GenomeNet

Database: PDB
Entry: 3K2E
LinkDB: 3K2E
Original site: 3K2E 
HEADER    OXIDOREDUCTASE                          30-SEP-09   3K2E              
TITLE     CRYSTAL STRUCTURE OF ENOYL-(ACYL-CARRIER-PROTEIN) REDUCTASE FROM      
TITLE    2 ANAPLASMA PHAGOCYTOPHILUM AT 1.9A RESOLUTION                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENOYL-(ACYL-CARRIER-PROTEIN) REDUCTASE;                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.3.1.9;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ANAPLASMA PHAGOCYTOPHILUM;                      
SOURCE   3 ORGANISM_TAXID: 948;                                                 
SOURCE   4 GENE: FABI, APH_0473;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: AVA0421                                   
KEYWDS    SSGCID, NIH, NIAID, SBRI, UW, DECODE, EONYL-(ACYL-CARRIER-PROTEIN)    
KEYWDS   2 REDUCTASE, ANAPLASMA PHAGOCYTOPHILUM, OXIDOREDUCTASE, STRUCTURAL     
KEYWDS   3 GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.ABENDROTH,B.STAKER                                                  
REVDAT   2   13-JUL-11 3K2E    1       VERSN                                    
REVDAT   1   13-OCT-09 3K2E    0                                                
JRNL        AUTH   J.ABENDROTH,B.STAKER                                         
JRNL        TITL   CRYSTAL STRUCTURE OF ENOYL-(ACYL-CARRIER-PROTEIN) REDUCTASE  
JRNL        TITL 2 FROM ANAPLASMA PHAGOCYTOPHILUM AT 1.9A RESOLUTION            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0104                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 44593                          
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) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.151                           
REMARK   3   FREE R VALUE                     : 0.194                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2251                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2813                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.41                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 155                          
REMARK   3   BIN FREE R VALUE                    : 0.3120                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3839                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 323                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.19                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.11000                                              
REMARK   3    B22 (A**2) : 0.23000                                              
REMARK   3    B33 (A**2) : -0.35000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.120         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.119         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.446         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3965 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2538 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5381 ; 1.673 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6239 ; 0.976 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   523 ; 5.734 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   144 ;37.672 ;24.583       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   622 ;12.351 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;17.911 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   633 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4431 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   770 ; 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):  2565 ; 0.956 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1072 ; 0.279 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4098 ; 1.663 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1400 ; 2.699 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1279 ; 4.232 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   -10        A  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.6583  14.8745  63.9395              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0264 T22:   0.0082                                     
REMARK   3      T33:   0.0207 T12:   0.0038                                     
REMARK   3      T13:  -0.0026 T23:   0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1846 L22:   0.1400                                     
REMARK   3      L33:   0.2793 L12:  -0.1032                                     
REMARK   3      L13:  -0.0162 L23:   0.0354                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0373 S12:   0.0252 S13:   0.0348                       
REMARK   3      S21:  -0.0432 S22:  -0.0275 S23:  -0.0241                       
REMARK   3      S31:  -0.0341 S32:  -0.0104 S33:  -0.0099                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   -10        B  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.9227   9.6967  94.3377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0109 T22:   0.0323                                     
REMARK   3      T33:   0.0159 T12:   0.0152                                     
REMARK   3      T13:   0.0007 T23:  -0.0113                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1240 L22:   0.1946                                     
REMARK   3      L33:   0.2169 L12:  -0.1100                                     
