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Database: PDB
Entry: 3B7U
LinkDB: 3B7U
Original site: 3B7U 
HEADER    HYDROLASE                               31-OCT-07   3B7U              
TITLE     LEUKOTRIENE A4 HYDROLASE COMPLEXED WITH KELATORPHAN                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUKOTRIENE A-4 HYDROLASE;                                 
COMPND   3 CHAIN: X;                                                            
COMPND   4 SYNONYM: LTA-4 HYDROLASE, LEUKOTRIENE A4, HYDROLASE;                 
COMPND   5 EC: 3.3.2.6;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LTA4H, LTA4;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM101;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT7T3                                     
KEYWDS    TRANSITION STATE, ANALOGUE PEPTIDE, HYDROLYSIS, ALTERNATIVE SPLICING, 
KEYWDS   2 CYTOPLASM, HYDROLASE, LEUKOTRIENE BIOSYNTHESIS, METAL-BINDING,       
KEYWDS   3 METALLOPROTEASE, MULTIFUNCTIONAL ENZYME, PROTEASE, ZINC              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.THOLANDER,J.HAEGGSTROM,M.THUNNISSEN,A.MUROYA,B.-P.ROQUES,M.-        
AUTHOR   2 C.FOURNIE-ZALUSKI                                                    
REVDAT   5   20-NOV-19 3B7U    1       SEQADV LINK                              
REVDAT   4   07-MAR-18 3B7U    1       REMARK                                   
REVDAT   3   24-FEB-09 3B7U    1       VERSN                                    
REVDAT   2   07-OCT-08 3B7U    1       JRNL                                     
REVDAT   1   16-SEP-08 3B7U    0                                                
JRNL        AUTH   F.THOLANDER,A.MUROYA,B.P.ROQUES,M.C.FOURNIE-ZALUSKI,         
JRNL        AUTH 2 M.M.THUNNISSEN,J.Z.HAEGGSTROM                                
JRNL        TITL   STRUCTURE-BASED DISSECTION OF THE ACTIVE SITE CHEMISTRY OF   
JRNL        TITL 2 LEUKOTRIENE A4 HYDROLASE: IMPLICATIONS FOR M1                
JRNL        TITL 3 AMINOPEPTIDASES AND INHIBITOR DESIGN.                        
JRNL        REF    CHEM.BIOL.                    V.  15   920 2008              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   18804029                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2008.07.018                               
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   F.THOLANDER,J.Z.HAEGGSTROM                                   
REMARK   1  TITL   ASSAY FOR RAPID ANALYSIS OF THE TRI-PEPTIDASE ACTIVITY OF    
REMARK   1  TITL 2 LTA4 HYDROLASE.                                              
REMARK   1  REF    PROTEINS                      V.  67  1113 2007              
REMARK   1  REFN                   ISSN 0887-3585                               
REMARK   1  PMID   17357161                                                     
REMARK   1  DOI    10.1002/PROT.21329                                           
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.C.RUDBERG,F.THOLANDER,M.ANDBERG,M.M.THUNNISSEN,            
REMARK   1  AUTH 2 J.Z.HAEGGSTROM                                               
REMARK   1  TITL   LEUKOTRIENE A4 HYDROLASE: IDENTIFICATION OF A COMMON         
REMARK   1  TITL 2 CARBOXYLATE RECOGNITION SITE FOR THE EPOXIDE HYDROLASE AND   
REMARK   1  TITL 3 AMINOPEPTIDASE SUBSTRATES.                                   
REMARK   1  REF    J.BIOL.CHEM.                  V. 279 27376 2004              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   15078870                                                     
REMARK   1  DOI    10.1074/JBC.M401031200                                       
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   P.C.RUDBERG,F.THOLANDER,M.M.THUNNISSEN,J.Z.HAEGGSTROM        
REMARK   1  TITL   LEUKOTRIENE A4 HYDROLASE/AMINOPEPTIDASE. GLUTAMATE 271 IS A  
REMARK   1  TITL 2 CATALYTIC RESIDUE WITH SPECIFIC ROLES IN TWO DISTINCT ENZYME 
REMARK   1  TITL 3 MECHANISMS.                                                  
REMARK   1  REF    J.BIOL.CHEM.                  V. 277  1398 2002              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   11675384                                                     
REMARK   1  DOI    10.1074/JBC.M106577200                                       
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   P.C.RUDBERG,F.THOLANDER,M.M.THUNNISSEN,B.SAMUELSSON,         
REMARK   1  AUTH 2 J.Z.HAEGGSTROM                                               
REMARK   1  TITL   LEUKOTRIENE A4 HYDROLASE: SELECTIVE ABROGATION OF            
REMARK   1  TITL 2 LEUKOTRIENE B4 FORMATION BY MUTATION OF ASPARTIC ACID 375.   
