMMONIUM SULFATE AND 60    
REMARK 280  MM SODIUM ACETATE TRIHYDRATE BUFFER, PH 4.6, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       27.84050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.55150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.84050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.55150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: MONOMER                                                      
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 EU    EU A 301  LIES ON A SPECIAL POSITION.                          
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     PHE A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     TYR A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ASN A   123                                                      
REMARK 465     ASP A   210                                                      
REMARK 465     SER A   211                                                      
REMARK 465     SER A   212                                                      
REMARK 465     ASP A   213                                                      
REMARK 465     ASP A   293                                                      
REMARK 465     ILE A   294                                                      
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     LYS A 215    CG   CD   CE   NZ                                   
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   NZ   LYS A   205     O    HOH A   385              2.17            
REMARK 500   N    GLU A     8     O    HOH A   416              2.18            
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    ASN A  45       43.46     75.21                                   
REMARK 500    LYS A 208        0.68    -53.46                                   
REMARK 500    ASP A 241     -154.15   -149.81                                   
REMARK 500    TYR A 291        5.09    -42.22                                   
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                              EU A 305  EU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  99   OD2                                                    
REMARK 620 2 ASP A 130   OD1 104.8                                              
REMARK 620 3 ASN A 132   OD1  82.4  76.5                                        
REMARK 620 4 ASP A  99   OD1  40.5 144.2 100.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              EU A 302  EU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  44   OE1                                                    
REMARK 620 2 GLU A  44   OE2  51.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              EU A 303  EU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 230   OD1                                                    
REMARK 620 2 ASP A 230   OD2  50.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              EU A 301  EU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A   8   OE1                                                    
REMARK 620 2 GLU A   8   OE2  45.3                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EU A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EU A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EU A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EU A 305                  
DBREF  3PY9 A    1   294  UNP    Q99UP8   Q99UP8_STAAM   371    664             
SEQRES   1 A  294  MET PHE GLY ASN LYS TYR GLU GLU THR PRO ASP VAL ILE          
SEQRES   2 A  294  GLY LYS SER VAL LYS GLU ALA GLU GLN ILE PHE ASN LYS          
SEQRES   3 A  294  ASN ASN LEU LYS LEU GLY LYS ILE SER ARG SER TYR SER          
SEQRES   4 A  294  ASP LYS TYR PRO GLU ASN GLU ILE ILE LYS THR THR PRO          
SEQRES   5 A  294  ASN THR GLY GLU ARG VAL GLU ARG GLY ASP SER VAL ASP          
SEQRES   6 A  294  VAL VAL ILE SER LYS GLY PRO GLU LYS VAL LYS MET PRO          
SEQRES   7 A  294  ASN VAL ILE GLY LEU PRO LYS GLU GLU ALA LEU GLN LYS          
SEQRES   8 A  294  LEU LYS SER LEU GLY LEU LYS ASP VAL THR ILE GLU LYS          
SEQRES   9 A  294  VAL TYR ASN ASN GLN ALA PRO LYS GLY TYR ILE ALA ASN          
SEQRES  10 A  294  GLN SER VAL THR ALA ASN THR GLU ILE ALA ILE HIS ASP          
SEQRES  11 A  294  SER ASN ILE LYS LEU TYR GLU SER LEU GLY ILE LYS GLN          
SEQRES  12 A  294  VAL TYR VAL GLU ASP PHE GLU HIS LYS SER PHE SER LYS          
SEQRES  13 A  294  ALA LYS LYS ALA LEU GLU GLU LYS GLY PHE LYS VAL GLU          
SEQRES  14 A  294  SER LYS GLU GLU TYR SER ASP ASP ILE ASP GLU GLY ASP          
SEQRES  15 A  294  VAL ILE SER GLN SER PRO LYS GLY LYS SER VAL ASP GLU          
SEQRES  16 A  294  GLY SER THR ILE SER PHE VAL VAL SER LYS GLY LYS LYS          