REMARK   3      L13:   0.0013 L23:  -0.0072                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0306 S12:  -0.0399 S13:  -0.0008                       
REMARK   3      S21:   0.0347 S22:   0.0340 S23:   0.0262                       
REMARK   3      S31:  -0.0216 S32:  -0.0331 S33:  -0.0035                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3K2E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055459.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-AUG-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44593                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.7100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3GRK MODIFIED WITH CCP4 PROGRAM CHAINSAW   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: JCSG+ SCREEN CONDITION E11: 100MM        
REMARK 280  IMIDAZOLE PH 80, 10% PEG 8000; ANPHA.00817.A AT 23MG/ML, PH 8.0,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       40.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.70000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.70000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19260 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000       80.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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   -20                                                      
REMARK 465     ALA A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     MET A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     THR A   -10                                                      
REMARK 465     LEU A    -9                                                      
REMARK 465     GLU A    -8                                                      
REMARK 465     ALA A    -7                                                      
REMARK 465     GLN A    -6                                                      
REMARK 465     THR A    -5                                                      
REMARK 465     GLN A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASP A   262                                                      
REMARK 465     ALA A   263                                                      
REMARK 465     PRO A   264                                                      
REMARK 465     ASP A   265                                                      
REMARK 465     ILE A   266                                                      
REMARK 465     SER A   267                                                      
REMARK 465     ARG A   268                                                      
REMARK 465     VAL A   269                                                      
REMARK 465     LYS A   270                                                      
REMARK 465     GLY A   271                                                      
REMARK 465     ASP A   272                                                      
REMARK 465     HIS A   273                                                      
REMARK 465     SER A   274                                                      
REMARK 465     VAL A   275                                                      
REMARK 465     MET B   -20                                                      
REMARK 465     ALA B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     MET B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     THR B   -10                                                      
REMARK 465     LEU B    -9                                                      
REMARK 465     GLU B    -8                                                      
REMARK 465     ALA B    -7                                                      
REMARK 465     GLN B    -6                                                      
REMARK 465     THR B    -5                                                      
REMARK 465     GLN B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B   196                                                      
REMARK 465     LEU B   197                                                      
REMARK 465     ALA B   198                                                      
REMARK 465     SER B   199                                                      
REMARK 465     SER B   200                                                      
REMARK 465     GLY B   201                                                      
REMARK 465     ILE B   202                                                      
REMARK 465     SER B   267                                                      
REMARK 465     ARG B   268                                                      
REMARK 465     VAL B   269                                                      
REMARK 465     LYS B   270                                                      
REMARK 465     GLY B   271                                                      
REMARK 465     ASP B   272                                                      
REMARK 465     HIS B   273                                                      
REMARK 465     SER B   274                                                      
REMARK 465     VAL B   275                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A   2    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  45    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  49    CG   CD   CE   NZ                                   
