GenomeNet

Database: PDB
Entry: 2VPQ
LinkDB: 2VPQ
Original site: 2VPQ 
HEADER    LIGASE                                  03-MAR-08   2VPQ              
TITLE     CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM S. AUREUS                
TITLE    2 COMPLEXED WITH AMPPNP                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYL-COA CARBOXYLASE;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: BIOTIN CARBOXYLASE;                                         
COMPND   5 EC: 6.3.4.14;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BACTERIA, ATP-GRASP DOMAIN, BIOTIN CARBOXYLASE, LIGASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.MOCHALKIN                                                           
REVDAT   3   24-FEB-09 2VPQ    1       VERSN                                    
REVDAT   2   30-SEP-08 2VPQ    1       JRNL                                     
REVDAT   1   09-SEP-08 2VPQ    0                                                
JRNL        AUTH   I.MOCHALKIN,J.R.MILLER,A.EVDOKIMOV,S.LIGHTLE,C.YAN,          
JRNL        AUTH 2 C.K.STOVER,G.L.WALDROP                                       
JRNL        TITL   STRUCTURAL EVIDENCE FOR SUBSTRATE-INDUCED                    
JRNL        TITL 2 SYNERGISM AND HALF-SITES REACTIVITY IN BIOTIN                
JRNL        TITL 3 CARBOXYLASE.                                                 
JRNL        REF    PROTEIN SCI.                  V.  17  1706 2008              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   18725455                                                     
JRNL        DOI    10.1110/PS.035584.108                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.1  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 52269                          
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) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2810                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2822                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 161                          
REMARK   3   BIN FREE R VALUE                    : 0.3360                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6991                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 817                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.35000                                              
REMARK   3    B22 (A**2) : -1.68000                                             
REMARK   3    B33 (A**2) : 1.23000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.21000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.289         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.240         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.205         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.212        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.878                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7184 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  4887 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9719 ; 1.231 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11957 ; 0.885 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   899 ; 6.009 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   330 ;36.811 ;24.788       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1274 ;16.201 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;15.623 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1075 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7997 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1395 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1561 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5333 ; 0.192 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3508 ; 0.171 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3825 ; 0.084 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   617 ; 0.182 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    21 ; 0.204 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    36 ; 0.246 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.175 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5823 ; 0.608 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7179 ; 0.707 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3137 ; 1.181 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2538 ; 1.790 ; 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 : 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          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2VPQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  04-MAR-08.                 