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  99  4215 2002              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  PMID   11917124                                                     
REMARK   1  DOI    10.1073/PNAS.072090099                                       
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   M.M.THUNNISSEN,P.NORDLUND,J.Z.HAEGGSTROM                     
REMARK   1  TITL   CRYSTAL STRUCTURE OF HUMAN LEUKOTRIENE A(4) HYDROLASE, A     
REMARK   1  TITL 2 BIFUNCTIONAL ENZYME IN INFLAMMATION.                         
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   8   131 2001              
REMARK   1  REFN                   ISSN 1072-8368                               
REMARK   1  PMID   11175901                                                     
REMARK   1  DOI    10.1038/84117                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 52364                          
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1727                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4877                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 420                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.35000                                              
REMARK   3    B22 (A**2) : -1.19000                                             
REMARK   3    B33 (A**2) : 0.83000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.141         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.137         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.091         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3B7U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000045187.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-OCT-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I711                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM, XFIT                       
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52364                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 14.667                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : 0.09500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.25200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: XFIT                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1H19                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CO-CRYSTALLIZED WITH LTA4H BY LIQUID     
REMARK 280  -LIQUID DIFFUSION IN MELTING-POINT CAPILLARIES. A TRIS-BUFFERED     
REMARK 280  (10 MM, PH 7.5) SOLUTION OF PROTEIN AND INHIBITOR IN                
REMARK 280  APPROXIMATELY EQUIMOLAR CONCENTRATIONS (~70 MICROM) WAS LAYERED     
REMARK 280  ON THE PRECIPITATE SOLUTION CONTAINING 28% (WEIGHT/VOLUME)          
REMARK 280  POLYETHYLENE GLYCOL (MW 8000), 50 MM NA ACETATE, 100 MM             
REMARK 280  IMIDAZOLE, PH 6.8, AND 5 MM YBCL3, LIQUID-LIQUID DIFFUSION,         
REMARK 280  TEMPERATURE 298K                                                    
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       38.91450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.59550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.56800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.59550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.91450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.56800            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X                                     
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     HIS X    -5                                                      
REMARK 465     HIS X    -4                                                      
REMARK 465     HIS X    -3                                                      
REMARK 465     HIS X    -2                                                      
REMARK 465     HIS X    -1                                                      
REMARK 465     HIS X     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH X  1044     O    HOH X  1058              2.00            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU X 522   CD    GLU X 522   OE1     0.067                       
