GenomeNet

Database: PDB
Entry: 5SYM
LinkDB: 5SYM
Original site: 5SYM 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           11-AUG-16   5SYM              
TITLE     COCRYSTAL STRUCTURE OF THE HUMAN ACYL PROTEIN THIOESTERASE 1 WITH AN  
TITLE    2 ISOFORM-SELECTIVE INHIBITOR, ML348                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACYL-PROTEIN THIOESTERASE 1;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HAPT1,LYSOPHOSPHOLIPASE 1,LYSOPHOSPHOLIPASE I,LYSOPLA I;    
COMPND   5 EC: 3.1.2.-;                                                         
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: LYPLA1, APT1, LPL1;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE, INHIBITOR, THIOESTERASE, HYDROLASE-HYDROLASE INHIBITOR     
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.STUCKEY,K.J.LABBY,J.L.MEAGHER,S.J.WON,B.R.MARTIN                  
REVDAT   5   04-DEC-19 5SYM    1       REMARK                                   
REVDAT   4   20-SEP-17 5SYM    1       REMARK                                   
REVDAT   3   28-DEC-16 5SYM    1       JRNL                                     
REVDAT   2   09-NOV-16 5SYM    1       JRNL                                     
REVDAT   1   26-OCT-16 5SYM    0                                                
JRNL        AUTH   S.J.WON,D.DAVDA,K.J.LABBY,S.Y.HWANG,R.PRICER,J.D.MAJMUDAR,   
JRNL        AUTH 2 K.A.ARMACOST,L.A.RODRIGUEZ,C.L.RODRIGUEZ,F.S.CHONG,          
JRNL        AUTH 3 K.A.TOROSSIAN,J.PALAKURTHI,E.S.HUR,J.L.MEAGHER,C.L.BROOKS,   
JRNL        AUTH 4 J.A.STUCKEY,B.R.MARTIN                                       
JRNL        TITL   MOLECULAR MECHANISM FOR ISOFORM-SELECTIVE INHIBITION OF ACYL 
JRNL        TITL 2 PROTEIN THIOESTERASES 1 AND 2 (APT1 AND APT2).               
JRNL        REF    ACS CHEM. BIOL.               V.  11  3374 2016              
JRNL        REFN                   ESSN 1554-8937                               
JRNL        PMID   27748579                                                     
JRNL        DOI    10.1021/ACSCHEMBIO.6B00720                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT 2.10.2                                    
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 63533                          
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)  : 0.180                          
REMARK   3   R VALUE            (WORKING SET)  : 0.179                          
REMARK   3   FREE R VALUE                      : 0.199                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.980                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3167                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.55                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.59                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 100.0                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4621                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : NULL                     
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4411                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2000                   
REMARK   3   BIN FREE R VALUE                        : 0.2310                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.54                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 210                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3350                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 88                                      
REMARK   3   SOLVENT ATOMS            : 363                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.99180                                             
REMARK   3    B22 (A**2) : 1.03250                                              
REMARK   3    B33 (A**2) : 0.95930                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.190               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.082               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.078               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.093               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.076               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 7082   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 12882  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1963   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 80     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1085   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 7082   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 482    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7945   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.09                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.75                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.52                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: {A|8 - 82}                                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -16.2310  -25.6110  -10.7310           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0488 T22:   -0.0244                                    
