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Database: PDB
Entry: 2CB8
LinkDB: 2CB8
Original site: 2CB8 
HEADER    TRANSPORT                               03-JAN-06   2CB8              
TITLE     HIGH RESOLUTION CRYSTAL STRUCTURE OF LIGANDED HUMAN L-ACBP            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACYL-COA-BINDING PROTEIN;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ACYL-COENZYME A BINDING PROTEIN, ACBP, DIAZEPAM-            
COMPND   5  BINDING INHIBITOR, DBI, ENDOZEPINE, EP;                             
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ACYL-COENZYME A BINDING PROTEIN, FATTY ACID, ACETYLATION,             
KEYWDS   2 ALTERNATIVE SPLICING, LIPID-BINDING, TRANSPORT                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.TASKINEN,D.M.VAN AALTEN,J.KNUDSEN,R.K.WIERENGA                    
REVDAT   3   24-FEB-09 2CB8    1       VERSN                                    
REVDAT   2   20-DEC-06 2CB8    1       JRNL                                     
REVDAT   1   25-OCT-06 2CB8    0                                                
JRNL        AUTH   J.P.TASKINEN,D.M.VAN AALTEN,J.KNUDSEN,R.K.WIERENGA           
JRNL        TITL   HIGH RESOLUTION CRYSTAL STRUCTURES OF UNLIGANDED             
JRNL        TITL 2 AND LIGANDED HUMAN LIVER ACBP REVEAL A NEW MODE OF           
JRNL        TITL 3 BINDING FOR THE ACYL-COA LIGAND.                             
JRNL        REF    PROTEINS: STRUCT., FUNCT.,    V.  66   229 2007              
JRNL        REF  2 BIOINF.                                                      
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   17044054                                                     
JRNL        DOI    10.1002/PROT.21124                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.4  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 53111                          
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.194                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1091                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.48                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7692                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 154                          
REMARK   3   BIN FREE R VALUE                    : 0.2370                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1475                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 154                                     
REMARK   3   SOLVENT ATOMS            : 289                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.055         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.052         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.040         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.048         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.964                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1660 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2231 ; 1.866 ; 2.056       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   173 ; 4.286 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   229 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1141 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   855 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   252 ; 0.172 ; 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):    79 ; 0.176 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    35 ; 0.129 ; 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):   873 ; 2.121 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1410 ; 2.932 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   787 ; 4.307 ; 7.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   814 ; 5.914 ;10.000       
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     2        A    87                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.2900  19.8420  39.6500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0641 T22:   0.0694                                     
REMARK   3      T33:   0.0577 T12:   0.0341                                     
REMARK   3      T13:   0.0496 T23:   0.0578                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1426 L22:   1.4506                                     
REMARK   3      L33:   1.5414 L12:  -0.6288                                     
REMARK   3      L13:  -0.3895 L23:   0.3616                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0699 S12:  -0.0625 S13:  -0.0579                       
REMARK   3      S21:   0.0248 S22:  -0.0109 S23:  -0.0046                       
REMARK   3      S31:   0.1560 S32:   0.0216 S33:   0.0808                       
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     2        B    87                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1220  31.2800  50.7780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0340 T22:   0.2563                                     
REMARK   3      T33:   0.0395 T12:   0.0330                                     
REMARK   3      T13:   0.0039 T23:   0.0238                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7976 L22:   1.8826                                     
REMARK   3      L33:   1.4592 L12:  -0.0650                                     
REMARK   3      L13:  -0.1256 L23:   0.0227                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0974 S12:  -0.4108 S13:   0.0768                       
REMARK   3      S21:  -0.0284 S22:   0.1165 S23:   0.0327                       
REMARK   3      S31:  -0.0267 S32:   0.0091 S33:  -0.0191                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2CB8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  03-JAN-06.                 