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    ASP X   5   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP X  58   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP X 175   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    LEU X 261   CA  -  CB  -  CG  ANGL. DEV. = -15.2 DEGREES          
REMARK 500    ASP X 312   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP X 371   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP X 422   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP X 423   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP X 426   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP X 461   CB  -  CG  -  OD2 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ASP X 481   CB  -  CG  -  OD2 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    ASP X 493   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG X 563   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 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    GLN X  79       68.56   -113.10                                   
REMARK 500    SER X  80     -124.37     33.80                                   
REMARK 500    ASN X  97       -2.56     79.27                                   
REMARK 500    ASP X 183       95.40   -178.66                                   
REMARK 500    GLU X 271       46.05    -84.44                                   
REMARK 500    CYS X 274      -14.75     75.96                                   
REMARK 500    LEU X 275       83.24   -152.02                                   
REMARK 500    TRP X 301      -65.77   -109.66                                   
REMARK 500    PHE X 432       41.06   -104.43                                   
REMARK 500    LYS X 546       38.20     72.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB X 704  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP X 175   OD2                                                    
REMARK 620 2 HOH X1081   O   151.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN X 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS X 295   NE2                                                    
REMARK 620 2 HIS X 299   NE2 103.7                                              
REMARK 620 3 GLU X 318   OE1  99.2 104.7                                        
REMARK 620 4 KEL X 707   O21 103.5 142.3  96.0                                  
REMARK 620 5 KEL X 707   O20  94.5  81.4 163.1  71.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB X 702  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP X 481   OD1                                                    
REMARK 620 2 ASP X 481   OD2  53.1                                              
REMARK 620 3 ACY X 706   OXT  79.0  73.7                                        
REMARK 620 4 ACY X 706   O   128.8 119.8  54.4                                  
REMARK 620 5 HOH X 747   O    84.5  72.7 146.1 146.2                            
REMARK 620 6 HOH X 771   O   134.4  81.4  90.7  71.9  80.1                      
REMARK 620 7 ASP X  47   OD1 125.7  73.1  79.5  69.8  86.7  12.4                
REMARK 620 8 ASP X  47   OD2 125.4  72.7  80.8  71.1  85.2  11.7   1.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB X 703  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP X 610   O                                                      
REMARK 620 2 HOH X1085   O    71.7                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN X 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB X 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB X 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB X 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD X 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KEL X 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY X 706                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2R59   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3B7R   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3B7S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3B7T   RELATED DB: PDB                                   
DBREF  3B7U X    1   610  UNP    P09960   LKHA4_HUMAN      2    611             
SEQADV 3B7U HIS X   -5  UNP  P09960              EXPRESSION TAG                 
SEQADV 3B7U HIS X   -4  UNP  P09960              EXPRESSION TAG                 
