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Database: PDB
Entry: 3N8D
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HEADER    LIGASE                                  28-MAY-10   3N8D              
TITLE     CRYSTAL STRUCTURE OF STAPHYLOCOCCUS AUREUS VRSA-9 D-ALA:D-ALA LIGASE  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: D-ALANYLALANINE SYNTHETASE, D-ALA-D-ALA LIGASE;             
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 STRAIN: VRSA-9;                                                      
SOURCE   5 GENE: DDL;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYS;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A(+)                                 
KEYWDS    VANCOMYCIN DEPENDENCE, CELL WALL SYNTHESIS, D-ALA:D-ALA LIGASE,       
KEYWDS   2 LIGASE                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.A.SAUL,A.HAOUZ,D.MEZIANE-CHERIF                                     
REVDAT   1   13-OCT-10 3N8D    0                                                
JRNL        AUTH   D.MEZIANE-CHERIF,F.A.SAUL,C.MOUBARECK,P.WEBER,A.HAOUZ,       
JRNL        AUTH 2 P.COURVALIN,B.PERICHON                                       
JRNL        TITL   MOLECULAR BASIS OF VANCOMYCIN DEPENDENCE IN VANA-TYPE        
JRNL        TITL 2 STAPHYLOCOCCUS AUREUS VRSA-9.                                
JRNL        REF    J.BACTERIOL.                  V. 192  5465 2010              
JRNL        REFN                   ISSN 0021-9193                               
JRNL        PMID   20729361                                                     
JRNL        DOI    10.1128/JB.00613-10                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 28076                          
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) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1482                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 40                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.33                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 838                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.35                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2330                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 41                           
REMARK   3   BIN FREE R VALUE                    : 0.3230                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5283                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 73                                      
REMARK   3   SOLVENT ATOMS            : 272                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.83000                                             
REMARK   3    B22 (A**2) : 0.18000                                              
REMARK   3    B33 (A**2) : 0.65000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.292         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.205         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.298         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5451 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3631 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7383 ; 1.358 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8935 ; 0.863 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   654 ; 6.327 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   265 ;39.175 ;26.113       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   975 ;16.967 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;24.404 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   821 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5957 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   999 ; 0.001 ; 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):  3295 ; 0.714 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1335 ; 0.114 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5317 ; 1.351 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2156 ; 1.862 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2066 ; 3.171 ; 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   : 1.40                                          
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 3N8D COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059508.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97919                            
REMARK 200  MONOCHROMATOR                  : MIRROR                             
REMARK 200  OPTICS                         : SI (111) CHANNEL-CUT               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29619                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.640                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
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 2I87                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 80MM TRIS-HCL, PH   
