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Database: PDB
Entry: 2VR1
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HEADER    LIGASE                                  24-MAR-08   2VR1              
TITLE     CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM E. COLI IN COMPLEX WITH  
TITLE    2 ATP ANALOG, ADPCF2P.                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIOTIN CARBOXYLASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ACETYL-COA CARBOXYLASE SUBUNIT A, ACC;                      
COMPND   5 EC: 6.3.4.14;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NUCLEOTIDE-BINDING, FATTY ACID BIOSYNTHESIS, LIPID SYNTHESIS, BIOTIN  
KEYWDS   2 CARBOXYLASE, FAS, LIGASE, BIOTIN, BACTERIAL, ATP-BINDING             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.MOCHALKIN,G.L.WALDROP                                               
REVDAT   5   05-JUL-17 2VR1    1       REMARK                                   
REVDAT   4   13-JUL-11 2VR1    1       VERSN                                    
REVDAT   3   24-FEB-09 2VR1    1       VERSN                                    
REVDAT   2   30-SEP-08 2VR1    1       JRNL                                     
REVDAT   1   09-SEP-08 2VR1    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 SYNERGISM AND      
JRNL        TITL 2 HALF-SITES REACTIVITY IN BIOTIN 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.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 31155                          
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) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1668                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2192                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 113                          
REMARK   3   BIN FREE R VALUE                    : 0.3120                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6755                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 233                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.83                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.96000                                             
REMARK   3    B22 (A**2) : 2.37000                                              
REMARK   3    B33 (A**2) : -1.41000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.773         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.316         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.222         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.689        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6916 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  6429 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9345 ; 1.111 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14930 ; 0.741 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   869 ; 5.334 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   311 ;34.653 ;23.666       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1210 ;15.294 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    57 ;17.388 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1034 ; 0.062 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7698 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1371 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1376 ; 0.190 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  6345 ; 0.172 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3338 ; 0.172 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  4237 ; 0.078 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   198 ; 0.138 ; 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):    14 ; 0.122 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    48 ; 0.163 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.074 ; 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):  5645 ; 0.509 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6960 ; 0.565 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2950 ; 0.895 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2385 ; 1.391 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   446                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.9183 -19.8802  24.6910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0601 T22:  -0.0589                                     
REMARK   3      T33:  -0.0517 T12:   0.0257                                     
REMARK   3      T13:  -0.0252 T23:  -0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6214 L22:   0.8974                                     