REMARK 100 THE PDBE ID CODE IS EBI-35534.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-AUG-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55214                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.10                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY                : 3.2                                
REMARK 200  R MERGE                    (I) : 0.14                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.07                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.43                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.90                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP, REFMAC                                        
REMARK 200 STARTING MODEL: PDB ENTRY 1DV2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 45.96                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M KCL; 20% PEG3350                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       31.65900            
REMARK 290   SMTRY3   2  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 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 3020 ANGSTROM**2                          
REMARK 350 TOTAL SURFACE AREA FOR THE COMPLEX:  41230 ANGSTROM**2               
REMARK 350 GAIN IN SOLVENT FREE ENERGY: -16 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     ASP A   449                                                      
REMARK 465     GLU A   450                                                      
REMARK 465     GLY A   451                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B   450                                                      
REMARK 465     GLY B   451                                                      
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     ILE A 245    CG1  CG2  CD1                                       
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   OE1  GLN A    26  -  O    HOH A  2027              2.17            
REMARK 500   O    HOH A  2135  -  O    HOH A  2298              2.19            
REMARK 500   O    HOH A  2179  -  O    HOH A  2201              2.15            
REMARK 500   O    HOH B  2306  -  O    HOH A  2332              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500                                                                      
REMARK 500   O    HOH B  2027     O    HOH B  2172     1545      2.16           
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 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    SER A  58      -84.27   -119.56                                   
REMARK 500    PHE A  83     -100.43     55.60                                   
REMARK 500    MET A 234      -36.30     78.60                                   
REMARK 500    ASN A 269     -158.40     72.60                                   
REMARK 500    ASN A 375        2.99     80.50                                   
REMARK 500    TYR A 382      -51.18   -131.74                                   
REMARK 500    SER B  58      -80.66   -124.95                                   
REMARK 500    PHE B  83     -104.36     55.01                                   
REMARK 500    ARG B 233       68.74     22.02                                   
REMARK 500    MET B 234      -22.54     80.62                                   
REMARK 500    ASN B 266       58.70     39.80                                   
REMARK 500    ASN B 269     -157.68     74.99                                   
REMARK 500    ASN B 375        1.86     84.22                                   
REMARK 500    PRO B 380       33.79    -81.52                                   