SEQADV 3B7U HIS X   -3  UNP  P09960              EXPRESSION TAG                 
SEQADV 3B7U HIS X   -2  UNP  P09960              EXPRESSION TAG                 
SEQADV 3B7U HIS X   -1  UNP  P09960              EXPRESSION TAG                 
SEQADV 3B7U HIS X    0  UNP  P09960              EXPRESSION TAG                 
SEQRES   1 X  616  HIS HIS HIS HIS HIS HIS PRO GLU ILE VAL ASP THR CYS          
SEQRES   2 X  616  SER LEU ALA SER PRO ALA SER VAL CYS ARG THR LYS HIS          
SEQRES   3 X  616  LEU HIS LEU ARG CYS SER VAL ASP PHE THR ARG ARG THR          
SEQRES   4 X  616  LEU THR GLY THR ALA ALA LEU THR VAL GLN SER GLN GLU          
SEQRES   5 X  616  ASP ASN LEU ARG SER LEU VAL LEU ASP THR LYS ASP LEU          
SEQRES   6 X  616  THR ILE GLU LYS VAL VAL ILE ASN GLY GLN GLU VAL LYS          
SEQRES   7 X  616  TYR ALA LEU GLY GLU ARG GLN SER TYR LYS GLY SER PRO          
SEQRES   8 X  616  MET GLU ILE SER LEU PRO ILE ALA LEU SER LYS ASN GLN          
SEQRES   9 X  616  GLU ILE VAL ILE GLU ILE SER PHE GLU THR SER PRO LYS          
SEQRES  10 X  616  SER SER ALA LEU GLN TRP LEU THR PRO GLU GLN THR SER          
SEQRES  11 X  616  GLY LYS GLU HIS PRO TYR LEU PHE SER GLN CYS GLN ALA          
SEQRES  12 X  616  ILE HIS CYS ARG ALA ILE LEU PRO CYS GLN ASP THR PRO          
SEQRES  13 X  616  SER VAL LYS LEU THR TYR THR ALA GLU VAL SER VAL PRO          
SEQRES  14 X  616  LYS GLU LEU VAL ALA LEU MET SER ALA ILE ARG ASP GLY          
SEQRES  15 X  616  GLU THR PRO ASP PRO GLU ASP PRO SER ARG LYS ILE TYR          
SEQRES  16 X  616  LYS PHE ILE GLN LYS VAL PRO ILE PRO CYS TYR LEU ILE          
SEQRES  17 X  616  ALA LEU VAL VAL GLY ALA LEU GLU SER ARG GLN ILE GLY          
SEQRES  18 X  616  PRO ARG THR LEU VAL TRP SER GLU LYS GLU GLN VAL GLU          
SEQRES  19 X  616  LYS SER ALA TYR GLU PHE SER GLU THR GLU SER MET LEU          
SEQRES  20 X  616  LYS ILE ALA GLU ASP LEU GLY GLY PRO TYR VAL TRP GLY          
SEQRES  21 X  616  GLN TYR ASP LEU LEU VAL LEU PRO PRO SER PHE PRO TYR          
SEQRES  22 X  616  GLY GLY MET GLU ASN PRO CYS LEU THR PHE VAL THR PRO          
SEQRES  23 X  616  THR LEU LEU ALA GLY ASP LYS SER LEU SER ASN VAL ILE          
SEQRES  24 X  616  ALA HIS GLU ILE SER HIS SER TRP THR GLY ASN LEU VAL          
SEQRES  25 X  616  THR ASN LYS THR TRP ASP HIS PHE TRP LEU ASN GLU GLY          
SEQRES  26 X  616  HIS THR VAL TYR LEU GLU ARG HIS ILE CYS GLY ARG LEU          
SEQRES  27 X  616  PHE GLY GLU LYS PHE ARG HIS PHE ASN ALA LEU GLY GLY          
SEQRES  28 X  616  TRP GLY GLU LEU GLN ASN SER VAL LYS THR PHE GLY GLU          
SEQRES  29 X  616  THR HIS PRO PHE THR LYS LEU VAL VAL ASP LEU THR ASP          
SEQRES  30 X  616  ILE ASP PRO ASP VAL ALA TYR SER SER VAL PRO TYR GLU          
SEQRES  31 X  616  LYS GLY PHE ALA LEU LEU PHE TYR LEU GLU GLN LEU LEU          
SEQRES  32 X  616  GLY GLY PRO GLU ILE PHE LEU GLY PHE LEU LYS ALA TYR          
SEQRES  33 X  616  VAL GLU LYS PHE SER TYR LYS SER ILE THR THR ASP ASP          
SEQRES  34 X  616  TRP LYS ASP PHE LEU TYR SER TYR PHE LYS ASP LYS VAL          
SEQRES  35 X  616  ASP VAL LEU ASN GLN VAL ASP TRP ASN ALA TRP LEU TYR          
SEQRES  36 X  616  SER PRO GLY LEU PRO PRO ILE LYS PRO ASN TYR ASP MET          
SEQRES  37 X  616  THR LEU THR ASN ALA CYS ILE ALA LEU SER GLN ARG TRP          
SEQRES  38 X  616  ILE THR ALA LYS GLU ASP ASP LEU ASN SER PHE ASN ALA          
SEQRES  39 X  616  THR ASP LEU LYS ASP LEU SER SER HIS GLN LEU ASN GLU          
SEQRES  40 X  616  PHE LEU ALA GLN THR LEU GLN ARG ALA PRO LEU PRO LEU          
SEQRES  41 X  616  GLY HIS ILE LYS ARG MET GLN GLU VAL TYR ASN PHE ASN          
SEQRES  42 X  616  ALA ILE ASN ASN SER GLU ILE ARG PHE ARG TRP LEU ARG          
SEQRES  43 X  616  LEU CYS ILE GLN SER LYS TRP GLU ASP ALA ILE PRO LEU          
SEQRES  44 X  616  ALA LEU LYS MET ALA THR GLU GLN GLY ARG MET LYS PHE          
SEQRES  45 X  616  THR ARG PRO LEU PHE LYS ASP LEU ALA ALA PHE ASP LYS          
SEQRES  46 X  616  SER HIS ASP GLN ALA VAL ARG THR TYR GLN GLU HIS LYS          
SEQRES  47 X  616  ALA SER MET HIS PRO VAL THR ALA MET LEU VAL GLY LYS          
SEQRES  48 X  616  ASP LEU LYS VAL ASP                                          
