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Database: PDB
Entry: 3DHU
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Original site: 3DHU 
HEADER    HYDROLASE                               18-JUN-08   3DHU              
TITLE     CRYSTAL STRUCTURE OF AN ALPHA-AMYLASE FROM LACTOBACILLUS              
TITLE    2 PLANTARUM                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE;                                             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 3.2.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOBACILLUS PLANTARUM;                        
SOURCE   3 ORGANISM_TAXID: 1590;                                                
SOURCE   4 GENE: AMY2, LP_0179;                                                 
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET26                            
KEYWDS    STRUCTURAL GENOMICS, HYDROLASE, GLYCOSIDASE, PSI-2, PROTEIN           
KEYWDS   2 STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR               
KEYWDS   3 STRUCTURAL GENOMICS, NYSGXRC                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.B.BONANNO,M.DICKEY,K.T.BAIN,M.IIZUKA,S.OZYURT,D.SMITH,              
AUTHOR   2 S.WASSERMAN,J.M.SAUDER,S.K.BURLEY,S.C.ALMO,NEW YORK SGX              
AUTHOR   3 RESEARCH CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)                    
REVDAT   2   24-FEB-09 3DHU    1       VERSN                                    
REVDAT   1   12-AUG-08 3DHU    0                                                
JRNL        AUTH   J.B.BONANNO,M.DICKEY,K.T.BAIN,M.IIZUKA,S.OZYURT,             
JRNL        AUTH 2 D.SMITH,S.WASSERMAN,J.M.SAUDER,S.K.BURLEY,S.C.ALMO           
JRNL        TITL   CRYSTAL STRUCTURE OF AN ALPHA-AMYLASE FROM                   
JRNL        TITL 2 LACTOBACILLUS PLANTARUM                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 129172                         
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                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6497                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8855                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.62                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 452                          
REMARK   3   BIN FREE R VALUE                    : 0.2640                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13401                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 1331                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.43000                                              
REMARK   3    B22 (A**2) : 0.59000                                              
REMARK   3    B33 (A**2) : -0.92000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.21000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.197         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.178         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.147         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.399         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.925                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.874                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13739 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18716 ; 1.419 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1674 ; 6.274 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   671 ;39.232 ;24.218       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2193 ;13.729 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    76 ;16.439 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2050 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10612 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  6719 ; 0.208 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  9307 ; 0.312 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1197 ; 0.142 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   108 ; 0.217 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    46 ; 0.177 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  8551 ; 0.816 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13421 ; 1.169 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6033 ; 2.044 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5295 ; 3.095 ; 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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3DHU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUN-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB048055.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97958                            
REMARK 200  MONOCHROMATOR                  : DIAMOND                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 130025                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.412                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.18300                            
REMARK 200  R SYM                      (I) : 0.18300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.56600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXC/D/E                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 280MM AMMONIUM SULFATE, 30% PEG 4K,      
REMARK 280  PH 7.0, VAPOR DIFFUSION, TEMPERATURE 294K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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      101.13950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.88650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      101.13950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.88650            
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, 3, 4                                              
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 300 REMARK: PROBABLE MONOMER                                             
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     THR A   428                                                      
REMARK 465     ASN A   429                                                      