REMARK 100 THE PDBE ID CODE IS EBI-27032.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-NOV-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.7453                             
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54202                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.440                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.6                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG-MME 550, 100 MM MES, PH          
REMARK 280  6.5, 10 MM ZNSO4                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      14555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      15555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      16555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      18555   Z+1/2,-X+1/2,-Y+1/2                                     
REMARK 290      19555   -Z+1/2,-X+1/2,Y+1/2                                     
REMARK 290      20555   -Z+1/2,X+1/2,-Y+1/2                                     
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      22555   -Y+1/2,Z+1/2,-X+1/2                                     
REMARK 290      23555   Y+1/2,-Z+1/2,-X+1/2                                     
REMARK 290      24555   -Y+1/2,-Z+1/2,X+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       59.24500            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       59.24500            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       59.24500            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       59.24500            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       59.24500            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       59.24500            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       59.24500            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       59.24500            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       59.24500            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       59.24500            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       59.24500            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       59.24500            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       59.24500            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       59.24500            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       59.24500            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       59.24500            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       59.24500            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       59.24500            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       59.24500            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       59.24500            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       59.24500            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       59.24500            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       59.24500            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       59.24500            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       59.24500            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       59.24500            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       59.24500            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       59.24500            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       59.24500            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       59.24500            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       59.24500            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       59.24500            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       59.24500            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       59.24500            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       59.24500            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       59.24500            
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 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 S    SO4 A1095  LIES ON A SPECIAL POSITION.                          
REMARK 375 ZN    ZN A1096  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A2003  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  BINDS MEDIUM- AND LONG-CHAIN ACYL-COA ESTERS WITH VERY              
REMARK 400  HIGH AFFINITY                                                       
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
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   OD2  ASP B    22  -  O    HOH B  2047              2.01            
REMARK 500   O10  MYA B  1088  -  O    HOH B  2128              2.04            
REMARK 500   O    HOH B  2061  -  O    HOH B  2066              1.69            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  36      -63.44   -106.80                                   
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 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    ILE B  87        23.2      L          L   OUTSIDE RANGE           
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 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     MYA B 1088                                                       
