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Entry: 3M9G
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HEADER    TRANSFERASE                             22-MAR-10   3M9G              
TITLE     CRYSTAL STRUCTURE OF THE THREE-PASTA-DOMAIN OF A SER/THR KINASE FROM  
TITLE    2 STAPHYLOCOCCUS AUREUS                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN KINASE;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 376-576;                                          
COMPND   5 SYNONYM: SER/THR KINASE STK1;                                        
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 158879;                                              
SOURCE   4 STRAIN: N315;                                                        
SOURCE   5 GENE: SA1063;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    PASTA DOMAIN, SER/THR KINASE, STK1, STAPHYLOCOCCUS AUREUS,            
KEYWDS   2 EXTRACELLULAR DOMAIN, TRANSFERASE, ATP-BINDING, KINASE, NUCLEOTIDE-  
KEYWDS   3 BINDING, SERINE/THREONINE-PROTEIN KINASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.PARACUELLOS,A.BALLANDRAS,X.ROBERT,C.CREZE,A.J.COZZONE,B.DUCLOS,     
AUTHOR   2 P.GOUET                                                              
REVDAT   3   29-DEC-10 3M9G    1       JRNL                                     
REVDAT   2   10-NOV-10 3M9G    1       JRNL                                     
REVDAT   1   03-NOV-10 3M9G    0                                                
JRNL        AUTH   P.PARACUELLOS,A.BALLANDRAS,X.ROBERT,R.KAHN,M.HERVE,          
JRNL        AUTH 2 D.MENGIN-LECREULX,A.J.COZZONE,B.DUCLOS,P.GOUET               
JRNL        TITL   THE EXTENDED CONFORMATION OF THE 2.9-A CRYSTAL STRUCTURE OF  
JRNL        TITL 2 THE THREE-PASTA DOMAIN OF A SER/THR KINASE FROM THE HUMAN    
JRNL        TITL 3 PATHOGEN STAPHYLOCOCCUS AUREUS                               
JRNL        REF    J.MOL.BIOL.                   V. 404   847 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20965199                                                     
JRNL        DOI    10.1016/J.JMB.2010.10.012                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.PARACUELLOS,A.BALLANDRAS,X.ROBERT,A.J.COZZONE,B.DUCLOS,    
REMARK   1  AUTH 2 P.GOUET                                                      
REMARK   1  TITL   CRYSTALLIZATION AND INITIAL X-RAY DIFFRACTION STUDY OF THE   
REMARK   1  TITL 2 THREE PASTA DOMAINS OF THE SER/THR KINASE STK1 FROM THE      
REMARK   1  TITL 3 HUMAN PATHOGEN STAPHYLOCOCCUS AUREUS                         
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  65  1187 2009              
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   19923747                                                     
REMARK   1  DOI    10.1107/S174430910904250X                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.77                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 7151                           
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) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.305                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 795                             
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.97                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 522                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 58                           
REMARK   3   BIN FREE R VALUE                    : 0.4660                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1572                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7                                       
REMARK   3   SOLVENT ATOMS            : 65                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.48000                                             
REMARK   3    B22 (A**2) : -1.76000                                             
REMARK   3    B33 (A**2) : 4.24000                                              
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): 0.580         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.439         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.339         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.253        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.918                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.849                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1594 ; 0.024 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2142 ; 2.609 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   200 ;10.288 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    70 ;41.626 ;27.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   318 ;24.916 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     3 ;14.422 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   239 ; 0.142 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1170 ; 0.016 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  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   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3M9G COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-APR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB058275.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-NOV-08; 10-NOV-08               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 5.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : ESRF; ESRF                         
REMARK 200  BEAMLINE                       : ID14-4; BM30A                      
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.28200; 1.28253, 1.28314,         
REMARK 200                                   1.27557                            
REMARK 200  MONOCHROMATOR                  : SYNCHROTRON MIRRORS; SYNCHROTRON   
REMARK 200                                   MIRRORS                            
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R; ADSC QUANTUM    