REMARK 465     THR A   430                                                      
REMARK 465     ALA A   431                                                      
REMARK 465     VAL A   432                                                      
REMARK 465     THR A   433                                                      
REMARK 465     LYS A   434                                                      
REMARK 465     VAL A   435                                                      
REMARK 465     ALA A   436                                                      
REMARK 465     ASP A   437                                                      
REMARK 465     GLN A   438                                                      
REMARK 465     SER A   439                                                      
REMARK 465     ASN A   440                                                      
REMARK 465     GLU A   441                                                      
REMARK 465     GLY A   442                                                      
REMARK 465     HIS A   443                                                      
REMARK 465     HIS A   444                                                      
REMARK 465     HIS A   445                                                      
REMARK 465     HIS A   446                                                      
REMARK 465     HIS A   447                                                      
REMARK 465     HIS A   448                                                      
REMARK 465     MET B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     LEU B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     ALA B   126                                                      
REMARK 465     ASP B   127                                                      
REMARK 465     GLY B   128                                                      
REMARK 465     GLN B   129                                                      
REMARK 465     THR B   428                                                      
REMARK 465     ASN B   429                                                      
REMARK 465     THR B   430                                                      
REMARK 465     ALA B   431                                                      
REMARK 465     VAL B   432                                                      
REMARK 465     THR B   433                                                      
REMARK 465     LYS B   434                                                      
REMARK 465     VAL B   435                                                      
REMARK 465     ALA B   436                                                      
REMARK 465     ASP B   437                                                      
REMARK 465     GLN B   438                                                      
REMARK 465     SER B   439                                                      
REMARK 465     ASN B   440                                                      
REMARK 465     GLU B   441                                                      
REMARK 465     GLY B   442                                                      
REMARK 465     HIS B   443                                                      
REMARK 465     HIS B   444                                                      
REMARK 465     HIS B   445                                                      
REMARK 465     HIS B   446                                                      
REMARK 465     HIS B   447                                                      
REMARK 465     HIS B   448                                                      
REMARK 465     MET C     0                                                      
REMARK 465     SER C     1                                                      
REMARK 465     LEU C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     ASP C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     THR C   428                                                      
REMARK 465     ASN C   429                                                      
REMARK 465     THR C   430                                                      
REMARK 465     ALA C   431                                                      
REMARK 465     VAL C   432                                                      
REMARK 465     THR C   433                                                      
REMARK 465     LYS C   434                                                      
REMARK 465     VAL C   435                                                      
REMARK 465     ALA C   436                                                      
REMARK 465     ASP C   437                                                      
REMARK 465     GLN C   438                                                      
REMARK 465     SER C   439                                                      
REMARK 465     ASN C   440                                                      
REMARK 465     GLU C   441                                                      
REMARK 465     GLY C   442                                                      
REMARK 465     HIS C   443                                                      
REMARK 465     HIS C   444                                                      
REMARK 465     HIS C   445                                                      
REMARK 465     HIS C   446                                                      
REMARK 465     HIS C   447                                                      
REMARK 465     HIS C   448                                                      
REMARK 465     MET D     0                                                      
REMARK 465     SER D     1                                                      
REMARK 465     LEU D     2                                                      
REMARK 465     ARG D     3                                                      