REMARK 470     ARG A  50    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  56    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  61    CG   CD   CE   NZ                                   
REMARK 470     LYS A 104    CG   CD   CE   NZ                                   
REMARK 470     LYS A 181    CG   CD   CE   NZ                                   
REMARK 470     ARG A 219    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 261    CG1  CG2                                            
REMARK 470     ARG B   2    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  21    CG   CD   CE   NZ                                   
REMARK 470     LYS B  49    CG   CD   CE   NZ                                   
REMARK 470     ARG B  50    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  56    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  61    CG   CD   CE   NZ                                   
REMARK 470     LYS B  79    CG   CD   CE   NZ                                   
REMARK 470     ASP B 204    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   407     O    HOH A   411              2.19            
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    TYR A 233   CZ    TYR A 233   OH      0.137                       
REMARK 500    TYR A 233   CE2   TYR A 233   CD2     0.093                       
REMARK 500    TYR B 233   CZ    TYR B 233   OH      0.129                       
REMARK 500    TYR B 233   CE2   TYR B 233   CD2     0.136                       
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    CYS A  66      114.69   -161.03                                   
REMARK 500    CYS A 123      -61.12   -120.29                                   
REMARK 500    MET A 137       78.08   -103.05                                   
REMARK 500    TYR A 158      -44.78   -130.45                                   
REMARK 500    ASN A 159     -116.85     46.16                                   
REMARK 500    ASP A 250       18.63   -145.65                                   
REMARK 500    MET A 258      -67.65   -150.84                                   
REMARK 500    LYS A 259      147.71   -175.37                                   
REMARK 500    CYS B  66      119.87   -162.54                                   
REMARK 500    ASN B 159     -115.95     36.16                                   
REMARK 500    ASP B 250       22.79   -147.76                                   
REMARK 500    LYS B 259      135.08    -38.92                                   
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 EDO A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: ANPHA.00817.A   RELATED DB: TARGETDB                     
DBREF  3K2E A    1   275  UNP    Q2GKM8   Q2GKM8_ANAPZ     1    275             
DBREF  3K2E B    1   275  UNP    Q2GKM8   Q2GKM8_ANAPZ     1    275             
SEQADV 3K2E MET A  -20  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E ALA A  -19  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E HIS A  -18  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E HIS A  -17  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E HIS A  -16  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E HIS A  -15  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E HIS A  -14  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E HIS A  -13  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E MET A  -12  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E GLY A  -11  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E THR A  -10  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E LEU A   -9  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E GLU A   -8  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E ALA A   -7  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E GLN A   -6  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E THR A   -5  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E GLN A   -4  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E GLY A   -3  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E PRO A   -2  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E GLY A   -1  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E SER A    0  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E MET B  -20  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E ALA B  -19  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E HIS B  -18  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E HIS B  -17  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E HIS B  -16  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E HIS B  -15  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E HIS B  -14  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E HIS B  -13  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E MET B  -12  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E GLY B  -11  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E THR B  -10  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E LEU B   -9  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E GLU B   -8  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E ALA B   -7  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E GLN B   -6  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E THR B   -5  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E GLN B   -4  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E GLY B   -3  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E PRO B   -2  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E GLY B   -1  UNP  Q2GKM8              EXPRESSION TAG                 
