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Database: PDB
Entry: 2I80
LinkDB: 2I80
Original site: 2I80 
HEADER    LIGASE                                  31-AUG-06   2I80              
TITLE     ALLOSTERIC INHIBITION OF STAPHYLOCOCCUS AUREUS D-ALANINE:D-ALANINE    
TITLE    2 LIGASE REVEALED BY CRYSTALLOGRAPHIC STUDIES                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE-D-ALANINE LIGASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: D-ALANYLALANINE SYNTHETASE, D-ALA-D-ALA LIGASE;             
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 STRAIN: STRAIN COL;                                                  
SOURCE   5 GENE: DDL, DDLA;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: M15[PREP4];                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PQE-60                                    
KEYWDS    PROTEIN-INHIBITOR COMPLEX, LIGASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.LIU,J.S.CHANG,J.T.HERBERG,M.-M.HORNG,P.K.TOMICH,A.H.LIN,K.R.MAROTTI 
REVDAT   4   13-JUL-11 2I80    1       VERSN                                    
REVDAT   3   24-FEB-09 2I80    1       VERSN                                    
REVDAT   2   24-OCT-06 2I80    1       JRNL                                     
REVDAT   1   26-SEP-06 2I80    0                                                
JRNL        AUTH   S.LIU,J.S.CHANG,J.T.HERBERG,M.M.HORNG,P.K.TOMICH,A.H.LIN,    
JRNL        AUTH 2 K.R.MAROTTI                                                  
JRNL        TITL   ALLOSTERIC INHIBITION OF STAPHYLOCOCCUS AUREUS               
JRNL        TITL 2 D-ALANINE:D-ALANINE LIGASE REVEALED BY CRYSTALLOGRAPHIC      
JRNL        TITL 3 STUDIES.                                                     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 103 15178 2006              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   17015835                                                     
JRNL        DOI    10.1073/PNAS.0604905103                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0003                                      
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) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 79.06                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 31696                          
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) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1667                            
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) : 2.19                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.25                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1752                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 70.70                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1860                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 89                           
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5496                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 80                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 32.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.35000                                              
REMARK   3    B22 (A**2) : 0.71000                                              
REMARK   3    B33 (A**2) : -1.00000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.27000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.335         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.241         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.165         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.854        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5647 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  5008 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7653 ; 1.715 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11735 ; 0.864 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   688 ; 7.234 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   277 ;39.565 ;25.957       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   993 ;17.784 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;20.331 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   848 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6259 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1050 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1272 ; 0.225 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5304 ; 0.187 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2768 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3517 ; 0.092 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   182 ; 0.172 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.359 ; 0.200       