REMARK   3     T33:   -0.0310 T12:   -0.0094                                    
REMARK   3     T13:   -0.0057 T23:    0.0255                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6627 L22:    0.6237                                    
REMARK   3     L33:    3.2617 L12:    0.3059                                    
REMARK   3     L13:    1.0604 L23:    0.8732                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0790 S12:   -0.0593 S13:   -0.1133                     
REMARK   3     S21:    0.0287 S22:    0.0457 S23:   -0.0060                     
REMARK   3     S31:    0.2033 S32:   -0.1073 S33:   -0.1247                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: {A|83 - 106}                                           
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.5634  -26.5602  -12.8091           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0696 T22:   -0.0216                                    
REMARK   3     T33:   -0.0167 T12:    0.0180                                    
REMARK   3     T13:   -0.0233 T23:    0.0085                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6986 L22:    0.6272                                    
REMARK   3     L33:    2.4997 L12:   -0.6992                                    
REMARK   3     L13:   -0.5291 L23:   -0.3465                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0425 S12:   -0.0936 S13:   -0.2358                     
REMARK   3     S21:    0.0150 S22:    0.0429 S23:    0.0322                     
REMARK   3     S31:    0.2337 S32:    0.2395 S33:   -0.0855                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: {A|107 - 218}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -11.4076  -13.2519  -16.7087           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0454 T22:   -0.0400                                    
REMARK   3     T33:   -0.0421 T12:   -0.0169                                    
REMARK   3     T13:   -0.0036 T23:   -0.0012                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8668 L22:    1.0220                                    
REMARK   3     L33:    0.9695 L12:   -0.0558                                    
REMARK   3     L13:    0.0705 L23:   -0.0495                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0217 S12:    0.0029 S13:    0.0552                     
REMARK   3     S21:    0.0253 S22:    0.0038 S23:   -0.0366                     
REMARK   3     S31:   -0.1767 S32:    0.0175 S33:   -0.0255                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: {A|219 - 230}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -18.4517  -20.0982  -30.5072           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0265 T22:   -0.0012                                    
REMARK   3     T33:   -0.0056 T12:   -0.0195                                    
REMARK   3     T13:   -0.0091 T23:   -0.0345                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0989 L22:    0.2865                                    
REMARK   3     L33:    1.3361 L12:   -1.4681                                    
REMARK   3     L13:    1.2269 L23:   -1.3653                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0053 S12:    0.0798 S13:    0.0224                     
REMARK   3     S21:   -0.1045 S22:    0.0233 S23:    0.0402                     
REMARK   3     S31:    0.0431 S32:   -0.0689 S33:   -0.0286                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: {B|8 - 19}                                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -25.1258  -33.6258   26.2076           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0124 T22:    0.0344                                    
REMARK   3     T33:   -0.0365 T12:    0.0209                                    
REMARK   3     T13:    0.0173 T23:   -0.0081                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5382 L22:    1.0898                                    
REMARK   3     L33:    0.6609 L12:    1.0910                                    
REMARK   3     L13:    0.0438 L23:   -0.4527                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0547 S12:   -0.0497 S13:   -0.0537                     
REMARK   3     S21:   -0.0047 S22:    0.0955 S23:    0.0813                     
REMARK   3     S31:    0.0969 S32:    0.0212 S33:   -0.0408                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: {B|20 - 153}                                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -26.9115  -19.1052   18.1021           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0932 T22:   -0.0012                                    
REMARK   3     T33:   -0.0394 T12:    0.0001                                    
REMARK   3     T13:    0.0109 T23:    0.0374                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2033 L22:    0.6395                                    
REMARK   3     L33:    1.8293 L12:    0.0090                                    