SEQADV 3K2E SER B    0  UNP  Q2GKM8              EXPRESSION TAG                 
SEQRES   1 A  296  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU          
SEQRES   2 A  296  ALA GLN THR GLN GLY PRO GLY SER MET ARG THR GLY MET          
SEQRES   3 A  296  LEU MET GLU GLY LYS LYS GLY VAL ILE ILE GLY VAL ALA          
SEQRES   4 A  296  ASN ASP LYS SER LEU ALA TRP GLY ILE ALA LYS ALA VAL          
SEQRES   5 A  296  CYS ALA GLN GLY ALA GLU VAL ALA LEU THR TYR LEU SER          
SEQRES   6 A  296  GLU THR PHE LYS LYS ARG VAL ASP PRO LEU ALA GLU SER          
SEQRES   7 A  296  LEU GLY VAL LYS LEU THR VAL PRO CYS ASP VAL SER ASP          
SEQRES   8 A  296  ALA GLU SER VAL ASP ASN MET PHE LYS VAL LEU ALA GLU          
SEQRES   9 A  296  GLU TRP GLY SER LEU ASP PHE VAL VAL HIS ALA VAL ALA          
SEQRES  10 A  296  PHE SER ASP LYS ASN GLU LEU LYS GLY ARG TYR VAL ASP          
SEQRES  11 A  296  THR SER LEU GLY ASN PHE LEU THR SER MET HIS ILE SER          
SEQRES  12 A  296  CYS TYR SER PHE THR TYR ILE ALA SER LYS ALA GLU PRO          
SEQRES  13 A  296  LEU MET THR ASN GLY GLY SER ILE LEU THR LEU SER TYR          
SEQRES  14 A  296  TYR GLY ALA GLU LYS VAL VAL PRO HIS TYR ASN VAL MET          
SEQRES  15 A  296  GLY VAL CYS LYS ALA ALA LEU GLU ALA SER VAL LYS TYR          
SEQRES  16 A  296  LEU ALA VAL ASP LEU GLY LYS GLN GLN ILE ARG VAL ASN          
SEQRES  17 A  296  ALA ILE SER ALA GLY PRO VAL ARG THR LEU ALA SER SER          
SEQRES  18 A  296  GLY ILE SER ASP PHE HIS TYR ILE LEU THR TRP ASN LYS          
SEQRES  19 A  296  TYR ASN SER PRO LEU ARG ARG ASN THR THR LEU ASP ASP          
SEQRES  20 A  296  VAL GLY GLY ALA ALA LEU TYR LEU LEU SER ASP LEU GLY          
SEQRES  21 A  296  ARG GLY THR THR GLY GLU THR VAL HIS VAL ASP CYS GLY          
SEQRES  22 A  296  TYR HIS VAL VAL GLY MET LYS SER VAL ASP ALA PRO ASP          
SEQRES  23 A  296  ILE SER ARG VAL LYS GLY ASP HIS SER VAL                      
SEQRES   1 B  296  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU          
SEQRES   2 B  296  ALA GLN THR GLN GLY PRO GLY SER MET ARG THR GLY MET          
SEQRES   3 B  296  LEU MET GLU GLY LYS LYS GLY VAL ILE ILE GLY VAL ALA          
SEQRES   4 B  296  ASN ASP LYS SER LEU ALA TRP GLY ILE ALA LYS ALA VAL          
SEQRES   5 B  296  CYS ALA GLN GLY ALA GLU VAL ALA LEU THR TYR LEU SER          
SEQRES   6 B  296  GLU THR PHE LYS LYS ARG VAL ASP PRO LEU ALA GLU SER          
SEQRES   7 B  296  LEU GLY VAL LYS LEU THR VAL PRO CYS ASP VAL SER ASP          
SEQRES   8 B  296  ALA GLU SER VAL ASP ASN MET PHE LYS VAL LEU ALA GLU          
SEQRES   9 B  296  GLU TRP GLY SER LEU ASP PHE VAL VAL HIS ALA VAL ALA          
SEQRES  10 B  296  PHE SER ASP LYS ASN GLU LEU LYS GLY ARG TYR VAL ASP          
SEQRES  11 B  296  THR SER LEU GLY ASN PHE LEU THR SER MET HIS ILE SER          
SEQRES  12 B  296  CYS TYR SER PHE THR TYR ILE ALA SER LYS ALA GLU PRO          
SEQRES  13 B  296  LEU MET THR ASN GLY GLY SER ILE LEU THR LEU SER TYR          
SEQRES  14 B  296  TYR GLY ALA GLU LYS VAL VAL PRO HIS TYR ASN VAL MET          
SEQRES  15 B  296  GLY VAL CYS LYS ALA ALA LEU GLU ALA SER VAL LYS TYR          
SEQRES  16 B  296  LEU ALA VAL ASP LEU GLY LYS GLN GLN ILE ARG VAL ASN          
SEQRES  17 B  296  ALA ILE SER ALA GLY PRO VAL ARG THR LEU ALA SER SER          
SEQRES  18 B  296  GLY ILE SER ASP PHE HIS TYR ILE LEU THR TRP ASN LYS          
SEQRES  19 B  296  TYR ASN SER PRO LEU ARG ARG ASN THR THR LEU ASP ASP          
SEQRES  20 B  296  VAL GLY GLY ALA ALA LEU TYR LEU LEU SER ASP LEU GLY          
SEQRES  21 B  296  ARG GLY THR THR GLY GLU THR VAL HIS VAL ASP CYS GLY          
SEQRES  22 B  296  TYR HIS VAL VAL GLY MET LYS SER VAL ASP ALA PRO ASP          
SEQRES  23 B  296  ILE SER ARG VAL LYS GLY ASP HIS SER VAL                      
HET    EDO  A 400       4                                                       
HET    EDO  A 401       4                                                       
HET    GOL  A 300       6                                                       
HET    GOL  A 301       6                                                       
HET    EDO  B 400       4                                                       
HET    EDO  B 401       4                                                       
HET    EDO  B 402       4                                                       
HET    GOL  B 300       6                                                       
HET    GOL  B 301       6                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     GOL GLYCEROL                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  EDO    5(C2 H6 O2)                                                  
FORMUL   5  GOL    4(C3 H8 O3)                                                  
FORMUL  12  HOH   *323(H2 O)                                                    
HELIX    1   1 SER A   22  GLN A   34  1                                  13    
HELIX    2   2 SER A   44  THR A   46  5                                   3    