REMARK 610     MYA A 1088                                                       
REMARK 610     MYA B 1089                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1089  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  31   NE2                                                    
REMARK 620 2 GLU B   7   OE1 126.4                                              
REMARK 620 3 GLU B   7   OE2  93.0  57.8                                        
REMARK 620 4 HOH A2150   O   100.7 101.2 159.0                                  
REMARK 620 5 HOH A2151   O   111.6 111.8  89.4 100.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1090  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MYA A1094   O7A                                                    
REMARK 620 2 MYA A1094   O3A 104.6                                              
REMARK 620 3 SO4 A1095   O1  137.0 108.9                                        
REMARK 620 4 SO4 A1095   O2  132.0 102.1  14.1                                  
REMARK 620 5 SO4 A1095   O3   87.4 119.0  52.9  44.6                            
REMARK 620 6 SO4 A1095   O4  115.7 102.3  31.1  18.3  29.2                      
REMARK 620 7 MYA A1088   O2A 111.0 114.1  78.9  93.0 116.2 109.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1091  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  11   OE1                                                    
REMARK 620 2 HIS A  15   NE2 112.3                                              
REMARK 620 3 ASP A  22   OD1 153.2  89.3                                        
REMARK 620 4 ASP A  22   OD2 101.4 119.6  52.6                                  
REMARK 620 5 MYA A1094   N1A 103.8 107.0  83.6 111.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1092  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  69   OD1                                                    
REMARK 620 2 GLU A  68   OE2 136.5                                              
REMARK 620 3 ASP B  69   OD2  60.9 117.4                                        
REMARK 620 4 HOH A2152   O    98.1 123.9  73.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1093  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SO4 A1095   O1                                                     
REMARK 620 2 SO4 A1095   O2   27.6                                              
REMARK 620 3 MYA A1088   O3A 118.6 129.4                                        
REMARK 620 4 MYA A1094   O2A 124.4  96.8  95.1                                  
REMARK 620 5 MYA A1088   O1A  95.7 103.3 121.7 102.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1096  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MYA A1094   O8A                                                    
REMARK 620 2 SO4 A1095   O3   88.0                                              
REMARK 620 3 MYA A1094   O8A 105.1 104.4                                        
REMARK 620 4 MYA A1094   O8A 105.5 139.4 108.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1090  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  11   OE2                                                    
REMARK 620 2 HOH B2131   O    92.7                                              
REMARK 620 3 GLU A  23   OE1 163.5  87.7                                        
REMARK 620 4 HIS B  15   NE2  96.2  96.3 100.2                                  
REMARK 620 5 HOH B2132   O    94.6 170.7  83.7  88.6                            
REMARK 620 6 GLU A  23   OE2 104.8  84.6  58.8 158.9  88.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1091  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A   7   OE2                                                    
REMARK 620 2 MYA B1088   O5A 100.5                                              
REMARK 620 3 HOH B2134   O    86.5  85.4                                        
REMARK 620 4 MYA B1088   O2A  86.3  86.2 167.8                                  
REMARK 620 5 GLU A   7   OE1  58.0 158.4  90.9  93.7                            
REMARK 620 6 HOH B2133   O   156.0 103.4  93.2  97.4  98.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1089                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1090                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1091                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1092                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1093                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1095                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1096                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1090                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1091                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYA A1088                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYA A1094                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYA B1088                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYA B1089                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MXE B1092                 
DBREF  2CB8 A    1     1  PDB    2CB8     2CB8             1      1             
DBREF  2CB8 A    2    87  UNP    P07108   ACBP_HUMAN       1     86             
DBREF  2CB8 B    1     1  PDB    2CB8     2CB8             1      1             
