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Database: PDB
Entry: 3OO2
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HEADER    ISOMERASE                               30-AUG-10   3OO2              
TITLE     2.37 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF AN ALANINE RACEMASE     
TITLE    2 (ALR) FROM STAPHYLOCOCCUS AUREUS SUBSP. AUREUS COL                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE RACEMASE 1;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;            
SOURCE   3 ORGANISM_TAXID: 93062;                                               
SOURCE   4 STRAIN: COL;                                                         
SOURCE   5 GENE: ALR, ALR1, SACOL2060;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/MAGIC;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    ALANINE RACEMASE, INFECTIOUS DISEASES, CENTER FOR STRUCTURAL GENOMICS 
KEYWDS   2 OF INFECTIOUS DISEASES (CSGID), ALANINE AND ASPARTATE METABOLISM AND 
KEYWDS   3 D-ALANINE METABOLISM, BIOSYNTHESIS AND DEGRADATION OF MUREIN         
KEYWDS   4 SACCULUS AND PEPTIDOGLYCAN, ISOMERASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.S.HALAVATY,L.SHUVALOVA,G.MINASOV,J.WINSOR,I.DUBROVSKA,K.KWON,       
AUTHOR   2 W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES   
AUTHOR   3 (CSGID)                                                              
REVDAT   1   06-OCT-10 3OO2    0                                                
JRNL        AUTH   A.S.HALAVATY,L.SHUVALOVA,G.MINASOV,J.WINSOR,I.DUBROVSKA,     
JRNL        AUTH 2 K.KWON,W.F.ANDERSON,                                         
JRNL        AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES        
JRNL        AUTH 4 (CSGID)                                                      
JRNL        TITL   2.37 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF AN ALANINE     
JRNL        TITL 2 RACEMASE (ALR) FROM STAPHYLOCOCCUS AUREUS SUBSP. AUREUS COL  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.37 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 2.37                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.59                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 28741                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1533                            
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) : 2.37                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.43                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2042                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.08                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 103                          
REMARK   3   BIN FREE R VALUE                    : 0.3650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5866                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 120                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.52000                                              
REMARK   3    B22 (A**2) : -1.62000                                             
REMARK   3    B33 (A**2) : 0.10000                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.285         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.218         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.971        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6051 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  4049 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8196 ; 1.567 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9932 ; 0.835 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   750 ; 3.007 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   273 ;29.905 ;24.689       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1081 ;11.545 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;14.623 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   933 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6682 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1160 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  3731 ; 1.105 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1513 ; 0.299 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6058 ; 1.949 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2320 ; 3.317 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2138 ; 4.850 ; 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     2        A   174                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.6358  53.2467 -10.2212              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0651 T22:   0.1110                                     