REMARK 465     ASP D     4                                                      
REMARK 465     THR D     5                                                      
REMARK 465     ALA D   126                                                      
REMARK 465     ASP D   127                                                      
REMARK 465     GLY D   128                                                      
REMARK 465     GLN D   129                                                      
REMARK 465     THR D   428                                                      
REMARK 465     ASN D   429                                                      
REMARK 465     THR D   430                                                      
REMARK 465     ALA D   431                                                      
REMARK 465     VAL D   432                                                      
REMARK 465     THR D   433                                                      
REMARK 465     LYS D   434                                                      
REMARK 465     VAL D   435                                                      
REMARK 465     ALA D   436                                                      
REMARK 465     ASP D   437                                                      
REMARK 465     GLN D   438                                                      
REMARK 465     SER D   439                                                      
REMARK 465     ASN D   440                                                      
REMARK 465     GLU D   441                                                      
REMARK 465     GLY D   442                                                      
REMARK 465     HIS D   443                                                      
REMARK 465     HIS D   444                                                      
REMARK 465     HIS D   445                                                      
REMARK 465     HIS D   446                                                      
REMARK 465     HIS D   447                                                      
REMARK 465     HIS D   448                                                      
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     GLN A   6    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  94    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 127    CG   OD1  OD2                                       
REMARK 470     LYS A 133    CG   CD   CE   NZ                                   
REMARK 470     GLU A 149    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 191    CG   CD   CE   NZ                                   
REMARK 470     GLU A 194    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 209    CG   CD   OE1  OE2                                  
REMARK 470     GLN B   6    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  94    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 133    CG   CD   CE   NZ                                   
REMARK 470     GLU B 149    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 191    CG   CD   CE   NZ                                   
REMARK 470     GLU B 194    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 209    CG   CD   OE1  OE2                                  
REMARK 470     GLN C   6    CG   CD   OE1  NE2                                  
REMARK 470     GLU C  94    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 133    CG   CD   CE   NZ                                   
REMARK 470     GLU C 149    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 191    CG   CD   CE   NZ                                   
REMARK 470     GLU C 194    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 209    CG   CD   OE1  OE2                                  
REMARK 470     GLN D   6    CG   CD   OE1  NE2                                  
REMARK 470     GLU D  94    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 133    CG   CD   CE   NZ                                   
REMARK 470     GLU D 149    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 191    CG   CD   CE   NZ                                   
REMARK 470     GLU D 194    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 209    CG   CD   OE1  OE2                                  
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   NE2  GLN D   244     O    HOH D   552              2.04            
REMARK 500   NE2  GLN C   244     O    HOH C   567              2.05            
REMARK 500   OD1  ASP C   125     OD1  ASP C   127              2.08            
REMARK 500   O    HIS B   148     O    HOH B   609              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 169   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG A 169   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    LEU A 415   CA  -  CB  -  CG  ANGL. DEV. =  19.7 DEGREES          
REMARK 500    MET B  13   CG  -  SD  -  CE  ANGL. DEV. = -10.0 DEGREES          
REMARK 500    LEU B 415   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    ARG C 302   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    LEU C 415   CA  -  CB  -  CG  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    LEU D 415   CA  -  CB  -  CG  ANGL. DEV. =  18.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 125     -158.16    -83.09                                   
REMARK 500    TRP A 137       47.80    -78.70                                   
REMARK 500    VAL A 172       53.22     29.76                                   
REMARK 500    ASP A 232       35.85    -71.17                                   
REMARK 500    VAL A 235      -10.84   -140.60                                   
REMARK 500    HIS A 286       12.28   -142.60                                   
REMARK 500    ASP A 325       57.60   -148.78                                   
REMARK 500    VAL A 361     -150.13   -117.26                                   
REMARK 500    ASP A 418       46.50    -99.62                                   
REMARK 500    VAL B 104       77.27   -116.82                                   