REMARK 200                                   315R                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8017                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 6.990                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.7100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.43300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.080                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M IMIDAZOLE PH7.5, 0.8M ZN SULFATE    
REMARK 280  PH 5.23, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
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       37.37500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.37500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       45.93000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.60500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       45.93000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.60500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       37.37500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       45.93000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.60500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       37.37500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       45.93000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.60500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ILE A   393     ND2  ASN A   397              2.03            
REMARK 500   O    SER A   407     N    LYS A   440              2.10            
REMARK 500   O    GLU A   532     O    LYS A   534              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 422   C   -  N   -  CA  ANGL. DEV. = -10.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 377      138.21    155.57                                   
REMARK 500    LYS A 396        3.88    -50.05                                   
REMARK 500    ASN A 398      -24.29     86.43                                   
REMARK 500    LYS A 403       98.48     94.17                                   
REMARK 500    ASP A 410      -73.51    -37.08                                   
REMARK 500    GLU A 414      121.42    -37.92                                   
REMARK 500    ASN A 415      -17.97     96.28                                   
REMARK 500    ASN A 423      143.48    100.64                                   
REMARK 500    LYS A 440       63.87   -103.80                                   
REMARK 500    GLU A 443      113.71    -34.11                                   
REMARK 500    SER A 464       84.40    -64.89                                   
REMARK 500    LEU A 465      -18.17    160.89                                   
REMARK 500    ASN A 478       46.22   -106.57                                   
REMARK 500    GLN A 479      -61.07   -172.97                                   
REMARK 500    SER A 489      -81.29    -58.71                                   
REMARK 500    ILE A 498       -1.38    -41.69                                   
REMARK 500    ASP A 500       36.48     73.04                                   
REMARK 500    GLU A 520       98.25    -58.80                                   
REMARK 500    HIS A 521      108.78     91.42                                   
REMARK 500    LYS A 522      145.23    139.09                                   
REMARK 500    ALA A 530      -85.78    -64.29                                   
REMARK 500    LEU A 531      -48.99    -28.25                                   
REMARK 500    GLU A 532      -79.84    -67.13                                   
REMARK 500    GLU A 533      109.19    -35.26                                   
REMARK 500    LYS A 534     -178.58    105.21                                   
REMARK 500    ASP A 546       51.41   -109.50                                   
REMARK 500    ASP A 547       10.26   -160.70                                   
REMARK 500    GLU A 550       89.26    -39.38                                   
REMARK 500    ASP A 552     -153.80    -82.21                                   
REMARK 500    SER A 557      -75.55    -68.51                                   
REMARK 500    LYS A 559       97.13    -45.09                                   
REMARK 500    ASP A 564     -143.61   -157.30                                   
REMARK 500    GLU A 565     -139.50    -93.80                                   
REMARK 500    SER A 567     -160.46    -67.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER A  409     ASP A  410                  145.72                    
REMARK 500 THR A  421     PRO A  422                  143.60                    
REMARK 500 GLY A  535     PHE A  536                 -138.94                    
REMARK 500 LYS A  561     SER A  562                  137.19                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1012        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH A1020        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH A1023        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH A1026        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH A1027        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH A1030        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH A1032        DISTANCE =  7.81 ANGSTROMS                       
REMARK 525    HOH A1033        DISTANCE =  6.49 ANGSTROMS                       
REMARK 525    HOH A1036        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH A1039        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH A1041        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH A1046        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH A1047        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH A1055        DISTANCE =  7.19 ANGSTROMS                       
REMARK 525    HOH A1061        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH A1064        DISTANCE =  6.17 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2000  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 539   OE1                                                    
REMARK 620 2 HOH A1000   O   120.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 546   OD1                                                    