HET     ZN  X 701       1                                                       
HET     YB  X 702       1                                                       
HET     YB  X 703       1                                                       
HET     YB  X 704       1                                                       
HET    IMD  X 705       5                                                       
HET    KEL  X 707      21                                                       
HET    ACY  X 706       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     KEL N-[(2R)-2-BENZYL-4-(HYDROXYAMINO)-4-OXOBUTANOYL]-L-              
HETNAM   2 KEL  ALANINE                                                         
HETNAM     ACY ACETIC ACID                                                      
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   YB    3(YB 3+)                                                     
FORMUL   6  IMD    C3 H5 N2 1+                                                  
FORMUL   7  KEL    C14 H18 N2 O5                                                
FORMUL   8  ACY    C2 H4 O2                                                     
FORMUL   9  HOH   *420(H2 O)                                                    
HELIX    1   1 GLN X   79  GLY X   83  5                                   5    
HELIX    2   2 THR X  119  THR X  123  5                                   5    
HELIX    3   3 HIS X  139  ILE X  143  5                                   5    
HELIX    4   4 TYR X  200  ILE X  202  5                                   3    
HELIX    5   5 GLU X  223  GLU X  225  5                                   3    
HELIX    6   6 GLN X  226  PHE X  234  1                                   9    
HELIX    7   7 GLU X  236  GLY X  249  1                                  14    
HELIX    8   8 PRO X  280  LEU X  283  5                                   4    
HELIX    9   9 SER X  290  HIS X  299  1                                  10    
HELIX   10  10 THR X  310  HIS X  313  5                                   4    
HELIX   11  11 PHE X  314  GLY X  334  1                                  21    
HELIX   12  12 GLY X  334  GLY X  357  1                                  24    
HELIX   13  13 HIS X  360  LYS X  364  5                                   5    
HELIX   14  14 ASP X  373  TYR X  378  1                                   6    
HELIX   15  15 SER X  380  LEU X  397  1                                  18    
HELIX   16  16 GLY X  399  SER X  415  1                                  17    
HELIX   17  17 THR X  420  PHE X  432  1                                  13    
HELIX   18  18 LYS X  435  ASN X  440  1                                   6    
HELIX   19  19 ASP X  443  SER X  450  1                                   8    
HELIX   20  20 THR X  465  ALA X  478  1                                  14    
HELIX   21  21 LYS X  479  PHE X  486  5                                   8    
HELIX   22  22 ASN X  487  LYS X  492  5                                   6    
HELIX   23  23 SER X  495  GLN X  508  1                                  14    
HELIX   24  24 PRO X  513  ASN X  525  1                                  13    
HELIX   25  25 PHE X  526  ILE X  529  5                                   4    
HELIX   26  26 ASN X  531  SER X  545  1                                  15    
HELIX   27  27 TRP X  547  ASP X  549  5                                   3    
HELIX   28  28 ALA X  550  GLN X  561  1                                  12    
HELIX   29  29 ARG X  563  PHE X  577  1                                  15    
HELIX   30  30 SER X  580  LYS X  592  1                                  13    
HELIX   31  31 ALA X  593  MET X  595  5                                   3    
HELIX   32  32 HIS X  596  LEU X  607  1                                  12    
SHEET    1   A 8 GLN X  69  GLU X  70  0                                        
SHEET    2   A 8 LEU X  59  ILE X  66 -1  N  ILE X  66   O  GLN X  69           
SHEET    3   A 8 GLU X  99  THR X 108 -1  O  GLU X 103   N  VAL X  65           
SHEET    4   A 8 THR X  33  SER X  44 -1  N  ALA X  38   O  ILE X 104           
SHEET    5   A 8 CYS X  16  ASP X  28 -1  N  ARG X  17   O  GLN X  43           
SHEET    6   A 8 LYS X 153  PRO X 163  1  O  SER X 161   N  CYS X  25           
