GenomeNet

Database: PDB
Entry: 4A3Q
LinkDB: 4A3Q
Original site: 4A3Q 
HEADER    ISOMERASE                               04-OCT-11   4A3Q              
TITLE     THE 2.15 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF STAPHYLOCOCCUS      
TITLE    2 AUREUS ALANINE RACEMASE                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE RACEMASE 1;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 STRAIN: MU50;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: PLYSS;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET26B                                     
KEYWDS    ISOMERASE, PLP-DEPENDENT ENZYMES                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.R.SCALETTI,S.R.LUCKNER,K.L.KRAUSE                                   
REVDAT   2   28-MAR-12 4A3Q    1       JRNL                                     
REVDAT   1   28-DEC-11 4A3Q    0                                                
JRNL        AUTH   E.R.SCALETTI,S.R.LUCKNER,K.L.KRAUSE                          
JRNL        TITL   STRUCTURAL FEATURES AND KINETIC CHARACTERIZATION OF ALANINE  
JRNL        TITL 2 RACEMASE FROM STAPHYLOCOCCUS AUREUS (MU50)                   
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  68    82 2012              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   22194336                                                     
JRNL        DOI    10.1107/S0907444911050682                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.41                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.57                          
REMARK   3   NUMBER OF REFLECTIONS             : 46865                          
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) : 0.19084                         
REMARK   3   R VALUE            (WORKING SET) : 0.18846                         
REMARK   3   FREE R VALUE                     : 0.23640                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2519                            
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) : 2.152                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.208                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3055                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.211                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 164                          
REMARK   3   BIN FREE R VALUE                    : 0.251                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5632                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 103                                     
REMARK   3   SOLVENT ATOMS            : 266                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.5                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.733                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00                                                 
REMARK   3    B22 (A**2) : 0.00                                                 
REMARK   3    B33 (A**2) : 0.00                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.215         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.188         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.110         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.093         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.910                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5837 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7910 ; 1.350 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   708 ; 6.087 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   261 ;36.179 ;24.866       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1031 ;14.219 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;16.955 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   896 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4288 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  3554 ; 0.881 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5756 ; 1.656 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2283 ; 2.427 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2154 ; 4.033 ; 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 : 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. RESIDUES 170-176 AND 257-274 ARE DISORDERED      
REMARK   4                                                                      
REMARK   4 4A3Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-OCT-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-49873.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 5.0                                
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                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE (R-AXIS IV)            
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU-MSC                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49388                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.15                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 51.91                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 3.8                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.19                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.30                               
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 1SFT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE TRIHYDRATE         