HELIX    3   3 PHE A   47  GLY A   59  1                                  13    
HELIX    4   4 ASP A   70  GLY A   86  1                                  17    
HELIX    5   5 ASP A   99  LYS A  104  1                                   6    
HELIX    6   6 GLY A  105  THR A  110  5                                   6    
HELIX    7   7 SER A  111  CYS A  123  1                                  13    
HELIX    8   8 CYS A  123  GLU A  134  1                                  12    
HELIX    9   9 PRO A  135  MET A  137  5                                   3    
HELIX   10  10 TYR A  148  GLU A  152  5                                   5    
HELIX   11  11 ASN A  159  LYS A  181  1                                  23    
HELIX   12  12 ILE A  202  SER A  216  1                                  15    
HELIX   13  13 THR A  223  SER A  236  1                                  14    
HELIX   14  14 ASP A  237  ARG A  240  5                                   4    
HELIX   15  15 GLY A  252  VAL A  256  5                                   5    
HELIX   16  16 SER B   22  GLN B   34  1                                  13    
HELIX   17  17 SER B   44  THR B   46  5                                   3    
HELIX   18  18 PHE B   47  GLY B   59  1                                  13    
HELIX   19  19 ASP B   70  GLY B   86  1                                  17    
HELIX   20  20 ASP B   99  GLY B  105  1                                   7    
HELIX   21  21 ARG B  106  THR B  110  5                                   5    
HELIX   22  22 SER B  111  CYS B  123  1                                  13    
HELIX   23  23 CYS B  123  GLU B  134  1                                  12    
HELIX   24  24 PRO B  135  MET B  137  5                                   3    
HELIX   25  25 TYR B  148  GLU B  152  5                                   5    
HELIX   26  26 TYR B  158  LYS B  181  1                                  24    
HELIX   27  27 SER B  203  SER B  216  1                                  14    
HELIX   28  28 THR B  223  SER B  236  1                                  14    
HELIX   29  29 ASP B  237  ARG B  240  5                                   4    
HELIX   30  30 GLY B  252  VAL B  256  5                                   5    
SHEET    1   A 7 LEU A  62  PRO A  65  0                                        
SHEET    2   A 7 GLU A  37  TYR A  42  1  N  LEU A  40   O  VAL A  64           
SHEET    3   A 7 LYS A  11  ILE A  15  1  N  ILE A  14   O  ALA A  39           
SHEET    4   A 7 PHE A  90  HIS A  93  1  O  VAL A  92   N  ILE A  15           
SHEET    5   A 7 GLY A 141  SER A 147  1  O  LEU A 144   N  HIS A  93           
SHEET    6   A 7 ILE A 184  ALA A 191  1  O  ILE A 189   N  SER A 147           
SHEET    7   A 7 THR A 246  VAL A 249  1  O  VAL A 249   N  SER A 190           
SHEET    1   B 7 LEU B  62  PRO B  65  0                                        
SHEET    2   B 7 GLU B  37  TYR B  42  1  N  LEU B  40   O  VAL B  64           
SHEET    3   B 7 LYS B  11  ILE B  15  1  N  GLY B  12   O  GLU B  37           
SHEET    4   B 7 PHE B  90  HIS B  93  1  O  VAL B  92   N  ILE B  15           
SHEET    5   B 7 GLY B 141  SER B 147  1  O  LEU B 144   N  HIS B  93           
SHEET    6   B 7 ILE B 184  ALA B 191  1  O  ILE B 189   N  SER B 147           
SHEET    7   B 7 THR B 246  VAL B 249  1  O  VAL B 247   N  ALA B 188           
SITE     1 AC1  6 VAL A  68  HIS A 120  SER A 125  TYR A 128                    
SITE     2 AC1  6 HOH A 283  HOH A 403                                          
SITE     1 AC2  5 VAL A  95  ALA A  96  LYS A 165  HOH A 315                    
SITE     2 AC2  5 HOH A 327                                                     
SITE     1 AC3  7 VAL B  68  SER B  69  ALA B  71  HIS B 120                    
SITE     2 AC3  7 SER B 125  TYR B 128  HOH B 311                               
SITE     1 AC4  5 VAL B  95  ALA B  96  LYS B 165  HOH B 290                    
SITE     2 AC4  5 HOH B 374                                                     
SITE     1 AC5  6 VAL A 154  MET B 258  LYS B 259  SER B 260                    
SITE     2 AC5  6 HOH B 344  HOH B 360                                          
SITE     1 AC6  9 GLY A 105  ARG A 106  TYR A 107  ASN A 159                    
SITE     2 AC6  9 HOH A 314  HOH A 340  HOH A 344  VAL B 177                    
SITE     3 AC6  9 ASP B 178                                                     
SITE     1 AC7  7 GLY A  16  VAL A  17  THR A  41  TYR A  42                    
SITE     2 AC7  7 LEU A  43  CYS A  66  VAL A  68                               
SITE     1 AC8  9 VAL A 177  ASP A 178  HOH A 311  GLY B 105                    
SITE     2 AC8  9 ARG B 106  TYR B 107  PRO B 156  HIS B 157                    
SITE     3 AC8  9 ASN B 159                                                     
SITE     1 AC9  8 GLY B  16  THR B  41  TYR B  42  LEU B  43                    
SITE     2 AC9  8 CYS B  66  ASP B  67  VAL B  68  HOH B 434                    
CRYST1   80.000   89.400   78.500  90.00  90.00  90.00 P 21 21 2     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      0.012500  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011186  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012739        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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