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 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (ANP): ATP               
REMARK 600  ANALOG                                                              
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1450  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 274   OE2                                                    
REMARK 620 2 GLU A 274   OE1  57.3                                              
REMARK 620 3 ANP A1449   O1G 101.2 156.1                                        
REMARK 620 4 HOH A2417   O    85.4  97.6  90.1                                  
REMARK 620 5 ANP A1449   O2A 146.5  97.7 106.1  75.6                            
REMARK 620 6 GLU A 288   OE1 111.3  86.5  93.1 162.0  86.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1451  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP A1449   O2G                                                    
REMARK 620 2 HOH A2266   O    96.9                                              
REMARK 620 3 GLU A 288   OE1  88.3  93.0                                        
REMARK 620 4 GLU A 288   OE2 143.9  95.2  57.2                                  
REMARK 620 5 ANP A1449   O1B  83.5 175.1  92.0  87.2                            
REMARK 620 6 HOH A2172   O   114.5  80.0 156.7 101.0  95.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1451  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 288   OE1                                                    
REMARK 620 2 ANP B1450   O2A  85.7                                              
REMARK 620 3 GLU B 274   OE1  75.7 108.7                                        
REMARK 620 4 GLU B 274   OE2  98.6 155.2  50.1                                  
REMARK 620 5 ANP B1450   O3G  80.0 113.5 128.9  91.3                            
REMARK 620 6 HOH B2398   O   177.4  96.7 102.4  78.7 100.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1452  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 288   OE1                                                    
REMARK 620 2 GLU B 288   OE2  54.2                                              
REMARK 620 3 ANP B1450   O1B  90.0  84.0                                        
REMARK 620 4 HOH B2243   O    98.3  94.6 168.8                                  
REMARK 620 5 ANP B1450   O1G  88.4 142.2  91.1  96.7                            
REMARK 620 6 HOH B2155   O   157.5 103.3  87.7  81.7 114.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B1450                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A1449                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1451                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1450                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1452                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1451                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1452                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1453                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2C00   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  PSEUDOMONAS AERUGINOSA IN APO FORM                                  
REMARK 900 RELATED ID: 2J9G   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  E. COLI IN COMPLEX WITH AMPPNP AND ADP                              
REMARK 900 RELATED ID: 2VQD   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  PSEUDOMONAS AERUGINOSA COMPLEXED WITH AMPCP                         
REMARK 900 RELATED ID: 2VR1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  E. COLI IN COMPLEX WITH ATP ANALOG,                                 
REMARK 900  ADPCF2P.                                                            
DBREF  2VPQ A    1   451  UNP    Q99TW7   Q99TW7_STAAM     1    451             
DBREF  2VPQ B    1   451  UNP    Q99TW7   Q99TW7_STAAM     1    451             
SEQRES   1 A  451  MET LYS LYS VAL LEU ILE ALA ASN ARG GLY GLU ILE ALA          
SEQRES   2 A  451  VAL ARG ILE ILE ARG ALA CYS ARG ASP LEU GLY ILE GLN          
SEQRES   3 A  451  THR VAL ALA ILE TYR SER GLU GLY ASP LYS ASP ALA LEU          
SEQRES   4 A  451  HIS THR GLN ILE ALA ASP GLU ALA TYR CYS VAL GLY PRO          