REMARK   3      L33:   0.6875 L12:   0.2496                                     
REMARK   3      L13:  -0.0361 L23:   0.0477                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0005 S12:  -0.0151 S13:  -0.0174                       
REMARK   3      S21:  -0.0526 S22:   0.0309 S23:   0.1155                       
REMARK   3      S31:   0.0183 S32:  -0.0295 S33:  -0.0315                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   446                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.5416  -0.2838  54.2956              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1146 T22:  -0.0445                                     
REMARK   3      T33:  -0.0781 T12:  -0.0155                                     
REMARK   3      T13:  -0.0305 T23:  -0.0265                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9808 L22:   1.4167                                     
REMARK   3      L33:   1.5044 L12:  -0.4924                                     
REMARK   3      L13:  -0.5248 L23:  -0.2259                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0744 S12:  -0.1839 S13:   0.0078                       
REMARK   3      S21:   0.1097 S22:   0.0484 S23:  -0.1584                       
REMARK   3      S31:   0.0379 S32:   0.2645 S33:   0.0259                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1448        A  1448                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1463 -23.1358  22.8207              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0036 T22:  -0.0012                                     
REMARK   3      T33:   0.0003 T12:  -0.0027                                     
REMARK   3      T13:  -0.0039 T23:   0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11: 100.9683 L22:  71.1864                                     
REMARK   3      L33:   8.8711 L12:  36.7914                                     
REMARK   3      L13:  28.5307 L23:  17.2336                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1068 S12:   0.5356 S13:   1.1290                       
REMARK   3      S21:  -2.9986 S22:  -0.9962 S23:  -4.3198                       
REMARK   3      S31:  -3.2194 S32:   0.1932 S33:   1.1030                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 2VR1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290035767.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAY-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SCALEPACK                          
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32843                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.8300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1DV2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M KCL, 3-8% PEG 8000                  
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       42.06450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.95500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.39200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.95500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.06450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.39200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   164                                                      
REMARK 465     GLY A   165                                                      
REMARK 465     GLN A   447                                                      
REMARK 465     GLU A   448                                                      
REMARK 465     LYS A   449                                                      
REMARK 465     GLY B   162                                                      
REMARK 465     GLY B   163                                                      
REMARK 465     GLY B   164                                                      
REMARK 465     GLY B   165                                                      
REMARK 465     GLY B   166                                                      
REMARK 465     ARG B   167                                                      
REMARK 465     GLY B   168                                                      
REMARK 465     MET B   169                                                      
REMARK 465     LYS B   190                                                      
REMARK 465     ALA B   191                                                      
REMARK 465     ALA B   192                                                      
REMARK 465     PHE B   193                                                      