REMARK 280  (PH 5.0), 1.8 M AMMONIUM SULFATE.                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       32.57000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.99500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.97000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.99500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.57000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.97000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -225.3 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A   170                                                      
REMARK 465     CYS A   171                                                      
REMARK 465     ALA A   172                                                      
REMARK 465     ASP A   173                                                      
REMARK 465     GLU A   174                                                      
REMARK 465     PRO A   175                                                      
REMARK 465     GLY A   176                                                      
REMARK 465     LEU A   257                                                      
REMARK 465     GLN A   258                                                      
REMARK 465     ALA A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLU A   261                                                      
REMARK 465     SER A   262                                                      
REMARK 465     VAL A   263                                                      
REMARK 465     SER A   264                                                      
REMARK 465     TYR A   265                                                      
REMARK 465     GLY A   266                                                      
REMARK 465     ALA A   267                                                      
REMARK 465     THR A   268                                                      
REMARK 465     TYR A   269                                                      
REMARK 465     THR A   270                                                      
REMARK 465     ALA A   271                                                      
REMARK 465     THR A   272                                                      
REMARK 465     ASP A   273                                                      
REMARK 465     PRO A   274                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B   170                                                      
REMARK 465     CYS B   171                                                      
REMARK 465     ALA B   172                                                      
REMARK 465     ASP B   173                                                      
REMARK 465     GLU B   174                                                      
REMARK 465     PRO B   175                                                      
REMARK 465     GLY B   176                                                      
REMARK 465     ASP B   177                                                      
REMARK 465     MET B   178                                                      
REMARK 465     GLN B   258                                                      
REMARK 465     ALA B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLU B   261                                                      
REMARK 465     SER B   262                                                      
REMARK 465     VAL B   263                                                      
REMARK 465     SER B   264                                                      
REMARK 465     TYR B   265                                                      
REMARK 465     GLY B   266                                                      
REMARK 465     ALA B   267                                                      
REMARK 465     THR B   268                                                      
REMARK 465     TYR B   269                                                      
REMARK 465     THR B   270                                                      
REMARK 465     ALA B   271                                                      
REMARK 465     THR B   272                                                      
REMARK 465     ASP B   273                                                      
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 138    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 256    OG1  CG2                                            
REMARK 470     MET B 136    CG   SD   CE                                        
REMARK 470     ARG B 138    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 257    CG   CD1  CD2                                       
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    HIS A  53   CB  -  CG  -  ND1 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    HIS A  76   CB  -  CG  -  ND1 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    HIS A 129   CB  -  CG  -  ND1 ANGL. DEV. =   9.4 DEGREES          
REMARK 500    HIS A 369   CB  -  CG  -  ND1 ANGL. DEV. =   9.5 DEGREES          
REMARK 500    HIS B  53   CB  -  CG  -  ND1 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    HIS B 129   CB  -  CG  -  ND1 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    HIS B 369   CB  -  CG  -  ND1 ANGL. DEV. =   9.9 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    ARG A 138     -129.20   -111.09                                   
REMARK 500    CYS A 201      -12.85   -140.63                                   