REMARK   3      T33:   0.1167 T12:  -0.0417                                     
REMARK   3      T13:  -0.0502 T23:   0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1587 L22:   2.1201                                     
REMARK   3      L33:   1.4655 L12:   0.8539                                     
REMARK   3      L13:  -0.1829 L23:   0.2976                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2172 S12:   0.1787 S13:  -0.0096                       
REMARK   3      S21:  -0.2563 S22:   0.0246 S23:   0.2592                       
REMARK   3      S31:  -0.0687 S32:  -0.1987 S33:   0.1925                       
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   175        A   269                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.8424  58.3328 -14.2222              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1352 T22:   0.1853                                     
REMARK   3      T33:   0.0201 T12:  -0.0963                                     
REMARK   3      T13:   0.0291 T23:   0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0595 L22:   2.5667                                     
REMARK   3      L33:   1.7450 L12:   0.4976                                     
REMARK   3      L13:  -0.1101 L23:   1.3320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2499 S12:   0.3557 S13:  -0.0490                       
REMARK   3      S21:  -0.5333 S22:   0.2619 S23:  -0.0976                       
REMARK   3      S31:  -0.2469 S32:   0.1609 S33:  -0.0120                       
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   270        A   382                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.0823  73.8442   0.4201              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1454 T22:   0.0816                                     
REMARK   3      T33:   0.0924 T12:  -0.0883                                     
REMARK   3      T13:  -0.0105 T23:   0.0512                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6508 L22:   1.7129                                     
REMARK   3      L33:   1.6845 L12:   0.2955                                     
REMARK   3      L13:   0.3235 L23:   0.6737                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0898 S12:   0.1323 S13:   0.2106                       
REMARK   3      S21:  -0.2788 S22:   0.1037 S23:  -0.1884                       
REMARK   3      S31:  -0.4397 S32:   0.1999 S33:  -0.0140                       
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     2        B   133                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.7112  75.8146  19.6582              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0545 T22:   0.1728                                     
REMARK   3      T33:   0.1026 T12:   0.0132                                     
REMARK   3      T13:  -0.0147 T23:  -0.0482                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2878 L22:   3.7578                                     
REMARK   3      L33:   1.1237 L12:   0.7871                                     
REMARK   3      L13:   0.5574 L23:   1.2069                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0073 S12:  -0.2201 S13:   0.1975                       
REMARK   3      S21:   0.1084 S22:  -0.2944 S23:   0.4285                       
REMARK   3      S31:  -0.0934 S32:  -0.3360 S33:   0.2871                       
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   134        B   200                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.5673  85.7827  28.0407              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2075 T22:   0.1557                                     
REMARK   3      T33:   0.1744 T12:  -0.0799                                     
REMARK   3      T13:  -0.1091 T23:   0.0203                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6551 L22:   4.9371                                     
