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Entry: 2Y0N
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HEADER    TRANSCRIPTION                           04-DEC-10   2Y0N              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN DOSAGE                       
TITLE    2 COMPENSATION FACTORS MSL1 AND MSL3                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MALE-SPECIFIC LETHAL 3 HOMOLOG;                            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: MRG DOMAIN, RESIDUES 167-289 AND 442-518;                  
COMPND   5 SYNONYM: MALE-SPECIFIC LETHAL-3 HOMOLOG 1, MALE-SPECIFIC LETHAL-3    
COMPND   6  PROTEIN-LIKE 1, MSL3-LIKE 1, MSL3;                                  
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: MALE-SPECIFIC LETHAL 1 HOMOLOG;                            
COMPND  10 CHAIN: E, F, G, H;                                                   
COMPND  11 FRAGMENT: PEHE DOMAIN, RESIDUES 545-597;                             
COMPND  12 SYNONYM: MSL-1, HAMPIN, MALE-SPECIFIC LETHAL 1-LIKE 1, MSL1-LIKE 1,  
COMPND  13  MALE-SPECIFIC LETHAL-1 HOMOLOG 1, MSL1;                             
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHA COLI;                                  
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PRSFDUET-1;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHA COLI;                                  
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VARIANT: STAR;                                     
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_VECTOR: PPROEXHTB                                  
KEYWDS    TRANSCRIPTION, CHROMATIN, X CHROMOSOME, MSL COMPLEX                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.KADLEC,E.HALLACLI,M.LIPP,H.HOLZ,J.SANCHEZ WEATHERBY,S.CUSACK,       
AUTHOR   2 A.AKHTAR                                                             
REVDAT   2   16-FEB-11 2Y0N    1       JRNL                                     
REVDAT   1   12-JAN-11 2Y0N    0                                                
JRNL        AUTH   J.KADLEC,E.HALLACLI,M.LIPP,H.HOLZ,J.SANCHEZ-WEATHERBY,       
JRNL        AUTH 2 S.CUSACK,A.AKHTAR                                            
JRNL        TITL   STRUCTURAL BASIS FOR MOF AND MSL3 RECRUITMENT INTO THE       
JRNL        TITL 2 DOSAGE COMPENSATION COMPLEX BY MSL1.                         
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  18   142 2011              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   21217699                                                     
JRNL        DOI    10.1038/NSMB.1960                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0085                                      
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.13                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.61                          
REMARK   3   NUMBER OF REFLECTIONS             : 23794                          
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) : 0.23337                         
REMARK   3   R VALUE            (WORKING SET) : 0.23229                         
REMARK   3   FREE R VALUE                     : 0.25295                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1260                            
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) : 3.002                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.080                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1693                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.59                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.384                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 71                           
REMARK   3   BIN FREE R VALUE                    : 0.415                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6492                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 100                            
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 100.475                        
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.54                                                 
REMARK   3    B22 (A**2) : -0.13                                                
REMARK   3    B33 (A**2) : -0.64                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -0.24                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.889         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.413         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.398         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 51.587        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6669 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9042 ; 1.118 ; 1.990       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   771 ; 5.021 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   297 ;31.562 ;23.872       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1142 ;17.769 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;19.879 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1014 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4976 ; 0.005 ; 0.022       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  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   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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 : 3                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 5                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    171       A     210      1                      
REMARK   3           1     B    171       B     210      1                      
REMARK   3           1     C    171       C     210      1                      
REMARK   3           1     D    171       D     210      1                      
REMARK   3           2     A    251       A     464      1                      
REMARK   3           2     B    251       B     464      1                      
REMARK   3           2     C    251       C     464      1                      
REMARK   3           2     D    251       D     464      1                      
REMARK   3           3     A    212       A     215      1                      
REMARK   3           3     B    212       B     215      1                      