REMARK 500    ASN A 300       49.24     36.86                                   
REMARK 500    ASN A 334       44.49    -88.29                                   
REMARK 500    GLU A 337       78.43   -104.12                                   
REMARK 500    THR A 351     -159.49   -145.85                                   
REMARK 500    THR B 134       48.26   -108.38                                   
REMARK 500    ARG B 138      -94.08    -90.74                                   
REMARK 500    ASN B 203     -164.94    -79.93                                   
REMARK 500    CYS B 212       71.13     50.44                                   
REMARK 500    ILE B 291       -9.81    -59.11                                   
REMARK 500    ASN B 300       49.57     34.46                                   
REMARK 500    ASN B 334       45.62    -85.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A1039                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1383                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1384                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1385                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1386                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1387                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1388                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1389                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B1039                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1383                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1384                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1385                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1386                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1387                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1388                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1389                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B1390                 
DBREF  4A3Q A    1   382  UNP    P63479   ALR1_STAAM       1    382             
DBREF  4A3Q B    1   382  UNP    P63479   ALR1_STAAM       1    382             
SEQRES   1 A  382  MET SER ASP LYS TYR TYR ARG SER ALA TYR MET ASN VAL          
SEQRES   2 A  382  ASP LEU ASN ALA VAL ALA SER ASN PHE LYS VAL PHE SER          
SEQRES   3 A  382  THR LEU HIS PRO ASN LYS THR VAL MET ALA VAL VAL LYS          
SEQRES   4 A  382  ALA ASN ALA TYR GLY LEU GLY SER VAL LYS VAL ALA ARG          
SEQRES   5 A  382  HIS LEU MET GLU ASN GLY ALA THR PHE PHE ALA VAL ALA          
SEQRES   6 A  382  THR LEU ASP GLU ALA ILE GLU LEU ARG MET HIS GLY ILE          
SEQRES   7 A  382  THR ALA LYS ILE LEU VAL LEU GLY VAL LEU PRO ALA LYS          
SEQRES   8 A  382  ASP ILE ASP LYS ALA ILE GLN HIS ARG VAL ALA LEU THR          
SEQRES   9 A  382  VAL PRO SER LYS GLN TRP LEU LYS GLU ALA ILE LYS ASN          
SEQRES  10 A  382  ILE SER GLY GLU GLN GLU LYS LYS LEU TRP LEU HIS ILE          
SEQRES  11 A  382  LYS LEU ASP THR GLY MET GLY ARG LEU GLY ILE LYS ASP          
SEQRES  12 A  382  THR ASN THR TYR GLN GLU VAL ILE GLU ILE ILE GLN GLN          
SEQRES  13 A  382  TYR GLU GLN LEU VAL PHE GLU GLY VAL PHE THR HIS PHE          
SEQRES  14 A  382  ALA CYS ALA ASP GLU PRO GLY ASP MET THR THR GLU GLN          
SEQRES  15 A  382  TYR GLN ARG PHE LYS ASP MET VAL ASN GLU ALA ILE LYS          
SEQRES  16 A  382  PRO GLU TYR ILE HIS CYS GLN ASN SER ALA GLY SER LEU          
SEQRES  17 A  382  LEU MET ASP CYS GLN PHE CYS ASN ALA ILE ARG PRO GLY          
SEQRES  18 A  382  ILE SER LEU TYR GLY TYR TYR PRO SER GLU TYR VAL GLN          
SEQRES  19 A  382  GLN LYS VAL LYS VAL HIS LEU LYS PRO SER VAL GLN LEU          
SEQRES  20 A  382  ILE ALA ASN VAL VAL GLN THR LYS THR LEU GLN ALA GLY          
SEQRES  21 A  382  GLU SER VAL SER TYR GLY ALA THR TYR THR ALA THR ASP          
SEQRES  22 A  382  PRO THR THR ILE ALA LEU LEU PRO ILE GLY TYR ALA ASP          
SEQRES  23 A  382  GLY TYR LEU ARG ILE MET GLN GLY SER PHE VAL ASN VAL          
SEQRES  24 A  382  ASN GLY HIS GLN CYS GLU VAL ILE GLY ARG VAL CYS MET          
SEQRES  25 A  382  ASP GLN THR ILE VAL LYS VAL PRO ASP GLN VAL LYS ALA          
SEQRES  26 A  382  GLY ASP SER VAL ILE LEU ILE ASP ASN HIS ARG GLU SER          
SEQRES  27 A  382  PRO GLN SER VAL GLU VAL VAL ALA GLU LYS GLN HIS THR          
SEQRES  28 A  382  ILE ASN TYR GLU VAL LEU CYS ASN LEU SER ARG ARG LEU          
SEQRES  29 A  382  PRO ARG ILE TYR HIS ASP GLY ASP GLN ARG PHE VAL THR          
SEQRES  30 A  382  ASN GLU LEU LEU LYS                                          
SEQRES   1 B  382  MET SER ASP LYS TYR TYR ARG SER ALA TYR MET ASN VAL          
SEQRES   2 B  382  ASP LEU ASN ALA VAL ALA SER ASN PHE LYS VAL PHE SER          
SEQRES   3 B  382  THR LEU HIS PRO ASN LYS THR VAL MET ALA VAL VAL LYS          
SEQRES   4 B  382  ALA ASN ALA TYR GLY LEU GLY SER VAL LYS VAL ALA ARG          
SEQRES   5 B  382  HIS LEU MET GLU ASN GLY ALA THR PHE PHE ALA VAL ALA          
SEQRES   6 B  382  THR LEU ASP GLU ALA ILE GLU LEU ARG MET HIS GLY ILE          
SEQRES   7 B  382  THR ALA LYS ILE LEU VAL LEU GLY VAL LEU PRO ALA LYS          
SEQRES   8 B  382  ASP ILE ASP LYS ALA ILE GLN HIS ARG VAL ALA LEU THR          
SEQRES   9 B  382  VAL PRO SER LYS GLN TRP LEU LYS GLU ALA ILE LYS ASN          