REMARK 465     SER B   194                                                      
REMARK 465     ASN B   195                                                      
REMARK 465     ASP B   196                                                      
REMARK 465     MET B   197                                                      
REMARK 465     GLN B   447                                                      
REMARK 465     GLU B   448                                                      
REMARK 465     LYS B   449                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A   9     -172.48   -175.34                                   
REMARK 500    SER A  59      -87.58   -123.76                                   
REMARK 500    PHE A  84     -119.73     32.90                                   
REMARK 500    ARG A 167      -65.13   -158.94                                   
REMARK 500    SER A 194       -2.94     59.48                                   
REMARK 500    LEU A 225       59.44   -117.43                                   
REMARK 500    ALA A 226     -161.75     62.24                                   
REMARK 500    PRO A 244     -179.57    -69.39                                   
REMARK 500    ILE A 287      -30.01   -130.94                                   
REMARK 500    ASN B   9     -170.32   -174.72                                   
REMARK 500    SER B  59      -86.29   -139.62                                   
REMARK 500    PHE B  84     -108.05     46.34                                   
REMARK 500    ASP B 135       65.85     60.79                                   
REMARK 500    ASP B 141      120.81    -39.80                                   
REMARK 500    ARG B 173       37.57   -147.21                                   
REMARK 500    GLN B 180       49.28    -79.38                                   
REMARK 500    SER B 181      -45.40   -139.49                                   
REMARK 500    ALA B 226     -157.83     55.85                                   
REMARK 500    ILE B 287      -68.10   -100.54                                   
REMARK 500    TYR B 381     -168.37   -115.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B2009        DISTANCE =  6.16 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1447                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1447                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATF A1448                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DV1   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF BIOTIN CARBOXYLASE (APO)                                
REMARK 900 RELATED ID: 1BNC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2GPS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE BIOTIN CARBOXYLASE SUBUNIT, E23RMUTANT, OF  
REMARK 900 ACETYL-COA CARBOXYLASE FROM ESCHERICHIA COLI.                        
REMARK 900 RELATED ID: 2GPW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE BIOTIN CARBOXYLASE SUBUNIT, F363AMUTANT,    
REMARK 900 OF ACETYL-COA CARBOXYLASE FROM ESCHERICHIA COLI.                     
REMARK 900 RELATED ID: 1K69   RELATED DB: PDB                                   
REMARK 900 MODEL INTERACTION BETWEEN BCCP AND ATP-BOUND CARBOXYLASESUBUNIT OF   
REMARK 900 ACETYL COA CARBOXYLASE                                               
REMARK 900 RELATED ID: 1DV2   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF BIOTIN CARBOXYLASE, MUTANT E288K, COMPLEXED WITH    
REMARK 900 ATP                                                                  
REMARK 900 RELATED ID: 2J9G   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM E. COLI IN COMPLEX      
REMARK 900 WITH AMPPNP AND ADP                                                  
REMARK 900 RELATED ID: 2C00   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM PSEUDOMONAS AERUGINOSA  
REMARK 900 IN APO FORM                                                          
REMARK 900 RELATED ID: 2VPQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM S. AUREUS COMPLEXED     
REMARK 900 WITH AMPPNP                                                          
REMARK 900 RELATED ID: 2VQD   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM PSEUDOMONAS AERUGINOSA  
REMARK 900 COMPLEXED WITH AMPCP                                                 
DBREF  2VR1 A    1   449  UNP    P24182   ACCC_ECOLI       1    449             
DBREF  2VR1 B    1   449  UNP    P24182   ACCC_ECOLI       1    449             
SEQRES   1 A  449  MET LEU ASP LYS ILE VAL ILE ALA ASN ARG GLY GLU ILE          