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):    32 ; 0.165 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    62 ; 0.229 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.222 ; 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):  4344 ; 1.220 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1401 ; 0.217 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5559 ; 1.517 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2568 ; 2.364 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2094 ; 3.475 ; 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  : 6                                          
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     3        A   125                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.9980   0.0850  -4.9130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0925 T22:   0.0062                                     
REMARK   3      T33:  -0.0438 T12:   0.0439                                     
REMARK   3      T13:   0.0423 T23:   0.0312                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8517 L22:   1.1428                                     
REMARK   3      L33:   3.4708 L12:   0.2203                                     
REMARK   3      L13:  -0.7548 L23:  -0.9285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0374 S12:   0.3100 S13:  -0.1070                       
REMARK   3      S21:  -0.1332 S22:  -0.1493 S23:  -0.1709                       
REMARK   3      S31:   0.2504 S32:   0.2279 S33:   0.1867                       
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 :   A   126        A   219                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.6770 -16.6140  20.8400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0782 T22:  -0.1003                                     
REMARK   3      T33:  -0.0452 T12:  -0.0595                                     
REMARK   3      T13:  -0.0152 T23:   0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3997 L22:   2.3813                                     
REMARK   3      L33:   2.3527 L12:  -0.8222                                     
REMARK   3      L13:   1.4470 L23:  -1.2374                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0996 S12:  -0.0952 S13:  -0.1905                       
REMARK   3      S21:  -0.0765 S22:   0.1218 S23:   0.1096                       
REMARK   3      S31:   0.5563 S32:  -0.2037 S33:  -0.2213                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   220        A   358                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.5180   1.3800   3.0950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1185 T22:  -0.0312                                     
REMARK   3      T33:  -0.0037 T12:   0.0081                                     
REMARK   3      T13:  -0.0106 T23:   0.0211                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8108 L22:   1.5539                                     
REMARK   3      L33:   1.0366 L12:   1.0123                                     
REMARK   3      L13:  -0.3552 L23:  -0.1576                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0170 S12:   0.1650 S13:   0.0574                       
REMARK   3      S21:  -0.0482 S22:   0.0229 S23:   0.1631                       
REMARK   3      S31:  -0.0223 S32:  -0.1590 S33:  -0.0399                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     3        B   125                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.1500   2.8980  17.4060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0760 T22:   0.0778                                     
REMARK   3      T33:  -0.0481 T12:  -0.0467                                     
REMARK   3      T13:  -0.0161 T23:   0.0460                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0499 L22:   0.9020                                     
REMARK   3      L33:   3.3656 L12:   0.3708                                     
REMARK   3      L13:   0.1157 L23:   0.4811                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0377 S12:   0.3088 S13:   0.0986                       
REMARK   3      S21:   0.0483 S22:   0.0559 S23:  -0.0761                       
REMARK   3      S31:  -0.3602 S32:   0.6227 S33:  -0.0182                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   126        B   219                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9860  14.8290  26.4650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0155 T22:  -0.0880                                     