SEQRES   5 A  451  THR LEU SER LYS ASP SER TYR LEU ASN ILE PRO ASN ILE          
SEQRES   6 A  451  LEU SER ILE ALA THR SER THR GLY CYS ASP GLY VAL HIS          
SEQRES   7 A  451  PRO GLY TYR GLY PHE LEU ALA GLU ASN ALA ASP PHE ALA          
SEQRES   8 A  451  GLU LEU CYS GLU ALA CYS GLN LEU LYS PHE ILE GLY PRO          
SEQRES   9 A  451  SER TYR GLN SER ILE GLN LYS MET GLY ILE LYS ASP VAL          
SEQRES  10 A  451  ALA LYS ALA GLU MET ILE LYS ALA ASN VAL PRO VAL VAL          
SEQRES  11 A  451  PRO GLY SER ASP GLY LEU MET LYS ASP VAL SER GLU ALA          
SEQRES  12 A  451  LYS LYS ILE ALA LYS LYS ILE GLY TYR PRO VAL ILE ILE          
SEQRES  13 A  451  LYS ALA THR ALA GLY GLY GLY GLY LYS GLY ILE ARG VAL          
SEQRES  14 A  451  ALA ARG ASP GLU LYS GLU LEU GLU THR GLY PHE ARG MET          
SEQRES  15 A  451  THR GLU GLN GLU ALA GLN THR ALA PHE GLY ASN GLY GLY          
SEQRES  16 A  451  LEU TYR MET GLU LYS PHE ILE GLU ASN PHE ARG HIS ILE          
SEQRES  17 A  451  GLU ILE GLN ILE VAL GLY ASP SER TYR GLY ASN VAL ILE          
SEQRES  18 A  451  HIS LEU GLY GLU ARG ASP CYS THR ILE GLN ARG ARG MET          
SEQRES  19 A  451  GLN LYS LEU VAL GLU GLU ALA PRO SER PRO ILE LEU ASP          
SEQRES  20 A  451  ASP GLU THR ARG ARG GLU MET GLY ASN ALA ALA VAL ARG          
SEQRES  21 A  451  ALA ALA LYS ALA VAL ASN TYR GLU ASN ALA GLY THR ILE          
SEQRES  22 A  451  GLU PHE ILE TYR ASP LEU ASN ASP ASN LYS PHE TYR PHE          
SEQRES  23 A  451  MET GLU MET ASN THR ARG ILE GLN VAL GLU HIS PRO VAL          
SEQRES  24 A  451  THR GLU MET VAL THR GLY ILE ASP LEU VAL LYS LEU GLN          
SEQRES  25 A  451  LEU GLN VAL ALA MET GLY ASP VAL LEU PRO TYR LYS GLN          
SEQRES  26 A  451  GLU ASP ILE LYS LEU THR GLY HIS ALA ILE GLU PHE ARG          
SEQRES  27 A  451  ILE ASN ALA GLU ASN PRO TYR LYS ASN PHE MET PRO SER          
SEQRES  28 A  451  PRO GLY LYS ILE GLU GLN TYR LEU ALA PRO GLY GLY TYR          
SEQRES  29 A  451  GLY VAL ARG ILE GLU SER ALA CYS TYR THR ASN TYR THR          
SEQRES  30 A  451  ILE PRO PRO TYR TYR ASP SER MET VAL ALA LYS LEU ILE          
SEQRES  31 A  451  ILE HIS GLU PRO THR ARG ASP GLU ALA ILE MET ALA GLY          
SEQRES  32 A  451  ILE ARG ALA LEU SER GLU PHE VAL VAL LEU GLY ILE ASP          
SEQRES  33 A  451  THR THR ILE PRO PHE HIS ILE LYS LEU LEU ASN ASN ASP          
SEQRES  34 A  451  ILE PHE ARG SER GLY LYS PHE ASN THR ASN PHE LEU GLU          
SEQRES  35 A  451  GLN ASN SER ILE MET ASN ASP GLU GLY                          
SEQRES   1 B  451  MET LYS LYS VAL LEU ILE ALA ASN ARG GLY GLU ILE ALA          
SEQRES   2 B  451  VAL ARG ILE ILE ARG ALA CYS ARG ASP LEU GLY ILE GLN          
SEQRES   3 B  451  THR VAL ALA ILE TYR SER GLU GLY ASP LYS ASP ALA LEU          
SEQRES   4 B  451  HIS THR GLN ILE ALA ASP GLU ALA TYR CYS VAL GLY PRO          
SEQRES   5 B  451  THR LEU SER LYS ASP SER TYR LEU ASN ILE PRO ASN ILE          
SEQRES   6 B  451  LEU SER ILE ALA THR SER THR GLY CYS ASP GLY VAL HIS          
SEQRES   7 B  451  PRO GLY TYR GLY PHE LEU ALA GLU ASN ALA ASP PHE ALA          
SEQRES   8 B  451  GLU LEU CYS GLU ALA CYS GLN LEU LYS PHE ILE GLY PRO          
SEQRES   9 B  451  SER TYR GLN SER ILE GLN LYS MET GLY ILE LYS ASP VAL          
SEQRES  10 B  451  ALA LYS ALA GLU MET ILE LYS ALA ASN VAL PRO VAL VAL          
SEQRES  11 B  451  PRO GLY SER ASP GLY LEU MET LYS ASP VAL SER GLU ALA          
SEQRES  12 B  451  LYS LYS ILE ALA LYS LYS ILE GLY TYR PRO VAL ILE ILE          
SEQRES  13 B  451  LYS ALA THR ALA GLY GLY GLY GLY LYS GLY ILE ARG VAL          
SEQRES  14 B  451  ALA ARG ASP GLU LYS GLU LEU GLU THR GLY PHE ARG MET          
SEQRES  15 B  451  THR GLU GLN GLU ALA GLN THR ALA PHE GLY ASN GLY GLY          
SEQRES  16 B  451  LEU TYR MET GLU LYS PHE ILE GLU ASN PHE ARG HIS ILE          
SEQRES  17 B  451  GLU ILE GLN ILE VAL GLY ASP SER TYR GLY ASN VAL ILE          
SEQRES  18 B  451  HIS LEU GLY GLU ARG ASP CYS THR ILE GLN ARG ARG MET          
SEQRES  19 B  451  GLN LYS LEU VAL GLU GLU ALA PRO SER PRO ILE LEU ASP          
SEQRES  20 B  451  ASP GLU THR ARG ARG GLU MET GLY ASN ALA ALA VAL ARG          