REMARK   3     L13:   -0.1884 L23:   -0.5155                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0035 S12:    0.0485 S13:    0.0378                     
REMARK   3     S21:    0.0084 S22:    0.1083 S23:    0.0774                     
REMARK   3     S31:   -0.0547 S32:   -0.1476 S33:   -0.1049                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: {B|154 - 163}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -33.1449   -4.2839   29.0024           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0117 T22:    0.0061                                    
REMARK   3     T33:    0.0682 T12:    0.0769                                    
REMARK   3     T13:    0.1129 T23:    0.0323                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4550 L22:    0.8222                                    
REMARK   3     L33:    0.2281 L12:   -1.0637                                    
REMARK   3     L13:    0.6488 L23:    0.9862                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0034 S12:    0.0106 S13:    0.0321                     
REMARK   3     S21:   -0.0139 S22:    0.0145 S23:    0.0468                     
REMARK   3     S31:   -0.0777 S32:    0.0008 S33:   -0.0179                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: {B|164 - 230}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -16.5144  -11.1907   24.0500           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0528 T22:   -0.0267                                    
REMARK   3     T33:   -0.0385 T12:   -0.0162                                    
REMARK   3     T13:    0.0191 T23:   -0.0124                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0363 L22:    1.1202                                    
REMARK   3     L33:    1.3511 L12:    0.2214                                    
REMARK   3     L13:   -0.7133 L23:   -0.8454                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0983 S12:   -0.0390 S13:    0.1818                     
REMARK   3     S21:    0.1320 S22:   -0.0038 S23:    0.0143                     
REMARK   3     S31:   -0.2476 S32:    0.0812 S33:   -0.0945                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5SYM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000222850.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63533                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.510                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.100                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: APT1-CHAINA, PDB:1FJ2                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CITRATE, 22-24% PEG 3350,    
REMARK 280  200 MM MGCL2, PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.84500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.91000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.84500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       40.91000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     CYS A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     MET A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     MET B     1                                                      
REMARK 465     CYS B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     ASN B     4                                                      
REMARK 465     ASN B     5                                                      
REMARK 465     MET B     6                                                      
REMARK 465     SER B     7                                                      
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     THR A   8    OG1  CG2                                            
REMARK 470     LEU A  10    CG   CD1  CD2                                       
REMARK 470     ASP B 230    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   H    GLN A   212     OD2  ASP B   101     4444     1.59            
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    LYS A  19      118.65    -31.97                                   
REMARK 500    ASN A  64       59.55   -118.07                                   
REMARK 500    SER A 119     -124.39     55.21                                   
REMARK 500    MET A 207     -145.06   -101.58                                   
REMARK 500    ASN B  64       58.73   -116.73                                   
REMARK 500    SER B 119     -119.46     54.36                                   
REMARK 500    MET B 207     -146.04   -101.75                                   
REMARK 500    SER B 209     -163.04   -160.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 588        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A 589        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH B 573        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH B 574        DISTANCE =  6.36 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 71Q A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 307                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 308                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 309                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 71Q B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 303                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5SYN   RELATED DB: PDB                                   