REMARK   3      T33:  -0.0255 T12:   0.0326                                     
REMARK   3      T13:   0.0101 T23:  -0.0259                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5807 L22:   3.0711                                     
REMARK   3      L33:   3.8770 L12:  -0.8968                                     
REMARK   3      L13:   0.3890 L23:  -1.1667                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1369 S12:  -0.0357 S13:   0.0330                       
REMARK   3      S21:   0.1747 S22:   0.1560 S23:   0.0753                       
REMARK   3      S31:  -0.5331 S32:  -0.2494 S33:  -0.0190                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   220        B   360                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.4820  -2.3170  33.6190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0087 T22:  -0.0892                                     
REMARK   3      T33:  -0.0579 T12:   0.0067                                     
REMARK   3      T13:  -0.0117 T23:   0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5624 L22:   1.2229                                     
REMARK   3      L33:   2.0389 L12:  -0.5306                                     
REMARK   3      L13:  -0.4701 L23:   0.5289                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0486 S12:  -0.0391 S13:  -0.0588                       
REMARK   3      S21:   0.2259 S22:  -0.0352 S23:   0.0067                       
REMARK   3      S31:   0.0539 S32:   0.1413 S33:   0.0838                       
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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2I80 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-SEP-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB039252.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-01                          
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) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33377                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 79.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : 0.05200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.17700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.810                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1EHI                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       33.04100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     TYR A   246                                                      
REMARK 465     ASP A   247                                                      
REMARK 465     TYR A   248                                                      
REMARK 465     LYS A   249                                                      
REMARK 465     SER A   250                                                      
REMARK 465     LYS A   251                                                      
REMARK 465     TYR A   252                                                      
REMARK 465     LYS A   253                                                      
REMARK 465     ASP A   254                                                      
REMARK 465     GLY A   255                                                      
REMARK 465     LYS A   256                                                      
REMARK 465     HIS A   359                                                      
REMARK 465     HIS A   360                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     TYR B   246                                                      
REMARK 465     ASP B   247                                                      
REMARK 465     TYR B   248                                                      
REMARK 465     LYS B   249                                                      
REMARK 465     SER B   250                                                      
REMARK 465     LYS B   251                                                      
REMARK 465     TYR B   252                                                      
REMARK 465     LYS B   253                                                      
REMARK 465     ASP B   254                                                      
REMARK 465     GLY B   255                                                      
REMARK 465     LYS B   256                                                      
REMARK 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   NZ   LYS A   352     OD1  ASN B    99              1.85            
REMARK 500   N    GLY B    97     O    GLU B   101              2.07            