DBREF  2CB8 B    2    87  UNP    P07108   ACBP_HUMAN       1     86             
SEQRES   1 A   87  MET SER GLN ALA GLU PHE GLU LYS ALA ALA GLU GLU VAL          
SEQRES   2 A   87  ARG HIS LEU LYS THR LYS PRO SER ASP GLU GLU MET LEU          
SEQRES   3 A   87  PHE ILE TYR GLY HIS TYR LYS GLN ALA THR VAL GLY ASP          
SEQRES   4 A   87  ILE ASN THR GLU ARG PRO GLY MET LEU ASP PHE THR GLY          
SEQRES   5 A   87  LYS ALA LYS TRP ASP ALA TRP ASN GLU LEU LYS GLY THR          
SEQRES   6 A   87  SER LYS GLU ASP ALA MET LYS ALA TYR ILE ASN LYS VAL          
SEQRES   7 A   87  GLU GLU LEU LYS LYS LYS TYR GLY ILE                          
SEQRES   1 B   87  MET SER GLN ALA GLU PHE GLU LYS ALA ALA GLU GLU VAL          
SEQRES   2 B   87  ARG HIS LEU LYS THR LYS PRO SER ASP GLU GLU MET LEU          
SEQRES   3 B   87  PHE ILE TYR GLY HIS TYR LYS GLN ALA THR VAL GLY ASP          
SEQRES   4 B   87  ILE ASN THR GLU ARG PRO GLY MET LEU ASP PHE THR GLY          
SEQRES   5 B   87  LYS ALA LYS TRP ASP ALA TRP ASN GLU LEU LYS GLY THR          
SEQRES   6 B   87  SER LYS GLU ASP ALA MET LYS ALA TYR ILE ASN LYS VAL          
SEQRES   7 B   87  GLU GLU LEU LYS LYS LYS TYR GLY ILE                          
HET     ZN  A1089       1                                                       
HET     ZN  A1090       1                                                       
HET     ZN  A1091       1                                                       
HET     ZN  A1092       1                                                       
HET     ZN  A1093       1                                                       
HET    SO4  A1095       5                                                       
HET     ZN  A1096       1                                                       
HET     ZN  B1090       1                                                       
HET     ZN  B1091       1                                                       
HET    MYA  A1088      27                                                       
HET    MYA  A1094      27                                                       
HET    MYA  B1088      63                                                       
HET    MYA  B1089      19                                                       
HET    MXE  B1092       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     MYA TETRADECANOYL-COA                                                
HETNAM     MXE 2-METHOXYETHANOL                                                 
FORMUL   3   ZN    8(ZN 2+)                                                     
FORMUL   8  SO4    O4 S 2-                                                      
FORMUL  12  MYA    4(C35 H62 N7 O17 P3 S)                                       
FORMUL  16  MXE    C3 H8 O2                                                     
FORMUL  17  HOH   *289(H2 O1)                                                   
HELIX    1   1 SER A    2  VAL A   13  1                                  12    
HELIX    2   2 ARG A   14  LEU A   16  5                                   3    
HELIX    3   3 SER A   21  VAL A   37  1                                  17    
HELIX    4   4 ASP A   49  GLU A   61  1                                  13    
HELIX    5   5 SER A   66  GLY A   86  1                                  21    
HELIX    6   6 GLN B    3  VAL B   13  1                                  11    
HELIX    7   7 ARG B   14  LEU B   16  5                                   3    
HELIX    8   8 SER B   21  VAL B   37  1                                  17    
HELIX    9   9 ASP B   49  GLU B   61  1                                  13    
HELIX   10  10 SER B   66  GLY B   86  1                                  21    
LINK         O1A MYA A1088                ZN    ZN A1093     1555   5555  1.96  
LINK         O3A MYA A1088                ZN    ZN A1093     1555   1555  1.89  
LINK        ZN    ZN A1089                 OE2 GLU B   7     1555   1555  2.23  
LINK        ZN    ZN A1089                 O   HOH A2150     1555   1555  2.23  
LINK        ZN    ZN A1089                 O   HOH A2151     1555   1555  2.03  
LINK        ZN    ZN A1089                 NE2 HIS A  31     1555   1555  2.16  
LINK        ZN    ZN A1089                 OE1 GLU B   7     1555   1555  2.26  
LINK        ZN    ZN A1090                 O1  SO4 A1095     1555   5555  2.74  
LINK        ZN    ZN A1090                 O2  SO4 A1095     1555   9555  1.83  
LINK        ZN    ZN A1090                 O3  SO4 A1095     1555   5555  2.04  
LINK        ZN    ZN A1090                 O4  SO4 A1095     1555   1555  2.01  
LINK        ZN    ZN A1090                 O2A MYA A1088     1555   1555  2.13  
LINK        ZN    ZN A1090                 O3A MYA A1094     1555   5555  1.94  
LINK        ZN    ZN A1090                 O7A MYA A1094     1555   1555  1.84  
LINK        ZN    ZN A1090                 O2  SO4 A1095     5555   1555  1.83  
LINK        ZN    ZN A1090                 O3  SO4 A1095     9555   1555  2.04  
LINK        ZN    ZN A1090                 O3A MYA A1094     9555   1555  1.94  
LINK        ZN    ZN A1091                 N1A MYA A1094     1555   1555  2.03  
LINK        ZN    ZN A1091                 OE1 GLU A  11     1555   9555  1.95  
LINK        ZN    ZN A1091                 OD2 ASP A  22     1555   1555  1.89  
LINK        ZN    ZN A1091                 NE2 HIS A  15     1555   9555  1.95  
