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Database: PDB
Entry: 4OJN
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HEADER    OXIDOREDUCTASE                          21-JAN-14   4OJN              
TITLE     CRYSTAL STRUCTURE OF HUMAN MUSCLE L-LACTATE DEHYDROGENASE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: L-LACTATE DEHYDROGENASE A CHAIN;                           
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: L-LACTATE DEHYDROGENASE M CHAIN, LDH-A, CELL PROLIFERATION- 
COMPND   5 INDUCING GENE 19 PROTEIN, LDH MUSCLE SUBUNIT, LDH-M, RENAL CARCINOMA 
COMPND   6 ANTIGEN NY-REN-59;                                                   
COMPND   7 EC: 1.1.1.27;                                                        
COMPND   8 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: LDHA, PIG19;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ROSSMANN FOLD, NADH/NAD+ COFACTOR, OXIDOREDUCTASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.KOLAPPAN,L.CRAIG                                                    
REVDAT   3   25-FEB-15 4OJN    1       JRNL                                     
REVDAT   2   11-FEB-15 4OJN    1       JRNL                                     
REVDAT   1   03-DEC-14 4OJN    0                                                
JRNL        AUTH   S.KOLAPPAN,D.L.SHEN,R.MOSI,J.SUN,E.J.MCEACHERN,D.J.VOCADLO,  
JRNL        AUTH 2 L.CRAIG                                                      
JRNL        TITL   STRUCTURES OF LACTATE DEHYDROGENASE A (LDHA) IN APO, TERNARY 
JRNL        TITL 2 AND INHIBITOR-BOUND FORMS.                                   
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  71   185 2015              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   25664730                                                     
JRNL        DOI    10.1107/S1399004714024791                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.84                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 154614                         
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) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8138                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10872                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.18                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2860                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 572                          
REMARK   3   BIN FREE R VALUE                    : 0.3080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 20566                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 146                                     
REMARK   3   SOLVENT ATOMS            : 527                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.30000                                             
REMARK   3    B22 (A**2) : -2.30000                                             
REMARK   3    B33 (A**2) : 7.45000                                              
REMARK   3    B12 (A**2) : -2.30000                                             
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): 0.296         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.229         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.180         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.861        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 21635 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 21590 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 29294 ; 1.304 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 49846 ; 0.763 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2757 ; 5.696 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   856 ;35.424 ;25.129       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  4031 ;15.220 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    92 ;18.944 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3387 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 24203 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  4569 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   333                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.6284 -23.7944 -28.7978              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4122 T22:   0.3687                                     
REMARK   3      T33:   0.1060 T12:  -0.0299                                     
REMARK   3      T13:  -0.0545 T23:  -0.0420                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9570 L22:   0.7782                                     
REMARK   3      L33:   0.6654 L12:  -0.2992                                     
REMARK   3      L13:  -0.1303 L23:  -0.1243                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0248 S12:   0.1235 S13:  -0.1915                       
REMARK   3      S21:  -0.1384 S22:  -0.0285 S23:  -0.1171                       
REMARK   3      S31:   0.1224 S32:   0.0280 S33:   0.0037                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B   332                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.9418  -3.1652 -22.5904              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3964 T22:   0.3805                                     
REMARK   3      T33:   0.0774 T12:  -0.0082                                     
REMARK   3      T13:  -0.0634 T23:   0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8254 L22:   0.8954                                     
REMARK   3      L33:   0.1544 L12:  -0.1455                                     
REMARK   3      L13:   0.0740 L23:  -0.0327                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0336 S12:   0.0756 S13:  -0.0243                       
REMARK   3      S21:  -0.0781 S22:   0.0010 S23:   0.2365                       
REMARK   3      S31:  -0.0496 S32:  -0.1035 S33:  -0.0346                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     2        C   333                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.6436 -12.6092   7.2112              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3725 T22:   0.3284                                     
REMARK   3      T33:   0.0186 T12:  -0.0595                                     
REMARK   3      T13:  -0.0760 T23:   0.0298                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6649 L22:   1.4370                                     
REMARK   3      L33:   0.8376 L12:   0.0166                                     
REMARK   3      L13:   0.0530 L23:  -0.2293                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0171 S12:  -0.1066 S13:  -0.0322                       
REMARK   3      S21:   0.1515 S22:  -0.0018 S23:  -0.0669                       
REMARK   3      S31:   0.0176 S32:   0.0015 S33:  -0.0153                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D   333                          
REMARK   3    ORIGIN FOR THE GROUP (A):  78.1861  12.2899 -13.5222              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3899 T22:   0.3338                                     
REMARK   3      T33:   0.0976 T12:  -0.0294                                     
REMARK   3      T13:  -0.0518 T23:   0.0223                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7629 L22:   1.1452                                     
REMARK   3      L33:   0.4451 L12:   0.1693                                     
REMARK   3      L13:   0.1040 L23:  -0.2451                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0080 S12:   0.0179 S13:   0.1063                       