REMARK 280  8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       42.18700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.89450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.63550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.89450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.18700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.63550            
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 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ASN A    69                                                      
REMARK 465     GLY A    70                                                      
REMARK 465     GLU A    71                                                      
REMARK 465     ALA A    72                                                      
REMARK 465     HIS A    96                                                      
REMARK 465     GLY A    97                                                      
REMARK 465     PRO A    98                                                      
REMARK 465     LYS A   241                                                      
REMARK 465     ASP A   242                                                      
REMARK 465     VAL A   243                                                      
REMARK 465     ALA A   244                                                      
REMARK 465     PHE A   245                                                      
REMARK 465     TYR A   246                                                      
REMARK 465     ASP A   247                                                      
REMARK 465     TYR A   248                                                      
REMARK 465     LYS A   249                                                      
REMARK 465     SER A   250                                                      
REMARK 465     LYS A   251                                                      
REMARK 465     TYR A   252                                                      
REMARK 465     LYS A   253                                                      
REMARK 465     ASP A   254                                                      
REMARK 465     GLY A   255                                                      
REMARK 465     LYS A   256                                                      
REMARK 465     LYS A   354                                                      
REMARK 465     ILE A   355                                                      
REMARK 465     ASP A   356                                                      
REMARK 465     LEU A   357                                                      
REMARK 465     GLU A   358                                                      
REMARK 465     HIS A   359                                                      
REMARK 465     HIS A   360                                                      
REMARK 465     HIS A   361                                                      
REMARK 465     HIS A   362                                                      
REMARK 465     HIS A   363                                                      
REMARK 465     HIS A   364                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASN B    69                                                      
REMARK 465     GLY B    70                                                      
REMARK 465     GLU B    71                                                      
REMARK 465     ALA B    72                                                      
REMARK 465     LEU B    73                                                      
REMARK 465     HIS B    96                                                      
REMARK 465     GLY B    97                                                      
REMARK 465     PRO B    98                                                      
REMARK 465     GLY B   182                                                      
REMARK 465     SER B   183                                                      
REMARK 465     SER B   184                                                      
REMARK 465     TYR B   246                                                      
REMARK 465     ASP B   247                                                      
REMARK 465     TYR B   248                                                      
REMARK 465     LYS B   249                                                      
REMARK 465     SER B   250                                                      
REMARK 465     LYS B   251                                                      
REMARK 465     TYR B   252                                                      
REMARK 465     LYS B   253                                                      
REMARK 465     ASP B   254                                                      
REMARK 465     GLY B   255                                                      
REMARK 465     LYS B   256                                                      
REMARK 465     VAL B   257                                                      
REMARK 465     HIS B   359                                                      