REMARK 500    HIS B 118       56.52   -146.18                                   
REMARK 500    VAL B 172       55.50     28.67                                   
REMARK 500    ASP B 232       31.04    -66.31                                   
REMARK 500    HIS B 286       20.44   -141.10                                   
REMARK 500    ASP B 325       54.09   -149.76                                   
REMARK 500    VAL B 361     -153.57   -117.66                                   
REMARK 500    ASP B 418       46.77    -96.64                                   
REMARK 500    VAL C 104       73.43   -118.24                                   
REMARK 500    VAL C 172       47.03     34.89                                   
REMARK 500    ASP C 232       32.87    -70.46                                   
REMARK 500    ASP C 325       55.93   -156.95                                   
REMARK 500    HIS C 332       41.78   -141.38                                   
REMARK 500    VAL C 361     -151.54   -124.01                                   
REMARK 500    ALA C 372      139.16   -172.31                                   
REMARK 500    ASP C 405       19.06     57.43                                   
REMARK 500    ASP C 418       54.32    -97.90                                   
REMARK 500    VAL D 104       76.73   -119.26                                   
REMARK 500    ASP D 136      -31.81    -38.43                                   
REMARK 500    VAL D 172       46.95     32.38                                   
REMARK 500    ASP D 232       29.05    -66.23                                   
REMARK 500    ASP D 325       59.43   -157.73                                   
REMARK 500    HIS D 332       44.87   -140.04                                   
REMARK 500    VAL D 361     -151.85   -120.65                                   
REMARK 500    ASP D 405       19.32     52.33                                   
REMARK 500    ASP D 418       55.70   -103.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 722        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH A 759        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH A 774        DISTANCE =  7.02 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-11098H   RELATED DB: TARGETDB                    
DBREF  3DHU A    3   440  UNP    Q88ZW5   Q88ZW5_LACPL     3    440             
DBREF  3DHU B    3   440  UNP    Q88ZW5   Q88ZW5_LACPL     3    440             
DBREF  3DHU C    3   440  UNP    Q88ZW5   Q88ZW5_LACPL     3    440             
DBREF  3DHU D    3   440  UNP    Q88ZW5   Q88ZW5_LACPL     3    440             
SEQADV 3DHU MET A    0  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU SER A    1  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU LEU A    2  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU GLU A  441  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU GLY A  442  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS A  443  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS A  444  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS A  445  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS A  446  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS A  447  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS A  448  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU MET B    0  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU SER B    1  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU LEU B    2  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU GLU B  441  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU GLY B  442  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS B  443  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS B  444  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS B  445  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS B  446  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS B  447  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS B  448  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU MET C    0  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU SER C    1  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU LEU C    2  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU GLU C  441  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU GLY C  442  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS C  443  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS C  444  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS C  445  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS C  446  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS C  447  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS C  448  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU MET D    0  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU SER D    1  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU LEU D    2  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU GLU D  441  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU GLY D  442  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS D  443  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS D  444  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS D  445  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS D  446  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS D  447  UNP  Q88ZW5              INSERTION                      
SEQADV 3DHU HIS D  448  UNP  Q88ZW5              INSERTION                      
SEQRES   1 A  449  MET SER LEU ARG ASP THR GLN THR GLN LEU ARG ASN GLU          
SEQRES   2 A  449  MET ILE TYR SER VAL PHE VAL ARG ASN TYR SER GLU ALA          
SEQRES   3 A  449  GLY ASN PHE ALA GLY VAL THR ALA ASP LEU GLN ARG ILE          
SEQRES   4 A  449  LYS ASP LEU GLY THR ASP ILE LEU TRP LEU LEU PRO ILE          
SEQRES   5 A  449  ASN PRO ILE GLY GLU VAL ASN ARG LYS GLY THR LEU GLY          
SEQRES   6 A  449  SER PRO TYR ALA ILE LYS ASP TYR ARG GLY ILE ASN PRO          