SEQRES  10 B  382  ILE SER GLY GLU GLN GLU LYS LYS LEU TRP LEU HIS ILE          
SEQRES  11 B  382  LYS LEU ASP THR GLY MET GLY ARG LEU GLY ILE LYS ASP          
SEQRES  12 B  382  THR ASN THR TYR GLN GLU VAL ILE GLU ILE ILE GLN GLN          
SEQRES  13 B  382  TYR GLU GLN LEU VAL PHE GLU GLY VAL PHE THR HIS PHE          
SEQRES  14 B  382  ALA CYS ALA ASP GLU PRO GLY ASP MET THR THR GLU GLN          
SEQRES  15 B  382  TYR GLN ARG PHE LYS ASP MET VAL ASN GLU ALA ILE LYS          
SEQRES  16 B  382  PRO GLU TYR ILE HIS CYS GLN ASN SER ALA GLY SER LEU          
SEQRES  17 B  382  LEU MET ASP CYS GLN PHE CYS ASN ALA ILE ARG PRO GLY          
SEQRES  18 B  382  ILE SER LEU TYR GLY TYR TYR PRO SER GLU TYR VAL GLN          
SEQRES  19 B  382  GLN LYS VAL LYS VAL HIS LEU LYS PRO SER VAL GLN LEU          
SEQRES  20 B  382  ILE ALA ASN VAL VAL GLN THR LYS THR LEU GLN ALA GLY          
SEQRES  21 B  382  GLU SER VAL SER TYR GLY ALA THR TYR THR ALA THR ASP          
SEQRES  22 B  382  PRO THR THR ILE ALA LEU LEU PRO ILE GLY TYR ALA ASP          
SEQRES  23 B  382  GLY TYR LEU ARG ILE MET GLN GLY SER PHE VAL ASN VAL          
SEQRES  24 B  382  ASN GLY HIS GLN CYS GLU VAL ILE GLY ARG VAL CYS MET          
SEQRES  25 B  382  ASP GLN THR ILE VAL LYS VAL PRO ASP GLN VAL LYS ALA          
SEQRES  26 B  382  GLY ASP SER VAL ILE LEU ILE ASP ASN HIS ARG GLU SER          
SEQRES  27 B  382  PRO GLN SER VAL GLU VAL VAL ALA GLU LYS GLN HIS THR          
SEQRES  28 B  382  ILE ASN TYR GLU VAL LEU CYS ASN LEU SER ARG ARG LEU          
SEQRES  29 B  382  PRO ARG ILE TYR HIS ASP GLY ASP GLN ARG PHE VAL THR          
SEQRES  30 B  382  ASN GLU LEU LEU LYS                                          
HET    PLP  A1039      15                                                       
HET    SO4  A1383       5                                                       
HET    SO4  A1384       5                                                       
HET    SO4  A1385       5                                                       
HET    SO4  A1386       5                                                       
HET    SO4  A1387       5                                                       
HET    SO4  A1388       5                                                       
HET    ACT  A1389       4                                                       
HET    PLP  B1039      15                                                       
HET    SO4  B1383       5                                                       
HET    SO4  B1384       5                                                       
HET    SO4  B1385       5                                                       
HET    SO4  B1386       5                                                       
HET    SO4  B1387       5                                                       
HET    SO4  B1388       5                                                       
HET    SO4  B1389       5                                                       
HET    ACT  B1390       4                                                       
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   3  PLP    2(C8 H10 N O6 P)                                             
FORMUL   4  SO4    13(O4 S 2-)                                                  
FORMUL   5  ACT    2(C2 H3 O2 1-)                                               
FORMUL   6  HOH   *266(H2 O)                                                    
HELIX    1   1 LEU A   15  LEU A   28  1                                  14    
HELIX    2   2 SER A   47  ASN A   57  1                                  11    
HELIX    3   3 LEU A   67  MET A   75  1                                   9    
HELIX    4   4 ILE A   93  HIS A   99  1                                   7    
HELIX    5   5 LYS A  108  ASN A  117  1                                  10    
HELIX    6   6 THR A  144  GLN A  156  1                                  13    
HELIX    7   7 ASP A  177  ASN A  191  1                                  15    
HELIX    8   8 SER A  204  LEU A  209  1                                   6    
HELIX    9   9 GLU A  231  LYS A  236  1                                   6    
HELIX   10  10 VAL A  342  GLN A  349  1                                   8    
HELIX   11  11 ASN A  353  ASN A  359  1                                   7    
HELIX   12  12 LEU B   15  LEU B   28  1                                  14    
HELIX   13  13 SER B   47  GLU B   56  1                                  10    
HELIX   14  14 LEU B   67  HIS B   76  1                                  10    
HELIX   15  15 ILE B   93  HIS B   99  1                                   7    
HELIX   16  16 LYS B  108  ASN B  117  1                                  10    
HELIX   17  17 THR B  144  GLN B  156  1                                  13    
HELIX   18  18 THR B  179  ASN B  191  1                                  13    
HELIX   19  19 SER B  204  LEU B  209  1                                   6    
HELIX   20  20 GLU B  231  LYS B  236  1                                   6    
HELIX   21  21 VAL B  342  GLN B  349  1                                   8    
HELIX   22  22 ASN B  353  ASN B  359  1                                   7    
SHEET    1   1 1 ALA A   9  ASP A  14  0                                        
SHEET    1   2 1 THR A  33  VAL A  34  0                                        
SHEET    1   3 1 ALA A  36  VAL A  37  0                                        
SHEET    1   4 1 PHE A  61  VAL A  64  0                                        