SEQRES   2 A  449  ALA LEU ARG ILE LEU ARG ALA CYS LYS GLU LEU GLY ILE          
SEQRES   3 A  449  LYS THR VAL ALA VAL HIS SER SER ALA ASP ARG ASP LEU          
SEQRES   4 A  449  LYS HIS VAL LEU LEU ALA ASP GLU THR VAL CYS ILE GLY          
SEQRES   5 A  449  PRO ALA PRO SER VAL LYS SER TYR LEU ASN ILE PRO ALA          
SEQRES   6 A  449  ILE ILE SER ALA ALA GLU ILE THR GLY ALA VAL ALA ILE          
SEQRES   7 A  449  HIS PRO GLY TYR GLY PHE LEU SER GLU ASN ALA ASN PHE          
SEQRES   8 A  449  ALA GLU GLN VAL GLU ARG SER GLY PHE ILE PHE ILE GLY          
SEQRES   9 A  449  PRO LYS ALA GLU THR ILE ARG LEU MET GLY ASP LYS VAL          
SEQRES  10 A  449  SER ALA ILE ALA ALA MET LYS LYS ALA GLY VAL PRO CYS          
SEQRES  11 A  449  VAL PRO GLY SER ASP GLY PRO LEU GLY ASP ASP MET ASP          
SEQRES  12 A  449  LYS ASN ARG ALA ILE ALA LYS ARG ILE GLY TYR PRO VAL          
SEQRES  13 A  449  ILE ILE LYS ALA SER GLY GLY GLY GLY GLY ARG GLY MET          
SEQRES  14 A  449  ARG VAL VAL ARG GLY ASP ALA GLU LEU ALA GLN SER ILE          
SEQRES  15 A  449  SER MET THR ARG ALA GLU ALA LYS ALA ALA PHE SER ASN          
SEQRES  16 A  449  ASP MET VAL TYR MET GLU LYS TYR LEU GLU ASN PRO ARG          
SEQRES  17 A  449  HIS VAL GLU ILE GLN VAL LEU ALA ASP GLY GLN GLY ASN          
SEQRES  18 A  449  ALA ILE TYR LEU ALA GLU ARG ASP CYS SER MET GLN ARG          
SEQRES  19 A  449  ARG HIS GLN LYS VAL VAL GLU GLU ALA PRO ALA PRO GLY          
SEQRES  20 A  449  ILE THR PRO GLU LEU ARG ARG TYR ILE GLY GLU ARG CYS          
SEQRES  21 A  449  ALA LYS ALA CYS VAL ASP ILE GLY TYR ARG GLY ALA GLY          
SEQRES  22 A  449  THR PHE GLU PHE LEU PHE GLU ASN GLY GLU PHE TYR PHE          
SEQRES  23 A  449  ILE GLU MET ASN THR ARG ILE GLN VAL GLU HIS PRO VAL          
SEQRES  24 A  449  THR GLU MET ILE THR GLY VAL ASP LEU ILE LYS GLU GLN          
SEQRES  25 A  449  LEU ARG ILE ALA ALA GLY GLN PRO LEU SER ILE LYS GLN          
SEQRES  26 A  449  GLU GLU VAL HIS VAL ARG GLY HIS ALA VAL GLU CYS ARG          
SEQRES  27 A  449  ILE ASN ALA GLU ASP PRO ASN THR PHE LEU PRO SER PRO          
SEQRES  28 A  449  GLY LYS ILE THR ARG PHE HIS ALA PRO GLY GLY PHE GLY          
SEQRES  29 A  449  VAL ARG TRP GLU SER HIS ILE TYR ALA GLY TYR THR VAL          
SEQRES  30 A  449  PRO PRO TYR TYR ASP SER MET ILE GLY LYS LEU ILE CYS          
SEQRES  31 A  449  TYR GLY GLU ASN ARG ASP VAL ALA ILE ALA ARG MET LYS          
SEQRES  32 A  449  ASN ALA LEU GLN GLU LEU ILE ILE ASP GLY ILE LYS THR          
SEQRES  33 A  449  ASN VAL ASP LEU GLN ILE ARG ILE MET ASN ASP GLU ASN          
SEQRES  34 A  449  PHE GLN HIS GLY GLY THR ASN ILE HIS TYR LEU GLU LYS          
SEQRES  35 A  449  LYS LEU GLY LEU GLN GLU LYS                                  
SEQRES   1 B  449  MET LEU ASP LYS ILE VAL ILE ALA ASN ARG GLY GLU ILE          
SEQRES   2 B  449  ALA LEU ARG ILE LEU ARG ALA CYS LYS GLU LEU GLY ILE          
SEQRES   3 B  449  LYS THR VAL ALA VAL HIS SER SER ALA ASP ARG ASP LEU          
SEQRES   4 B  449  LYS HIS VAL LEU LEU ALA ASP GLU THR VAL CYS ILE GLY          
SEQRES   5 B  449  PRO ALA PRO SER VAL LYS SER TYR LEU ASN ILE PRO ALA          
SEQRES   6 B  449  ILE ILE SER ALA ALA GLU ILE THR GLY ALA VAL ALA ILE          
SEQRES   7 B  449  HIS PRO GLY TYR GLY PHE LEU SER GLU ASN ALA ASN PHE          
SEQRES   8 B  449  ALA GLU GLN VAL GLU ARG SER GLY PHE ILE PHE ILE GLY          
SEQRES   9 B  449  PRO LYS ALA GLU THR ILE ARG LEU MET GLY ASP LYS VAL          
SEQRES  10 B  449  SER ALA ILE ALA ALA MET LYS LYS ALA GLY VAL PRO CYS          
SEQRES  11 B  449  VAL PRO GLY SER ASP GLY PRO LEU GLY ASP ASP MET ASP          
SEQRES  12 B  449  LYS ASN ARG ALA ILE ALA LYS ARG ILE GLY TYR PRO VAL          
SEQRES  13 B  449  ILE ILE LYS ALA SER GLY GLY GLY GLY GLY ARG GLY MET          
SEQRES  14 B  449  ARG VAL VAL ARG GLY ASP ALA GLU LEU ALA GLN SER ILE          
SEQRES  15 B  449  SER MET THR ARG ALA GLU ALA LYS ALA ALA PHE SER ASN          
SEQRES  16 B  449  ASP MET VAL TYR MET GLU LYS TYR LEU GLU ASN PRO ARG          
SEQRES  17 B  449  HIS VAL GLU ILE GLN VAL LEU ALA ASP GLY GLN GLY ASN          
SEQRES  18 B  449  ALA ILE TYR LEU ALA GLU ARG ASP CYS SER MET GLN ARG          
SEQRES  19 B  449  ARG HIS GLN LYS VAL VAL GLU GLU ALA PRO ALA PRO GLY          
SEQRES  20 B  449  ILE THR PRO GLU LEU ARG ARG TYR ILE GLY GLU ARG CYS          
SEQRES  21 B  449  ALA LYS ALA CYS VAL ASP ILE GLY TYR ARG GLY ALA GLY          
SEQRES  22 B  449  THR PHE GLU PHE LEU PHE GLU ASN GLY GLU PHE TYR PHE          