SEQRES  21 B  451  ALA ALA LYS ALA VAL ASN TYR GLU ASN ALA GLY THR ILE          
SEQRES  22 B  451  GLU PHE ILE TYR ASP LEU ASN ASP ASN LYS PHE TYR PHE          
SEQRES  23 B  451  MET GLU MET ASN THR ARG ILE GLN VAL GLU HIS PRO VAL          
SEQRES  24 B  451  THR GLU MET VAL THR GLY ILE ASP LEU VAL LYS LEU GLN          
SEQRES  25 B  451  LEU GLN VAL ALA MET GLY ASP VAL LEU PRO TYR LYS GLN          
SEQRES  26 B  451  GLU ASP ILE LYS LEU THR GLY HIS ALA ILE GLU PHE ARG          
SEQRES  27 B  451  ILE ASN ALA GLU ASN PRO TYR LYS ASN PHE MET PRO SER          
SEQRES  28 B  451  PRO GLY LYS ILE GLU GLN TYR LEU ALA PRO GLY GLY TYR          
SEQRES  29 B  451  GLY VAL ARG ILE GLU SER ALA CYS TYR THR ASN TYR THR          
SEQRES  30 B  451  ILE PRO PRO TYR TYR ASP SER MET VAL ALA LYS LEU ILE          
SEQRES  31 B  451  ILE HIS GLU PRO THR ARG ASP GLU ALA ILE MET ALA GLY          
SEQRES  32 B  451  ILE ARG ALA LEU SER GLU PHE VAL VAL LEU GLY ILE ASP          
SEQRES  33 B  451  THR THR ILE PRO PHE HIS ILE LYS LEU LEU ASN ASN ASP          
SEQRES  34 B  451  ILE PHE ARG SER GLY LYS PHE ASN THR ASN PHE LEU GLU          
SEQRES  35 B  451  GLN ASN SER ILE MET ASN ASP GLU GLY                          
HET    ANP  B1450      31                                                       
HET    ANP  A1449      31                                                       
HET     MG  B1451       1                                                       
HET     MG  A1450       1                                                       
HET     MG  B1452       1                                                       
HET     MG  A1451       1                                                       
HET     CL  A1452       1                                                       
HET     CL  B1453       1                                                       
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3  ANP    2(C10 H17 N6 O12 P3)                                         
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   5   MG    4(MG 2+)                                                     
FORMUL   6  HOH   *817(H2 O1)                                                   
HELIX    1   1 ARG A    9  LEU A   23  1                                  15    
HELIX    2   2 GLY A   34  LYS A   36  5                                   3    
HELIX    3   3 ALA A   38  ALA A   44  1                                   7    
HELIX    4   4 LEU A   54  SER A   58  5                                   5    
HELIX    5   5 ASN A   61  THR A   72  1                                  12    
HELIX    6   6 ASN A   87  ALA A   96  1                                  10    
HELIX    7   7 SER A  105  ILE A  114  1                                  10    
HELIX    8   8 ILE A  114  ALA A  125  1                                  12    
HELIX    9   9 ASP A  139  GLY A  151  1                                  13    
HELIX   10  10 ASP A  172  GLY A  192  1                                  21    
HELIX   11  11 ASP A  247  VAL A  265  1                                  19    
HELIX   12  12 GLU A  296  GLY A  305  1                                  10    
HELIX   13  13 ASP A  307  MET A  317  1                                  11    
HELIX   14  14 LYS A  324  ILE A  328  5                                   5    
HELIX   15  15 ASN A  343  ASN A  347  5                                   5    
HELIX   16  16 THR A  395  GLU A  409  1                                  15    
HELIX   17  17 THR A  418  ASN A  427  1                                  10    
HELIX   18  18 ASN A  428  GLY A  434  1                                   7    
HELIX   19  19 ARG B    9  LEU B   23  1                                  15    
HELIX   20  20 GLY B   34  LYS B   36  5                                   3    
HELIX   21  21 ALA B   38  ALA B   44  1                                   7    
HELIX   22  22 LEU B   54  SER B   58  5                                   5    
HELIX   23  23 ASN B   61  THR B   72  1                                  12    
HELIX   24  24 ASN B   87  CYS B   97  1                                  11    
HELIX   25  25 SER B  105  ILE B  114  1                                  10    