SHEET    7   A 8 ARG X 186  PRO X 198 -1  O  GLN X 193   N  TYR X 156           
SHEET    8   A 8 ILE X 173  PRO X 179 -1  N  THR X 178   O  ILE X 188           
SHEET    1   B 3 LEU X  49  THR X  56  0                                        
SHEET    2   B 3 SER X  84  LEU X  94 -1  O  ILE X  88   N  LEU X  52           
SHEET    3   B 3 TYR X  73  LEU X  75 -1  N  ALA X  74   O  GLU X  87           
SHEET    1   C 4 LEU X 115  LEU X 118  0                                        
SHEET    2   C 4 TYR X 130  SER X 133 -1  O  TYR X 130   N  LEU X 118           
SHEET    3   C 4 LEU X 204  GLY X 207 -1  O  VAL X 206   N  LEU X 131           
SHEET    4   C 4 VAL X 167  MET X 170 -1  N  VAL X 167   O  GLY X 207           
SHEET    1   D 5 GLU X 210  GLY X 215  0                                        
SHEET    2   D 5 THR X 218  SER X 222 -1  O  VAL X 220   N  ARG X 212           
SHEET    3   D 5 ASP X 257  VAL X 260  1  O  VAL X 260   N  TRP X 221           
SHEET    4   D 5 LEU X 275  VAL X 278  1  O  VAL X 278   N  LEU X 259           
SHEET    5   D 5 GLY X 269  MET X 270 -1  N  MET X 270   O  PHE X 277           
SHEET    1   E 2 VAL X 306  ASN X 308  0                                        
SHEET    2   E 2 LYS X 417  ILE X 419  1  O  ILE X 419   N  THR X 307           
LINK         OD2 ASP X 175                YB    YB X 704     1555   1555  2.14  
LINK         NE2 HIS X 295                ZN    ZN X 701     1555   1555  2.13  
LINK         NE2 HIS X 299                ZN    ZN X 701     1555   1555  2.03  
LINK         OE1 GLU X 318                ZN    ZN X 701     1555   1555  2.01  
LINK         OD1 ASP X 481                YB    YB X 702     1555   1555  2.46  
LINK         OD2 ASP X 481                YB    YB X 702     1555   1555  2.34  
LINK         O   ASP X 610                YB    YB X 703     1555   1555  3.45  
LINK        ZN    ZN X 701                 O21 KEL X 707     1555   1555  2.06  
LINK        ZN    ZN X 701                 O20 KEL X 707     1555   1555  2.34  
LINK        YB    YB X 702                 OXT ACY X 706     1555   1555  2.35  
LINK        YB    YB X 702                 O   ACY X 706     1555   1555  2.54  
LINK        YB    YB X 702                 O   HOH X 747     1555   1555  2.30  
LINK        YB    YB X 702                 O   HOH X 771     1555   1555  2.36  
LINK        YB    YB X 703                 O   HOH X1085     1555   1555  2.76  
LINK         OD1 ASP X  47                YB    YB X 702     1555   1545  2.44  
LINK         OD2 ASP X  47                YB    YB X 702     1555   1545  2.43  
LINK        YB    YB X 704                 O   HOH X1081     1555   4545  3.09  
CISPEP   1 GLN X  136    ALA X  137          0        -1.97                     
CISPEP   2 ALA X  510    PRO X  511          0         2.10                     
SITE     1 AC1  3 HIS X 295  HIS X 299  GLU X 318                               
SITE     1 AC2  4 ASP X  47  ASP X 481  HOH X 747  HOH X 771                    
SITE     1 AC3  3 ASP X 426  ASP X 610  HOH X1085                               
SITE     1 AC4  2 ASP X 175  HOH X1081                                          
SITE     1 AC5  7 GLY X 344  GLY X 347  GLU X 348  ASN X 351                    
SITE     2 AC5  7 GLU X 501  ALA X 504  GLN X 508                               
SITE     1 AC6 17 TYR X 267  GLY X 268  GLY X 269  GLU X 271                    
SITE     2 AC6 17 ASN X 291  HIS X 295  GLU X 296  HIS X 299                    
SITE     3 AC6 17 GLU X 318  TYR X 378  TYR X 383  ARG X 563                    
SITE     4 AC6 17 LYS X 565  HOH X 734  HOH X 822  HOH X 958                    
SITE     5 AC6 17 HOH X 969                                                     
SITE     1 AC7  7 ASP X  47  ASN X  48  ARG X 174  LYS X 479                    
SITE     2 AC7  7 ASP X 481  HOH X 741  HOH X 771                               
CRYST1   77.829   87.136   99.191  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012849  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011476  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010082        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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