REMARK   3           3     C    212       C     215      1                      
REMARK   3           3     D    212       D     215      1                      
REMARK   3           4     A    466       A     488      1                      
REMARK   3           4     B    466       B     488      1                      
REMARK   3           4     C    466       C     488      1                      
REMARK   3           4     D    466       D     488      1                      
REMARK   3           5     A    490       A     503      1                      
REMARK   3           5     B    490       B     503      1                      
REMARK   3           5     C    490       C     503      1                      
REMARK   3           5     D    490       D     503      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL    1   A     (A):   1196 ;  0.02 ;  0.05          
REMARK   3   TIGHT POSITIONAL    1   B     (A):   1196 ;  0.02 ;  0.05          
REMARK   3   TIGHT POSITIONAL    1   C     (A):   1196 ;  0.02 ;  0.05          
REMARK   3   TIGHT POSITIONAL    1   D     (A):   1196 ;  0.02 ;  0.05          
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : E F                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     E    569       E     594      1                      
REMARK   3           1     F    569       F     594      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL    2   E     (A):    202 ;  0.02 ;  0.05          
REMARK   3   TIGHT POSITIONAL    2   F     (A):    202 ;  0.02 ;  0.05          
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : G H                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     G    569       G     590      1                      
REMARK   3           1     H    569       H     590      1                      
REMARK   3           2     G    553       G     558      1                      
REMARK   3           2     H    553       H     558      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL    3   G     (A):    222 ;  0.01 ;  0.05          
REMARK   3   TIGHT POSITIONAL    3   H     (A):    222 ;  0.01 ;  0.05          
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   171        A   508                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.5077 -21.1499  13.8155              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2526 T22:   0.0853                                     
REMARK   3      T33:   0.2864 T12:  -0.0329                                     
REMARK   3      T13:  -0.2093 T23:  -0.0621                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.9508 L22:   8.9156                                     
REMARK   3      L33:   6.9648 L12:   1.0877                                     
REMARK   3      L13:   2.1099 L23:   2.2891                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5673 S12:  -0.0156 S13:  -0.8110                       
REMARK   3      S21:  -0.4664 S22:   0.0752 S23:   0.2157                       
REMARK   3      S31:   0.7734 S32:  -0.0439 S33:  -0.6425                       
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   171        B   508                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.4163  19.6086  56.2284              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2317 T22:   0.1029                                     
REMARK   3      T33:   0.2848 T12:   0.0251                                     
REMARK   3      T13:   0.2099 T23:  -0.0594                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.4236 L22:   9.7408                                     
REMARK   3      L33:   6.7464 L12:  -0.8696                                     
REMARK   3      L13:  -1.7041 L23:   2.4641                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5599 S12:   0.0185 S13:   0.6892                       
REMARK   3      S21:   0.4949 S22:   0.0472 S23:   0.2982                       
REMARK   3      S31:  -0.8006 S32:  -0.0565 S33:  -0.6071                       
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   171        C   508                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.3423  12.4575  11.1380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6538 T22:   0.2838                                     
REMARK   3      T33:   0.2899 T12:  -0.2323                                     
REMARK   3      T13:   0.2430 T23:   0.0231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8682 L22:   7.2985                                     
REMARK   3      L33:  10.9508 L12:  -1.3209                                     
REMARK   3      L13:  -0.5753 L23:  -2.5117                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5894 S12:   0.5730 S13:   1.1159                       
REMARK   3      S21:  -0.6289 S22:   0.0027 S23:  -0.0863                       
REMARK   3      S31:  -1.9993 S32:   0.7991 S33:  -0.5920                       
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   171        D   508                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.4250 -13.9681  58.9181              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6332 T22:   0.2839                                     
REMARK   3      T33:   0.2968 T12:   0.2437                                     
REMARK   3      T13:  -0.2375 T23:   0.0250                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8552 L22:   6.6783                                     
REMARK   3      L33:  11.5455 L12:   1.1565                                     
REMARK   3      L13:   0.4456 L23:  -2.3490                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6288 S12:  -0.5306 S13:  -0.9699                       
REMARK   3      S21:   0.6163 S22:  -0.0197 S23:  -0.0831                       
REMARK   3      S31:   2.0183 S32:   0.8551 S33:  -0.6092                       
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   551        E   594                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6629  -9.6438  32.8313              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2926 T22:   0.4477                                     
REMARK   3      T33:   0.2604 T12:  -0.0380                                     