REMARK 620 2 HOH A1010   O   129.3                                              
REMARK 620 3 GLY A 576   OXT 114.2  80.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 432   OD2                                                    
REMARK 620 2 GLU A 429   OE1 116.3                                              
REMARK 620 3 HOH A1009   O    91.7  63.1                                        
REMARK 620 4 ASP A 432   OD1  52.8 129.4 144.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 543   OE2                                                    
REMARK 620 2 GLU A 543   OE1  60.7                                              
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 ZN A 2000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2006                 
DBREF  3M9G A  376   576  UNP    Q7A5Z8   Q7A5Z8_STAAN   376    576             
SEQRES   1 A  201  TYR GLU GLU THR PRO ASP VAL ILE GLY LYS SER VAL LYS          
SEQRES   2 A  201  GLU ALA GLU GLN ILE PHE ASN LYS ASN ASN LEU LYS LEU          
SEQRES   3 A  201  GLY LYS ILE SER ARG SER TYR SER ASP LYS TYR PRO GLU          
SEQRES   4 A  201  ASN GLU ILE ILE LYS THR THR PRO ASN THR GLY GLU ARG          
SEQRES   5 A  201  VAL GLU ARG GLY ASP SER VAL ASP VAL VAL ILE SER LYS          
SEQRES   6 A  201  GLY PRO GLU LYS VAL LYS MET PRO ASN VAL ILE GLY LEU          
SEQRES   7 A  201  PRO LYS GLU GLU ALA LEU GLN LYS LEU LYS SER LEU GLY          
SEQRES   8 A  201  LEU LYS ASP VAL THR ILE GLU LYS VAL TYR ASN ASN GLN          
SEQRES   9 A  201  ALA PRO LYS GLY TYR ILE ALA ASN GLN SER VAL THR ALA          
SEQRES  10 A  201  ASN THR GLU ILE ALA ILE HIS ASP SER ASN ILE LYS LEU          
SEQRES  11 A  201  TYR GLU SER LEU GLY ILE LYS GLN VAL TYR VAL GLU ASP          
SEQRES  12 A  201  PHE GLU HIS LYS SER PHE SER LYS ALA LYS LYS ALA LEU          
SEQRES  13 A  201  GLU GLU LYS GLY PHE LYS VAL GLU SER LYS GLU GLU TYR          
SEQRES  14 A  201  SER ASP ASP ILE ASP GLU GLY ASP VAL ILE SER GLN SER          
SEQRES  15 A  201  PRO LYS GLY LYS SER VAL ASP GLU GLY SER THR ILE SER          
SEQRES  16 A  201  PHE VAL VAL SER LYS GLY                                      
HET     ZN  A2000       1                                                       
HET     ZN  A2001       1                                                       
HET     ZN  A2002       1                                                       
HET     ZN  A2003       1                                                       
HET     ZN  A2004       1                                                       
HET     ZN  A2005       1                                                       
HET     ZN  A2006       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    7(ZN 2+)                                                     
FORMUL   9  HOH   *65(H2 O)                                                     
HELIX    1   1 SER A  386  LYS A  396  1                                  11    
HELIX    2   2 PRO A  454  SER A  464  1                                  11    
HELIX    3   3 SER A  523  GLU A  533  1                                  11    
SHEET    1   A 3 LYS A 400  SER A 407  0                                        
SHEET    2   A 3 SER A 433  SER A 439  1  O  ILE A 438   N  SER A 405           
SHEET    3   A 3 ILE A 417  THR A 420 -1  N  ILE A 418   O  VAL A 437           
SHEET    1   B 2 LYS A 444  LYS A 446  0                                        
SHEET    2   B 2 GLU A 495  ALA A 497 -1  O  ILE A 496   N  VAL A 445           
SHEET    1   C 3 VAL A 470  VAL A 475  0                                        
SHEET    2   C 3 ILE A 503  SER A 508  1  O  ILE A 503   N  THR A 471           
SHEET    3   C 3 ILE A 485  GLN A 488 -1  N  ALA A 486   O  TYR A 506           
SHEET    1   D 2 VAL A 514  TYR A 515  0                                        
SHEET    2   D 2 VAL A 563  ASP A 564 -1  O  ASP A 564   N  VAL A 514           
SHEET    1   E 3 LYS A 537  GLU A 543  0                                        
SHEET    2   E 3 THR A 568  SER A 574  1  O  ILE A 569   N  LYS A 537           
SHEET    3   E 3 VAL A 553  GLN A 556 -1  N  ILE A 554   O  VAL A 572           
LINK         OE1 GLU A 539                ZN    ZN A2000     1555   1555  1.81  
LINK         OD1 ASP A 546                ZN    ZN A2002     1555   1555  1.82  
LINK        ZN    ZN A2002                 O   HOH A1010     1555   1555  1.84  
LINK         OD2 ASP A 432                ZN    ZN A2001     1555   1555  1.95  
LINK         OE2 GLU A 543                ZN    ZN A2003     1555   1555  2.00  
LINK         NE2 HIS A 521                ZN    ZN A2006     1555   1555  2.04  
LINK         OE1 GLU A 429                ZN    ZN A2001     1555   1555  2.09  
LINK         OE1 GLU A 543                ZN    ZN A2003     1555   1555  2.27  
LINK        ZN    ZN A2004                 O   HOH A1011     1555   1555  2.33  
LINK        ZN    ZN A2001                 O   HOH A1009     1555   1555  2.50  
LINK         OXT GLY A 576                ZN    ZN A2002     1555   1555  2.57  
LINK         OD1 ASP A 432                ZN    ZN A2001     1555   1555  2.64  
LINK        ZN    ZN A2000                 O   HOH A1000     1555   1555  2.68  
SITE     1 AC1  3 GLU A 416  GLU A 539  HOH A1000                               
SITE     1 AC2  4 GLU A 429  ASP A 432  GLU A 457  HOH A1009                    
SITE     1 AC3  4 ASP A 469  ASP A 546  GLY A 576  HOH A1010                    
SITE     1 AC4  4 HIS A 499  ASP A 500  GLU A 543  ASP A 547                    
SITE     1 AC5  3 ASP A 552  HOH A1011  HOH A1065                               
SITE     1 AC6  1 ASP A 381                                                     
SITE     1 AC7  1 HIS A 521                                                     
CRYST1   91.860  101.210   74.750  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010886  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009880  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013378        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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