REMARK 500   O    PHE A   206     OD1  ASN B   351              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A   7   CB    CYS A   7   SG     -0.097                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 152   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 219   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 219   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  14      150.26    -37.53                                   
REMARK 500    ALA A  15       -5.90    -58.58                                   
REMARK 500    ASN A  54       62.52     63.23                                   
REMARK 500    LEU A  67     -112.73     53.15                                   
REMARK 500    LEU A 181      160.54     55.88                                   
REMARK 500    SER A 183        5.31     54.36                                   
REMARK 500    SER A 184     -133.66    -96.95                                   
REMARK 500    ASN A 228      -82.08   -119.99                                   
REMARK 500    ASP A 299       36.14    -97.88                                   
REMARK 500    ASN A 300       26.82     49.77                                   
REMARK 500    PHE A 313       20.75   -141.39                                   
REMARK 500    ALA B  15       41.97    -77.99                                   
REMARK 500    ASN B  45       49.86    -69.00                                   
REMARK 500    ASP B  46      -17.07   -154.78                                   
REMARK 500    GLU B  71       95.60    -50.72                                   
REMARK 500    ALA B  72      -22.68    -37.15                                   
REMARK 500    LEU B  73      166.94    -48.69                                   
REMARK 500    LEU B  94       48.74    -86.41                                   
REMARK 500    PRO B  98       10.58    -53.55                                   
REMARK 500    ASN B 228      -83.63   -125.15                                   
REMARK 500    ASN B 305      -62.64    -92.42                                   
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 ARG A  357     SER A  358                  145.34                    
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 G1L A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G1L B 400                 
DBREF  2I80 A    1   356  UNP    Q5HEB7   DDL_STAAC        1    356             
DBREF  2I80 B    1   356  UNP    Q5HEB7   DDL_STAAC        1    356             
SEQADV 2I80 ARG A  357  UNP  Q5HEB7              CLONING ARTIFACT               
SEQADV 2I80 SER A  358  UNP  Q5HEB7              CLONING ARTIFACT               
SEQADV 2I80 HIS A  359  UNP  Q5HEB7              CLONING ARTIFACT               
SEQADV 2I80 HIS A  360  UNP  Q5HEB7              CLONING ARTIFACT               
SEQADV 2I80 ARG B  357  UNP  Q5HEB7              CLONING ARTIFACT               
SEQADV 2I80 SER B  358  UNP  Q5HEB7              CLONING ARTIFACT               
SEQADV 2I80 HIS B  359  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I80 HIS B  360  UNP  Q5HEB7              EXPRESSION TAG                 
SEQRES   1 A  360  MET THR LYS GLU ASN ILE CYS ILE VAL PHE GLY GLY LYS          
SEQRES   2 A  360  SER ALA GLU HIS GLU VAL SER ILE LEU THR ALA GLN ASN          
SEQRES   3 A  360  VAL LEU ASN ALA ILE ASP LYS ASP LYS TYR HIS VAL ASP          
SEQRES   4 A  360  ILE ILE TYR ILE THR ASN ASP GLY ASP TRP ARG LYS GLN          
SEQRES   5 A  360  ASN ASN ILE THR ALA GLU ILE LYS SER THR ASP GLU LEU          
SEQRES   6 A  360  HIS LEU GLU ASN GLY GLU ALA LEU GLU ILE SER GLN LEU          
SEQRES   7 A  360  LEU LYS GLU SER SER SER GLY GLN PRO TYR ASP ALA VAL          
SEQRES   8 A  360  PHE PRO LEU LEU HIS GLY PRO ASN GLY GLU ASP GLY THR          
SEQRES   9 A  360  ILE GLN GLY LEU PHE GLU VAL LEU ASP VAL PRO TYR VAL          
SEQRES  10 A  360  GLY ASN GLY VAL LEU SER ALA ALA SER SER MET ASP LYS          
SEQRES  11 A  360  LEU VAL MET LYS GLN LEU PHE GLU HIS ARG GLY LEU PRO          
SEQRES  12 A  360  GLN LEU PRO TYR ILE SER PHE LEU ARG SER GLU TYR GLU          
SEQRES  13 A  360  LYS TYR GLU HIS ASN ILE LEU LYS LEU VAL ASN ASP LYS          
SEQRES  14 A  360  LEU ASN TYR PRO VAL PHE VAL LYS PRO ALA ASN LEU GLY          
SEQRES  15 A  360  SER SER VAL GLY ILE SER LYS CYS ASN ASN GLU ALA GLU          
SEQRES  16 A  360  LEU LYS GLU GLY ILE LYS GLU ALA PHE GLN PHE ASP ARG          
SEQRES  17 A  360  LYS LEU VAL ILE GLU GLN GLY VAL ASN ALA ARG GLU ILE          
SEQRES  18 A  360  GLU VAL ALA VAL LEU GLY ASN ASP TYR PRO GLU ALA THR          
SEQRES  19 A  360  TRP PRO GLY GLU VAL VAL LYS ASP VAL ALA PHE TYR ASP          