HELIX   26  26 ILE B  114  ALA B  125  1                                  12    
HELIX   27  27 ASP B  139  GLY B  151  1                                  13    
HELIX   28  28 ASP B  172  GLY B  192  1                                  21    
HELIX   29  29 ASP B  247  VAL B  265  1                                  19    
HELIX   30  30 GLU B  296  GLY B  305  1                                  10    
HELIX   31  31 ASP B  307  MET B  317  1                                  11    
HELIX   32  32 LYS B  324  ILE B  328  5                                   5    
HELIX   33  33 ASN B  343  ASN B  347  5                                   5    
HELIX   34  34 THR B  395  PHE B  410  1                                  16    
HELIX   35  35 THR B  418  ASN B  427  1                                  10    
HELIX   36  36 ASN B  428  GLY B  434  1                                   7    
HELIX   37  37 ASN B  439  ASN B  444  1                                   6    
HELIX   38  38 SER B  445  ASP B  449  5                                   5    
SHEET    1  AA 5 GLU A  46  GLY A  51  0                                        
SHEET    2  AA 5 GLN A  26  SER A  32  1  O  THR A  27   N  GLU A  46           
SHEET    3  AA 5 LYS A   3  ILE A   6  1  O  VAL A   4   N  VAL A  28           
SHEET    4  AA 5 GLY A  76  HIS A  78  1  O  GLY A  76   N  LEU A   5           
SHEET    5  AA 5 LYS A 100  PHE A 101  1  O  LYS A 100   N  VAL A  77           
SHEET    1  AB 3 ILE A 167  ALA A 170  0                                        
SHEET    2  AB 3 VAL A 154  ALA A 158 -1  O  VAL A 154   N  ALA A 170           
SHEET    3  AB 3 LEU A 196  LYS A 200 -1  O  TYR A 197   N  LYS A 157           
SHEET    1  AC 8 PHE A 284  ASN A 290  0                                        
SHEET    2  AC 8 ASN A 269  ASP A 278 -1  O  THR A 272   N  ASN A 290           
SHEET    3  AC 8 PHE A 205  GLY A 214 -1  O  ARG A 206   N  TYR A 277           
SHEET    4  AC 8 VAL A 220  ARG A 232 -1  O  ILE A 221   N  VAL A 213           
SHEET    5  AC 8 GLN A 235  ALA A 241 -1  O  GLN A 235   N  ARG A 232           
SHEET    6  AC 8 HIS A 333  ASN A 340 -1  O  ALA A 334   N  ALA A 241           
SHEET    7  AC 8 MET A 385  GLU A 393 -1  N  VAL A 386   O  ILE A 339           
SHEET    8  AC 8 VAL A 366  GLU A 369 -1  O  ARG A 367   N  ILE A 390           
SHEET    1  AD 2 GLN A 357  LEU A 359  0                                        
SHEET    2  AD 2 VAL A 411  LEU A 413 -1  O  VAL A 411   N  LEU A 359           
SHEET    1  BA 5 GLU B  46  GLY B  51  0                                        
SHEET    2  BA 5 GLN B  26  SER B  32  1  O  THR B  27   N  GLU B  46           
SHEET    3  BA 5 LYS B   3  ILE B   6  1  O  VAL B   4   N  VAL B  28           
SHEET    4  BA 5 GLY B  76  HIS B  78  1  O  GLY B  76   N  LEU B   5           
SHEET    5  BA 5 LYS B 100  PHE B 101  1  O  LYS B 100   N  VAL B  77           
SHEET    1  BB 3 ILE B 167  ALA B 170  0                                        
SHEET    2  BB 3 VAL B 154  ALA B 158 -1  O  VAL B 154   N  ALA B 170           
SHEET    3  BB 3 LEU B 196  LYS B 200 -1  O  TYR B 197   N  LYS B 157           
SHEET    1  BC 8 LYS B 283  ASN B 290  0                                        
SHEET    2  BC 8 ASN B 269  ASP B 278 -1  O  THR B 272   N  ASN B 290           
SHEET    3  BC 8 PHE B 205  GLY B 214 -1  O  ARG B 206   N  TYR B 277           
SHEET    4  BC 8 VAL B 220  ARG B 232 -1  O  ILE B 221   N  VAL B 213           
SHEET    5  BC 8 GLN B 235  ALA B 241 -1  O  GLN B 235   N  ARG B 232           
SHEET    6  BC 8 HIS B 333  ASN B 340 -1  O  ALA B 334   N  ALA B 241           
SHEET    7  BC 8 MET B 385  GLU B 393 -1  N  VAL B 386   O  ILE B 339           
SHEET    8  BC 8 VAL B 366  SER B 370 -1  O  ARG B 367   N  ILE B 390           
SHEET    1  BD 2 GLN B 357  LEU B 359  0                                        
SHEET    2  BD 2 VAL B 411  LEU B 413 -1  O  VAL B 411   N  LEU B 359           
LINK         O2G ANP A1449                MG    MG A1451     1555   1555  1.76  
LINK        MG    MG A1450                 OE2 GLU A 274     1555   1555  2.46  