SEQRES  23 B  449  ILE GLU MET ASN THR ARG ILE GLN VAL GLU HIS PRO VAL          
SEQRES  24 B  449  THR GLU MET ILE THR GLY VAL ASP LEU ILE LYS GLU GLN          
SEQRES  25 B  449  LEU ARG ILE ALA ALA GLY GLN PRO LEU SER ILE LYS GLN          
SEQRES  26 B  449  GLU GLU VAL HIS VAL ARG GLY HIS ALA VAL GLU CYS ARG          
SEQRES  27 B  449  ILE ASN ALA GLU ASP PRO ASN THR PHE LEU PRO SER PRO          
SEQRES  28 B  449  GLY LYS ILE THR ARG PHE HIS ALA PRO GLY GLY PHE GLY          
SEQRES  29 B  449  VAL ARG TRP GLU SER HIS ILE TYR ALA GLY TYR THR VAL          
SEQRES  30 B  449  PRO PRO TYR TYR ASP SER MET ILE GLY LYS LEU ILE CYS          
SEQRES  31 B  449  TYR GLY GLU ASN ARG ASP VAL ALA ILE ALA ARG MET LYS          
SEQRES  32 B  449  ASN ALA LEU GLN GLU LEU ILE ILE ASP GLY ILE LYS THR          
SEQRES  33 B  449  ASN VAL ASP LEU GLN ILE ARG ILE MET ASN ASP GLU ASN          
SEQRES  34 B  449  PHE GLN HIS GLY GLY THR ASN ILE HIS TYR LEU GLU LYS          
SEQRES  35 B  449  LYS LEU GLY LEU GLN GLU LYS                                  
HET     CL  A1447       1                                                       
HET    ATF  A1448      33                                                       
HET     CL  B1447       1                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ATF PHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER             
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   4  ATF    C11 H16 F2 N5 O12 P3                                         
FORMUL   6  HOH   *233(H2 O)                                                    
HELIX    1   1 ARG A   10  LEU A   24  1                                  15    
HELIX    2   2 ALA A   35  ARG A   37  5                                   3    
HELIX    3   3 LEU A   39  ALA A   45  1                                   7    
HELIX    4   4 PRO A   55  SER A   59  5                                   5    
HELIX    5   5 ASN A   62  GLY A   74  1                                  13    
HELIX    6   6 ASN A   88  GLY A   99  1                                  12    
HELIX    7   7 LYS A  106  GLY A  114  1                                   9    
HELIX    8   8 ASP A  115  GLY A  127  1                                  13    
HELIX    9   9 ASP A  141  GLY A  153  1                                  13    
HELIX   10  10 GLY A  174  SER A  194  1                                  21    
HELIX   11  11 THR A  249  ILE A  267  1                                  19    
HELIX   12  12 GLU A  296  GLY A  305  1                                  10    
HELIX   13  13 ASP A  307  ALA A  317  1                                  11    
HELIX   14  14 LYS A  324  VAL A  328  5                                   5    
HELIX   15  15 ASN A  394  LEU A  409  1                                  16    
HELIX   16  16 ASN A  417  ASN A  426  1                                  10    
HELIX   17  17 ASP A  427  GLY A  433  1                                   7    
HELIX   18  18 HIS A  438  GLY A  445  1                                   8    
HELIX   19  19 ARG B   10  GLY B   25  1                                  16    
HELIX   20  20 SER B   33  ARG B   37  5                                   5    
HELIX   21  21 LEU B   39  ALA B   45  1                                   7    
HELIX   22  22 PRO B   55  SER B   59  5                                   5    
HELIX   23  23 ASN B   62  GLY B   74  1                                  13    
HELIX   24  24 ASN B   88  SER B   98  1                                  11    
HELIX   25  25 LYS B  106  ASP B  115  1                                  10    
HELIX   26  26 ASP B  115  GLY B  127  1                                  13    
HELIX   27  27 ASP B  141  GLY B  153  1                                  13    
HELIX   28  28 LEU B  178  ALA B  187  1                                  10    
HELIX   29  29 THR B  249  GLY B  268  1                                  20    
HELIX   30  30 GLU B  296  GLY B  305  1                                  10    
HELIX   31  31 ASP B  307  ALA B  317  1                                  11    
HELIX   32  32 LYS B  324  VAL B  328  5                                   5    
HELIX   33  33 ASN B  394  LEU B  409  1                                  16    
HELIX   34  34 ASN B  417  ASP B  427  1                                  11    
HELIX   35  35 ASP B  427  GLY B  433  1                                   7    
HELIX   36  36 HIS B  438  LEU B  444  1                                   7    
SHEET    1  AA 5 GLU A  47  GLY A  52  0                                        
