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Database: PDB
Entry: 2C00
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Original site: 2C00 
HEADER    LIGASE                                  21-MAR-08   2C00              
TITLE     CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM PSEUDOMONAS              
TITLE    2 AERUGINOSA IN APO FORM                                               
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: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NUCLEOTIDE-BINDING, FATTY ACID BIOSYNTHESIS, ATP-GRASP DOMAIN,        
KEYWDS   2 BIOTIN CARBOXYLASE, LIGASE, BIOTIN, ATP-BINDING, LIPID SYNTHESIS     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.MOCHALKIN                                                           
REVDAT   4   13-JUL-11 2C00    1       VERSN                                    
REVDAT   3   24-FEB-09 2C00    1       VERSN                                    
REVDAT   2   30-SEP-08 2C00    1       JRNL                                     
REVDAT   1   09-SEP-08 2C00    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.    2.5  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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.13                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 71168                          
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3769                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5189                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3010                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 289                          
REMARK   3   BIN FREE R VALUE                    : 0.3450                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6748                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 488                                     
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) : 32.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.52000                                              
REMARK   3    B22 (A**2) : 0.52000                                              
REMARK   3    B33 (A**2) : -0.77000                                             
REMARK   3    B12 (A**2) : 0.26000                                              
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): 0.207         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.182         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.116         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.635         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6873 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  4720 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9288 ; 1.083 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11498 ; 0.842 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   877 ; 5.811 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   308 ;36.593 ;23.734       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1189 ;13.867 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    57 ;17.158 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1041 ; 0.069 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7707 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1354 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1237 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4738 ; 0.190 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3310 ; 0.168 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3725 ; 0.081 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   348 ; 0.120 ; 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):     6 ; 0.091 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    17 ; 0.224 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    17 ; 0.152 ; 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):  5684 ; 0.723 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7005 ; 0.786 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2833 ; 1.195 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2283 ; 1.800 ; 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  : 2                                          
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   445                          
REMARK   3    ORIGIN FOR THE GROUP (A): -76.1696  42.3981   2.4376              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0937 T22:  -0.0695                                     
REMARK   3      T33:  -0.0530 T12:  -0.0407                                     
REMARK   3      T13:  -0.0328 T23:   0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6312 L22:   0.8516                                     
REMARK   3      L33:   1.8344 L12:  -0.3192                                     
REMARK   3      L13:   0.0411 L23:   0.2320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0660 S12:  -0.0212 S13:   0.0933                       
REMARK   3      S21:   0.0114 S22:   0.0245 S23:  -0.0658                       
REMARK   3      S31:  -0.1094 S32:  -0.1260 S33:   0.0415                       
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   445                          
REMARK   3    ORIGIN FOR THE GROUP (A): -65.8566   1.2111  12.3108              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1485 T22:  -0.0991                                     
REMARK   3      T33:  -0.0108 T12:   0.0343                                     
REMARK   3      T13:  -0.0249 T23:   0.0631                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4504 L22:   2.2808                                     
REMARK   3      L33:   0.0192 L12:   0.4869                                     
REMARK   3      L13:   0.0920 L23:   0.0736                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0437 S12:  -0.0709 S13:  -0.2154                       
REMARK   3      S21:   0.2847 S22:   0.0265 S23:  -0.3524                       
REMARK   3      S31:   0.2325 S32:   0.0302 S33:   0.0172                       
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          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2C00 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAR-08.                  