SEQRES  17 A  294  SER ASP SER SER ASP VAL LYS THR THR THR GLU SER VAL          
SEQRES  18 A  294  ASP VAL PRO TYR THR GLY LYS ASN ASP LYS SER GLN LYS          
SEQRES  19 A  294  VAL LYS VAL TYR ILE LYS ASP LYS ASP ASN ASP GLY SER          
SEQRES  20 A  294  THR GLU LYS GLY SER PHE ASP ILE THR SER ASP GLN ARG          
SEQRES  21 A  294  ILE ASP ILE PRO LEU ARG ILE GLU LYS GLY LYS THR ALA          
SEQRES  22 A  294  SER TYR ILE VAL LYS VAL ASP GLY LYS THR VAL ALA GLU          
SEQRES  23 A  294  LYS GLU VAL SER TYR ASP ASP ILE                              
HET     EU  A 301       1                                                       
HET     EU  A 302       1                                                       
HET     EU  A 303       1                                                       
HET     EU  A 305       1                                                       
HETNAM      EU EUROPIUM ION                                                     
FORMUL   2   EU    4(EU 2+)                                                     
FORMUL   6  HOH   *124(H2 O)                                                    
HELIX    1   1 SER A   16  ASN A   27  1                                  12    
HELIX    2   2 PRO A   84  SER A   94  1                                  11    
HELIX    3   3 SER A  153  GLU A  163  1                                  11    
SHEET    1   A 3 LYS A  30  SER A  37  0                                        
SHEET    2   A 3 SER A  63  SER A  69  1  O  ILE A  68   N  SER A  35           
SHEET    3   A 3 ILE A  47  THR A  51 -1  N  ILE A  48   O  VAL A  67           
SHEET    1   B 2 LYS A  74  LYS A  76  0                                        
SHEET    2   B 2 GLU A 125  ALA A 127 -1  O  ILE A 126   N  VAL A  75           
SHEET    1   C 3 VAL A 100  VAL A 105  0                                        
SHEET    2   C 3 ILE A 133  SER A 138  1  O  LEU A 135   N  THR A 101           
SHEET    3   C 3 ILE A 115  GLN A 118 -1  N  ALA A 116   O  TYR A 136           
SHEET    1   D 2 GLN A 143  VAL A 146  0                                        
SHEET    2   D 2 LYS A 191  ASP A 194 -1  O  LYS A 191   N  VAL A 146           
SHEET    1   E 3 LYS A 167  GLU A 173  0                                        
SHEET    2   E 3 THR A 198  SER A 204  1  O  ILE A 199   N  LYS A 167           
SHEET    3   E 3 VAL A 183  SER A 187 -1  N  SER A 187   O  SER A 200           
SHEET    1   F 2 THR A 217  VAL A 223  0                                        
SHEET    2   F 2 GLN A 259  LEU A 265 -1  O  ILE A 263   N  GLU A 219           
SHEET    1   G 3 ASN A 244  ASP A 245  0                                        
SHEET    2   G 3 GLN A 233  ASP A 241 -1  N  ASP A 241   O  ASN A 244           
SHEET    3   G 3 GLY A 251  ILE A 255 -1  O  PHE A 253   N  VAL A 235           
SHEET    1   H 4 ASN A 244  ASP A 245  0                                        
SHEET    2   H 4 GLN A 233  ASP A 241 -1  N  ASP A 241   O  ASN A 244           
SHEET    3   H 4 THR A 272  VAL A 279 -1  O  ILE A 276   N  TYR A 238           
SHEET    4   H 4 LYS A 282  SER A 290 -1  O  VAL A 289   N  ALA A 273           
LINK         OD2 ASP A  99                EU    EU A 305     1555   1555  2.42  
LINK         OD1 ASP A 130                EU    EU A 305     1555   1555  2.43  
LINK         OE1 GLU A  44                EU    EU A 302     1555   1555  2.51  
LINK         OD1 ASP A 230                EU    EU A 303     1555   1555  2.54  
LINK         OE2 GLU A  44                EU    EU A 302     1555   1555  2.58  
LINK         OD2 ASP A 230                EU    EU A 303     1555   1555  2.60  
LINK         OD1 ASN A 132                EU    EU A 305     1555   1555  2.63  
LINK         OE1 GLU A   8                EU    EU A 301     1555   1555  2.84  
LINK         OE2 GLU A   8                EU    EU A 301     1555   1555  2.89  
LINK         OD1 ASP A  99                EU    EU A 305     1555   1555  3.37  
CISPEP   1 THR A   51    PRO A   52          0        -3.71                     
CISPEP   2 SER A  187    PRO A  188          0        -9.74                     
SITE     1 AC1  1 GLU A   8                                                     
SITE     1 AC2  1 GLU A  44                                                     
SITE     1 AC3  1 ASP A 230                                                     
SITE     1 AC4  3 ASP A  99  ASP A 130  ASN A 132                               
CRYST1   55.681   69.103   88.430  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017959  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014471  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011308        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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