REMARK   3      L33:   4.5033 L12:  -2.4659                                     
REMARK   3      L13:   0.1869 L23:  -0.6157                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0913 S12:  -0.1444 S13:   0.6552                       
REMARK   3      S21:   0.6680 S22:  -0.1613 S23:  -0.5345                       
REMARK   3      S31:   0.1054 S32:   0.2453 S33:   0.2526                       
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   201        B   382                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1354  53.0417  13.8799              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0746 T22:   0.0711                                     
REMARK   3      T33:   0.0749 T12:  -0.0326                                     
REMARK   3      T13:  -0.0202 T23:   0.0694                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4348 L22:   2.5931                                     
REMARK   3      L33:   1.8772 L12:   0.3096                                     
REMARK   3      L13:   0.5670 L23:   1.2946                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0684 S12:  -0.1267 S13:  -0.1975                       
REMARK   3      S21:   0.4174 S22:  -0.0668 S23:   0.0037                       
REMARK   3      S31:   0.2058 S32:  -0.0013 S33:  -0.0016                       
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 3OO2 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061358.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-AUG-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : DIAMOND[111]                       
REMARK 200  OPTICS                         : BE-LENSES/DIAMOND LAUE MONO        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30323                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.370                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.3600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.660                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: BALBES MODEL                                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 7.6 MG/ML PROTEIN IN 10 MM TRIS/HCL PH   
REMARK 280  8.3, 0.5 M NACL, 5 MM BME. CRYSTALS GREW FROM 0.1 M MIB BUFFER PH   
REMARK 280  5.0, 25 % (W/V) PEG1500 (THE PACT SUITE CONDITION #14), VAPOR       
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 295K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       23.86750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.50400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.15500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.50400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.86750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.15500            
REMARK 290   SMTRY3   4  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: 7200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 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     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A   267                                                      
REMARK 465     THR A   268                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B   120                                                      
REMARK 465     GLU B   121                                                      
REMARK 465     GLN B   122                                                      
REMARK 465     GLU B   123                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLU B   261                                                      
REMARK 465     SER B   262                                                      
REMARK 465     VAL B   263                                                      
REMARK 465     SER B   264                                                      
REMARK 465     TYR B   265                                                      
REMARK 465     GLY B   266                                                      
REMARK 465     ALA B   267                                                      
REMARK 465     THR B   268                                                      
REMARK 465     TYR B   269                                                      