REMARK   3      S21:  -0.0729 S22:   0.0035 S23:  -0.2182                       
REMARK   3      S31:  -0.0499 S32:   0.0211 S33:   0.0046                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     2        E   332                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.4912 -52.5491 -80.6027              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4434 T22:   0.4420                                     
REMARK   3      T33:   0.0207 T12:  -0.0300                                     
REMARK   3      T13:  -0.0524 T23:   0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2256 L22:   0.9269                                     
REMARK   3      L33:   0.7837 L12:  -0.0664                                     
REMARK   3      L13:  -0.1877 L23:   0.0549                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0124 S12:   0.2592 S13:   0.0935                       
REMARK   3      S21:  -0.2330 S22:   0.0131 S23:   0.0947                       
REMARK   3      S31:  -0.0367 S32:  -0.1038 S33:  -0.0256                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     2        F   332                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.8838 -69.8463 -51.7786              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3728 T22:   0.3766                                     
REMARK   3      T33:   0.0989 T12:  -0.0361                                     
REMARK   3      T13:  -0.0211 T23:   0.0024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9676 L22:   1.2049                                     
REMARK   3      L33:   0.4596 L12:   0.2193                                     
REMARK   3      L13:   0.0041 L23:  -0.0787                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0408 S12:  -0.0636 S13:  -0.2313                       
REMARK   3      S21:   0.0642 S22:  -0.0690 S23:   0.0378                       
REMARK   3      S31:   0.0527 S32:  -0.0428 S33:   0.1098                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     2        G   332                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.7941 -46.5932 -60.7321              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3797 T22:   0.3424                                     
REMARK   3      T33:   0.0810 T12:  -0.0306                                     
REMARK   3      T13:  -0.0052 T23:  -0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1323 L22:   0.4428                                     
REMARK   3      L33:   0.4421 L12:   0.0080                                     
REMARK   3      L13:  -0.2756 L23:   0.1703                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0265 S12:   0.0297 S13:   0.0110                       
REMARK   3      S21:  -0.0342 S22:   0.0108 S23:  -0.1608                       
REMARK   3      S31:   0.0151 S32:   0.0588 S33:   0.0157                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     2        H   332                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.8719 -32.8569 -46.1028              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3966 T22:   0.4115                                     
REMARK   3      T33:   0.0801 T12:  -0.0055                                     
REMARK   3      T13:  -0.0268 T23:  -0.0406                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7671 L22:   0.7951                                     
REMARK   3      L33:   0.4720 L12:   0.0987                                     
REMARK   3      L13:  -0.1718 L23:  -0.0355                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0107 S12:  -0.0759 S13:   0.2341                       
REMARK   3      S21:   0.1014 S22:   0.0025 S23:   0.0759                       
REMARK   3      S31:  -0.0900 S32:  -0.0931 S33:  -0.0132                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4OJN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084576.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 162753                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.58100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS-TRIS PROPANE, PH 7.0, 20%     
REMARK 280  PEG400, 100 MM LITHIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      111.08000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      222.16000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      222.16000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      111.08000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 23790 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 46990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -142.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 23660 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 46830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -142.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
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 A   334                                                      
REMARK 465     HIS A   335                                                      
REMARK 465     HIS A   336                                                      
REMARK 465     HIS A   337                                                      
REMARK 465     HIS A   338                                                      
REMARK 465     HIS B   333                                                      
REMARK 465     HIS B   334                                                      
REMARK 465     HIS B   335                                                      
REMARK 465     HIS B   336                                                      
REMARK 465     HIS B   337                                                      
REMARK 465     HIS B   338                                                      
REMARK 465     HIS C   334                                                      
REMARK 465     HIS C   335                                                      
REMARK 465     HIS C   336                                                      
REMARK 465     HIS C   337                                                      
REMARK 465     HIS C   338                                                      
REMARK 465     HIS D   334                                                      
REMARK 465     HIS D   335                                                      
REMARK 465     HIS D   336                                                      
REMARK 465     HIS D   337                                                      
REMARK 465     HIS D   338                                                      
REMARK 465     HIS E   333                                                      
REMARK 465     HIS E   334                                                      
REMARK 465     HIS E   335                                                      
REMARK 465     HIS E   336                                                      
REMARK 465     HIS E   337                                                      
REMARK 465     HIS E   338                                                      
REMARK 465     HIS F   333                                                      
REMARK 465     HIS F   334                                                      
REMARK 465     HIS F   335                                                      
REMARK 465     HIS F   336                                                      
REMARK 465     HIS F   337                                                      