SEQRES   7 A  449  GLU TYR GLY THR LEU ALA ASP PHE LYS ALA LEU THR ASP          
SEQRES   8 A  449  ARG ALA HIS GLU LEU GLY MET LYS VAL MET LEU ASP ILE          
SEQRES   9 A  449  VAL TYR ASN HIS THR SER PRO ASP SER VAL LEU ALA THR          
SEQRES  10 A  449  GLU HIS PRO GLU TRP PHE TYR HIS ASP ALA ASP GLY GLN          
SEQRES  11 A  449  LEU THR ASN LYS VAL GLY ASP TRP SER ASP VAL LYS ASP          
SEQRES  12 A  449  LEU ASP TYR GLY HIS HIS GLU LEU TRP GLN TYR GLN ILE          
SEQRES  13 A  449  ASP THR LEU LEU TYR TRP SER GLN PHE VAL ASP GLY TYR          
SEQRES  14 A  449  ARG CYS ASP VAL ALA PRO LEU VAL PRO LEU ASP PHE TRP          
SEQRES  15 A  449  LEU GLU ALA ARG LYS GLN VAL ASN ALA LYS TYR PRO GLU          
SEQRES  16 A  449  THR LEU TRP LEU ALA GLU SER ALA GLY SER GLY PHE ILE          
SEQRES  17 A  449  GLU GLU LEU ARG SER GLN GLY TYR THR GLY LEU SER ASP          
SEQRES  18 A  449  SER GLU LEU TYR GLN ALA PHE ASP MET THR TYR ASP TYR          
SEQRES  19 A  449  ASP VAL PHE GLY ASP PHE LYS ASP TYR TRP GLN GLY ARG          
SEQRES  20 A  449  SER THR VAL GLU ARG TYR VAL ASP LEU LEU GLN ARG GLN          
SEQRES  21 A  449  ASP ALA THR PHE PRO GLY ASN TYR VAL LYS MET ARG PHE          
SEQRES  22 A  449  LEU GLU ASN HIS ASP ASN ALA ARG MET MET SER LEU MET          
SEQRES  23 A  449  HIS SER LYS ALA GLU ALA VAL ASN ASN LEU THR TRP ILE          
SEQRES  24 A  449  PHE MET GLN ARG GLY ILE PRO LEU ILE TYR ASN GLY GLN          
SEQRES  25 A  449  GLU PHE LEU ALA GLU HIS GLN PRO SER LEU PHE ASP ARG          
SEQRES  26 A  449  ASP THR MET VAL ALA ASP ARG HIS GLY ASP VAL THR PRO          
SEQRES  27 A  449  LEU ILE GLN LYS LEU VAL THR ILE LYS GLN LEU PRO LEU          
SEQRES  28 A  449  LEU ARG ALA ALA ASP TYR GLN LEU ALA VAL VAL GLU GLU          
SEQRES  29 A  449  GLY ILE VAL LYS ILE THR TYR ARG ALA ALA GLY GLU ALA          
SEQRES  30 A  449  LEU THR ALA TRP ILE PRO LEU LYS GLY GLN VAL THR ALA          
SEQRES  31 A  449  VAL ALA THR LYS LEU ALA ALA GLY SER TYR GLN ASN LEU          
SEQRES  32 A  449  LEU THR ASP GLY PRO THR GLU VAL VAL ASP GLY LYS LEU          
SEQRES  33 A  449  THR VAL ASP GLY GLN PRO VAL LEU ILE LYS TYR VAL THR          
SEQRES  34 A  449  ASN THR ALA VAL THR LYS VAL ALA ASP GLN SER ASN GLU          
SEQRES  35 A  449  GLY HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B  449  MET SER LEU ARG ASP THR GLN THR GLN LEU ARG ASN GLU          
SEQRES   2 B  449  MET ILE TYR SER VAL PHE VAL ARG ASN TYR SER GLU ALA          
SEQRES   3 B  449  GLY ASN PHE ALA GLY VAL THR ALA ASP LEU GLN ARG ILE          
SEQRES   4 B  449  LYS ASP LEU GLY THR ASP ILE LEU TRP LEU LEU PRO ILE          
SEQRES   5 B  449  ASN PRO ILE GLY GLU VAL ASN ARG LYS GLY THR LEU GLY          
SEQRES   6 B  449  SER PRO TYR ALA ILE LYS ASP TYR ARG GLY ILE ASN PRO          
SEQRES   7 B  449  GLU TYR GLY THR LEU ALA ASP PHE LYS ALA LEU THR ASP          
SEQRES   8 B  449  ARG ALA HIS GLU LEU GLY MET LYS VAL MET LEU ASP ILE          
SEQRES   9 B  449  VAL TYR ASN HIS THR SER PRO ASP SER VAL LEU ALA THR          
SEQRES  10 B  449  GLU HIS PRO GLU TRP PHE TYR HIS ASP ALA ASP GLY GLN          
SEQRES  11 B  449  LEU THR ASN LYS VAL GLY ASP TRP SER ASP VAL LYS ASP          
SEQRES  12 B  449  LEU ASP TYR GLY HIS HIS GLU LEU TRP GLN TYR GLN ILE          
SEQRES  13 B  449  ASP THR LEU LEU TYR TRP SER GLN PHE VAL ASP GLY TYR          
SEQRES  14 B  449  ARG CYS ASP VAL ALA PRO LEU VAL PRO LEU ASP PHE TRP          
SEQRES  15 B  449  LEU GLU ALA ARG LYS GLN VAL ASN ALA LYS TYR PRO GLU          
SEQRES  16 B  449  THR LEU TRP LEU ALA GLU SER ALA GLY SER GLY PHE ILE          
SEQRES  17 B  449  GLU GLU LEU ARG SER GLN GLY TYR THR GLY LEU SER ASP          
SEQRES  18 B  449  SER GLU LEU TYR GLN ALA PHE ASP MET THR TYR ASP TYR          
SEQRES  19 B  449  ASP VAL PHE GLY ASP PHE LYS ASP TYR TRP GLN GLY ARG          
SEQRES  20 B  449  SER THR VAL GLU ARG TYR VAL ASP LEU LEU GLN ARG GLN          
SEQRES  21 B  449  ASP ALA THR PHE PRO GLY ASN TYR VAL LYS MET ARG PHE          
SEQRES  22 B  449  LEU GLU ASN HIS ASP ASN ALA ARG MET MET SER LEU MET          
SEQRES  23 B  449  HIS SER LYS ALA GLU ALA VAL ASN ASN LEU THR TRP ILE          
SEQRES  24 B  449  PHE MET GLN ARG GLY ILE PRO LEU ILE TYR ASN GLY GLN          
SEQRES  25 B  449  GLU PHE LEU ALA GLU HIS GLN PRO SER LEU PHE ASP ARG          
SEQRES  26 B  449  ASP THR MET VAL ALA ASP ARG HIS GLY ASP VAL THR PRO          
SEQRES  27 B  449  LEU ILE GLN LYS LEU VAL THR ILE LYS GLN LEU PRO LEU          
SEQRES  28 B  449  LEU ARG ALA ALA ASP TYR GLN LEU ALA VAL VAL GLU GLU          
SEQRES  29 B  449  GLY ILE VAL LYS ILE THR TYR ARG ALA ALA GLY GLU ALA          
SEQRES  30 B  449  LEU THR ALA TRP ILE PRO LEU LYS GLY GLN VAL THR ALA          
SEQRES  31 B  449  VAL ALA THR LYS LEU ALA ALA GLY SER TYR GLN ASN LEU          
SEQRES  32 B  449  LEU THR ASP GLY PRO THR GLU VAL VAL ASP GLY LYS LEU          
SEQRES  33 B  449  THR VAL ASP GLY GLN PRO VAL LEU ILE LYS TYR VAL THR          
SEQRES  34 B  449  ASN THR ALA VAL THR LYS VAL ALA ASP GLN SER ASN GLU          
SEQRES  35 B  449  GLY HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 C  449  MET SER LEU ARG ASP THR GLN THR GLN LEU ARG ASN GLU          
SEQRES   2 C  449  MET ILE TYR SER VAL PHE VAL ARG ASN TYR SER GLU ALA          
SEQRES   3 C  449  GLY ASN PHE ALA GLY VAL THR ALA ASP LEU GLN ARG ILE          
SEQRES   4 C  449  LYS ASP LEU GLY THR ASP ILE LEU TRP LEU LEU PRO ILE          
SEQRES   5 C  449  ASN PRO ILE GLY GLU VAL ASN ARG LYS GLY THR LEU GLY          
SEQRES   6 C  449  SER PRO TYR ALA ILE LYS ASP TYR ARG GLY ILE ASN PRO          
SEQRES   7 C  449  GLU TYR GLY THR LEU ALA ASP PHE LYS ALA LEU THR ASP          
SEQRES   8 C  449  ARG ALA HIS GLU LEU GLY MET LYS VAL MET LEU ASP ILE          
SEQRES   9 C  449  VAL TYR ASN HIS THR SER PRO ASP SER VAL LEU ALA THR          
SEQRES  10 C  449  GLU HIS PRO GLU TRP PHE TYR HIS ASP ALA ASP GLY GLN          
SEQRES  11 C  449  LEU THR ASN LYS VAL GLY ASP TRP SER ASP VAL LYS ASP          