REMARK 100 THE PDBE ID CODE IS EBI-35551.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-AUG-06                          
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   : 75554                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.4                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 33.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.37                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.70                               
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 1DV1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 76.93                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS (PH 7.0); 0.2M MGCL2;          
REMARK 280  17-21% PEG3350                                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.92133            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       97.84267            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       97.84267            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       48.92133            
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   163                                                      
REMARK 465     GLY A   164                                                      
REMARK 465     GLY A   165                                                      
REMARK 465     ALA A   191                                                      
REMARK 465     ALA A   192                                                      
REMARK 465     MET A   446                                                      
REMARK 465     ASP A   447                                                      
REMARK 465     LYS A   448                                                      
REMARK 465     HIS A   449                                                      
REMARK 465     GLY A   450                                                      
REMARK 465     SER A   451                                                      
REMARK 465     GLU A   452                                                      
REMARK 465     ASN A   453                                                      
REMARK 465     LEU A   454                                                      
REMARK 465     TYR A   455                                                      
REMARK 465     PHE A   456                                                      
REMARK 465     GLN A   457                                                      
REMARK 465     GLY A   458                                                      
REMARK 465     HIS A   459                                                      
REMARK 465     HIS A   460                                                      
REMARK 465     HIS A   461                                                      
REMARK 465     HIS A   462                                                      
REMARK 465     HIS A   463                                                      
REMARK 465     HIS A   464                                                      
REMARK 465     GLY B   164                                                      
REMARK 465     GLY B   165                                                      
REMARK 465     GLY B   166                                                      
REMARK 465     ARG B   167                                                      
REMARK 465     ALA B   192                                                      
REMARK 465     PHE B   193                                                      
REMARK 465     MET B   446                                                      
REMARK 465     ASP B   447                                                      
REMARK 465     LYS B   448                                                      
REMARK 465     HIS B   449                                                      
REMARK 465     GLY B   450                                                      
REMARK 465     SER B   451                                                      
REMARK 465     GLU B   452                                                      
REMARK 465     ASN B   453                                                      
REMARK 465     LEU B   454                                                      
REMARK 465     TYR B   455                                                      
REMARK 465     PHE B   456                                                      
REMARK 465     GLN B   457                                                      
REMARK 465     GLY B   458                                                      
REMARK 465     HIS B   459                                                      
REMARK 465     HIS B   460                                                      
REMARK 465     HIS B   461                                                      