REMARK 465     HIS F   338                                                      
REMARK 465     HIS G   333                                                      
REMARK 465     HIS G   334                                                      
REMARK 465     HIS G   335                                                      
REMARK 465     HIS G   336                                                      
REMARK 465     HIS G   337                                                      
REMARK 465     HIS G   338                                                      
REMARK 465     HIS H   333                                                      
REMARK 465     HIS H   334                                                      
REMARK 465     HIS H   335                                                      
REMARK 465     HIS H   336                                                      
REMARK 465     HIS H   337                                                      
REMARK 465     HIS H   338                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG D 171   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 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    LYS A  14     -126.09    -71.29                                   
REMARK 500    GLU A  15      178.10     57.86                                   
REMARK 500    GLU A  16      -89.84    -96.40                                   
REMARK 500    ASN A  21       55.11   -142.15                                   
REMARK 500    SER A 249      -54.35   -159.45                                   
REMARK 500    LEU B  13      124.39    -39.15                                   
REMARK 500    ASN B 130       41.20   -109.10                                   
REMARK 500    SER B 249      -59.50   -158.88                                   
REMARK 500    ASN C  21       57.15   -141.51                                   
REMARK 500    SER C 249      -53.22   -154.14                                   
REMARK 500    LYS D  14     -160.14   -112.96                                   
REMARK 500    GLN D  17      -70.89     77.54                                   
REMARK 500    ASN D  21       56.37   -141.53                                   
REMARK 500    TYR D 247      176.53    178.80                                   
REMARK 500    SER D 249      -52.37   -164.47                                   
REMARK 500    LEU E  12     -148.64    -98.40                                   
REMARK 500    LEU E  13      153.00    -42.45                                   
REMARK 500    GLN E  17       74.97    -63.24                                   
REMARK 500    SER E 137      135.67    -39.96                                   
REMARK 500    LYS E 222       30.24    -95.26                                   
REMARK 500    SER E 249      -62.63   -154.04                                   
REMARK 500    ILE E 277       43.43   -107.63                                   
REMARK 500    TYR E 281       19.12     52.44                                   
REMARK 500    GLU F  16     -152.31   -128.66                                   
REMARK 500    ASN F  21       49.04   -142.84                                   
REMARK 500    ASN F 130       51.50    -97.14                                   
REMARK 500    SER F 196       47.84   -103.74                                   
REMARK 500    SER F 249      -50.51   -149.48                                   
REMARK 500    ASN G 130       62.36   -107.25                                   
REMARK 500    SER G 249      -56.21   -161.90                                   
REMARK 500    GLU H  15       81.79    -61.74                                   
REMARK 500    GLN H  17      116.88     41.96                                   
REMARK 500    THR H  18       88.94    165.84                                   
REMARK 500    SER H 249      -56.88   -158.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE C 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE E 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE F 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE G 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE H 400                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4OKN   RELATED DB: PDB                                   
DBREF  4OJN A    2   332  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  4OJN B    2   332  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  4OJN C    2   332  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  4OJN D    2   332  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  4OJN E    2   332  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  4OJN F    2   332  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  4OJN G    2   332  UNP    P00338   LDHA_HUMAN       2    332             
DBREF  4OJN H    2   332  UNP    P00338   LDHA_HUMAN       2    332             
SEQADV 4OJN HIS A  333  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS A  334  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS A  335  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS A  336  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS A  337  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS A  338  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS B  333  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS B  334  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS B  335  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS B  336  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS B  337  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS B  338  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS C  333  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS C  334  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS C  335  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS C  336  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS C  337  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS C  338  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS D  333  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS D  334  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS D  335  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS D  336  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS D  337  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS D  338  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS E  333  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS E  334  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS E  335  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS E  336  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS E  337  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS E  338  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS F  333  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS F  334  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS F  335  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS F  336  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS F  337  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS F  338  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS G  333  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS G  334  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS G  335  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS G  336  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS G  337  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS G  338  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS H  333  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS H  334  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS H  335  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS H  336  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS H  337  UNP  P00338              EXPRESSION TAG                 