LINK        ZN    ZN A1091                 OD1 ASP A  22     1555   1555  2.69  
LINK        ZN    ZN A1092                 OD2 ASP B  69     1555  22545  2.05  
LINK        ZN    ZN A1092                 O   HOH A2152     1555   1555  2.61  
LINK        ZN    ZN A1092                 OE2 GLU A  68     1555   1555  2.55  
LINK        ZN    ZN A1092                 OD1 ASP B  69     1555  22545  2.18  
LINK        ZN    ZN A1093                 O2A MYA A1094     1555   1555  1.86  
LINK        ZN    ZN A1093                 O1  SO4 A1095     1555   1555  1.93  
LINK        ZN    ZN A1093                 O1A MYA A1088     1555   9555  1.96  
LINK        ZN    ZN A1093                 O2  SO4 A1095     1555   5555  2.28  
LINK         O8A MYA A1094                ZN    ZN A1096     1555   5555  1.98  
LINK         O8A MYA A1094                ZN    ZN A1096     1555   1555  1.97  
LINK        ZN    ZN A1096                 O3  SO4 A1095     1555   5555  2.19  
LINK        ZN    ZN A1096                 O3  SO4 A1095     1555   1555  2.16  
LINK        ZN    ZN A1096                 O8A MYA A1094     1555   9555  1.98  
LINK        ZN    ZN A1096                 O3  SO4 A1095     1555   9555  2.21  
LINK         O2A MYA B1088                ZN    ZN B1091     1555   1555  2.00  
LINK         O5A MYA B1088                ZN    ZN B1091     1555   1555  1.91  
LINK        ZN    ZN B1090                 OE2 GLU A  23     1555   1555  1.94  
LINK        ZN    ZN B1090                 O   HOH B2132     1555   1555  2.26  
LINK        ZN    ZN B1090                 NE2 HIS B  15     1555   1555  1.97  
LINK        ZN    ZN B1090                 OE1 GLU A  23     1555   1555  2.42  
LINK        ZN    ZN B1090                 O   HOH B2131     1555   1555  2.18  
LINK        ZN    ZN B1090                 OE2 GLU B  11     1555   1555  2.00  
LINK        ZN    ZN B1091                 O   HOH B2133     1555   1555  2.04  
LINK        ZN    ZN B1091                 OE1 GLU A   7     1555   9555  2.30  
LINK        ZN    ZN B1091                 O   HOH B2134     1555   1555  2.07  
LINK        ZN    ZN B1091                 OE2 GLU A   7     1555   9555  2.26  
SITE     1 AC1  4 HIS A  31  HOH A2150  HOH A2151  GLU B   7                    
SITE     1 AC2  4 MYA A1088   ZN A1093  MYA A1094  SO4 A1095                    
SITE     1 AC3  4 GLU A  11  HIS A  15  ASP A  22  MYA A1094                    
SITE     1 AC4  4 SER A   2  GLU A  68  HOH A2152  ASP B  69                    
SITE     1 AC5  4 MYA A1088   ZN A1090  MYA A1094  SO4 A1095                    
SITE     1 AC6  5 MYA A1088   ZN A1090   ZN A1093  MYA A1094                    
SITE     2 AC6  5  ZN A1096                                                     
SITE     1 AC7  2 MYA A1094  SO4 A1095                                          
SITE     1 AC8  5 GLU A  23  GLU B  11  HIS B  15  HOH B2131                    
SITE     2 AC8  5 HOH B2132                                                     
SITE     1 AC9  4 GLU A   7  MYA B1088  HOH B2133  HOH B2134                    
SITE     1 BC1 23 ALA A  10  ARG A  14  ILE A  28  TYR A  29                    
SITE     2 BC1 23 TYR A  32  LYS A  33  LYS A  55  TYR A  74                    
SITE     3 BC1 23  ZN A1090   ZN A1093  MYA A1094  SO4 A1095                    
SITE     4 BC1 23 HOH A2026  HOH A2100  HOH A2106  HOH A2143                    
SITE     5 BC1 23 HOH A2144  HOH A2145  HOH A2146  HOH A2147                    
SITE     6 BC1 23 HOH A2148  HOH A2149  MYA B1088                               
SITE     1 BC2 18 GLU A  11  ARG A  14  HIS A  15  LYS A  19                    
SITE     2 BC2 18 ASP A  22  THR A  51  MYA A1088   ZN A1090                    
SITE     3 BC2 18  ZN A1091   ZN A1093  SO4 A1095   ZN A1096                    
SITE     4 BC2 18 HOH A2025  HOH A2106  HOH A2153  HOH A2154                    
SITE     5 BC2 18 HOH A2155  MYA B1088                                          
SITE     1 BC3 35 ALA A   4  GLU A   7  LYS A   8  GLU A  11                    
SITE     2 BC3 35 ARG A  14  LYS A  19  ASP A  22  ARG A  44                    
SITE     3 BC3 35 LYS A  53  ALA A  54  ASP A  57  MYA A1088                    
SITE     4 BC3 35 MYA A1094  HOH A2114  ALA B  10  ARG B  14                    
SITE     5 BC3 35 ILE B  28  TYR B  29  TYR B  32  LYS B  33                    
SITE     6 BC3 35 LYS B  55  TYR B  74  MYA B1089   ZN B1091                    
SITE     7 BC3 35 HOH B2088  HOH B2123  HOH B2124  HOH B2125                    
SITE     8 BC3 35 HOH B2126  HOH B2127  HOH B2128  HOH B2129                    
SITE     9 BC3 35 HOH B2130  HOH B2133  HOH B2134                               
SITE     1 BC4  8 VAL B  13  ARG B  14  LEU B  16  LYS B  19                    
SITE     2 BC4  8 PRO B  20  MET B  25  MYA B1088  MXE B1092                    
SITE     1 BC5  5 ASP A  39  THR A  65  HOH A2077  MYA B1089                    
SITE     2 BC5  5 HOH B2045                                                     
CRYST1  118.490  118.490  118.490  90.00  90.00  90.00 I 2 3        48          
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      0.008440  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008440  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008440        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system