SHEET    1   5 1 LYS A  81  VAL A  84  0                                        
SHEET    1   6 1 VAL A 101  VAL A 105  0                                        
SHEET    1   7 1 LEU A 126  LYS A 131  0                                        
SHEET    1   8 1 LEU A 160  PHE A 166  0                                        
SHEET    1   9 1 TYR A 198  GLN A 202  0                                        
SHEET    1  10 1 ALA A 217  ILE A 218  0                                        
SHEET    1  11 1 VAL A 245  VAL A 251  0                                        
SHEET    1  12 1 GLN A 253  LYS A 255  0                                        
SHEET    1  13 1 THR A 276  LEU A 280  0                                        
SHEET    1  14 1 SER A 295  VAL A 299  0                                        
SHEET    1  15 1 HIS A 302  VAL A 306  0                                        
SHEET    1  16 1 THR A 315  VAL A 319  0                                        
SHEET    1  17 1 ASP A 327  ILE A 332  0                                        
SHEET    1  18 1 ARG A 366  ASP A 370  0                                        
SHEET    1  19 1 GLN A 373  THR A 377  0                                        
SHEET    1  20 1 ALA B   9  ASP B  14  0                                        
SHEET    1  21 1 THR B  33  VAL B  34  0                                        
SHEET    1  22 1 ALA B  36  VAL B  37  0                                        
SHEET    1  23 1 PHE B  61  VAL B  64  0                                        
SHEET    1  24 1 LYS B  81  VAL B  84  0                                        
SHEET    1  25 1 LEU B 103  VAL B 105  0                                        
SHEET    1  26 1 LEU B 126  LYS B 131  0                                        
SHEET    1  27 1 LEU B 160  PHE B 166  0                                        
SHEET    1  28 1 TYR B 198  HIS B 200  0                                        
SHEET    1  29 1 ALA B 217  ILE B 218  0                                        
SHEET    1  30 1 VAL B 245  VAL B 251  0                                        
SHEET    1  31 1 GLN B 253  THR B 256  0                                        
SHEET    1  32 1 THR B 276  LEU B 280  0                                        
SHEET    1  33 1 SER B 295  VAL B 299  0                                        
SHEET    1  34 1 HIS B 302  VAL B 306  0                                        
SHEET    1  35 1 THR B 315  LYS B 318  0                                        
SHEET    1  36 1 ASP B 327  ILE B 332  0                                        
SHEET    1  37 1 ARG B 366  ASP B 370  0                                        
SHEET    1  38 1 GLN B 373  THR B 377  0                                        
LINK         NZ  LYS A  39                 C4A PLP A1039     1555   1555  1.36  
LINK         NZ  LYS B  39                 C4A PLP B1039     1555   1555  1.36  
SITE     1 AC1 10 LYS A  39  TYR A  43  HIS A 168  ASN A 203                    
SITE     2 AC1 10 SER A 204  ARG A 219  GLY A 221  ILE A 222                    
SITE     3 AC1 10 TYR A 354  HOH A2032                                          
SITE     1 AC2  6 TYR A 228  GLN A 234  HIS A 240  LEU A 241                    
SITE     2 AC2  6 ARG A 336  HOH A2118                                          
SITE     1 AC3  4 SER A 107  LYS A 108  GLN A 109  THR A 146                    
SITE     1 AC4  4 VAL A  48  LYS A  49  ARG A  52  HIS A  76                    
SITE     1 AC5  4 HIS A 335  ARG A 336  GLU A 337  HOH A2138                    
SITE     1 AC6  4 HIS A  29  PRO A  30  ASN A  31  LYS A  32                    
SITE     1 AC7  6 LYS A 131  ARG A 138  LEU A 139  HIS A 168                    
SITE     2 AC7  6 HOH A2080  GLN B 314                                          
SITE     1 AC8  5 CYS A 311  MET A 312  HOH A2135  LYS B  39                    
SITE     2 AC8  5 PLP B1039                                                     
SITE     1 AC9 10 ACT A1389  LYS B  39  TYR B  43  HIS B 168                    
SITE     2 AC9 10 SER B 204  ARG B 219  GLY B 221  ILE B 222                    
SITE     3 AC9 10 TYR B 354  HOH B2015                                          
SITE     1 BC1  7 TYR B 228  GLN B 234  HIS B 240  LEU B 241                    
SITE     2 BC1  7 ARG B 336  HOH B2067  HOH B2076                               
SITE     1 BC2  3 LYS B  49  ARG B  52  HIS B  76                               
SITE     1 BC3  7 SER A 361  ARG A 362  HOH A2152  LEU B 360                    
SITE     2 BC3  7 SER B 361  ARG B 362  HOH B2105                               
SITE     1 BC4  3 SER B 107  LYS B 108  GLN B 109                               
SITE     1 BC5  4 HIS B 335  ARG B 336  GLU B 337  HOH B2096                    
SITE     1 BC6  8 LYS A 108  LYS A 112  HIS B  29  PRO B  30                    
SITE     2 BC6  8 ASN B  31  LYS B  32  ASP B 211  GLN B 213                    
SITE     1 BC7  4 LYS B 131  ARG B 138  LEU B 139  HIS B 168                    
SITE     1 BC8  7 LYS A  39  TYR A 354  TYR B 284  CYS B 311                    
SITE     2 BC8  7 MET B 312  HOH B2078  HOH B2091                               
CRYST1   65.140  113.940  125.990  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015352  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008777  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007937        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system