REMARK 465     HIS B   360                                                      
REMARK 465     HIS B   361                                                      
REMARK 465     HIS B   362                                                      
REMARK 465     HIS B   363                                                      
REMARK 465     HIS B   364                                                      
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     THR A   2    OG1  CG2                                            
REMARK 470     THR B   2    OG1  CG2                                            
REMARK 470     GLU B  74    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   496     O    HOH B   497              2.13            
REMARK 500   OE1  GLU B   306     O    HOH B   367              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU B 131   CA  -  CB  -  CG  ANGL. DEV. =  14.6 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    ASP A  32       95.37    -66.90                                   
REMARK 500    ASN A  54       56.92     71.03                                   
REMARK 500    GLU A 101       35.52    -74.87                                   
REMARK 500    ASP A 102        3.85   -155.75                                   
REMARK 500    SER A 183      162.74    165.21                                   
REMARK 500    ASN A 228      -88.99   -118.63                                   
REMARK 500    ALA B  90      146.55   -170.35                                   
REMARK 500    TYR B 158       46.72   -142.82                                   
REMARK 500    ASN B 228      -87.24   -111.06                                   
REMARK 500    ASP B 285       46.79     71.01                                   
REMARK 500    ASP B 299       32.11    -93.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2I87   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2I80   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2I8C   RELATED DB: PDB                                   
DBREF  3N8D A    1   356  UNP    Q5HEB7   DDL_STAAC        1    356             
DBREF  3N8D B    1   356  UNP    Q5HEB7   DDL_STAAC        1    356             
SEQADV 3N8D LYS A  260  UNP  Q5HEB7    GLN   260 VARIANT                        
SEQADV 3N8D GLU A  283  UNP  Q5HEB7    ALA   283 VARIANT                        
SEQADV 3N8D LEU A  357  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 3N8D GLU A  358  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 3N8D HIS A  359  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 3N8D HIS A  360  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 3N8D HIS A  361  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 3N8D HIS A  362  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 3N8D HIS A  363  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 3N8D HIS A  364  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 3N8D LYS B  260  UNP  Q5HEB7    GLN   260 VARIANT                        
SEQADV 3N8D GLU B  283  UNP  Q5HEB7    ALA   283 VARIANT                        
SEQADV 3N8D LEU B  357  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 3N8D GLU B  358  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 3N8D HIS B  359  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 3N8D HIS B  360  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 3N8D HIS B  361  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 3N8D HIS B  362  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 3N8D HIS B  363  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 3N8D HIS B  364  UNP  Q5HEB7              EXPRESSION TAG                 
SEQRES   1 A  364  MET THR LYS GLU ASN ILE CYS ILE VAL PHE GLY GLY LYS          
SEQRES   2 A  364  SER ALA GLU HIS GLU VAL SER ILE LEU THR ALA GLN ASN          
SEQRES   3 A  364  VAL LEU ASN ALA ILE ASP LYS ASP LYS TYR HIS VAL ASP          
SEQRES   4 A  364  ILE ILE TYR ILE THR ASN ASP GLY ASP TRP ARG LYS GLN          
SEQRES   5 A  364  ASN ASN ILE THR ALA GLU ILE LYS SER THR ASP GLU LEU          
SEQRES   6 A  364  HIS LEU GLU ASN GLY GLU ALA LEU GLU ILE SER GLN LEU          
SEQRES   7 A  364  LEU LYS GLU SER SER SER GLY GLN PRO TYR ASP ALA VAL          
SEQRES   8 A  364  PHE PRO LEU LEU HIS GLY PRO ASN GLY GLU ASP GLY THR          
SEQRES   9 A  364  ILE GLN GLY LEU PHE GLU VAL LEU ASP VAL PRO TYR VAL          
SEQRES  10 A  364  GLY ASN GLY VAL LEU SER ALA ALA SER SER MET ASP LYS          
SEQRES  11 A  364  LEU VAL MET LYS GLN LEU PHE GLU HIS ARG GLY LEU PRO          
SEQRES  12 A  364  GLN LEU PRO TYR ILE SER PHE LEU ARG SER GLU TYR GLU          
SEQRES  13 A  364  LYS TYR GLU HIS ASN ILE LEU LYS LEU VAL ASN ASP LYS          
SEQRES  14 A  364  LEU ASN TYR PRO VAL PHE VAL LYS PRO ALA ASN LEU GLY          
SEQRES  15 A  364  SER SER VAL GLY ILE SER LYS CYS ASN ASN GLU ALA GLU          
SEQRES  16 A  364  LEU LYS GLU GLY ILE LYS GLU ALA PHE GLN PHE ASP ARG          
SEQRES  17 A  364  LYS LEU VAL ILE GLU GLN GLY VAL ASN ALA ARG GLU ILE          