REMARK   3      T13:  -0.0863 T23:   0.0446                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7652 L22:   3.3156                                     
REMARK   3      L33:   6.1217 L12:   1.2127                                     
REMARK   3      L13:   2.0582 L23:   2.8495                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6102 S12:  -0.5963 S13:  -0.6044                       
REMARK   3      S21:   0.7080 S22:  -0.2411 S23:  -0.4032                       
REMARK   3      S31:   0.7471 S32:   0.4581 S33:  -0.3690                       
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 :   G   551        G   594                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6563   3.6858  30.2523              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5526 T22:   0.5510                                     
REMARK   3      T33:   0.1337 T12:  -0.3457                                     
REMARK   3      T13:   0.1130 T23:  -0.2488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1098 L22:   1.1446                                     
REMARK   3      L33:  12.6908 L12:  -1.1301                                     
REMARK   3      L13:  -3.2624 L23:   1.2191                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4902 S12:  -0.3662 S13:   0.1246                       
REMARK   3      S21:   0.2960 S22:  -0.4666 S23:   0.2022                       
REMARK   3      S31:  -1.2899 S32:  -0.2049 S33:  -0.0236                       
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 :   F   551        F   594                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.4734   7.8266  37.8492              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3024 T22:   0.4228                                     
REMARK   3      T33:   0.2515 T12:   0.0889                                     
REMARK   3      T13:   0.0553 T23:   0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7203 L22:   2.4991                                     
REMARK   3      L33:   7.0967 L12:  -0.8827                                     
REMARK   3      L13:  -2.7379 L23:   2.6526                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5499 S12:   0.6089 S13:   0.5755                       
REMARK   3      S21:  -0.6409 S22:  -0.1892 S23:  -0.2495                       
REMARK   3      S31:  -0.7161 S32:   0.2924 S33:  -0.3606                       
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   551        H   594                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6329  -5.2278  39.7978              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5915 T22:   0.5514                                     
REMARK   3      T33:   0.2228 T12:   0.4052                                     
REMARK   3      T13:  -0.2052 T23:  -0.2839                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9573 L22:   1.9788                                     
REMARK   3      L33:  13.5975 L12:   1.7648                                     
REMARK   3      L13:   2.7002 L23:   2.5329                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3297 S12:   0.2118 S13:  -0.1049                       
REMARK   3      S21:  -0.0501 S22:  -0.2862 S23:   0.1299                       
REMARK   3      S31:   1.3032 S32:  -0.2323 S33:  -0.0435                       
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          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 2Y0N COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-DEC-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-46560.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 4)                    
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25057                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.00                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.5                               
REMARK 200  DATA REDUNDANCY                : 2.2                                
REMARK 200  R MERGE                    (I) : 0.03                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.37                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.2                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.52                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.04                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2F5J                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.8                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M ADA (PH 6.5), 0.1M LI2SO4,          
REMARK 280  0.9M MGSO4.                                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       63.63500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19080 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -148.3 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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     MET A   165                                                      
REMARK 465     GLY A   166                                                      
REMARK 465     MET A   167                                                      
REMARK 465     GLU A   168                                                      
REMARK 465     GLU A   169                                                      
REMARK 465     ARG A   170                                                      
REMARK 465     ASN A   226                                                      
REMARK 465     GLU A   227                                                      
REMARK 465     ARG A   228                                                      
REMARK 465     PRO A   229                                                      
REMARK 465     ARG A   230                                                      
REMARK 465     HIS A   231                                                      
REMARK 465     HIS A   232                                                      
REMARK 465     HIS A   233                                                      
REMARK 465     VAL A   234                                                      
REMARK 465     MET A   235                                                      
REMARK 465     PRO A   236                                                      
REMARK 465     HIS A   237                                                      