SEQADV 4OJN HIS H  338  UNP  P00338              EXPRESSION TAG                 
SEQRES   1 A  337  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 A  337  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 A  337  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 A  337  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 A  337  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 A  337  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 A  337  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 A  337  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 A  337  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 A  337  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 A  337  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 A  337  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 A  337  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 A  337  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 A  337  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 A  337  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 A  337  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 A  337  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 A  337  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 A  337  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 A  337  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 A  337  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 A  337  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 A  337  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 A  337  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 A  337  GLN LYS GLU LEU GLN PHE HIS HIS HIS HIS HIS HIS              
SEQRES   1 B  337  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 B  337  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 B  337  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 B  337  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 B  337  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 B  337  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 B  337  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 B  337  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 B  337  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 B  337  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 B  337  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 B  337  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 B  337  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 B  337  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 B  337  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 B  337  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 B  337  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 B  337  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 B  337  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 B  337  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 B  337  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 B  337  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 B  337  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 B  337  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 B  337  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 B  337  GLN LYS GLU LEU GLN PHE HIS HIS HIS HIS HIS HIS              
SEQRES   1 C  337  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 C  337  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 C  337  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 C  337  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 C  337  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 C  337  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 C  337  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 C  337  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 C  337  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 C  337  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 C  337  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 C  337  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 C  337  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 C  337  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 C  337  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 C  337  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 C  337  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 C  337  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 C  337  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 C  337  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 C  337  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 C  337  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 C  337  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 C  337  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 C  337  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 C  337  GLN LYS GLU LEU GLN PHE HIS HIS HIS HIS HIS HIS              
SEQRES   1 D  337  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 D  337  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 D  337  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 D  337  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 D  337  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 D  337  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 D  337  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 D  337  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 D  337  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 D  337  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 D  337  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 D  337  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 D  337  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 D  337  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 D  337  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 D  337  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 D  337  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 D  337  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 D  337  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 D  337  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 D  337  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 D  337  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 D  337  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 D  337  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 D  337  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 D  337  GLN LYS GLU LEU GLN PHE HIS HIS HIS HIS HIS HIS              