DBREF  5SYM A    1   230  UNP    O75608   LYPA1_HUMAN      1    230             
DBREF  5SYM B    1   230  UNP    O75608   LYPA1_HUMAN      1    230             
SEQRES   1 A  230  MET CYS GLY ASN ASN MET SER THR PRO LEU PRO ALA ILE          
SEQRES   2 A  230  VAL PRO ALA ALA ARG LYS ALA THR ALA ALA VAL ILE PHE          
SEQRES   3 A  230  LEU HIS GLY LEU GLY ASP THR GLY HIS GLY TRP ALA GLU          
SEQRES   4 A  230  ALA PHE ALA GLY ILE ARG SER SER HIS ILE LYS TYR ILE          
SEQRES   5 A  230  CYS PRO HIS ALA PRO VAL ARG PRO VAL THR LEU ASN MET          
SEQRES   6 A  230  ASN VAL ALA MET PRO SER TRP PHE ASP ILE ILE GLY LEU          
SEQRES   7 A  230  SER PRO ASP SER GLN GLU ASP GLU SER GLY ILE LYS GLN          
SEQRES   8 A  230  ALA ALA GLU ASN ILE LYS ALA LEU ILE ASP GLN GLU VAL          
SEQRES   9 A  230  LYS ASN GLY ILE PRO SER ASN ARG ILE ILE LEU GLY GLY          
SEQRES  10 A  230  PHE SER GLN GLY GLY ALA LEU SER LEU TYR THR ALA LEU          
SEQRES  11 A  230  THR THR GLN GLN LYS LEU ALA GLY VAL THR ALA LEU SER          
SEQRES  12 A  230  CYS TRP LEU PRO LEU ARG ALA SER PHE PRO GLN GLY PRO          
SEQRES  13 A  230  ILE GLY GLY ALA ASN ARG ASP ILE SER ILE LEU GLN CYS          
SEQRES  14 A  230  HIS GLY ASP CYS ASP PRO LEU VAL PRO LEU MET PHE GLY          
SEQRES  15 A  230  SER LEU THR VAL GLU LYS LEU LYS THR LEU VAL ASN PRO          
SEQRES  16 A  230  ALA ASN VAL THR PHE LYS THR TYR GLU GLY MET MET HIS          
SEQRES  17 A  230  SER SER CYS GLN GLN GLU MET MET ASP VAL LYS GLN PHE          
SEQRES  18 A  230  ILE ASP LYS LEU LEU PRO PRO ILE ASP                          
SEQRES   1 B  230  MET CYS GLY ASN ASN MET SER THR PRO LEU PRO ALA ILE          
SEQRES   2 B  230  VAL PRO ALA ALA ARG LYS ALA THR ALA ALA VAL ILE PHE          
SEQRES   3 B  230  LEU HIS GLY LEU GLY ASP THR GLY HIS GLY TRP ALA GLU          
SEQRES   4 B  230  ALA PHE ALA GLY ILE ARG SER SER HIS ILE LYS TYR ILE          
SEQRES   5 B  230  CYS PRO HIS ALA PRO VAL ARG PRO VAL THR LEU ASN MET          
SEQRES   6 B  230  ASN VAL ALA MET PRO SER TRP PHE ASP ILE ILE GLY LEU          
SEQRES   7 B  230  SER PRO ASP SER GLN GLU ASP GLU SER GLY ILE LYS GLN          
SEQRES   8 B  230  ALA ALA GLU ASN ILE LYS ALA LEU ILE ASP GLN GLU VAL          
SEQRES   9 B  230  LYS ASN GLY ILE PRO SER ASN ARG ILE ILE LEU GLY GLY          
SEQRES  10 B  230  PHE SER GLN GLY GLY ALA LEU SER LEU TYR THR ALA LEU          
SEQRES  11 B  230  THR THR GLN GLN LYS LEU ALA GLY VAL THR ALA LEU SER          
SEQRES  12 B  230  CYS TRP LEU PRO LEU ARG ALA SER PHE PRO GLN GLY PRO          
SEQRES  13 B  230  ILE GLY GLY ALA ASN ARG ASP ILE SER ILE LEU GLN CYS          
SEQRES  14 B  230  HIS GLY ASP CYS ASP PRO LEU VAL PRO LEU MET PHE GLY          
SEQRES  15 B  230  SER LEU THR VAL GLU LYS LEU LYS THR LEU VAL ASN PRO          
SEQRES  16 B  230  ALA ASN VAL THR PHE LYS THR TYR GLU GLY MET MET HIS          
SEQRES  17 B  230  SER SER CYS GLN GLN GLU MET MET ASP VAL LYS GLN PHE          
SEQRES  18 B  230  ILE ASP LYS LEU LEU PRO PRO ILE ASP                          
HET    71Q  A 301      38                                                       
HET    EDO  A 302       4                                                       
HET    EDO  A 303       4                                                       
HET    EDO  A 304       4                                                       
HET    EDO  A 305       4                                                       
HET    EDO  A 306       4                                                       
HET     CL  A 307       1                                                       
HET     CL  A 308       1                                                       
HET     CL  A 309       1                                                       
HET    EDO  A 310       4                                                       
HET    71Q  B 301      38                                                       
HET    EDO  B 302       4                                                       
HET     CL  B 303       1                                                       
HETNAM     71Q N-[2-CHLORO-5-(TRIFLUOROMETHYL)PHENYL]-2-[4-(FURAN-2-            
HETNAM   2 71Q  CARBONYL)PIPERAZIN-1-YL]ACETAMIDE                               
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      CL CHLORIDE ION                                                     
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  71Q    2(C18 H17 CL F3 N3 O3)                                       
FORMUL   4  EDO    7(C2 H6 O2)                                                  
FORMUL   9   CL    4(CL 1-)                                                     
FORMUL  16  HOH   *363(H2 O)                                                    
HELIX    1 AA1 GLY A   34  GLY A   43  1                                  10    
HELIX    2 AA2 THR A   62  MET A   65  5                                   4    