REMARK 465     THR B   270                                                      
REMARK 465     ALA B   271                                                      
REMARK 465     THR B   272                                                      
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    MET A 136       90.89    -56.29                                   
REMARK 500    ARG A 138      -86.54   -118.04                                   
REMARK 500    GLN A 253      149.95   -171.93                                   
REMARK 500    ASN A 300       48.98     36.55                                   
REMARK 500    ASN A 334       54.08    -90.64                                   
REMARK 500    LEU A 360      105.83    -53.59                                   
REMARK 500    ALA B  90      -55.04    -28.55                                   
REMARK 500    LYS B  91      -59.73    -26.35                                   
REMARK 500    ILE B 115       43.02    -73.55                                   
REMARK 500    LYS B 116      -14.49   -145.19                                   
REMARK 500    ARG B 138      100.68    -26.66                                   
REMARK 500    LEU B 139      134.23    -23.13                                   
REMARK 500    CYS B 212       72.34     49.15                                   
REMARK 500    VAL B 239      127.95    -32.38                                   
REMARK 500    ASN B 334       41.75    -84.14                                   
REMARK 500    THR B 351     -157.78   -148.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              NA A 383  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 160   O                                                      
REMARK 620 2 TYR A 157   O    99.1                                              
REMARK 620 3 ILE A 154   O    96.8  72.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 383  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE B 154   O                                                      
REMARK 620 2 LEU B 160   O   105.2                                              
REMARK 620 3 HOH B 446   O    76.7 148.2                                        
REMARK 620 4 TYR B 157   O    72.1  83.9  66.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 383                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 384                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 385                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 386                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 383                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 384                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 385                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: IDP00688   RELATED DB: TARGETDB                          
DBREF  3OO2 A    1   382  UNP    Q5HED1   ALR1_STAAC       1    382             
DBREF  3OO2 B    1   382  UNP    Q5HED1   ALR1_STAAC       1    382             
SEQADV 3OO2 SER A   -2  UNP  Q5HED1              EXPRESSION TAG                 
SEQADV 3OO2 ASN A   -1  UNP  Q5HED1              EXPRESSION TAG                 
SEQADV 3OO2 ALA A    0  UNP  Q5HED1              EXPRESSION TAG                 
SEQADV 3OO2 SER B   -2  UNP  Q5HED1              EXPRESSION TAG                 
SEQADV 3OO2 ASN B   -1  UNP  Q5HED1              EXPRESSION TAG                 
SEQADV 3OO2 ALA B    0  UNP  Q5HED1              EXPRESSION TAG                 
SEQRES   1 A  385  SER ASN ALA MET SER ASP LYS TYR TYR ARG SER ALA TYR          
SEQRES   2 A  385  MET ASN VAL ASP LEU ASN ALA VAL ALA SER ASN PHE LYS          
SEQRES   3 A  385  VAL PHE SER THR LEU HIS PRO ASN LYS THR VAL MET ALA          
SEQRES   4 A  385  VAL VAL LYS ALA ASN ALA TYR GLY LEU GLY SER VAL LYS          
SEQRES   5 A  385  VAL ALA ARG HIS LEU MET GLU ASN GLY ALA THR PHE PHE          
SEQRES   6 A  385  ALA VAL ALA THR LEU ASP GLU ALA ILE GLU LEU ARG MET          
SEQRES   7 A  385  HIS GLY ILE THR ALA LYS ILE LEU VAL LEU GLY VAL LEU          
SEQRES   8 A  385  PRO ALA LYS ASP ILE ASP LYS ALA ILE GLN HIS ARG VAL          
SEQRES   9 A  385  ALA LEU THR VAL PRO SER LYS GLN TRP LEU LYS GLU ALA          
SEQRES  10 A  385  ILE LYS ASN ILE SER GLY GLU GLN GLU LYS LYS LEU TRP          