REMARK 465     ALA A   238                                                      
REMARK 465     ASN A   239                                                      
REMARK 465     MET A   240                                                      
REMARK 465     ASN A   241                                                      
REMARK 465     VAL A   242                                                      
REMARK 465     HIS A   243                                                      
REMARK 465     TYR A   244                                                      
REMARK 465     ILE A   245                                                      
REMARK 465     PRO A   246                                                      
REMARK 465     LYS A   289                                                      
REMARK 465     TYR A   290                                                      
REMARK 465     ASP A   291                                                      
REMARK 465     ILE A   292                                                      
REMARK 465     PRO A   293                                                      
REMARK 465     PRO A   294                                                      
REMARK 465     THR A   295                                                      
REMARK 465     THR A   296                                                      
REMARK 465     CYS A   508                                                      
REMARK 465     GLU A   509                                                      
REMARK 465     ALA A   510                                                      
REMARK 465     HIS A   511                                                      
REMARK 465     TYR A   512                                                      
REMARK 465     SER A   513                                                      
REMARK 465     THR A   514                                                      
REMARK 465     LYS A   515                                                      
REMARK 465     ASN A   516                                                      
REMARK 465     PRO A   517                                                      
REMARK 465     ARG A   518                                                      
REMARK 465     MET B   165                                                      
REMARK 465     GLY B   166                                                      
REMARK 465     MET B   167                                                      
REMARK 465     GLU B   168                                                      
REMARK 465     GLU B   169                                                      
REMARK 465     ARG B   170                                                      
REMARK 465     ASN B   226                                                      
REMARK 465     GLU B   227                                                      
REMARK 465     ARG B   228                                                      
REMARK 465     PRO B   229                                                      
REMARK 465     ARG B   230                                                      
REMARK 465     HIS B   231                                                      
REMARK 465     HIS B   232                                                      
REMARK 465     HIS B   233                                                      
REMARK 465     VAL B   234                                                      
REMARK 465     MET B   235                                                      
REMARK 465     PRO B   236                                                      
REMARK 465     HIS B   237                                                      
REMARK 465     ALA B   238                                                      
REMARK 465     ASN B   239                                                      
REMARK 465     MET B   240                                                      
REMARK 465     ASN B   241                                                      
REMARK 465     VAL B   242                                                      
REMARK 465     HIS B   243                                                      
REMARK 465     TYR B   244                                                      
REMARK 465     ILE B   245                                                      
REMARK 465     PRO B   246                                                      
REMARK 465     LYS B   289                                                      
REMARK 465     TYR B   290                                                      
REMARK 465     ASP B   291                                                      
REMARK 465     ILE B   292                                                      
REMARK 465     PRO B   293                                                      
REMARK 465     PRO B   294                                                      
REMARK 465     THR B   295                                                      
REMARK 465     THR B   296                                                      
REMARK 465     CYS B   508                                                      
REMARK 465     GLU B   509                                                      
REMARK 465     ALA B   510                                                      
REMARK 465     HIS B   511                                                      
REMARK 465     TYR B   512                                                      
REMARK 465     SER B   513                                                      
REMARK 465     THR B   514                                                      
REMARK 465     LYS B   515                                                      
REMARK 465     ASN B   516                                                      
REMARK 465     PRO B   517                                                      
REMARK 465     ARG B   518                                                      
REMARK 465     MET C   165                                                      
REMARK 465     GLY C   166                                                      
REMARK 465     MET C   167                                                      
REMARK 465     GLU C   168                                                      
REMARK 465     GLU C   169                                                      