REMARK 465     HIS B   462                                                      
REMARK 465     HIS B   463                                                      
REMARK 465     HIS B   464                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  2066     O    HOH A  2153              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A   9     -173.16   -172.25                                   
REMARK 500    SER A  59      -85.68   -140.97                                   
REMARK 500    PHE A  84     -114.70     47.53                                   
REMARK 500    GLU A 188       46.74    -77.91                                   
REMARK 500    ALA A 189       93.54    170.89                                   
REMARK 500    PRO A 196       41.30    -90.04                                   
REMARK 500    ASN A 281       69.91     29.47                                   
REMARK 500    ARG A 292      169.84    178.69                                   
REMARK 500    SER A 322      -91.72     40.86                                   
REMARK 500    ASN B   9     -167.77   -171.86                                   
REMARK 500    SER B  59      -86.34   -146.88                                   
REMARK 500    PHE B  84     -122.85     45.96                                   
REMARK 500    ARG B 292      168.25    179.88                                   
REMARK 500    TYR B 381     -159.24   -116.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A  321     SER A  322                   72.58                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    SER A 322        21.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1446                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1446                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
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: 2VPQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  S. AUREUS COMPLEXED WITH AMPPNP                                     
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.                                                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 C-TERMINAL HIS-TAG PRESENT                                           
DBREF  2C00 A    1   449  UNP    P37798   ACCC_PSEAE       1    449             
DBREF  2C00 A  450   464  PDB    2C00     2C00           450    464             
DBREF  2C00 B    1   449  UNP    P37798   ACCC_PSEAE       1    449             
DBREF  2C00 B  450   464  PDB    2C00     2C00           450    464             
SEQRES   1 A  464  MET LEU GLU LYS VAL LEU ILE ALA ASN ARG GLY GLU ILE          
SEQRES   2 A  464  ALA LEU ARG ILE LEU ARG ALA CYS LYS GLU LEU GLY ILE          
SEQRES   3 A  464  LYS THR VAL ALA VAL HIS SER THR ALA ASP ARG GLU LEU          
SEQRES   4 A  464  MET HIS LEU SER LEU ALA ASP GLU SER VAL CYS ILE GLY          
SEQRES   5 A  464  PRO ALA PRO ALA THR GLN SER TYR LEU GLN ILE PRO ALA          
SEQRES   6 A  464  ILE ILE ALA ALA ALA GLU VAL THR GLY ALA THR ALA ILE          
SEQRES   7 A  464  HIS PRO GLY TYR GLY PHE LEU ALA GLU ASN ALA ASP PHE          
SEQRES   8 A  464  ALA GLU GLN ILE GLU ARG SER GLY PHE THR PHE VAL GLY          
SEQRES   9 A  464  PRO THR ALA GLU VAL ILE ARG LEU MET GLY ASP LYS VAL          
SEQRES  10 A  464  SER ALA LYS ASP ALA MET LYS ARG ALA GLY VAL PRO THR          
SEQRES  11 A  464  VAL PRO GLY SER ASP GLY PRO LEU PRO GLU ASP GLU GLU          
SEQRES  12 A  464  THR ALA LEU ALA ILE ALA ARG GLU VAL GLY TYR PRO VAL          
SEQRES  13 A  464  ILE ILE LYS ALA ALA GLY GLY GLY GLY GLY ARG GLY MET          
SEQRES  14 A  464  ARG VAL VAL TYR ASP GLU SER GLU LEU ILE LYS SER ALA          
SEQRES  15 A  464  LYS LEU THR ARG THR GLU ALA GLY ALA ALA PHE GLY ASN          
SEQRES  16 A  464  PRO MET VAL TYR LEU GLU LYS PHE LEU THR ASN PRO ARG          
SEQRES  17 A  464  HIS VAL GLU VAL GLN VAL LEU SER ASP GLY GLN GLY ASN          
SEQRES  18 A  464  ALA ILE HIS LEU GLY ASP ARG ASP CYS SER LEU GLN ARG          
SEQRES  19 A  464  ARG HIS GLN LYS VAL ILE GLU GLU ALA PRO ALA PRO GLY          
SEQRES  20 A  464  ILE ASP GLU LYS ALA ARG GLN GLU VAL PHE ALA ARG CYS          
SEQRES  21 A  464  VAL GLN ALA CYS ILE GLU ILE GLY TYR ARG GLY ALA GLY          
SEQRES  22 A  464  THR PHE GLU PHE LEU TYR GLU ASN GLY ARG PHE TYR PHE          
SEQRES  23 A  464  ILE GLU MET ASN THR ARG VAL GLN VAL GLU HIS PRO VAL          
SEQRES  24 A  464  SER GLU MET VAL THR GLY VAL ASP ILE VAL LYS GLU MET          
SEQRES  25 A  464  LEU ARG ILE ALA SER GLY GLU LYS LEU SER ILE ARG GLN          
SEQRES  26 A  464  GLU ASP VAL VAL ILE ARG GLY HIS ALA LEU GLU CYS ARG          
SEQRES  27 A  464  ILE ASN ALA GLU ASP PRO LYS THR PHE MET PRO SER PRO          
SEQRES  28 A  464  GLY LYS VAL LYS HIS PHE HIS ALA PRO GLY GLY ASN GLY          
SEQRES  29 A  464  VAL ARG VAL ASP SER HIS LEU TYR SER GLY TYR SER VAL          