SEQRES  18 A  364  GLU VAL ALA VAL LEU GLY ASN ASP TYR PRO GLU ALA THR          
SEQRES  19 A  364  TRP PRO GLY GLU VAL VAL LYS ASP VAL ALA PHE TYR ASP          
SEQRES  20 A  364  TYR LYS SER LYS TYR LYS ASP GLY LYS VAL GLN LEU LYS          
SEQRES  21 A  364  ILE PRO ALA ASP LEU ASP GLU ASP VAL GLN LEU THR LEU          
SEQRES  22 A  364  ARG ASN MET ALA LEU GLU ALA PHE LYS GLU THR ASP CYS          
SEQRES  23 A  364  SER GLY LEU VAL ARG ALA ASP PHE PHE VAL THR GLU ASP          
SEQRES  24 A  364  ASN GLN ILE TYR ILE ASN GLU THR ASN ALA MET PRO GLY          
SEQRES  25 A  364  PHE THR ALA PHE SER MET TYR PRO LYS LEU TRP GLU ASN          
SEQRES  26 A  364  MET GLY LEU SER TYR PRO GLU LEU ILE THR LYS LEU ILE          
SEQRES  27 A  364  GLU LEU ALA LYS GLU ARG HIS GLN ASP LYS GLN LYS ASN          
SEQRES  28 A  364  LYS TYR LYS ILE ASP LEU GLU HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  364  MET THR LYS GLU ASN ILE CYS ILE VAL PHE GLY GLY LYS          
SEQRES   2 B  364  SER ALA GLU HIS GLU VAL SER ILE LEU THR ALA GLN ASN          
SEQRES   3 B  364  VAL LEU ASN ALA ILE ASP LYS ASP LYS TYR HIS VAL ASP          
SEQRES   4 B  364  ILE ILE TYR ILE THR ASN ASP GLY ASP TRP ARG LYS GLN          
SEQRES   5 B  364  ASN ASN ILE THR ALA GLU ILE LYS SER THR ASP GLU LEU          
SEQRES   6 B  364  HIS LEU GLU ASN GLY GLU ALA LEU GLU ILE SER GLN LEU          
SEQRES   7 B  364  LEU LYS GLU SER SER SER GLY GLN PRO TYR ASP ALA VAL          
SEQRES   8 B  364  PHE PRO LEU LEU HIS GLY PRO ASN GLY GLU ASP GLY THR          
SEQRES   9 B  364  ILE GLN GLY LEU PHE GLU VAL LEU ASP VAL PRO TYR VAL          
SEQRES  10 B  364  GLY ASN GLY VAL LEU SER ALA ALA SER SER MET ASP LYS          
SEQRES  11 B  364  LEU VAL MET LYS GLN LEU PHE GLU HIS ARG GLY LEU PRO          
SEQRES  12 B  364  GLN LEU PRO TYR ILE SER PHE LEU ARG SER GLU TYR GLU          
SEQRES  13 B  364  LYS TYR GLU HIS ASN ILE LEU LYS LEU VAL ASN ASP LYS          
SEQRES  14 B  364  LEU ASN TYR PRO VAL PHE VAL LYS PRO ALA ASN LEU GLY          
SEQRES  15 B  364  SER SER VAL GLY ILE SER LYS CYS ASN ASN GLU ALA GLU          
SEQRES  16 B  364  LEU LYS GLU GLY ILE LYS GLU ALA PHE GLN PHE ASP ARG          
SEQRES  17 B  364  LYS LEU VAL ILE GLU GLN GLY VAL ASN ALA ARG GLU ILE          
SEQRES  18 B  364  GLU VAL ALA VAL LEU GLY ASN ASP TYR PRO GLU ALA THR          
SEQRES  19 B  364  TRP PRO GLY GLU VAL VAL LYS ASP VAL ALA PHE TYR ASP          
SEQRES  20 B  364  TYR LYS SER LYS TYR LYS ASP GLY LYS VAL GLN LEU LYS          
SEQRES  21 B  364  ILE PRO ALA ASP LEU ASP GLU ASP VAL GLN LEU THR LEU          
SEQRES  22 B  364  ARG ASN MET ALA LEU GLU ALA PHE LYS GLU THR ASP CYS          
SEQRES  23 B  364  SER GLY LEU VAL ARG ALA ASP PHE PHE VAL THR GLU ASP          
SEQRES  24 B  364  ASN GLN ILE TYR ILE ASN GLU THR ASN ALA MET PRO GLY          
SEQRES  25 B  364  PHE THR ALA PHE SER MET TYR PRO LYS LEU TRP GLU ASN          
SEQRES  26 B  364  MET GLY LEU SER TYR PRO GLU LEU ILE THR LYS LEU ILE          
SEQRES  27 B  364  GLU LEU ALA LYS GLU ARG HIS GLN ASP LYS GLN LYS ASN          
SEQRES  28 B  364  LYS TYR LYS ILE ASP LEU GLU HIS HIS HIS HIS HIS HIS          
HET    ANP  A 400      31                                                       
HET    SO4  A 401       5                                                       
HET     CL  A 402       1                                                       
HET    ANP  B 400      31                                                       
HET    SO4  B 401       5                                                       
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3  ANP    2(C10 H17 N6 O12 P3)                                         
FORMUL   4  SO4    2(O4 S 2-)                                                   
FORMUL   5   CL    CL 1-                                                        
FORMUL   8  HOH   *272(H2 O)                                                    
HELIX    1   1 GLU A   16  ILE A   31  1                                  16    
HELIX    2   2 SER A   61  HIS A   66  1                                   6    
HELIX    3   3 GLU A   74  GLU A   81  1                                   8    
HELIX    4   4 GLY A  103  ASP A  113  1                                  11    
HELIX    5   5 GLY A  120  SER A  127  1                                   8    
HELIX    6   6 ASP A  129  GLY A  141  1                                  13    
HELIX    7   7 ARG A  152  LEU A  170  1                                  19    
HELIX    8   8 ASN A  192  PHE A  204  1                                  13    
HELIX    9   9 ASP A  266  THR A  284  1                                  19    
HELIX   10  10 SER A  317  ASN A  325  1                                   9    
HELIX   11  11 SER A  329  ASN A  351  1                                  23    
HELIX   12  12 GLU B   16  ASN B   29  1                                  14    
HELIX   13  13 SER B   61  HIS B   66  5                                   6    