HELIX    3 AA3 ASP A   85  ASN A  106  1                                  22    
HELIX    4 AA4 PRO A  109  ASN A  111  5                                   3    
HELIX    5 AA5 SER A  119  LEU A  130  1                                  12    
HELIX    6 AA6 LEU A  148  PHE A  152  5                                   5    
HELIX    7 AA7 PRO A  178  VAL A  193  1                                  16    
HELIX    8 AA8 ASN A  194  ALA A  196  5                                   3    
HELIX    9 AA9 CYS A  211  LEU A  226  1                                  16    
HELIX   10 AB1 GLY B   34  GLY B   43  1                                  10    
HELIX   11 AB2 THR B   62  MET B   65  5                                   4    
HELIX   12 AB3 ASP B   85  ASN B  106  1                                  22    
HELIX   13 AB4 PRO B  109  ASN B  111  5                                   3    
HELIX   14 AB5 SER B  119  THR B  132  1                                  14    
HELIX   15 AB6 LEU B  148  PHE B  152  5                                   5    
HELIX   16 AB7 PRO B  178  VAL B  193  1                                  16    
HELIX   17 AB8 ASN B  194  ALA B  196  5                                   3    
HELIX   18 AB9 CYS B  211  LEU B  226  1                                  16    
SHEET    1 AA1 7 ALA A  12  VAL A  14  0                                        
SHEET    2 AA1 7 ILE A  49  CYS A  53 -1  O  CYS A  53   N  ALA A  12           
SHEET    3 AA1 7 ALA A  22  LEU A  27  1  N  VAL A  24   O  ILE A  52           
SHEET    4 AA1 7 ILE A 113  PHE A 118  1  O  ILE A 114   N  ILE A  25           
SHEET    5 AA1 7 GLY A 138  LEU A 142  1  O  LEU A 142   N  GLY A 117           
SHEET    6 AA1 7 SER A 165  GLY A 171  1  O  LEU A 167   N  VAL A 139           
SHEET    7 AA1 7 VAL A 198  TYR A 203  1  O  THR A 199   N  GLN A 168           
SHEET    1 AA2 2 VAL A  58  PRO A  60  0                                        
SHEET    2 AA2 2 ALA A  68  PRO A  70 -1  O  MET A  69   N  ARG A  59           
SHEET    1 AA3 7 ALA B  12  VAL B  14  0                                        
SHEET    2 AA3 7 ILE B  49  CYS B  53 -1  O  CYS B  53   N  ALA B  12           
SHEET    3 AA3 7 ALA B  22  LEU B  27  1  N  VAL B  24   O  ILE B  52           
SHEET    4 AA3 7 ILE B 113  PHE B 118  1  O  ILE B 114   N  ILE B  25           
SHEET    5 AA3 7 GLY B 138  LEU B 142  1  O  LEU B 142   N  GLY B 117           
SHEET    6 AA3 7 SER B 165  GLY B 171  1  O  LEU B 167   N  ALA B 141           
SHEET    7 AA3 7 VAL B 198  TYR B 203  1  O  THR B 199   N  GLN B 168           
SHEET    1 AA4 2 VAL B  58  PRO B  60  0                                        
SHEET    2 AA4 2 ALA B  68  PRO B  70 -1  O  MET B  69   N  ARG B  59           
CISPEP   1 THR A    8    PRO A    9          0         5.14                     
SITE     1 AC1 15 ILE A  75  GLY A  77  LEU A  78  SER A  79                    
SITE     2 AC1 15 PRO A  80  TRP A 145  LEU A 146  ARG A 149                    
SITE     3 AC1 15 LEU A 176  VAL A 177  PHE A 181  THR A 185                    
SITE     4 AC1 15  CL A 308  HOH A 431  HOH A 456                               
SITE     1 AC2  4 GLY A  36  TRP A  37  SER A 210  MET B  65                    
SITE     1 AC3  4 SER A 210  CYS A 211  MET A 215  HOH A 531                    
SITE     1 AC4  8 LYS A  97  THR A 131  THR A 132  GLN A 133                    
SITE     2 AC4  8 HOH A 403  HOH A 423  GLU B 204  GLN B 213                    
SITE     1 AC5  6 LYS A  19  ALA A  20  ASN A 106   CL A 307                    
SITE     2 AC5  6 HOH A 428  ARG B  45                                          
SITE     1 AC6  3 GLN A  83  GLU A  84  HOH A 459                               
SITE     1 AC7  4 ALA A  20  EDO A 305  ARG B  45  HOH B 547                    
SITE     1 AC8  5 LEU A  30  SER A 119  GLN A 120  71Q A 301                    
SITE     2 AC8  5 HOH B 414                                                     
SITE     1 AC9  4 ARG A  18  THR A  21  PRO A 228  ILE A 229                    
SITE     1 AD1  5 MET A  65  HOH A 466  GLY B  36  TRP B  37                    
SITE     2 AD1  5 SER B 210                                                     
SITE     1 AD2 16 LEU B  30  ILE B  75  GLY B  77  LEU B  78                    
SITE     2 AD2 16 SER B  79  PRO B  80  TRP B 145  LEU B 146                    
SITE     3 AD2 16 ARG B 149  LEU B 176  VAL B 177  PHE B 181                    
SITE     4 AD2 16 THR B 185   CL B 303  HOH B 408  HOH B 411                    
SITE     1 AD3  7 ASN A  66  GLY A 159  MET B 207  SER B 209                    
SITE     2 AD3  7 HOH B 417  HOH B 426  HOH B 450                               
SITE     1 AD4  5 HOH A 420  LEU B  30  SER B 119  GLN B 120                    
SITE     2 AD4  5 71Q B 301                                                     
CRYST1   71.670   73.690   81.820  90.00  90.00  90.00 P 2 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      0.013953  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013570  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012222        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system