SEQRES   1 E  337  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 E  337  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 E  337  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 E  337  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 E  337  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 E  337  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 E  337  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 E  337  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 E  337  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 E  337  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 E  337  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 E  337  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 E  337  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 E  337  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 E  337  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 E  337  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 E  337  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 E  337  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 E  337  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 E  337  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 E  337  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 E  337  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 E  337  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 E  337  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 E  337  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 E  337  GLN LYS GLU LEU GLN PHE HIS HIS HIS HIS HIS HIS              
SEQRES   1 F  337  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 F  337  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 F  337  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 F  337  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 F  337  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 F  337  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 F  337  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 F  337  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 F  337  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 F  337  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 F  337  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 F  337  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 F  337  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 F  337  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 F  337  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 F  337  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 F  337  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 F  337  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 F  337  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 F  337  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 F  337  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 F  337  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 F  337  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 F  337  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 F  337  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 F  337  GLN LYS GLU LEU GLN PHE HIS HIS HIS HIS HIS HIS              
SEQRES   1 G  337  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 G  337  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 G  337  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 G  337  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 G  337  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 G  337  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 G  337  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 G  337  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 G  337  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 G  337  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 G  337  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 G  337  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 G  337  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 G  337  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 G  337  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 G  337  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 G  337  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 G  337  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 G  337  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 G  337  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 G  337  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 G  337  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 G  337  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 G  337  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 G  337  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 G  337  GLN LYS GLU LEU GLN PHE HIS HIS HIS HIS HIS HIS              
SEQRES   1 H  337  ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU LYS          
SEQRES   2 H  337  GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL GLY          
SEQRES   3 H  337  VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE LEU          
SEQRES   4 H  337  MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP VAL          
SEQRES   5 H  337  ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU GLN          
SEQRES   6 H  337  HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL SER          
SEQRES   7 H  337  GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU VAL          
SEQRES   8 H  337  ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU SER          
SEQRES   9 H  337  ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE LYS          
SEQRES  10 H  337  PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN CYS          
SEQRES  11 H  337  LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU THR          
SEQRES  12 H  337  TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN ARG          
SEQRES  13 H  337  VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG PHE          
SEQRES  14 H  337  ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO LEU          
SEQRES  15 H  337  SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP SER          
SEQRES  16 H  337  SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY VAL          
SEQRES  17 H  337  SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP LYS          
SEQRES  18 H  337  ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL VAL          
SEQRES  19 H  337  GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR          
SEQRES  20 H  337  SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU          
SEQRES  21 H  337  SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL SER          
SEQRES  22 H  337  THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP VAL          
SEQRES  23 H  337  PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY ILE          
SEQRES  24 H  337  SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU GLU          
SEQRES  25 H  337  ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY ILE          
SEQRES  26 H  337  GLN LYS GLU LEU GLN PHE HIS HIS HIS HIS HIS HIS              
HET    1PE  A 400      16                                                       
HET    1PE  B 400      16                                                       
HET    1PE  C 400      16                                                       
HET    1PE  D 401      16                                                       
HET    GOL  D 402       6                                                       
HET    GOL  D 403       6                                                       
HET    1PE  E 401      16                                                       
HET    GOL  E 402       6                                                       
HET    1PE  F 400      16                                                       
HET    1PE  G 400      16                                                       
HET    1PE  H 400      16                                                       
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     GOL GLYCEROL                                                         
HETSYN     1PE PEG400                                                           