SEQRES  30 A  464  PRO PRO ASN TYR ASP SER LEU VAL GLY LYS VAL ILE THR          
SEQRES  31 A  464  TYR GLY ALA ASP ARG ASP GLU ALA LEU ALA ARG MET ARG          
SEQRES  32 A  464  ASN ALA LEU ASP GLU LEU ILE VAL ASP GLY ILE LYS THR          
SEQRES  33 A  464  ASN THR GLU LEU HIS LYS ASP LEU VAL ARG ASP ALA ALA          
SEQRES  34 A  464  PHE CYS LYS GLY GLY VAL ASN ILE HIS TYR LEU GLU LYS          
SEQRES  35 A  464  LYS LEU GLY MET ASP LYS HIS GLY SER GLU ASN LEU TYR          
SEQRES  36 A  464  PHE GLN GLY HIS HIS HIS HIS HIS HIS                          
SEQRES   1 B  464  MET LEU GLU LYS VAL LEU ILE ALA ASN ARG GLY GLU ILE          
SEQRES   2 B  464  ALA LEU ARG ILE LEU ARG ALA CYS LYS GLU LEU GLY ILE          
SEQRES   3 B  464  LYS THR VAL ALA VAL HIS SER THR ALA ASP ARG GLU LEU          
SEQRES   4 B  464  MET HIS LEU SER LEU ALA ASP GLU SER VAL CYS ILE GLY          
SEQRES   5 B  464  PRO ALA PRO ALA THR GLN SER TYR LEU GLN ILE PRO ALA          
SEQRES   6 B  464  ILE ILE ALA ALA ALA GLU VAL THR GLY ALA THR ALA ILE          
SEQRES   7 B  464  HIS PRO GLY TYR GLY PHE LEU ALA GLU ASN ALA ASP PHE          
SEQRES   8 B  464  ALA GLU GLN ILE GLU ARG SER GLY PHE THR PHE VAL GLY          
SEQRES   9 B  464  PRO THR ALA GLU VAL ILE ARG LEU MET GLY ASP LYS VAL          
SEQRES  10 B  464  SER ALA LYS ASP ALA MET LYS ARG ALA GLY VAL PRO THR          
SEQRES  11 B  464  VAL PRO GLY SER ASP GLY PRO LEU PRO GLU ASP GLU GLU          
SEQRES  12 B  464  THR ALA LEU ALA ILE ALA ARG GLU VAL GLY TYR PRO VAL          
SEQRES  13 B  464  ILE ILE LYS ALA ALA GLY GLY GLY GLY GLY ARG GLY MET          
SEQRES  14 B  464  ARG VAL VAL TYR ASP GLU SER GLU LEU ILE LYS SER ALA          
SEQRES  15 B  464  LYS LEU THR ARG THR GLU ALA GLY ALA ALA PHE GLY ASN          
SEQRES  16 B  464  PRO MET VAL TYR LEU GLU LYS PHE LEU THR ASN PRO ARG          
SEQRES  17 B  464  HIS VAL GLU VAL GLN VAL LEU SER ASP GLY GLN GLY ASN          
SEQRES  18 B  464  ALA ILE HIS LEU GLY ASP ARG ASP CYS SER LEU GLN ARG          
SEQRES  19 B  464  ARG HIS GLN LYS VAL ILE GLU GLU ALA PRO ALA PRO GLY          
SEQRES  20 B  464  ILE ASP GLU LYS ALA ARG GLN GLU VAL PHE ALA ARG CYS          
SEQRES  21 B  464  VAL GLN ALA CYS ILE GLU ILE GLY TYR ARG GLY ALA GLY          
SEQRES  22 B  464  THR PHE GLU PHE LEU TYR GLU ASN GLY ARG PHE TYR PHE          
SEQRES  23 B  464  ILE GLU MET ASN THR ARG VAL GLN VAL GLU HIS PRO VAL          
SEQRES  24 B  464  SER GLU MET VAL THR GLY VAL ASP ILE VAL LYS GLU MET          
SEQRES  25 B  464  LEU ARG ILE ALA SER GLY GLU LYS LEU SER ILE ARG GLN          
SEQRES  26 B  464  GLU ASP VAL VAL ILE ARG GLY HIS ALA LEU GLU CYS ARG          
SEQRES  27 B  464  ILE ASN ALA GLU ASP PRO LYS THR PHE MET PRO SER PRO          
SEQRES  28 B  464  GLY LYS VAL LYS HIS PHE HIS ALA PRO GLY GLY ASN GLY          
SEQRES  29 B  464  VAL ARG VAL ASP SER HIS LEU TYR SER GLY TYR SER VAL          
SEQRES  30 B  464  PRO PRO ASN TYR ASP SER LEU VAL GLY LYS VAL ILE THR          
SEQRES  31 B  464  TYR GLY ALA ASP ARG ASP GLU ALA LEU ALA ARG MET ARG          
SEQRES  32 B  464  ASN ALA LEU ASP GLU LEU ILE VAL ASP GLY ILE LYS THR          
SEQRES  33 B  464  ASN THR GLU LEU HIS LYS ASP LEU VAL ARG ASP ALA ALA          
SEQRES  34 B  464  PHE CYS LYS GLY GLY VAL ASN ILE HIS TYR LEU GLU LYS          
SEQRES  35 B  464  LYS LEU GLY MET ASP LYS HIS GLY SER GLU ASN LEU TYR          
SEQRES  36 B  464  PHE GLN GLY HIS HIS HIS HIS HIS HIS                          
HET    SO4  A1446       5                                                       
HET    SO4  B1446       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   4  HOH   *488(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 HIS A   41  ALA A   45  5                                   5    
HELIX    4   4 PRO A   55  SER A   59  5                                   5    
HELIX    5   5 GLN A   62  GLY A   74  1                                  13    
HELIX    6   6 ASN A   88  GLY A   99  1                                  12    
HELIX    7   7 THR A  106  ASP A  115  1                                  10    
HELIX    8   8 ASP A  115  ALA A  126  1                                  12    
HELIX    9   9 ASP A  141  GLY A  153  1                                  13    
HELIX   10  10 ASP A  174  SER A  176  5                                   3    
HELIX   11  11 GLU A  177  GLU A  188  1                                  12    
HELIX   12  12 ASP A  249  GLY A  268  1                                  20    
HELIX   13  13 GLU A  296  GLY A  305  1                                  10    
HELIX   14  14 ASP A  307  SER A  317  1                                  11    
HELIX   15  15 ARG A  324  VAL A  328  5                                   5    
HELIX   16  16 ASP A  394  LEU A  409  1                                  16    