SEQRES  11 A  385  LEU HIS ILE LYS LEU ASP THR GLY MET GLY ARG LEU GLY          
SEQRES  12 A  385  ILE LYS ASP THR LYS THR TYR GLN GLU VAL ILE GLU ILE          
SEQRES  13 A  385  ILE GLN GLN TYR GLU GLN LEU VAL PHE GLU GLY VAL PHE          
SEQRES  14 A  385  THR HIS PHE ALA CYS ALA ASP GLU PRO GLY ASP MET THR          
SEQRES  15 A  385  THR GLU GLN TYR GLN ARG PHE LYS ASP MET VAL ASN GLU          
SEQRES  16 A  385  ALA ILE LYS PRO GLU TYR ILE HIS CYS GLN ASN SER ALA          
SEQRES  17 A  385  GLY SER LEU LEU MET ASP CYS GLN PHE CYS ASN ALA ILE          
SEQRES  18 A  385  ARG PRO GLY ILE SER LEU TYR GLY TYR TYR PRO SER GLU          
SEQRES  19 A  385  TYR VAL GLN GLN LYS VAL LYS VAL HIS LEU LYS PRO SER          
SEQRES  20 A  385  VAL GLN LEU ILE ALA ASN VAL VAL GLN THR LYS THR LEU          
SEQRES  21 A  385  GLN ALA GLY GLU SER VAL SER TYR GLY ALA THR TYR THR          
SEQRES  22 A  385  ALA THR ASP PRO THR THR ILE ALA LEU LEU PRO ILE GLY          
SEQRES  23 A  385  TYR ALA ASP GLY TYR LEU ARG ILE MET GLN GLY SER PHE          
SEQRES  24 A  385  VAL ASN VAL ASN GLY HIS GLN CYS GLU VAL ILE GLY ARG          
SEQRES  25 A  385  VAL CYS MET ASP GLN THR ILE VAL LYS VAL PRO ASP GLN          
SEQRES  26 A  385  VAL LYS ALA GLY ASP SER VAL ILE LEU ILE ASP ASN HIS          
SEQRES  27 A  385  ARG GLU SER PRO GLN SER VAL GLU VAL VAL ALA GLU LYS          
SEQRES  28 A  385  GLN HIS THR ILE ASN TYR GLU VAL LEU CYS ASN LEU SER          
SEQRES  29 A  385  ARG ARG LEU PRO ARG ILE TYR HIS ASP GLY ASP GLN ARG          
SEQRES  30 A  385  PHE VAL THR ASN GLU LEU LEU LYS                              
SEQRES   1 B  385  SER ASN ALA MET SER ASP LYS TYR TYR ARG SER ALA TYR          
SEQRES   2 B  385  MET ASN VAL ASP LEU ASN ALA VAL ALA SER ASN PHE LYS          
SEQRES   3 B  385  VAL PHE SER THR LEU HIS PRO ASN LYS THR VAL MET ALA          
SEQRES   4 B  385  VAL VAL LYS ALA ASN ALA TYR GLY LEU GLY SER VAL LYS          
SEQRES   5 B  385  VAL ALA ARG HIS LEU MET GLU ASN GLY ALA THR PHE PHE          
SEQRES   6 B  385  ALA VAL ALA THR LEU ASP GLU ALA ILE GLU LEU ARG MET          
SEQRES   7 B  385  HIS GLY ILE THR ALA LYS ILE LEU VAL LEU GLY VAL LEU          
SEQRES   8 B  385  PRO ALA LYS ASP ILE ASP LYS ALA ILE GLN HIS ARG VAL          
SEQRES   9 B  385  ALA LEU THR VAL PRO SER LYS GLN TRP LEU LYS GLU ALA          
SEQRES  10 B  385  ILE LYS ASN ILE SER GLY GLU GLN GLU LYS LYS LEU TRP          
SEQRES  11 B  385  LEU HIS ILE LYS LEU ASP THR GLY MET GLY ARG LEU GLY          
SEQRES  12 B  385  ILE LYS ASP THR LYS THR TYR GLN GLU VAL ILE GLU ILE          
SEQRES  13 B  385  ILE GLN GLN TYR GLU GLN LEU VAL PHE GLU GLY VAL PHE          
SEQRES  14 B  385  THR HIS PHE ALA CYS ALA ASP GLU PRO GLY ASP MET THR          
SEQRES  15 B  385  THR GLU GLN TYR GLN ARG PHE LYS ASP MET VAL ASN GLU          
SEQRES  16 B  385  ALA ILE LYS PRO GLU TYR ILE HIS CYS GLN ASN SER ALA          
SEQRES  17 B  385  GLY SER LEU LEU MET ASP CYS GLN PHE CYS ASN ALA ILE          
SEQRES  18 B  385  ARG PRO GLY ILE SER LEU TYR GLY TYR TYR PRO SER GLU          
SEQRES  19 B  385  TYR VAL GLN GLN LYS VAL LYS VAL HIS LEU LYS PRO SER          
SEQRES  20 B  385  VAL GLN LEU ILE ALA ASN VAL VAL GLN THR LYS THR LEU          
SEQRES  21 B  385  GLN ALA GLY GLU SER VAL SER TYR GLY ALA THR TYR THR          
SEQRES  22 B  385  ALA THR ASP PRO THR THR ILE ALA LEU LEU PRO ILE GLY          
SEQRES  23 B  385  TYR ALA ASP GLY TYR LEU ARG ILE MET GLN GLY SER PHE          
SEQRES  24 B  385  VAL ASN VAL ASN GLY HIS GLN CYS GLU VAL ILE GLY ARG          
SEQRES  25 B  385  VAL CYS MET ASP GLN THR ILE VAL LYS VAL PRO ASP GLN          
SEQRES  26 B  385  VAL LYS ALA GLY ASP SER VAL ILE LEU ILE ASP ASN HIS          
SEQRES  27 B  385  ARG GLU SER PRO GLN SER VAL GLU VAL VAL ALA GLU LYS          
SEQRES  28 B  385  GLN HIS THR ILE ASN TYR GLU VAL LEU CYS ASN LEU SER          
SEQRES  29 B  385  ARG ARG LEU PRO ARG ILE TYR HIS ASP GLY ASP GLN ARG          
SEQRES  30 B  385  PHE VAL THR ASN GLU LEU LEU LYS                              
HET     NA  A 383       1                                                       
HET    BME  A 384       4                                                       
HET    BME  A 385       4                                                       