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   9  1PE    8(C10 H22 O6)                                                
FORMUL  13  GOL    3(C3 H8 O3)                                                  
FORMUL  20  HOH   *527(H2 O)                                                    
HELIX    1   1 THR A    3  LEU A    8  1                                   6    
HELIX    2   2 GLY A   29  LYS A   42  1                                  14    
HELIX    3   3 ILE A   54  HIS A   67  1                                  14    
HELIX    4   4 GLY A   68  LEU A   72  5                                   5    
HELIX    5   5 ASP A   82  ALA A   87  5                                   6    
HELIX    6   6 SER A  105  SER A  128  1                                  24    
HELIX    7   7 PRO A  139  GLY A  152  1                                  14    
HELIX    8   8 PRO A  154  ASN A  156  5                                   3    
HELIX    9   9 CYS A  163  GLY A  179  1                                  17    
HELIX   10  10 HIS A  181  LEU A  183  5                                   3    
HELIX   11  11 TRP A  201  GLY A  203  5                                   3    
HELIX   12  12 LEU A  211  HIS A  215  1                                   5    
HELIX   13  13 TRP A  227  GLY A  246  1                                  20    
HELIX   14  14 SER A  249  LYS A  265  1                                  17    
HELIX   15  15 THR A  309  LYS A  328  1                                  20    
HELIX   16  16 THR B    3  LEU B    8  1                                   6    
HELIX   17  17 GLY B   29  LYS B   42  1                                  14    
HELIX   18  18 ILE B   54  HIS B   67  1                                  14    
HELIX   19  19 GLY B   68  LEU B   72  5                                   5    
HELIX   20  20 ASP B   82  ALA B   87  5                                   6    
HELIX   21  21 SER B  105  SER B  128  1                                  24    
HELIX   22  22 PRO B  139  GLY B  152  1                                  14    
HELIX   23  23 PRO B  154  ASN B  156  5                                   3    
HELIX   24  24 CYS B  163  GLY B  179  1                                  17    
HELIX   25  25 HIS B  181  CYS B  185  5                                   5    
HELIX   26  26 LEU B  211  HIS B  215  1                                   5    
HELIX   27  27 TRP B  227  GLY B  246  1                                  20    
HELIX   28  28 SER B  249  LYS B  265  1                                  17    
HELIX   29  29 THR B  309  LYS B  328  1                                  20    
HELIX   30  30 THR C    3  LEU C    8  1                                   6    
HELIX   31  31 GLY C   29  LYS C   42  1                                  14    
HELIX   32  32 ILE C   54  HIS C   67  1                                  14    
HELIX   33  33 GLY C   68  LEU C   72  5                                   5    
HELIX   34  34 ASP C   82  ALA C   87  5                                   6    
HELIX   35  35 SER C  105  SER C  128  1                                  24    
HELIX   36  36 PRO C  139  GLY C  152  1                                  14    
HELIX   37  37 PRO C  154  ASN C  156  5                                   3    
HELIX   38  38 CYS C  163  GLY C  179  1                                  17    
HELIX   39  39 HIS C  181  CYS C  185  5                                   5    
HELIX   40  40 TRP C  201  GLY C  203  5                                   3    
HELIX   41  41 LEU C  211  HIS C  215  1                                   5    
HELIX   42  42 TRP C  227  GLU C  236  1                                  10    
HELIX   43  43 GLU C  236  GLY C  246  1                                  11    
HELIX   44  44 SER C  249  LYS C  265  1                                  17    
HELIX   45  45 THR C  309  LYS C  328  1                                  20    
HELIX   46  46 THR D    3  LEU D    8  1                                   6    
HELIX   47  47 GLY D   29  LYS D   42  1                                  14    
HELIX   48  48 ILE D   54  HIS D   67  1                                  14    
HELIX   49  49 GLY D   68  LEU D   72  5                                   5    
HELIX   50  50 ASP D   82  ALA D   87  5                                   6    
HELIX   51  51 SER D  105  SER D  128  1                                  24    
HELIX   52  52 PRO D  139  GLY D  152  1                                  14    
HELIX   53  53 PRO D  154  ASN D  156  5                                   3    
HELIX   54  54 CYS D  163  GLY D  179  1                                  17    
HELIX   55  55 HIS D  181  LEU D  183  5                                   3    
HELIX   56  56 TRP D  201  GLY D  203  5                                   3    
HELIX   57  57 LEU D  211  HIS D  215  1                                   5    
HELIX   58  58 TRP D  227  GLU D  236  1                                  10    
HELIX   59  59 GLU D  236  GLY D  246  1                                  11    
HELIX   60  60 SER D  249  LYS D  265  1                                  17    
HELIX   61  61 GLY D  279  ILE D  283  5                                   5    
HELIX   62  62 THR D  309  LYS D  328  1                                  20    
HELIX   63  63 THR E    3  LEU E    8  1                                   6    
HELIX   64  64 GLY E   29  LYS E   42  1                                  14    
HELIX   65  65 ILE E   54  HIS E   67  1                                  14    
HELIX   66  66 GLY E   68  LEU E   72  5                                   5    
HELIX   67  67 ASP E   82  ALA E   87  5                                   6    
HELIX   68  68 SER E  105  SER E  128  1                                  24    
HELIX   69  69 PRO E  139  GLY E  152  1                                  14    
HELIX   70  70 PRO E  154  ASN E  156  5                                   3    
HELIX   71  71 CYS E  163  GLY E  179  1                                  17    
HELIX   72  72 HIS E  181  LEU E  183  5                                   3    
HELIX   73  73 LEU E  211  HIS E  215  1                                   5    
HELIX   74  74 TRP E  227  GLY E  246  1                                  20    
HELIX   75  75 SER E  249  LYS E  265  1                                  17    
HELIX   76  76 THR E  309  LYS E  328  1                                  20    
HELIX   77  77 THR F    3  LEU F    8  1                                   6    
HELIX   78  78 GLY F   29  LYS F   42  1                                  14    
HELIX   79  79 ILE F   54  HIS F   67  1                                  14    
HELIX   80  80 GLY F   68  LEU F   72  5                                   5    
HELIX   81  81 ASP F   82  ALA F   87  5                                   6    
HELIX   82  82 SER F  105  SER F  128  1                                  24    
HELIX   83  83 PRO F  139  GLY F  152  1                                  14    
HELIX   84  84 PRO F  154  ASN F  156  5                                   3    
HELIX   85  85 CYS F  163  GLY F  179  1                                  17    
HELIX   86  86 HIS F  181  LEU F  183  5                                   3    
HELIX   87  87 TRP F  201  GLY F  203  5                                   3    
HELIX   88  88 LEU F  211  HIS F  215  1                                   5    
HELIX   89  89 TRP F  227  GLY F  246  1                                  20    
HELIX   90  90 SER F  249  ASN F  266  1                                  18    