LINK        MG    MG A1450                 OE1 GLU A 274     1555   1555  2.04  
LINK        MG    MG A1450                 O1G ANP A1449     1555   1555  1.95  
LINK        MG    MG A1450                 O   HOH A2417     1555   1555  2.23  
LINK        MG    MG A1450                 O2A ANP A1449     1555   1555  2.14  
LINK        MG    MG A1450                 OE1 GLU A 288     1555   1555  2.40  
LINK        MG    MG A1451                 O   HOH A2266     1555   1555  1.93  
LINK        MG    MG A1451                 OE1 GLU A 288     1555   1555  2.24  
LINK        MG    MG A1451                 OE2 GLU A 288     1555   1555  2.27  
LINK        MG    MG A1451                 O1B ANP A1449     1555   1555  2.06  
LINK        MG    MG A1451                 O   HOH A2172     1555   1555  2.00  
LINK         O1G ANP B1450                MG    MG B1452     1555   1555  1.75  
LINK        MG    MG B1451                 O2A ANP B1450     1555   1555  1.94  
LINK        MG    MG B1451                 OE1 GLU B 274     1555   1555  1.98  
LINK        MG    MG B1451                 OE2 GLU B 274     1555   1555  2.84  
LINK        MG    MG B1451                 O3G ANP B1450     1555   1555  1.91  
LINK        MG    MG B1451                 O   HOH B2398     1555   1555  2.04  
LINK        MG    MG B1451                 OE1 GLU B 288     1555   1555  2.57  
LINK        MG    MG B1452                 OE2 GLU B 288     1555   1555  2.39  
LINK        MG    MG B1452                 O1B ANP B1450     1555   1555  1.90  
LINK        MG    MG B1452                 O   HOH B2243     1555   1555  1.83  
LINK        MG    MG B1452                 O   HOH B2155     1555   1555  2.15  
LINK        MG    MG B1452                 OE1 GLU B 288     1555   1555  2.37  
CISPEP   1 TYR A  152    PRO A  153          0         5.95                     
CISPEP   2 ALA A  241    PRO A  242          0       -12.33                     
CISPEP   3 TYR B  152    PRO B  153          0         3.04                     
CISPEP   4 ALA B  241    PRO B  242          0        -8.78                     
SITE     1 AC1 28 LYS B 115  ILE B 155  LYS B 157  GLY B 161                    
SITE     2 AC1 28 GLY B 162  GLY B 163  GLY B 164  ILE B 167                    
SITE     3 AC1 28 GLU B 199  LYS B 200  PHE B 201  ILE B 202                    
SITE     4 AC1 28 HIS B 207  GLN B 231  MET B 234  GLU B 274                    
SITE     5 AC1 28 ILE B 276  MET B 287  GLU B 288  ASN B 290                    
SITE     6 AC1 28  MG B1451   MG B1452  HOH B2155  HOH B2243                    
SITE     7 AC1 28 HOH B2393  HOH B2394  HOH B2397  HOH B2398                    
SITE     1 AC2 26 LYS A 115  ILE A 155  LYS A 157  GLY A 161                    
SITE     2 AC2 26 GLY A 162  GLY A 163  GLY A 164  ILE A 167                    
SITE     3 AC2 26 GLU A 199  LYS A 200  PHE A 201  ILE A 202                    
SITE     4 AC2 26 HIS A 207  GLN A 231  GLU A 274  ILE A 276                    
SITE     5 AC2 26 MET A 287  GLU A 288  ASN A 290   MG A1450                    
SITE     6 AC2 26  MG A1451  HOH A2172  HOH A2180  HOH A2266                    
SITE     7 AC2 26 HOH A2416  HOH A2417                                          
SITE     1 AC3  4 GLU B 274  GLU B 288  ANP B1450  HOH B2398                    
SITE     1 AC4  4 GLU A 274  GLU A 288  ANP A1449  HOH A2417                    
SITE     1 AC5  5 GLU B 288  ASN B 290  ANP B1450  HOH B2155                    
SITE     2 AC5  5 HOH B2243                                                     
SITE     1 AC6  5 GLU A 288  ASN A 290  ANP A1449  HOH A2172                    
SITE     2 AC6  5 HOH A2266                                                     
SITE     1 AC7  4 ARG A 292  GLN A 294  VAL A 295  HOH A2270                    
SITE     1 AC8  4 ARG B 292  GLN B 294  VAL B 295  HOH B2247                    
CRYST1   78.247   63.318  105.142  90.00 103.82  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012780  0.000000  0.003144        0.00000                         
SCALE2      0.000000  0.015793  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009794        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system