HET    PO4  A 386       5                                                       
HET     NA  B 383       1                                                       
HET    BME  B 384       4                                                       
HET    PO4  B 385       5                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   3   NA    2(NA 1+)                                                     
FORMUL   4  BME    3(C2 H6 O S)                                                 
FORMUL   6  PO4    2(O4 P 3-)                                                   
FORMUL  10  HOH   *120(H2 O)                                                    
HELIX    1   1 LEU A   15  HIS A   29  1                                  15    
HELIX    2   2 VAL A   38  GLY A   44  1                                   7    
HELIX    3   3 GLY A   46  ASN A   57  1                                  12    
HELIX    4   4 THR A   66  MET A   75  1                                  10    
HELIX    5   5 PRO A   89  LYS A   91  5                                   3    
HELIX    6   6 ASP A   92  HIS A   99  1                                   8    
HELIX    7   7 SER A  107  ASN A  117  1                                  11    
HELIX    8   8 ASP A  143  GLN A  155  1                                  13    
HELIX    9   9 ASP A  177  GLU A  192  1                                  16    
HELIX   10  10 ASN A  203  MET A  210  1                                   8    
HELIX   11  11 GLY A  221  GLY A  226  5                                   6    
HELIX   12  12 SER A  230  VAL A  237  1                                   8    
HELIX   13  13 GLY A  283  GLY A  287  5                                   5    
HELIX   14  14 LEU A  289  GLN A  293  5                                   5    
HELIX   15  15 SER A  341  GLN A  349  1                                   9    
HELIX   16  16 ILE A  352  LEU A  360  1                                   9    
HELIX   17  17 ASN A  378  LYS A  382  5                                   5    
HELIX   18  18 LEU B   15  HIS B   29  1                                  15    
HELIX   19  19 VAL B   38  GLY B   44  1                                   7    
HELIX   20  20 GLY B   46  GLU B   56  1                                  11    
HELIX   21  21 THR B   66  HIS B   76  1                                  11    
HELIX   22  22 PRO B   89  LYS B   91  5                                   3    
HELIX   23  23 ASP B   92  HIS B   99  1                                   8    
HELIX   24  24 SER B  107  ILE B  115  1                                   9    
HELIX   25  25 ASP B  143  TYR B  157  1                                  15    
HELIX   26  26 ASP B  177  ASN B  191  1                                  15    
HELIX   27  27 ASN B  203  MET B  210  1                                   8    
HELIX   28  28 GLY B  221  GLY B  226  5                                   6    
HELIX   29  29 SER B  230  GLN B  235  1                                   6    
HELIX   30  30 GLY B  283  GLY B  287  5                                   5    
HELIX   31  31 LEU B  289  GLN B  293  5                                   5    
HELIX   32  32 SER B  341  GLN B  349  1                                   9    
HELIX   33  33 ILE B  352  LEU B  360  1                                   9    
HELIX   34  34 ASN B  378  LYS B  382  5                                   5    
SHEET    1   A10 GLN A 253  LEU A 257  0                                        
SHEET    2   A10 THR A 275  LEU A 280 -1  O  LEU A 279   N  GLN A 253           
SHEET    3   A10 THR A 315  VAL A 319 -1  O  THR A 315   N  LEU A 280           
SHEET    4   A10 HIS A 302  ILE A 307 -1  N  GLU A 305   O  LYS A 318           
SHEET    5   A10 PHE A 296  VAL A 299 -1  N  VAL A 299   O  HIS A 302           
SHEET    6   A10 SER A 328  ILE A 332 -1  O  ILE A 330   N  ASN A 298           
SHEET    7   A10 VAL A 245  ASN A 250 -1  N  LEU A 247   O  LEU A 331           
SHEET    8   A10 ALA A   9  ASP A  14 -1  N  TYR A  10   O  ILE A 248           
SHEET    9   A10 ARG A 366  ASP A 370  1  O  ILE A 367   N  VAL A  13           
SHEET   10   A10 GLN A 373  THR A 377 -1  O  PHE A 375   N  TYR A 368           
SHEET    1   B 9 THR A  33  VAL A  37  0                                        