HELIX   91  91 GLY F  279  ILE F  283  5                                   5    
HELIX   92  92 THR F  309  LYS F  328  1                                  20    
HELIX   93  93 THR G    3  LEU G    8  1                                   6    
HELIX   94  94 GLY G   29  LYS G   42  1                                  14    
HELIX   95  95 ILE G   54  GLY G   68  1                                  15    
HELIX   96  96 SER G   69  LEU G   72  5                                   4    
HELIX   97  97 ASP G   82  ALA G   87  5                                   6    
HELIX   98  98 SER G  105  SER G  128  1                                  24    
HELIX   99  99 PRO G  139  GLY G  152  1                                  14    
HELIX  100 100 PRO G  154  ASN G  156  5                                   3    
HELIX  101 101 CYS G  163  GLY G  179  1                                  17    
HELIX  102 102 HIS G  181  LEU G  183  5                                   3    
HELIX  103 103 TRP G  201  GLY G  203  5                                   3    
HELIX  104 104 LEU G  211  HIS G  215  1                                   5    
HELIX  105 105 TRP G  227  GLY G  246  1                                  20    
HELIX  106 106 SER G  249  LYS G  265  1                                  17    
HELIX  107 107 THR G  309  LYS G  328  1                                  20    
HELIX  108 108 THR H    3  LEU H    8  1                                   6    
HELIX  109 109 GLY H   29  LYS H   42  1                                  14    
HELIX  110 110 ILE H   54  HIS H   67  1                                  14    
HELIX  111 111 GLY H   68  LEU H   72  5                                   5    
HELIX  112 112 ASP H   82  ALA H   87  5                                   6    
HELIX  113 113 SER H  105  SER H  128  1                                  24    
HELIX  114 114 PRO H  139  GLY H  152  1                                  14    
HELIX  115 115 PRO H  154  ASN H  156  5                                   3    
HELIX  116 116 CYS H  163  GLY H  179  1                                  17    
HELIX  117 117 HIS H  181  LEU H  183  5                                   3    
HELIX  118 118 TRP H  201  GLY H  203  5                                   3    
HELIX  119 119 LEU H  211  HIS H  215  1                                   5    
HELIX  120 120 TRP H  227  GLU H  236  1                                  10    
HELIX  121 121 GLU H  236  GLY H  246  1                                  11    
HELIX  122 122 SER H  249  LYS H  265  1                                  17    
HELIX  123 123 THR H  309  LYS H  328  1                                  20    
SHEET    1   A 4 ILE A   9  ASN A  11  0                                        
SHEET    2   A 4 GLY D 299  VAL D 304 -1  O  LEU D 303   N  TYR A  10           
SHEET    3   A 4 PHE D 288  GLY D 296 -1  N  PRO D 292   O  VAL D 304           
SHEET    4   A 4 ARG D 269  MET D 276 -1  N  HIS D 271   O  CYS D 293           
SHEET    1   B 6 LYS A  76  SER A  79  0                                        
SHEET    2   B 6 GLU A  47  VAL A  51  1  N  LEU A  48   O  VAL A  78           
SHEET    3   B 6 LYS A  22  VAL A  26  1  N  VAL A  25   O  ALA A  49           
SHEET    4   B 6 LEU A  91  ILE A  94  1  O  ILE A  93   N  VAL A  26           
SHEET    5   B 6 LYS A 132  ILE A 135  1  O  LEU A 134   N  VAL A  92           
SHEET    6   B 6 VAL A 158  GLY A 160  1  O  ILE A 159   N  LEU A 133           
SHEET    1   C 3 CYS A 185  HIS A 186  0                                        
SHEET    2   C 3 ASN A 205  VAL A 206 -1  O  ASN A 205   N  HIS A 186           
SHEET    3   C 3 VAL A 209  SER A 210 -1  O  VAL A 209   N  VAL A 206           
SHEET    1   D 2 VAL A 189  LEU A 190  0                                        
SHEET    2   D 2 VAL A 198  PRO A 199 -1  O  VAL A 198   N  LEU A 190           
SHEET    1   E 4 ARG A 269  MET A 276  0                                        
SHEET    2   E 4 PHE A 288  GLY A 296 -1  O  CYS A 293   N  HIS A 271           
SHEET    3   E 4 GLY A 299  VAL A 304 -1  O  VAL A 304   N  PRO A 292           
SHEET    4   E 4 ILE D   9  ASN D  11 -1  O  TYR D  10   N  LEU A 303           
SHEET    1   F 4 ILE B   9  ASN B  11  0                                        
SHEET    2   F 4 GLY C 299  VAL C 304 -1  O  LEU C 303   N  TYR B  10           
SHEET    3   F 4 PHE C 288  GLY C 296 -1  N  ILE C 294   O  SER C 301           
SHEET    4   F 4 ARG C 269  MET C 276 -1  N  HIS C 271   O  CYS C 293           
SHEET    1   G 6 LYS B  76  SER B  79  0                                        
SHEET    2   G 6 GLU B  47  VAL B  51  1  N  LEU B  48   O  VAL B  78           
SHEET    3   G 6 LYS B  22  VAL B  26  1  N  VAL B  25   O  ALA B  49           
SHEET    4   G 6 LEU B  91  ILE B  94  1  O  ILE B  93   N  THR B  24           
SHEET    5   G 6 LYS B 132  ILE B 135  1  O  LEU B 134   N  VAL B  92           
SHEET    6   G 6 VAL B 158  GLY B 160  1  O  ILE B 159   N  ILE B 135           
SHEET    1   H 2 VAL B 189  LEU B 190  0                                        
SHEET    2   H 2 VAL B 198  PRO B 199 -1  O  VAL B 198   N  LEU B 190           
SHEET    1   I 2 ASN B 205  VAL B 206  0                                        
SHEET    2   I 2 VAL B 209  SER B 210 -1  O  VAL B 209   N  VAL B 206           
SHEET    1   J 4 ARG B 269  MET B 276  0                                        
SHEET    2   J 4 PHE B 288  GLY B 296 -1  O  CYS B 293   N  HIS B 271           
SHEET    3   J 4 GLY B 299  VAL B 304 -1  O  VAL B 304   N  PRO B 292           
SHEET    4   J 4 ILE C   9  ASN C  11 -1  O  TYR C  10   N  LEU B 303           
SHEET    1   K 6 LYS C  76  SER C  79  0                                        
SHEET    2   K 6 GLU C  47  VAL C  51  1  N  LEU C  48   O  VAL C  78           
SHEET    3   K 6 LYS C  22  VAL C  26  1  N  VAL C  25   O  ALA C  49           
SHEET    4   K 6 LEU C  91  ILE C  94  1  O  ILE C  93   N  VAL C  26           
SHEET    5   K 6 LYS C 132  ILE C 135  1  O  LEU C 134   N  ILE C  94           
SHEET    6   K 6 VAL C 158  GLY C 160  1  O  ILE C 159   N  ILE C 135           
SHEET    1   L 2 VAL C 189  LEU C 190  0                                        
SHEET    2   L 2 VAL C 198  PRO C 199 -1  O  VAL C 198   N  LEU C 190           
SHEET    1   M 2 ASN C 205  VAL C 206  0                                        
SHEET    2   M 2 VAL C 209  SER C 210 -1  O  VAL C 209   N  VAL C 206           
SHEET    1   N 6 LYS D  76  SER D  79  0                                        
SHEET    2   N 6 GLU D  47  VAL D  51  1  N  LEU D  48   O  LYS D  76           
SHEET    3   N 6 LYS D  22  VAL D  26  1  N  VAL D  25   O  ALA D  49           
SHEET    4   N 6 LEU D  91  ILE D  94  1  O  ILE D  93   N  VAL D  26           
SHEET    5   N 6 LYS D 132  ILE D 135  1  O  LEU D 134   N  ILE D  94           
SHEET    6   N 6 VAL D 158  GLY D 160  1  O  ILE D 159   N  ILE D 135           
SHEET    1   O 3 CYS D 185  HIS D 186  0                                        
SHEET    2   O 3 ASN D 205  VAL D 206 -1  O  ASN D 205   N  HIS D 186           
SHEET    3   O 3 VAL D 209  SER D 210 -1  O  VAL D 209   N  VAL D 206           
SHEET    1   P 2 VAL D 189  GLY D 191  0                                        
SHEET    2   P 2 SER D 197  PRO D 199 -1  O  VAL D 198   N  LEU D 190           
SHEET    1   Q 4 ILE E   9  ASN E  11  0                                        
SHEET    2   Q 4 GLY H 299  VAL H 304 -1  O  LEU H 303   N  TYR E  10           