SEQRES  12 C  449  LEU ASP TYR GLY HIS HIS GLU LEU TRP GLN TYR GLN ILE          
SEQRES  13 C  449  ASP THR LEU LEU TYR TRP SER GLN PHE VAL ASP GLY TYR          
SEQRES  14 C  449  ARG CYS ASP VAL ALA PRO LEU VAL PRO LEU ASP PHE TRP          
SEQRES  15 C  449  LEU GLU ALA ARG LYS GLN VAL ASN ALA LYS TYR PRO GLU          
SEQRES  16 C  449  THR LEU TRP LEU ALA GLU SER ALA GLY SER GLY PHE ILE          
SEQRES  17 C  449  GLU GLU LEU ARG SER GLN GLY TYR THR GLY LEU SER ASP          
SEQRES  18 C  449  SER GLU LEU TYR GLN ALA PHE ASP MET THR TYR ASP TYR          
SEQRES  19 C  449  ASP VAL PHE GLY ASP PHE LYS ASP TYR TRP GLN GLY ARG          
SEQRES  20 C  449  SER THR VAL GLU ARG TYR VAL ASP LEU LEU GLN ARG GLN          
SEQRES  21 C  449  ASP ALA THR PHE PRO GLY ASN TYR VAL LYS MET ARG PHE          
SEQRES  22 C  449  LEU GLU ASN HIS ASP ASN ALA ARG MET MET SER LEU MET          
SEQRES  23 C  449  HIS SER LYS ALA GLU ALA VAL ASN ASN LEU THR TRP ILE          
SEQRES  24 C  449  PHE MET GLN ARG GLY ILE PRO LEU ILE TYR ASN GLY GLN          
SEQRES  25 C  449  GLU PHE LEU ALA GLU HIS GLN PRO SER LEU PHE ASP ARG          
SEQRES  26 C  449  ASP THR MET VAL ALA ASP ARG HIS GLY ASP VAL THR PRO          
SEQRES  27 C  449  LEU ILE GLN LYS LEU VAL THR ILE LYS GLN LEU PRO LEU          
SEQRES  28 C  449  LEU ARG ALA ALA ASP TYR GLN LEU ALA VAL VAL GLU GLU          
SEQRES  29 C  449  GLY ILE VAL LYS ILE THR TYR ARG ALA ALA GLY GLU ALA          
SEQRES  30 C  449  LEU THR ALA TRP ILE PRO LEU LYS GLY GLN VAL THR ALA          
SEQRES  31 C  449  VAL ALA THR LYS LEU ALA ALA GLY SER TYR GLN ASN LEU          
SEQRES  32 C  449  LEU THR ASP GLY PRO THR GLU VAL VAL ASP GLY LYS LEU          
SEQRES  33 C  449  THR VAL ASP GLY GLN PRO VAL LEU ILE LYS TYR VAL THR          
SEQRES  34 C  449  ASN THR ALA VAL THR LYS VAL ALA ASP GLN SER ASN GLU          
SEQRES  35 C  449  GLY HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 D  449  MET SER LEU ARG ASP THR GLN THR GLN LEU ARG ASN GLU          
SEQRES   2 D  449  MET ILE TYR SER VAL PHE VAL ARG ASN TYR SER GLU ALA          
SEQRES   3 D  449  GLY ASN PHE ALA GLY VAL THR ALA ASP LEU GLN ARG ILE          
SEQRES   4 D  449  LYS ASP LEU GLY THR ASP ILE LEU TRP LEU LEU PRO ILE          
SEQRES   5 D  449  ASN PRO ILE GLY GLU VAL ASN ARG LYS GLY THR LEU GLY          
SEQRES   6 D  449  SER PRO TYR ALA ILE LYS ASP TYR ARG GLY ILE ASN PRO          
SEQRES   7 D  449  GLU TYR GLY THR LEU ALA ASP PHE LYS ALA LEU THR ASP          
SEQRES   8 D  449  ARG ALA HIS GLU LEU GLY MET LYS VAL MET LEU ASP ILE          
SEQRES   9 D  449  VAL TYR ASN HIS THR SER PRO ASP SER VAL LEU ALA THR          
SEQRES  10 D  449  GLU HIS PRO GLU TRP PHE TYR HIS ASP ALA ASP GLY GLN          
SEQRES  11 D  449  LEU THR ASN LYS VAL GLY ASP TRP SER ASP VAL LYS ASP          
SEQRES  12 D  449  LEU ASP TYR GLY HIS HIS GLU LEU TRP GLN TYR GLN ILE          
SEQRES  13 D  449  ASP THR LEU LEU TYR TRP SER GLN PHE VAL ASP GLY TYR          
SEQRES  14 D  449  ARG CYS ASP VAL ALA PRO LEU VAL PRO LEU ASP PHE TRP          
SEQRES  15 D  449  LEU GLU ALA ARG LYS GLN VAL ASN ALA LYS TYR PRO GLU          
SEQRES  16 D  449  THR LEU TRP LEU ALA GLU SER ALA GLY SER GLY PHE ILE          
SEQRES  17 D  449  GLU GLU LEU ARG SER GLN GLY TYR THR GLY LEU SER ASP          
SEQRES  18 D  449  SER GLU LEU TYR GLN ALA PHE ASP MET THR TYR ASP TYR          
SEQRES  19 D  449  ASP VAL PHE GLY ASP PHE LYS ASP TYR TRP GLN GLY ARG          
SEQRES  20 D  449  SER THR VAL GLU ARG TYR VAL ASP LEU LEU GLN ARG GLN          
SEQRES  21 D  449  ASP ALA THR PHE PRO GLY ASN TYR VAL LYS MET ARG PHE          
SEQRES  22 D  449  LEU GLU ASN HIS ASP ASN ALA ARG MET MET SER LEU MET          
SEQRES  23 D  449  HIS SER LYS ALA GLU ALA VAL ASN ASN LEU THR TRP ILE          
SEQRES  24 D  449  PHE MET GLN ARG GLY ILE PRO LEU ILE TYR ASN GLY GLN          
SEQRES  25 D  449  GLU PHE LEU ALA GLU HIS GLN PRO SER LEU PHE ASP ARG          
SEQRES  26 D  449  ASP THR MET VAL ALA ASP ARG HIS GLY ASP VAL THR PRO          
SEQRES  27 D  449  LEU ILE GLN LYS LEU VAL THR ILE LYS GLN LEU PRO LEU          
SEQRES  28 D  449  LEU ARG ALA ALA ASP TYR GLN LEU ALA VAL VAL GLU GLU          
SEQRES  29 D  449  GLY ILE VAL LYS ILE THR TYR ARG ALA ALA GLY GLU ALA          
SEQRES  30 D  449  LEU THR ALA TRP ILE PRO LEU LYS GLY GLN VAL THR ALA          
SEQRES  31 D  449  VAL ALA THR LYS LEU ALA ALA GLY SER TYR GLN ASN LEU          
SEQRES  32 D  449  LEU THR ASP GLY PRO THR GLU VAL VAL ASP GLY LYS LEU          
SEQRES  33 D  449  THR VAL ASP GLY GLN PRO VAL LEU ILE LYS TYR VAL THR          
SEQRES  34 D  449  ASN THR ALA VAL THR LYS VAL ALA ASP GLN SER ASN GLU          
SEQRES  35 D  449  GLY HIS HIS HIS HIS HIS HIS                                  
FORMUL   5  HOH   *1331(H2 O)                                                   
HELIX    1   1 GLN A    6  GLU A   12  5                                   7    
HELIX    2   2 PHE A   18  SER A   23  1                                   6    
HELIX    3   3 ASN A   27  ALA A   33  1                                   7    
HELIX    4   4 ASP A   34  GLY A   42  1                                   9    
HELIX    5   5 ASN A   76  GLY A   80  5                                   5    
HELIX    6   6 THR A   81  LEU A   95  1                                  15    
HELIX    7   7 SER A  112  HIS A  118  1                                   7    
HELIX    8   8 PRO A  119  PHE A  122  5                                   4    
HELIX    9   9 HIS A  147  SER A  162  1                                  16    
HELIX   10  10 VAL A  172  VAL A  176  5                                   5    
HELIX   11  11 PRO A  177  TYR A  192  1                                  16    
HELIX   12  12 GLY A  203  GLN A  213  1                                  11    
HELIX   13  13 SER A  219  GLN A  225  1                                   7    
HELIX   14  14 VAL A  235  GLN A  244  1                                  10    
HELIX   15  15 THR A  248  ALA A  261  1                                  14    