SHEET    2   B 9 PHE A  61  VAL A  64  1  O  ALA A  63   N  ALA A  36           
SHEET    3   B 9 LYS A  81  VAL A  84  1  O  LEU A  83   N  PHE A  62           
SHEET    4   B 9 VAL A 101  VAL A 105  1  O  ALA A 102   N  ILE A  82           
SHEET    5   B 9 LEU A 126  LYS A 131  1  O  HIS A 129   N  LEU A 103           
SHEET    6   B 9 LEU A 160  PHE A 166  1  O  GLY A 164   N  ILE A 130           
SHEET    7   B 9 TYR A 198  GLN A 202  1  O  TYR A 198   N  GLU A 163           
SHEET    8   B 9 ALA A 217  ILE A 218  1  O  ALA A 217   N  ILE A 199           
SHEET    9   B 9 THR A  33  VAL A  37  1  N  MET A  35   O  ILE A 218           
SHEET    1   C10 GLN B 253  LEU B 257  0                                        
SHEET    2   C10 THR B 275  LEU B 280 -1  O  THR B 275   N  LEU B 257           
SHEET    3   C10 THR B 315  VAL B 319 -1  O  VAL B 319   N  THR B 276           
SHEET    4   C10 HIS B 302  ILE B 307 -1  N  GLU B 305   O  LYS B 318           
SHEET    5   C10 PHE B 296  VAL B 299 -1  N  VAL B 299   O  HIS B 302           
SHEET    6   C10 SER B 328  ILE B 332 -1  O  ILE B 330   N  ASN B 298           
SHEET    7   C10 VAL B 245  ASN B 250 -1  N  ALA B 249   O  VAL B 329           
SHEET    8   C10 ALA B   9  ASP B  14 -1  N  TYR B  10   O  ILE B 248           
SHEET    9   C10 ARG B 366  HIS B 369  1  O  ILE B 367   N  MET B  11           
SHEET   10   C10 ARG B 374  THR B 377 -1  O  PHE B 375   N  TYR B 368           
SHEET    1   D 6 THR B  33  VAL B  34  0                                        
SHEET    2   D 6 ALA B 217  ILE B 218  1  O  ILE B 218   N  THR B  33           
SHEET    3   D 6 TYR B 198  GLN B 202  1  N  ILE B 199   O  ALA B 217           
SHEET    4   D 6 LEU B 160  PHE B 166  1  N  GLU B 163   O  TYR B 198           
SHEET    5   D 6 LEU B 126  LYS B 131  1  N  ILE B 130   O  GLY B 164           
SHEET    6   D 6 LEU B 103  VAL B 105  1  N  LEU B 103   O  TRP B 127           
SHEET    1   E 3 ALA B  36  VAL B  37  0                                        
SHEET    2   E 3 PHE B  61  VAL B  64  1  O  ALA B  63   N  ALA B  36           
SHEET    3   E 3 LYS B  81  VAL B  84  1  O  LYS B  81   N  PHE B  62           
SSBOND   1 CYS A  201    CYS A  215                          1555   1555  2.08  
SSBOND   2 CYS B  201    CYS B  215                          1555   1555  2.10  
LINK         O   LEU A 160                NA    NA A 383     1555   1555  2.24  
LINK         O   TYR A 157                NA    NA A 383     1555   1555  2.32  
LINK         O   ILE B 154                NA    NA B 383     1555   1555  2.36  
LINK         O   LEU B 160                NA    NA B 383     1555   1555  2.44  
LINK        NA    NA B 383                 O   HOH B 446     1555   1555  2.47  
LINK         O   TYR B 157                NA    NA B 383     1555   1555  2.52  
LINK         O   ILE A 154                NA    NA A 383     1555   1555  2.64  
LINK         SG BCYS B 311                 S2 BBME B 384     1555   1555  2.13  
LINK         SG ACYS A 311                 S2 ABME A 385     1555   1555  1.94  
LINK         SG BCYS A 171                 S2 BBME A 384     1555   1555  2.31  
SITE     1 AC1  3 ILE A 154  TYR A 157  LEU A 160                               
SITE     1 AC2  5 ALA A 170  CYS A 171  ASP A 173  GLU A 174                    
SITE     2 AC2  5 ARG B 309                                                     
SITE     1 AC3  2 CYS A 311  ARG B 138                                          
SITE     1 AC4  6 TYR A  43  ASN A 203  SER A 204  GLY A 221                    
SITE     2 AC4  6 ILE A 222  TYR A 354                                          
SITE     1 AC5  4 ILE B 154  TYR B 157  LEU B 160  HOH B 446                    
SITE     1 AC6  2 ARG B 309  CYS B 311                                          
SITE     1 AC7  8 TYR B  43  ASN B 203  SER B 204  GLY B 221                    
SITE     2 AC7  8 ILE B 222  TYR B 354  HOH B 402  HOH B 409                    
CRYST1   47.735  118.310  129.008  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020949  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008452  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007751        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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