SHEET    3   Q 4 PHE H 288  GLY H 296 -1  N  PRO H 292   O  VAL H 304           
SHEET    4   Q 4 ARG H 269  MET H 276 -1  N  HIS H 271   O  CYS H 293           
SHEET    1   R 6 LYS E  76  SER E  79  0                                        
SHEET    2   R 6 GLU E  47  VAL E  51  1  N  LEU E  48   O  LYS E  76           
SHEET    3   R 6 LYS E  22  VAL E  26  1  N  VAL E  25   O  ALA E  49           
SHEET    4   R 6 LEU E  91  ILE E  94  1  O  ILE E  93   N  VAL E  26           
SHEET    5   R 6 LYS E 132  ILE E 135  1  O  LEU E 134   N  ILE E  94           
SHEET    6   R 6 VAL E 158  GLY E 160  1  O  ILE E 159   N  LEU E 133           
SHEET    1   S 3 CYS E 185  HIS E 186  0                                        
SHEET    2   S 3 ASN E 205  VAL E 206 -1  O  ASN E 205   N  HIS E 186           
SHEET    3   S 3 VAL E 209  SER E 210 -1  O  VAL E 209   N  VAL E 206           
SHEET    1   T 2 VAL E 189  GLY E 191  0                                        
SHEET    2   T 2 SER E 197  PRO E 199 -1  O  VAL E 198   N  LEU E 190           
SHEET    1   U 4 ARG E 269  MET E 276  0                                        
SHEET    2   U 4 PHE E 288  GLY E 296 -1  O  CYS E 293   N  HIS E 271           
SHEET    3   U 4 GLY E 299  VAL E 304 -1  O  VAL E 304   N  PRO E 292           
SHEET    4   U 4 ILE H   9  ASN H  11 -1  O  TYR H  10   N  LEU E 303           
SHEET    1   V 4 ILE F   9  ASN F  11  0                                        
SHEET    2   V 4 GLY G 299  VAL G 304 -1  O  LEU G 303   N  TYR F  10           
SHEET    3   V 4 PHE G 288  GLY G 296 -1  N  PRO G 292   O  VAL G 304           
SHEET    4   V 4 ARG G 269  MET G 276 -1  N  HIS G 271   O  CYS G 293           
SHEET    1   W 6 LYS F  76  SER F  79  0                                        
SHEET    2   W 6 GLU F  47  VAL F  51  1  N  LEU F  48   O  VAL F  78           
SHEET    3   W 6 LYS F  22  VAL F  26  1  N  VAL F  25   O  ALA F  49           
SHEET    4   W 6 LEU F  91  ILE F  94  1  O  ILE F  93   N  VAL F  26           
SHEET    5   W 6 LYS F 132  ILE F 135  1  O  LEU F 134   N  ILE F  94           
SHEET    6   W 6 VAL F 158  GLY F 160  1  O  ILE F 159   N  LEU F 133           
SHEET    1   X 3 CYS F 185  HIS F 186  0                                        
SHEET    2   X 3 ASN F 205  VAL F 206 -1  O  ASN F 205   N  HIS F 186           
SHEET    3   X 3 VAL F 209  SER F 210 -1  O  VAL F 209   N  VAL F 206           
SHEET    1   Y 2 VAL F 189  GLY F 191  0                                        
SHEET    2   Y 2 SER F 197  PRO F 199 -1  O  VAL F 198   N  LEU F 190           
SHEET    1   Z 4 ARG F 269  MET F 276  0                                        
SHEET    2   Z 4 PHE F 288  GLY F 296 -1  O  CYS F 293   N  HIS F 271           
SHEET    3   Z 4 GLY F 299  VAL F 304 -1  O  GLY F 299   N  GLY F 296           
SHEET    4   Z 4 ILE G   9  ASN G  11 -1  O  TYR G  10   N  LEU F 303           
SHEET    1  AA 6 LYS G  76  SER G  79  0                                        
SHEET    2  AA 6 GLU G  47  VAL G  51  1  N  LEU G  48   O  VAL G  78           
SHEET    3  AA 6 LYS G  22  VAL G  26  1  N  VAL G  25   O  ALA G  49           
SHEET    4  AA 6 LEU G  91  ILE G  94  1  O  ILE G  93   N  VAL G  26           
SHEET    5  AA 6 LYS G 132  ILE G 135  1  O  LYS G 132   N  VAL G  92           
SHEET    6  AA 6 VAL G 158  GLY G 160  1  O  ILE G 159   N  LEU G 133           
SHEET    1  AB 3 CYS G 185  HIS G 186  0                                        
SHEET    2  AB 3 ASN G 205  VAL G 206 -1  O  ASN G 205   N  HIS G 186           
SHEET    3  AB 3 VAL G 209  SER G 210 -1  O  VAL G 209   N  VAL G 206           
SHEET    1  AC 2 VAL G 189  GLY G 191  0                                        
SHEET    2  AC 2 SER G 197  PRO G 199 -1  O  VAL G 198   N  LEU G 190           
SHEET    1  AD 6 ILE H  77  SER H  79  0                                        
SHEET    2  AD 6 GLU H  47  VAL H  51  1  N  LEU H  48   O  VAL H  78           
SHEET    3  AD 6 LYS H  22  VAL H  26  1  N  VAL H  25   O  ALA H  49           
SHEET    4  AD 6 LEU H  91  ILE H  94  1  O  ILE H  93   N  THR H  24           
SHEET    5  AD 6 LYS H 132  ILE H 135  1  O  LEU H 134   N  VAL H  92           
SHEET    6  AD 6 VAL H 158  GLY H 160  1  O  ILE H 159   N  ILE H 135           
SHEET    1  AE 3 CYS H 185  HIS H 186  0                                        
SHEET    2  AE 3 ASN H 205  VAL H 206 -1  O  ASN H 205   N  HIS H 186           
SHEET    3  AE 3 VAL H 209  SER H 210 -1  O  VAL H 209   N  VAL H 206           
SHEET    1  AF 2 VAL H 189  GLY H 191  0                                        
SHEET    2  AF 2 SER H 197  PRO H 199 -1  O  VAL H 198   N  LEU H 190           
CISPEP   1 GLU A   15    GLU A   16          0        -1.35                     
CISPEP   2 ASN A  138    PRO A  139          0        -8.09                     
CISPEP   3 ASN B  138    PRO B  139          0        -6.22                     
CISPEP   4 ASN C  138    PRO C  139          0        -6.77                     
CISPEP   5 ASN D  138    PRO D  139          0       -10.05                     
CISPEP   6 ASN E  138    PRO E  139          0        -8.99                     
CISPEP   7 ASN F  138    PRO F  139          0       -10.07                     
CISPEP   8 ASN G  138    PRO G  139          0        -3.72                     
CISPEP   9 ASN H  138    PRO H  139          0        -4.53                     
SITE     1 AC1  8 VAL A  31  THR A  95  ALA A  98  VAL A 136                    
SITE     2 AC1  8 SER A 137  ASN A 138  TYR A 239  THR A 248                    
SITE     1 AC2  6 THR B  95  ALA B  98  VAL B 136  ASN B 138                    
SITE     2 AC2  6 ALA B 238  THR B 248                                          
SITE     1 AC3  8 VAL C  31  THR C  95  ALA C  98  VAL C 136                    
SITE     2 AC3  8 SER C 137  ASN C 138  THR C 248  HOH C 522                    
SITE     1 AC4  5 VAL D  31  THR D  95  VAL D 136  SER D 137                    
SITE     2 AC4  5 ASN D 138                                                     
SITE     1 AC5  9 ARG B 171  HIS B 186  TRP B 188  VAL B 270                    
SITE     2 AC5  9 HOH B 547  SER D 184  HIS D 186  ALA D 207                    
SITE     3 AC5  9 HOH D 529                                                     
SITE     1 AC6  1 ASN D  84                                                     
SITE     1 AC7  6 VAL E  31  THR E  95  VAL E 136  SER E 137                    
SITE     2 AC7  6 ASN E 138  THR E 248                                          
SITE     1 AC8  1 GLN E 226                                                     
SITE     1 AC9 10 VAL F  31  THR F  95  GLY F  97  ALA F  98                    
SITE     2 AC9 10 VAL F 136  SER F 137  ASN F 138  THR F 248                    
SITE     3 AC9 10 HOH F 551  HOH F 552                                          
SITE     1 BC1  6 THR G  95  ALA G  98  VAL G 136  ASN G 138                    
SITE     2 BC1  6 ALA G 238  THR G 248                                          
SITE     1 BC2  7 VAL H  31  THR H  95  ALA H  98  VAL H 136                    
SITE     2 BC2  7 SER H 137  ASN H 138  THR H 248                               
CRYST1  147.140  147.140  333.240  90.00  90.00 120.00 P 31 2 1     48          
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      0.006796  0.003924  0.000000        0.00000                         
SCALE2      0.000000  0.007848  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003001        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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