HELIX   16  16 ARG A  280  MET A  285  1                                   6    
HELIX   17  17 SER A  287  GLN A  301  1                                  15    
HELIX   18  18 GLY A  310  LEU A  314  5                                   5    
HELIX   19  19 VAL A  335  GLN A  347  1                                  13    
HELIX   20  20 LEU A  348  ALA A  353  5                                   6    
HELIX   21  21 GLU A  362  GLY A  364  5                                   3    
HELIX   22  22 GLN B    6  GLU B   12  5                                   7    
HELIX   23  23 PHE B   18  SER B   23  1                                   6    
HELIX   24  24 ASN B   27  ALA B   33  1                                   7    
HELIX   25  25 ASP B   34  GLY B   42  1                                   9    
HELIX   26  26 THR B   81  GLY B   96  1                                  16    
HELIX   27  27 SER B  112  HIS B  118  1                                   7    
HELIX   28  28 PRO B  119  PHE B  122  5                                   4    
HELIX   29  29 HIS B  147  SER B  162  1                                  16    
HELIX   30  30 VAL B  172  VAL B  176  5                                   5    
HELIX   31  31 PRO B  177  TYR B  192  1                                  16    
HELIX   32  32 GLY B  203  GLN B  213  1                                  11    
HELIX   33  33 SER B  219  PHE B  227  1                                   9    
HELIX   34  34 VAL B  235  GLN B  244  1                                  10    
HELIX   35  35 THR B  248  ALA B  261  1                                  14    
HELIX   36  36 ARG B  280  MET B  285  1                                   6    
HELIX   37  37 SER B  287  GLN B  301  1                                  15    
HELIX   38  38 GLY B  310  LEU B  314  5                                   5    
HELIX   39  39 VAL B  335  GLN B  347  1                                  13    
HELIX   40  40 LEU B  348  ALA B  353  5                                   6    
HELIX   41  41 GLU B  362  GLY B  364  5                                   3    
HELIX   42  42 GLN C    6  GLU C   12  5                                   7    
HELIX   43  43 PHE C   18  SER C   23  1                                   6    
HELIX   44  44 ASN C   27  ALA C   33  1                                   7    
HELIX   45  45 ASP C   34  GLY C   42  1                                   9    
HELIX   46  46 ASN C   76  GLY C   80  5                                   5    
HELIX   47  47 THR C   81  LEU C   95  1                                  15    
HELIX   48  48 SER C  112  HIS C  118  1                                   7    
HELIX   49  49 PRO C  119  PHE C  122  5                                   4    
HELIX   50  50 HIS C  148  SER C  162  1                                  15    
HELIX   51  51 VAL C  172  VAL C  176  5                                   5    
HELIX   52  52 PRO C  177  TYR C  192  1                                  16    
HELIX   53  53 GLY C  203  GLN C  213  1                                  11    
HELIX   54  54 SER C  219  TYR C  224  1                                   6    
HELIX   55  55 VAL C  235  GLN C  244  1                                  10    
HELIX   56  56 THR C  248  PHE C  263  1                                  16    
HELIX   57  57 ARG C  280  MET C  285  1                                   6    
HELIX   58  58 SER C  287  GLN C  301  1                                  15    
HELIX   59  59 GLY C  310  LEU C  314  5                                   5    
HELIX   60  60 VAL C  335  GLN C  347  1                                  13    
HELIX   61  61 LEU C  348  ALA C  353  5                                   6    
HELIX   62  62 GLU C  362  GLY C  364  5                                   3    
HELIX   63  63 GLN D    6  GLU D   12  5                                   7    
HELIX   64  64 PHE D   18  SER D   23  1                                   6    
HELIX   65  65 ASN D   27  ALA D   33  1                                   7    
HELIX   66  66 ASP D   34  GLY D   42  1                                   9    
HELIX   67  67 ASN D   76  GLY D   80  5                                   5    
HELIX   68  68 THR D   81  LEU D   95  1                                  15    
HELIX   69  69 SER D  112  HIS D  118  1                                   7    
HELIX   70  70 PRO D  119  PHE D  122  5                                   4    
HELIX   71  71 HIS D  147  SER D  162  1                                  16    
HELIX   72  72 VAL D  172  VAL D  176  5                                   5    
HELIX   73  73 PRO D  177  TYR D  192  1                                  16    
HELIX   74  74 GLY D  203  GLN D  213  1                                  11    
HELIX   75  75 SER D  219  GLN D  225  1                                   7    
HELIX   76  76 VAL D  235  GLN D  244  1                                  10    
HELIX   77  77 THR D  248  PHE D  263  1                                  16    
HELIX   78  78 ARG D  280  MET D  285  1                                   6    
HELIX   79  79 SER D  287  GLN D  301  1                                  15    
HELIX   80  80 GLY D  310  LEU D  314  5                                   5    
HELIX   81  81 VAL D  335  GLN D  347  1                                  13    
HELIX   82  82 LEU D  348  ALA D  353  5                                   6    
HELIX   83  83 GLU D  362  GLY D  364  5                                   3    
SHEET    1   A 9 ILE A  14  VAL A  17  0                                        
SHEET    2   A 9 ILE A  45  LEU A  48  1  O  TRP A  47   N  VAL A  17           
SHEET    3   A 9 LYS A  98  ILE A 103  1  O  LYS A  98   N  LEU A  46           
SHEET    4   A 9 GLY A 167  CYS A 170  1  O  ARG A 169   N  ILE A 103           
SHEET    5   A 9 LEU A 196  ALA A 199  1  O  LEU A 198   N  CYS A 170           
SHEET    6   A 9 MET A 229  TYR A 231  1  O  MET A 229   N  ALA A 199           