SEQRES  20 A  360  TYR LYS SER LYS TYR LYS ASP GLY LYS VAL GLN LEU GLN          
SEQRES  21 A  360  ILE PRO ALA ASP LEU ASP GLU ASP VAL GLN LEU THR LEU          
SEQRES  22 A  360  ARG ASN MET ALA LEU GLU ALA PHE LYS ALA THR ASP CYS          
SEQRES  23 A  360  SER GLY LEU VAL ARG ALA ASP PHE PHE VAL THR GLU ASP          
SEQRES  24 A  360  ASN GLN ILE TYR ILE ASN GLU THR ASN ALA MET PRO GLY          
SEQRES  25 A  360  PHE THR ALA PHE SER MET TYR PRO LYS LEU TRP GLU ASN          
SEQRES  26 A  360  MET GLY LEU SER TYR PRO GLU LEU ILE THR LYS LEU ILE          
SEQRES  27 A  360  GLU LEU ALA LYS GLU ARG HIS GLN ASP LYS GLN LYS ASN          
SEQRES  28 A  360  LYS TYR LYS ILE ASP ARG SER HIS HIS                          
SEQRES   1 B  360  MET THR LYS GLU ASN ILE CYS ILE VAL PHE GLY GLY LYS          
SEQRES   2 B  360  SER ALA GLU HIS GLU VAL SER ILE LEU THR ALA GLN ASN          
SEQRES   3 B  360  VAL LEU ASN ALA ILE ASP LYS ASP LYS TYR HIS VAL ASP          
SEQRES   4 B  360  ILE ILE TYR ILE THR ASN ASP GLY ASP TRP ARG LYS GLN          
SEQRES   5 B  360  ASN ASN ILE THR ALA GLU ILE LYS SER THR ASP GLU LEU          
SEQRES   6 B  360  HIS LEU GLU ASN GLY GLU ALA LEU GLU ILE SER GLN LEU          
SEQRES   7 B  360  LEU LYS GLU SER SER SER GLY GLN PRO TYR ASP ALA VAL          
SEQRES   8 B  360  PHE PRO LEU LEU HIS GLY PRO ASN GLY GLU ASP GLY THR          
SEQRES   9 B  360  ILE GLN GLY LEU PHE GLU VAL LEU ASP VAL PRO TYR VAL          
SEQRES  10 B  360  GLY ASN GLY VAL LEU SER ALA ALA SER SER MET ASP LYS          
SEQRES  11 B  360  LEU VAL MET LYS GLN LEU PHE GLU HIS ARG GLY LEU PRO          
SEQRES  12 B  360  GLN LEU PRO TYR ILE SER PHE LEU ARG SER GLU TYR GLU          
SEQRES  13 B  360  LYS TYR GLU HIS ASN ILE LEU LYS LEU VAL ASN ASP LYS          
SEQRES  14 B  360  LEU ASN TYR PRO VAL PHE VAL LYS PRO ALA ASN LEU GLY          
SEQRES  15 B  360  SER SER VAL GLY ILE SER LYS CYS ASN ASN GLU ALA GLU          
SEQRES  16 B  360  LEU LYS GLU GLY ILE LYS GLU ALA PHE GLN PHE ASP ARG          
SEQRES  17 B  360  LYS LEU VAL ILE GLU GLN GLY VAL ASN ALA ARG GLU ILE          
SEQRES  18 B  360  GLU VAL ALA VAL LEU GLY ASN ASP TYR PRO GLU ALA THR          
SEQRES  19 B  360  TRP PRO GLY GLU VAL VAL LYS ASP VAL ALA PHE TYR ASP          
SEQRES  20 B  360  TYR LYS SER LYS TYR LYS ASP GLY LYS VAL GLN LEU GLN          
SEQRES  21 B  360  ILE PRO ALA ASP LEU ASP GLU ASP VAL GLN LEU THR LEU          
SEQRES  22 B  360  ARG ASN MET ALA LEU GLU ALA PHE LYS ALA THR ASP CYS          
SEQRES  23 B  360  SER GLY LEU VAL ARG ALA ASP PHE PHE VAL THR GLU ASP          
SEQRES  24 B  360  ASN GLN ILE TYR ILE ASN GLU THR ASN ALA MET PRO GLY          
SEQRES  25 B  360  PHE THR ALA PHE SER MET TYR PRO LYS LEU TRP GLU ASN          
SEQRES  26 B  360  MET GLY LEU SER TYR PRO GLU LEU ILE THR LYS LEU ILE          
SEQRES  27 B  360  GLU LEU ALA LYS GLU ARG HIS GLN ASP LYS GLN LYS ASN          
SEQRES  28 B  360  LYS TYR LYS ILE ASP ARG SER HIS HIS                          
HET    G1L  A 400      36                                                       
HET    G1L  B 400      18                                                       
HETNAM     G1L 3-CHLORO-2,2-DIMETHYL-N-[4-(TRIFLUOROMETHYL)                     
HETNAM   2 G1L  PHENYL]PROPANAMIDE                                              
FORMUL   3  G1L    2(C12 H13 CL F3 N O)                                         
FORMUL   5  HOH   *80(H2 O)                                                     
HELIX    1   1 GLU A   16  ALA A   30  1                                  15    
HELIX    2   2 SER A   61  LEU A   65  5                                   5    
HELIX    3   3 HIS A   66  GLY A   70  5                                   5    
HELIX    4   4 SER A   76  GLU A   81  5                                   6    
HELIX    5   5 GLY A  103  LEU A  112  1                                  10    
HELIX    6   6 GLY A  120  MET A  128  1                                   9    
HELIX    7   7 ASP A  129  ARG A  140  1                                  12    
HELIX    8   8 ARG A  152  LEU A  170  1                                  19    
HELIX    9   9 ASN A  192  PHE A  204  1                                  13    
HELIX   10  10 ASP A  266  THR A  284  1                                  19    
HELIX   11  11 SER A  317  ASN A  325  1                                   9    
HELIX   12  12 SER A  329  ARG A  357  1                                  29    
HELIX   13  13 GLU B   16  ILE B   31  1                                  16    
HELIX   14  14 SER B   61  HIS B   66  5                                   6    