SHEET    2  AA 5 LYS A  27  SER A  33  1  O  THR A  28   N  GLU A  47           
SHEET    3  AA 5 LYS A   4  ILE A   7  1  O  ILE A   5   N  VAL A  29           
SHEET    4  AA 5 ALA A  77  HIS A  79  1  O  ALA A  77   N  VAL A   6           
SHEET    5  AA 5 ILE A 101  PHE A 102  1  O  ILE A 101   N  ILE A  78           
SHEET    1  AB 3 MET A 169  VAL A 172  0                                        
SHEET    2  AB 3 VAL A 156  ALA A 160 -1  O  VAL A 156   N  VAL A 172           
SHEET    3  AB 3 VAL A 198  LYS A 202 -1  O  TYR A 199   N  LYS A 159           
SHEET    1  AC 4 ALA A 222  ASP A 229  0                                        
SHEET    2  AC 4 ARG A 208  ALA A 216 -1  O  GLU A 211   N  ARG A 228           
SHEET    3  AC 4 GLY A 271  GLU A 280 -1  O  GLY A 271   N  ALA A 216           
SHEET    4  AC 4 GLU A 283  ASN A 290 -1  O  GLU A 283   N  GLU A 280           
SHEET    1  AD 2 GLN A 233  ARG A 234  0                                        
SHEET    2  AD 2 GLN A 237  LYS A 238 -1  O  GLN A 237   N  ARG A 234           
SHEET    1  AE 4 VAL A 240  ALA A 243  0                                        
SHEET    2  AE 4 HIS A 333  ASN A 340 -1  O  ALA A 334   N  ALA A 243           
SHEET    3  AE 4 MET A 384  GLY A 392 -1  O  GLY A 386   N  ILE A 339           
SHEET    4  AE 4 VAL A 365  SER A 369 -1  O  ARG A 366   N  ILE A 389           
SHEET    1  AF 2 GLY A 352  LYS A 353  0                                        
SHEET    2  AF 2 THR A 376  VAL A 377 -1  O  VAL A 377   N  GLY A 352           
SHEET    1  AG 2 ARG A 356  HIS A 358  0                                        
SHEET    2  AG 2 ILE A 410  ASP A 412 -1  O  ILE A 410   N  HIS A 358           
SHEET    1  BA 5 GLU B  47  CYS B  50  0                                        
SHEET    2  BA 5 LYS B  27  HIS B  32  1  O  THR B  28   N  GLU B  47           
SHEET    3  BA 5 LYS B   4  ILE B   7  1  O  ILE B   5   N  VAL B  29           
SHEET    4  BA 5 ALA B  77  HIS B  79  1  O  ALA B  77   N  VAL B   6           
SHEET    5  BA 5 ILE B 101  PHE B 102  1  O  ILE B 101   N  ILE B  78           
SHEET    1  BB 3 VAL B 171  VAL B 172  0                                        
SHEET    2  BB 3 VAL B 156  LYS B 159 -1  O  VAL B 156   N  VAL B 172           
SHEET    3  BB 3 TYR B 199  LYS B 202 -1  O  TYR B 199   N  LYS B 159           
SHEET    1  BC 8 PHE B 284  ASN B 290  0                                        
SHEET    2  BC 8 ARG B 270  PHE B 279 -1  O  THR B 274   N  ASN B 290           
SHEET    3  BC 8 ARG B 208  ASP B 217 -1  O  ARG B 208   N  PHE B 279           
SHEET    4  BC 8 ALA B 222  ARG B 234 -1  O  ILE B 223   N  LEU B 215           
SHEET    5  BC 8 GLN B 237  ALA B 243 -1  O  GLN B 237   N  ARG B 234           
SHEET    6  BC 8 HIS B 333  ASN B 340 -1  O  ALA B 334   N  ALA B 243           
SHEET    7  BC 8 MET B 384  GLY B 392 -1  N  ILE B 385   O  ILE B 339           
SHEET    8  BC 8 VAL B 365  SER B 369 -1  O  ARG B 366   N  ILE B 389           
SHEET    1  BD 2 GLY B 352  LYS B 353  0                                        
SHEET    2  BD 2 THR B 376  VAL B 377 -1  O  VAL B 377   N  GLY B 352           
SHEET    1  BE 2 ARG B 356  HIS B 358  0                                        
SHEET    2  BE 2 ILE B 410  ASP B 412 -1  O  ILE B 410   N  HIS B 358           
CISPEP   1 TYR A  154    PRO A  155          0        -5.41                     
CISPEP   2 ALA A  243    PRO A  244          0        -9.10                     
CISPEP   3 TYR B  154    PRO B  155          0         1.21                     
CISPEP   4 ALA B  243    PRO B  244          0        -7.38                     
SITE     1 AC1  3 ARG A 292  VAL A 295  HOH A2083                               
SITE     1 AC2  3 ARG B 292  VAL B 295  HOH B2060                               
SITE     1 AC3 18 LYS A 116  LYS A 159  GLY A 166  ARG A 167                    
SITE     2 AC3 18 MET A 169  GLU A 201  LYS A 202  TYR A 203                    
SITE     3 AC3 18 LEU A 204  GLN A 233  HIS A 236  GLU A 276                    
SITE     4 AC3 18 LEU A 278  GLU A 288  ASN A 290  ILE A 437                    
SITE     5 AC3 18 HOH A2121  HOH A2122                                          
CRYST1   84.129  106.784  121.910  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      0.011887  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009365  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008203        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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