HELIX   14  14 GLU B   74  LYS B   80  1                                   7    
HELIX   15  15 GLY B  103  LEU B  112  1                                  10    
HELIX   16  16 GLY B  120  ASP B  129  1                                  10    
HELIX   17  17 ASP B  129  GLY B  141  1                                  13    
HELIX   18  18 ARG B  152  LEU B  170  1                                  19    
HELIX   19  19 ASN B  192  ASP B  207  1                                  16    
HELIX   20  20 ASP B  266  THR B  284  1                                  19    
HELIX   21  21 SER B  317  ASN B  325  1                                   9    
HELIX   22  22 SER B  329  GLU B  358  1                                  30    
SHEET    1   A 4 TRP A  49  GLN A  52  0                                        
SHEET    2   A 4 TYR A  36  ILE A  43 -1  N  TYR A  42   O  ARG A  50           
SHEET    3   A 4 GLU A   4  GLY A  11  1  N  ILE A   8   O  ILE A  41           
SHEET    4   A 4 ALA A  90  PRO A  93  1  O  PHE A  92   N  CYS A   7           
SHEET    1   B 4 TYR A 147  LEU A 151  0                                        
SHEET    2   B 4 LYS A 209  GLN A 214 -1  O  ILE A 212   N  ILE A 148           
SHEET    3   B 4 VAL A 174  PRO A 178 -1  N  PHE A 175   O  GLU A 213           
SHEET    4   B 4 SER A 188  CYS A 190 -1  O  CYS A 190   N  VAL A 174           
SHEET    1   C 4 GLU A 232  ALA A 233  0                                        
SHEET    2   C 4 ARG A 219  GLY A 227 -1  N  LEU A 226   O  GLU A 232           
SHEET    3   C 4 GLY A 237  VAL A 239 -1  O  GLY A 237   N  GLU A 222           
SHEET    4   C 4 LEU A 259  LYS A 260 -1  O  LYS A 260   N  GLU A 238           
SHEET    1   D 4 GLU A 232  ALA A 233  0                                        
SHEET    2   D 4 ARG A 219  GLY A 227 -1  N  LEU A 226   O  GLU A 232           
SHEET    3   D 4 GLY A 288  VAL A 296 -1  O  PHE A 294   N  ILE A 221           
SHEET    4   D 4 ILE A 302  ASN A 308 -1  O  ASN A 305   N  ASP A 293           
SHEET    1   E 4 TRP B  49  GLN B  52  0                                        
SHEET    2   E 4 TYR B  36  ILE B  43 -1  N  TYR B  42   O  ARG B  50           
SHEET    3   E 4 GLU B   4  GLY B  11  1  N  GLU B   4   O  HIS B  37           
SHEET    4   E 4 ALA B  90  PRO B  93  1  O  PHE B  92   N  CYS B   7           
SHEET    1   F 4 TYR B 147  LEU B 151  0                                        
SHEET    2   F 4 LYS B 209  GLN B 214 -1  O  ILE B 212   N  ILE B 148           
SHEET    3   F 4 VAL B 174  PRO B 178 -1  N  LYS B 177   O  VAL B 211           
SHEET    4   F 4 SER B 188  CYS B 190 -1  O  CYS B 190   N  VAL B 174           
SHEET    1   G 4 GLU B 232  ALA B 233  0                                        
SHEET    2   G 4 ARG B 219  GLY B 227 -1  N  LEU B 226   O  GLU B 232           
SHEET    3   G 4 GLY B 237  VAL B 239 -1  O  GLY B 237   N  GLU B 222           
SHEET    4   G 4 LEU B 259  LYS B 260 -1  O  LYS B 260   N  GLU B 238           
SHEET    1   H 4 GLU B 232  ALA B 233  0                                        
SHEET    2   H 4 ARG B 219  GLY B 227 -1  N  LEU B 226   O  GLU B 232           
SHEET    3   H 4 GLY B 288  VAL B 296 -1  O  PHE B 294   N  ILE B 221           
SHEET    4   H 4 ILE B 302  ASN B 308 -1  O  GLU B 306   N  ASP B 293           
CISPEP   1 TYR A  172    PRO A  173          0        -2.21                     
CISPEP   2 ILE A  261    PRO A  262          0        -3.19                     
CISPEP   3 TYR B  172    PRO B  173          0         2.93                     
CISPEP   4 ILE B  261    PRO B  262          0        -2.53                     
SITE     1 AC1 17 LEU A 145  PHE A 175  LYS A 177  SER A 183                    
SITE     2 AC1 17 SER A 184  ILE A 187  GLU A 213  GLN A 214                    
SITE     3 AC1 17 GLY A 215  VAL A 216  GLU A 220  PHE A 295                    
SITE     4 AC1 17 ASN A 305  GLU A 306  HOH A 371  SO4 A 401                    
SITE     5 AC1 17 HOH A 418                                                     
SITE     1 AC2  6 ARG A 291  ASN A 308  PRO A 311  GLY A 312                    
SITE     2 AC2  6 HOH A 370  ANP A 400                                          
SITE     1 AC3  3 ASN A 228  ASP A 229  TYR A 230                               
SITE     1 AC4 12 LEU B 145  PHE B 175  LYS B 177  ILE B 187                    
SITE     2 AC4 12 GLU B 213  GLN B 214  GLY B 215  VAL B 216                    
SITE     3 AC4 12 GLU B 220  ASN B 305  GLU B 306  HOH B 367                    
SITE     1 AC5  6 ARG B 291  ASN B 308  PRO B 311  GLY B 312                    
SITE     2 AC5  6 HOH B 424  HOH B 496                                          
CRYST1   84.374   87.271   91.789  90.00  90.00  90.00 P 21 21 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      0.011852  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011459  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010895        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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