HELIX   15  15 GLU B   74  GLU B   81  1                                   8    
HELIX   16  16 GLY B  103  ASP B  113  1                                  11    
HELIX   17  17 GLY B  120  ASP B  129  1                                  10    
HELIX   18  18 ASP B  129  GLY B  141  1                                  13    
HELIX   19  19 ARG B  152  LEU B  170  1                                  19    
HELIX   20  20 ASN B  192  GLN B  205  1                                  14    
HELIX   21  21 ASP B  266  THR B  284  1                                  19    
HELIX   22  22 SER B  317  MET B  326  1                                  10    
HELIX   23  23 SER B  329  HIS B  360  1                                  32    
SHEET    1   A 5 GLU A  71  LEU A  73  0                                        
SHEET    2   A 5 TRP A  49  GLN A  52 -1  N  LYS A  51   O  GLU A  71           
SHEET    3   A 5 TYR A  36  ILE A  43 -1  N  ILE A  40   O  GLN A  52           
SHEET    4   A 5 GLU A   4  GLY A  11  1  N  GLU A   4   O  HIS A  37           
SHEET    5   A 5 ALA A  90  LEU A  94  1  O  PHE A  92   N  VAL A   9           
SHEET    1   B 4 TYR A 147  LEU A 151  0                                        
SHEET    2   B 4 LYS A 209  GLN A 214 -1  O  ILE A 212   N  ILE A 148           
SHEET    3   B 4 VAL A 174  PRO A 178 -1  N  PHE A 175   O  GLU A 213           
SHEET    4   B 4 SER A 188  CYS A 190 -1  O  CYS A 190   N  VAL A 174           
SHEET    1   C 4 GLU A 232  ALA A 233  0                                        
SHEET    2   C 4 ARG A 219  GLY A 227 -1  N  LEU A 226   O  GLU A 232           
SHEET    3   C 4 GLY A 237  VAL A 239 -1  O  GLY A 237   N  GLU A 222           
SHEET    4   C 4 LEU A 259  GLN A 260 -1  O  GLN A 260   N  GLU A 238           
SHEET    1   D 4 GLU A 232  ALA A 233  0                                        
SHEET    2   D 4 ARG A 219  GLY A 227 -1  N  LEU A 226   O  GLU A 232           
SHEET    3   D 4 GLY A 288  VAL A 296 -1  O  PHE A 294   N  ILE A 221           
SHEET    4   D 4 ILE A 302  ASN A 308 -1  O  TYR A 303   N  PHE A 295           
SHEET    1   E 4 TRP B  49  GLN B  52  0                                        
SHEET    2   E 4 TYR B  36  ILE B  43 -1  N  TYR B  42   O  ARG B  50           
SHEET    3   E 4 GLU B   4  GLY B  11  1  N  GLU B   4   O  HIS B  37           
SHEET    4   E 4 ALA B  90  PRO B  93  1  O  PHE B  92   N  VAL B   9           
SHEET    1   F 4 TYR B 147  LEU B 151  0                                        
SHEET    2   F 4 LYS B 209  GLN B 214 -1  O  ILE B 212   N  ILE B 148           
SHEET    3   F 4 VAL B 174  PRO B 178 -1  N  PHE B 175   O  GLU B 213           
SHEET    4   F 4 SER B 188  CYS B 190 -1  O  CYS B 190   N  VAL B 174           
SHEET    1   G 4 GLU B 232  ALA B 233  0                                        
SHEET    2   G 4 ARG B 219  GLY B 227 -1  N  LEU B 226   O  GLU B 232           
SHEET    3   G 4 GLY B 237  VAL B 239 -1  O  GLY B 237   N  GLU B 222           
SHEET    4   G 4 LEU B 259  GLN B 260 -1  O  GLN B 260   N  GLU B 238           
SHEET    1   H 4 GLU B 232  ALA B 233  0                                        
SHEET    2   H 4 ARG B 219  GLY B 227 -1  N  LEU B 226   O  GLU B 232           
SHEET    3   H 4 GLY B 288  VAL B 296 -1  O  PHE B 294   N  ILE B 221           
SHEET    4   H 4 ILE B 302  ASN B 308 -1  O  TYR B 303   N  PHE B 295           
CISPEP   1 TYR A  172    PRO A  173          0        -5.08                     
CISPEP   2 ILE A  261    PRO A  262          0        -0.34                     
CISPEP   3 TYR B  172    PRO B  173          0        -7.21                     
CISPEP   4 ILE B  261    PRO B  262          0        -0.56                     
SITE     1 AC1 14 SER A  20  THR A  23  PHE A  92  PRO A  93                    
SITE     2 AC1 14 LEU A  94  LEU A  95  HIS A  96  VAL A 117                    
SITE     3 AC1 14 GLY A 118  LEU A 289  MET A 310  PRO A 311                    
SITE     4 AC1 14 GLY A 312  HOH A 414                                          
SITE     1 AC2 11 GLU B  16  PHE B  92  PRO B  93  LEU B  94                    
SITE     2 AC2 11 LEU B  95  HIS B  96  VAL B 117  GLY B 118                    
SITE     3 AC2 11 LEU B 289  MET B 310  PRO B 311                               
CRYST1   67.730   66.082   78.789  90.00  96.57  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014765  0.000000  0.001700        0.00000                         
SCALE2      0.000000  0.015133  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012776        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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