REMARK 465     ARG C   170                                                      
REMARK 465     SER C   224                                                      
REMARK 465     ALA C   225                                                      
REMARK 465     ASN C   226                                                      
REMARK 465     GLU C   227                                                      
REMARK 465     ARG C   228                                                      
REMARK 465     PRO C   229                                                      
REMARK 465     ARG C   230                                                      
REMARK 465     HIS C   231                                                      
REMARK 465     HIS C   232                                                      
REMARK 465     HIS C   233                                                      
REMARK 465     VAL C   234                                                      
REMARK 465     MET C   235                                                      
REMARK 465     PRO C   236                                                      
REMARK 465     HIS C   237                                                      
REMARK 465     ALA C   238                                                      
REMARK 465     ASN C   239                                                      
REMARK 465     MET C   240                                                      
REMARK 465     ASN C   241                                                      
REMARK 465     VAL C   242                                                      
REMARK 465     HIS C   243                                                      
REMARK 465     TYR C   244                                                      
REMARK 465     ILE C   245                                                      
REMARK 465     LYS C   289                                                      
REMARK 465     TYR C   290                                                      
REMARK 465     ASP C   291                                                      
REMARK 465     ILE C   292                                                      
REMARK 465     PRO C   293                                                      
REMARK 465     PRO C   294                                                      
REMARK 465     THR C   295                                                      
REMARK 465     THR C   296                                                      
REMARK 465     CYS C   508                                                      
REMARK 465     GLU C   509                                                      
REMARK 465     ALA C   510                                                      
REMARK 465     HIS C   511                                                      
REMARK 465     TYR C   512                                                      
REMARK 465     SER C   513                                                      
REMARK 465     THR C   514                                                      
REMARK 465     LYS C   515                                                      
REMARK 465     ASN C   516                                                      
REMARK 465     PRO C   517                                                      
REMARK 465     ARG C   518                                                      
REMARK 465     MET D   165                                                      
REMARK 465     GLY D   166                                                      
REMARK 465     MET D   167                                                      
REMARK 465     GLU D   168                                                      
REMARK 465     GLU D   169                                                      
REMARK 465     ARG D   170                                                      
REMARK 465     SER D   224                                                      
REMARK 465     ALA D   225                                                      
REMARK 465     ASN D   226                                                      
REMARK 465     GLU D   227                                                      
REMARK 465     ARG D   228                                                      
REMARK 465     PRO D   229                                                      
REMARK 465     ARG D   230                                                      
REMARK 465     HIS D   231                                                      
REMARK 465     HIS D   232                                                      
REMARK 465     HIS D   233                                                      
REMARK 465     VAL D   234                                                      
REMARK 465     MET D   235                                                      
REMARK 465     PRO D   236                                                      
REMARK 465     HIS D   237                                                      
REMARK 465     ALA D   238                                                      
REMARK 465     ASN D   239                                                      
REMARK 465     MET D   240                                                      
REMARK 465     ASN D   241                                                      
REMARK 465     VAL D   242                                                      
REMARK 465     HIS D   243                                                      
REMARK 465     TYR D   244                                                      
REMARK 465     ILE D   245                                                      
REMARK 465     LYS D   289                                                      
REMARK 465     TYR D   290                                                      
REMARK 465     ASP D   291                                                      
REMARK 465     ILE D   292                                                      
REMARK 465     PRO D   293                                                      
REMARK 465     PRO D   294                                                      
REMARK 465     THR D   295                                                      
REMARK 465     THR D   296                                                      