SHEET    7   A 9 VAL A 268  ARG A 271  1  O  MET A 270   N  THR A 230           
SHEET    8   A 9 ILE A 304  TYR A 308  1  O  ILE A 304   N  LYS A 269           
SHEET    9   A 9 ILE A  14  VAL A  17  1  N  ILE A  14   O  PRO A 305           
SHEET    1   B 2 HIS A 107  THR A 108  0                                        
SHEET    2   B 2 LYS A 141  ASP A 142 -1  O  LYS A 141   N  THR A 108           
SHEET    1   C 4 ASP A 355  VAL A 360  0                                        
SHEET    2   C 4 VAL A 366  ALA A 372 -1  O  LYS A 367   N  ALA A 359           
SHEET    3   C 4 GLU A 375  ILE A 381 -1  O  ILE A 381   N  VAL A 366           
SHEET    4   C 4 VAL A 422  TYR A 426 -1  O  VAL A 422   N  TRP A 380           
SHEET    1   D 2 VAL A 387  ALA A 391  0                                        
SHEET    2   D 2 LYS A 414  ASP A 418 -1  O  LEU A 415   N  VAL A 390           
SHEET    1   E 2 GLY A 397  ASN A 401  0                                        
SHEET    2   E 2 GLY A 406  VAL A 410 -1  O  VAL A 410   N  GLY A 397           
SHEET    1   F 9 ILE B  14  VAL B  17  0                                        
SHEET    2   F 9 ILE B  45  LEU B  48  1  O  ILE B  45   N  TYR B  15           
SHEET    3   F 9 LYS B  98  ILE B 103  1  O  MET B 100   N  LEU B  46           
SHEET    4   F 9 GLY B 167  CYS B 170  1  O  ARG B 169   N  ILE B 103           
SHEET    5   F 9 LEU B 196  ALA B 199  1  O  LEU B 196   N  TYR B 168           
SHEET    6   F 9 MET B 229  TYR B 231  1  O  MET B 229   N  ALA B 199           
SHEET    7   F 9 VAL B 268  ARG B 271  1  O  MET B 270   N  THR B 230           
SHEET    8   F 9 ILE B 304  TYR B 308  1  O  LEU B 306   N  ARG B 271           
SHEET    9   F 9 ILE B  14  VAL B  17  1  N  ILE B  14   O  PRO B 305           
SHEET    1   G 2 HIS B 107  THR B 108  0                                        
SHEET    2   G 2 LYS B 141  ASP B 142 -1  O  LYS B 141   N  THR B 108           
SHEET    1   H 4 ASP B 355  VAL B 360  0                                        
SHEET    2   H 4 VAL B 366  ALA B 372 -1  O  LYS B 367   N  ALA B 359           
SHEET    3   H 4 GLU B 375  ILE B 381 -1  O  ILE B 381   N  VAL B 366           
SHEET    4   H 4 VAL B 422  TYR B 426 -1  O  TYR B 426   N  ALA B 376           
SHEET    1   I 4 VAL B 387  ALA B 391  0                                        
SHEET    2   I 4 LYS B 414  ASP B 418 -1  O  LEU B 415   N  VAL B 390           
SHEET    3   I 4 PRO B 407  VAL B 411 -1  N  VAL B 411   O  LYS B 414           
SHEET    4   I 4 GLY B 397  GLN B 400 -1  N  GLY B 397   O  VAL B 410           
SHEET    1   J 9 ILE C  14  VAL C  17  0                                        
SHEET    2   J 9 ILE C  45  LEU C  48  1  O  TRP C  47   N  VAL C  17           
SHEET    3   J 9 LYS C  98  ILE C 103  1  O  LYS C  98   N  LEU C  46           
SHEET    4   J 9 GLY C 167  CYS C 170  1  O  ARG C 169   N  ILE C 103           
SHEET    5   J 9 LEU C 196  ALA C 199  1  O  LEU C 198   N  CYS C 170           
SHEET    6   J 9 MET C 229  TYR C 231  1  O  MET C 229   N  ALA C 199           
SHEET    7   J 9 VAL C 268  ARG C 271  1  O  MET C 270   N  THR C 230           
SHEET    8   J 9 ILE C 304  TYR C 308  1  O  ILE C 304   N  LYS C 269           
SHEET    9   J 9 ILE C  14  VAL C  17  1  N  ILE C  14   O  ILE C 307           
SHEET    1   K 2 HIS C 107  THR C 108  0                                        
SHEET    2   K 2 LYS C 141  ASP C 142 -1  O  LYS C 141   N  THR C 108           
SHEET    1   L 4 ASP C 355  VAL C 360  0                                        
SHEET    2   L 4 VAL C 366  ALA C 372 -1  O  LYS C 367   N  ALA C 359           
SHEET    3   L 4 GLU C 375  ILE C 381 -1  O  ILE C 381   N  VAL C 366           
SHEET    4   L 4 VAL C 422  TYR C 426 -1  O  ILE C 424   N  THR C 378           
SHEET    1   M 4 VAL C 387  ALA C 391  0                                        
SHEET    2   M 4 LYS C 414  ASP C 418 -1  O  LEU C 415   N  VAL C 390           
SHEET    3   M 4 PRO C 407  VAL C 411 -1  N  VAL C 411   O  LYS C 414           
SHEET    4   M 4 GLY C 397  GLN C 400 -1  N  TYR C 399   O  THR C 408           
SHEET    1   N 9 ILE D  14  VAL D  17  0                                        
SHEET    2   N 9 ILE D  45  LEU D  48  1  O  TRP D  47   N  VAL D  17           
SHEET    3   N 9 LYS D  98  ILE D 103  1  O  LYS D  98   N  LEU D  46           
SHEET    4   N 9 GLY D 167  CYS D 170  1  O  ARG D 169   N  LEU D 101           
SHEET    5   N 9 LEU D 196  ALA D 199  1  O  LEU D 198   N  CYS D 170           
SHEET    6   N 9 MET D 229  TYR D 231  1  O  MET D 229   N  ALA D 199           
SHEET    7   N 9 LYS D 269  ARG D 271  1  O  MET D 270   N  THR D 230           
SHEET    8   N 9 ILE D 304  TYR D 308  1  O  ILE D 304   N  ARG D 271           
SHEET    9   N 9 ILE D  14  VAL D  17  1  N  ILE D  14   O  PRO D 305           
SHEET    1   O 2 HIS D 107  THR D 108  0                                        
SHEET    2   O 2 LYS D 141  ASP D 142 -1  O  LYS D 141   N  THR D 108           
SHEET    1   P 4 ASP D 355  VAL D 360  0                                        
SHEET    2   P 4 VAL D 366  ALA D 372 -1  O  LYS D 367   N  ALA D 359           
SHEET    3   P 4 GLU D 375  ILE D 381 -1  O  ALA D 379   N  ILE D 368           
SHEET    4   P 4 VAL D 422  TYR D 426 -1  O  ILE D 424   N  THR D 378           
SHEET    1   Q 4 VAL D 387  ALA D 391  0                                        
SHEET    2   Q 4 LYS D 414  ASP D 418 -1  O  VAL D 417   N  THR D 388           
SHEET    3   Q 4 PRO D 407  VAL D 411 -1  N  VAL D 411   O  LYS D 414           
SHEET    4   Q 4 GLY D 397  GLN D 400 -1  N  TYR D 399   O  THR D 408           
CRYST1  202.279   63.773  155.677  90.00 102.93  90.00 C 1 2 1      16          
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      0.004944  0.000000  0.001135        0.00000                         
SCALE2      0.000000  0.015681  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006591        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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