HELIX   17  17 ASN A  417  VAL A  425  1                                   9    
HELIX   18  18 ASP A  427  GLY A  433  1                                   7    
HELIX   19  19 HIS A  438  GLY A  445  1                                   8    
HELIX   20  20 ARG B   10  LEU B   24  1                                  15    
HELIX   21  21 ALA B   35  ARG B   37  5                                   3    
HELIX   22  22 LEU B   39  ALA B   45  5                                   7    
HELIX   23  23 PRO B   55  SER B   59  5                                   5    
HELIX   24  24 GLN B   62  GLY B   74  1                                  13    
HELIX   25  25 ASN B   88  SER B   98  1                                  11    
HELIX   26  26 THR B  106  ASP B  115  1                                  10    
HELIX   27  27 ASP B  115  GLY B  127  1                                  13    
HELIX   28  28 ASP B  141  GLY B  153  1                                  13    
HELIX   29  29 GLU B  177  GLY B  190  1                                  14    
HELIX   30  30 ASP B  249  GLY B  268  1                                  20    
HELIX   31  31 GLU B  296  GLY B  305  1                                  10    
HELIX   32  32 ASP B  307  SER B  317  1                                  11    
HELIX   33  33 ARG B  324  VAL B  328  5                                   5    
HELIX   34  34 ASP B  394  LEU B  409  1                                  16    
HELIX   35  35 ASN B  417  VAL B  425  1                                   9    
HELIX   36  36 ASP B  427  GLY B  433  1                                   7    
HELIX   37  37 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  VAL A   5   N  VAL A  29           
SHEET    4  AA 5 ALA A  77  HIS A  79  1  O  ALA A  77   N  LEU A   6           
SHEET    5  AA 5 THR A 101  PHE A 102  1  O  THR A 101   N  ILE A  78           
SHEET    1  AB 3 ARG A 170  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  ASP A 217 -1  O  GLU A 211   N  ARG A 228           
SHEET    3  AC 4 ARG A 270  GLU A 280 -1  O  GLY A 271   N  SER A 216           
SHEET    4  AC 4 ARG A 283  ASN A 290 -1  O  ARG 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 ILE 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 LEU A 384  GLY A 392 -1  N  VAL A 385   O  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 SER A 376  VAL A 377 -1  O  VAL A 377   N  GLY A 352           
SHEET    1  AG 2 HIS 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  GLY B  52  0                                        
SHEET    2  BA 5 LYS B  27  SER B  33  1  O  THR B  28   N  GLU B  47           
SHEET    3  BA 5 LYS B   4  ILE B   7  1  O  VAL B   5   N  VAL B  29           
SHEET    4  BA 5 ALA B  77  HIS B  79  1  O  ALA B  77   N  LEU B   6           
SHEET    5  BA 5 THR B 101  PHE B 102  1  O  THR B 101   N  ILE B  78           
SHEET    1  BB 3 MET B 169  VAL B 172  0                                        
SHEET    2  BB 3 VAL B 156  ALA B 160 -1  O  VAL B 156   N  VAL B 172           
SHEET    3  BB 3 VAL B 198  LYS B 202 -1  O  TYR B 199   N  LYS B 159           
SHEET    1  BC 8 ARG B 283  ASN B 290  0                                        
SHEET    2  BC 8 ARG B 270  GLU B 280 -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  TYR 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 LEU B 384  GLY B 392 -1  N  VAL 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 SER B 376  VAL B 377 -1  O  VAL B 377   N  GLY B 352           
SHEET    1  BE 2 HIS 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 ASP A  135    GLY A  136          0        -7.61                     
CISPEP   2 TYR A  154    PRO A  155          0        -5.99                     
CISPEP   3 ALA A  189    GLY A  190          0         5.34                     
CISPEP   4 ALA A  243    PRO A  244          0        -9.17                     
CISPEP   5 TYR B  154    PRO B  155          0        -1.43                     
CISPEP   6 ALA B  243    PRO B  244          0       -11.43                     
SITE     1 AC1  9 LYS A 238  ARG A 292  GLN A 294  VAL A 295                    
SITE     2 AC1  9 GLU A 296  ARG A 338  HOH A2185  HOH A2310                    
SITE     3 AC1  9 HOH A2311                                                     
SITE     1 AC2  7 LYS B 238  ARG B 292  GLN B 294  VAL B 295                    
SITE     2 AC2  7 GLU B 296  ARG B 338  HOH B2177                               
CRYST1  160.402  160.402  146.764  90.00  90.00 120.00 P 31 2 1     12          
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      0.006234  0.003599  0.000000        0.00000                         
SCALE2      0.000000  0.007199  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006814        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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