REMARK 465     CYS D   508                                                      
REMARK 465     GLU D   509                                                      
REMARK 465     ALA D   510                                                      
REMARK 465     HIS D   511                                                      
REMARK 465     TYR D   512                                                      
REMARK 465     SER D   513                                                      
REMARK 465     THR D   514                                                      
REMARK 465     LYS D   515                                                      
REMARK 465     ASN D   516                                                      
REMARK 465     PRO D   517                                                      
REMARK 465     ARG D   518                                                      
REMARK 465     GLY E   542                                                      
REMARK 465     ALA E   543                                                      
REMARK 465     MET E   544                                                      
REMARK 465     GLY E   545                                                      
REMARK 465     ILE E   546                                                      
REMARK 465     GLN E   547                                                      
REMARK 465     GLU E   548                                                      
REMARK 465     SER E   549                                                      
REMARK 465     GLU E   550                                                      
REMARK 465     GLU E   559                                                      
REMARK 465     PRO E   560                                                      
REMARK 465     ASP E   561                                                      
REMARK 465     ASP E   562                                                      
REMARK 465     VAL E   563                                                      
REMARK 465     ASP E   595                                                      
REMARK 465     GLU E   596                                                      
REMARK 465     ARG E   597                                                      
REMARK 465     GLY F   542                                                      
REMARK 465     ALA F   543                                                      
REMARK 465     MET F   544                                                      
REMARK 465     GLY F   545                                                      
REMARK 465     ILE F   546                                                      
REMARK 465     GLN F   547                                                      
REMARK 465     GLU F   548                                                      
REMARK 465     SER F   549                                                      
REMARK 465     GLU F   550                                                      
REMARK 465     PRO F   551                                                      
REMARK 465     GLU F   552                                                      
REMARK 465     GLU F   559                                                      
REMARK 465     PRO F   560                                                      
REMARK 465     ASP F   561                                                      
REMARK 465     ASP F   562                                                      
REMARK 465     VAL F   563                                                      
REMARK 465     LEU F   594                                                      
REMARK 465     ASP F   595                                                      
REMARK 465     GLU F   596                                                      
REMARK 465     ARG F   597                                                      
REMARK 465     GLY G   542                                                      
REMARK 465     ALA G   543                                                      
REMARK 465     MET G   544                                                      
REMARK 465     GLY G   545                                                      
REMARK 465     ILE G   546                                                      
REMARK 465     GLN G   547                                                      
REMARK 465     GLU G   548                                                      
REMARK 465     SER G   549                                                      
REMARK 465     GLU G   550                                                      
REMARK 465     PRO G   551                                                      
REMARK 465     GLU G   552                                                      
REMARK 465     GLU G   559                                                      
REMARK 465     PRO G   560                                                      
REMARK 465     ASP G   561                                                      
REMARK 465     ASP G   562                                                      
REMARK 465     VAL G   563                                                      
REMARK 465     GLU G   564                                                      
REMARK 465     SER G   565                                                      
REMARK 465     LEU G   566                                                      
REMARK 465     LEU G   567                                                      
REMARK 465     LEU G   591                                                      
REMARK 465     PRO G   592                                                      
REMARK 465     TRP G   593                                                      
REMARK 465     LEU G   594                                                      
REMARK 465     ASP G   595                                                      
REMARK 465     GLU G   596                                                      
REMARK 465     ARG G   597                                                      
REMARK 465     GLY H   542                                                      
REMARK 465     ALA H   543                                                      
REMARK 465     MET H   544                                                      
REMARK 465     GLY H   545                                                      
REMARK 465     ILE H   546                                                      
REMARK 465     GLN H   547                                                      
REMARK 465     GLU H   548                                                      
REMARK 465     SER H   549                                                      
REMARK 465     GLU H   550                                                      
REMARK 465     PRO H   551                                                      
REMARK 465     GLU H   552                                                      
REMARK 465     GLU H   559                                                      
REMARK 465     PRO H   560                                                      
REMARK 465     ASP H   561                                                      
REMARK 465     ASP H   562                                                      
REMARK 465     VAL H   563                                                      
REMARK 465     GLU H   564                                                      
REMARK 465     SER H   565                                                      
REMARK 465     LEU H   566                                                      
REMARK 465     LEU H   567                                                      
REMARK 465     LEU H   591                                                      
REMARK 465     PRO H   592                                                      
REMARK 465     TRP H   593                                                      
REMARK 465     LEU H   594                                                      
REMARK 465     ASP H   595                                                      
REMARK 465     GLU H   596                                                      
REMARK 465     ARG H   597                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    VAL C 505   CB    VAL C 505   CG1    -0.163                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 193      -59.43   -128.44                                   
REMARK 500    ALA A 506       28.70   -145.86                                   
REMARK 500    ARG B 193      -59.23   -128.62                                   
REMARK 500    ALA B 221      -64.61    -93.82                                   
REMARK 500    SER B 224      136.56    169.63                                   
REMARK 500    ARG C 193      -58.91   -129.06                                   
REMARK 500    ASP C 442       39.18     70.23                                   
REMARK 500    ALA C 506       69.16   -153.34                                   
REMARK 500    ARG D 193      -58.75   -128.84                                   
REMARK 500    ALA D 247      -85.81   -129.65                                   
REMARK 500    ALA D 506      -63.51   -101.83                                   
REMARK 500    GLU E 552     -167.20    -68.89                                   
REMARK 500    PRO E 586      143.53    -33.85                                   
REMARK 500    PRO E 592        7.35    -58.78                                   
REMARK 500    PRO F 586      144.56    -34.29                                   
REMARK 500    PRO F 592        5.31    -59.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUES 290-441 IN UNP Q8N5Y2  WERE SUBSTITUTED WITH AN             
REMARK 999 INSERTION SEQUENCE YDIPPTTEF. YDIPPTT WERE ASSIGNED RESIDUE          
REMARK 999 NUMBERS 290-296; EF WAS ASSIGNED RESIDUE NUMBERS 440 AND 441.        
DBREF  2Y0N A  167   289  UNP    Q8N5Y2   MS3L1_HUMAN    167    289             
DBREF  2Y0N A  442   518  UNP    Q8N5Y2   MS3L1_HUMAN    442    518             
DBREF  2Y0N B  167   289  UNP    Q8N5Y2   MS3L1_HUMAN    167    289             
DBREF  2Y0N B  442   518  UNP    Q8N5Y2   MS3L1_HUMAN    442    518             
DBREF  2Y0N C  167   289  UNP    Q8N5Y2   MS3L1_HUMAN    167    289             
DBREF  2Y0N C  442   518  UNP    Q8N5Y2   MS3L1_HUMAN    442    518             
DBREF  2Y0N D  167   289  UNP    Q8N5Y2   MS3L1_HUMAN    167    289             
DBREF  2Y0N D  442   518  UNP    Q8N5Y2   MS3L1_HUMAN    442    518             
DBREF  2Y0N E  545   597  UNP    Q6PDM1   MSL1_MOUSE     545    597             
DBREF  2Y0N F  545   597  UNP    Q6PDM1   MSL1_MOUSE     545    597             
DBREF  2Y0N G  545   597  UNP    Q6PDM1   MSL1_MOUSE     545    597             
DBREF  2Y0N H  545   597  UNP    Q6PDM1   MSL1_MOUSE     545    597             
SEQADV 2Y0N MET A  165  UNP  Q8N5Y2              EXPRESSION TAG                 
SEQADV 2Y0N GLY A  166  UNP  Q8N5Y2              EXPRESSION TAG                 
SEQADV 2Y0N TYR A  290  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N ASP A  291  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N ILE A  292  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N PRO A  293  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N PRO A  294  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N THR A  295  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N THR A  296  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N GLU A  440  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N PHE A  441  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N MET B  165  UNP  Q8N5Y2              EXPRESSION TAG                 
SEQADV 2Y0N GLY B  166  UNP  Q8N5Y2              EXPRESSION TAG                 
SEQADV 2Y0N TYR B  290  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N ASP B  291  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N ILE B  292  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N PRO B  293  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N PRO B  294  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N THR B  295  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N THR B  296  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N GLU B  440  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N PHE B  441  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N MET C  165  UNP  Q8N5Y2              EXPRESSION TAG                 
SEQADV 2Y0N GLY C  166  UNP  Q8N5Y2              EXPRESSION TAG                 
SEQADV 2Y0N TYR C  290  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N ASP C  291  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N ILE C  292  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N PRO C  293  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N PRO C  294  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N THR C  295  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N THR C  296  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N GLU C  440  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N PHE C  441  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N MET D  165  UNP  Q8N5Y2              EXPRESSION TAG                 
SEQADV 2Y0N GLY D  166  UNP  Q8N5Y2              EXPRESSION TAG                 
SEQADV 2Y0N TYR D  290  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N ASP D  291  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N ILE D  292  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N PRO D  293  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N PRO D  294  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N THR D  295  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N THR D  296  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N GLU D  440  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N PHE D  441  UNP  Q8N5Y2              INSERTION                      
SEQADV 2Y0N GLY E  542  UNP  Q6PDM1              EXPRESSION TAG                 
SEQADV 2Y0N ALA E  543  UNP  Q6PDM1              EXPRESSION TAG                 
SEQADV 2Y0N MET E  544  UNP  Q6PDM1              EXPRESSION TAG                 
SEQADV 2Y0N GLY F  542  UNP  Q6PDM1              EXPRESSION TAG                 
SEQADV 2Y0N ALA F  543  UNP  Q6PDM1              EXPRESSION TAG                 
SEQADV 2Y0N MET F  544  UNP  Q6PDM1              EXPRESSION TAG                 
SEQADV 2Y0N GLY G  542  UNP  Q6PDM1              EXPRESSION TAG                 
SEQADV 2Y0N ALA G  543  UNP  Q6PDM1              EXPRESSION TAG                 
SEQADV 2Y0N MET G  544  UNP  Q6PDM1              EXPRESSION TAG                 
SEQADV 2Y0N GLY H  542  UNP  Q6PDM1              EXPRESSION TAG                 
SEQADV 2Y0N ALA H  543  UNP  Q6PDM1              EXPRESSION TAG                 
SEQADV 2Y0N MET H  544  UNP  Q6PDM1              EXPRESSION TAG                 
SEQRES   1 A  211  MET GLY MET GLU GLU ARG THR ILE THR ILE GLU ILE PRO          
SEQRES   2 A  211  GLU VAL LEU LYS LYS GLN LEU GLU ASP ASP CYS TYR TYR          
SEQRES   3 A  211  ILE ASN ARG ARG LYS ARG LEU VAL LYS LEU PRO CYS GLN          
SEQRES   4 A  211  THR ASN ILE ILE THR ILE LEU GLU SER TYR VAL LYS HIS          
SEQRES   5 A  211  PHE ALA ILE ASN ALA ALA PHE SER ALA ASN GLU ARG PRO          
SEQRES   6 A  211  ARG HIS HIS HIS VAL MET PRO HIS ALA ASN MET ASN VAL          
SEQRES   7 A  211  HIS TYR ILE PRO ALA GLU LYS ASN VAL ASP LEU CYS LYS          
SEQRES   8 A  211  GLU MET VAL ASP GLY LEU ARG ILE THR PHE ASP TYR THR          
SEQRES   9 A  211  LEU PRO LEU VAL LEU LEU TYR PRO TYR GLU GLN ALA GLN          
SEQRES  10 A  211  TYR LYS LYS VAL THR SER SER LYS TYR ASP ILE PRO PRO          
SEQRES  11 A  211  THR THR GLU PHE ASP GLN PRO PRO PRO PRO SER TYR ILE          
SEQRES  12 A  211  TYR GLY ALA GLN HIS LEU LEU ARG LEU PHE VAL LYS LEU          
SEQRES  13 A  211  PRO GLU ILE LEU GLY LYS MET SER PHE SER GLU LYS ASN          
SEQRES  14 A  211  LEU LYS ALA LEU LEU LYS HIS PHE ASP LEU PHE LEU ARG          
SEQRES  15 A  211  PHE LEU ALA GLU TYR HIS ASP ASP PHE PHE PRO GLU SER          
SEQRES  16 A  211  ALA TYR VAL ALA ALA CYS GLU ALA HIS TYR SER THR LYS          
SEQRES  17 A  211  ASN PRO ARG                                                  
SEQRES   1 B  211  MET GLY MET GLU GLU ARG THR ILE THR ILE GLU ILE PRO          
SEQRES   2 B  211  GLU VAL LEU LYS LYS GLN LEU GLU ASP ASP CYS TYR TYR          
SEQRES   3 B  211  ILE ASN ARG ARG LYS ARG LEU VAL LYS LEU PRO CYS GLN          
SEQRES   4 B  211  THR ASN ILE ILE THR ILE LEU GLU SER TYR VAL LYS HIS          
SEQRES   5 B  211  PHE ALA ILE ASN ALA ALA PHE SER ALA ASN GLU ARG PRO          
SEQRES   6 B  211  ARG HIS HIS HIS VAL MET PRO HIS ALA ASN MET ASN VAL          
SEQRES   7 B  211  HIS TYR ILE PRO ALA GLU LYS ASN VAL ASP LEU CYS LYS          
SEQRES   8 B  211  GLU MET VAL ASP GLY LEU ARG ILE THR PHE ASP TYR THR          
SEQRES   9 B  211  LEU PRO LEU VAL LEU LEU TYR PRO TYR GLU GLN ALA GLN          
SEQRES  10 B  211  TYR LYS LYS VAL THR SER SER LYS TYR ASP ILE PRO PRO          
SEQRES  11 B  211  THR THR GLU PHE ASP GLN PRO PRO PRO PRO SER TYR ILE          
SEQRES  12 B  211  TYR GLY ALA GLN HIS LEU LEU ARG LEU PHE VAL LYS LEU          
SEQRES  13 B  211  PRO GLU ILE LEU GLY LYS MET SER PHE SER GLU LYS ASN          
SEQRES  14 B  211  LEU LYS ALA LEU LEU LYS HIS PHE ASP LEU PHE LEU ARG          
SEQRES  15 B  211  PHE LEU ALA GLU TYR HIS ASP ASP PHE PHE PRO GLU SER          
SEQRES  16 B  211  ALA TYR VAL ALA ALA CYS GLU ALA HIS TYR SER THR LYS          
SEQRES  17 B  211  ASN PRO ARG                                                  
SEQRES   1 C  211  MET GLY MET GLU GLU ARG THR ILE THR ILE GLU ILE PRO          
SEQRES   2 C  211  GLU VAL LEU LYS LYS GLN LEU GLU ASP ASP CYS TYR TYR          
SEQRES   3 C  211  ILE ASN ARG ARG LYS ARG LEU VAL LYS LEU PRO CYS GLN          
SEQRES   4 C  211  THR ASN ILE ILE THR ILE LEU GLU SER TYR VAL LYS HIS          
SEQRES   5 C  211  PHE ALA ILE ASN ALA ALA PHE SER ALA ASN GLU ARG PRO          
SEQRES   6 C  211  ARG HIS HIS HIS VAL MET PRO HIS ALA ASN MET ASN VAL          
SEQRES   7 C  211  HIS TYR ILE PRO ALA GLU LYS ASN VAL ASP LEU CYS LYS          
SEQRES   8 C  211  GLU MET VAL ASP GLY LEU ARG ILE THR PHE ASP TYR THR          
SEQRES   9 C  211  LEU PRO LEU VAL LEU LEU TYR PRO TYR GLU GLN ALA GLN          
SEQRES  10 C  211  TYR LYS LYS VAL THR SER SER LYS TYR ASP ILE PRO PRO          
SEQRES  11 C  211  THR THR GLU PHE ASP GLN PRO PRO PRO PRO SER TYR ILE          
SEQRES  12 C  211  TYR GLY ALA GLN HIS LEU LEU ARG LEU PHE VAL LYS LEU          
SEQRES  13 C  211  PRO GLU ILE LEU GLY LYS MET SER PHE SER GLU LYS ASN          
SEQRES  14 C  211  LEU LYS ALA LEU LEU LYS HIS PHE ASP LEU PHE LEU ARG          
SEQRES  15 C  211  PHE LEU ALA GLU TYR HIS ASP ASP PHE PHE PRO GLU SER          
SEQRES  16 C  211  ALA TYR VAL ALA ALA CYS GLU ALA HIS TYR SER THR LYS          
SEQRES  17 C  211  ASN PRO ARG                                                  
SEQRES   1 D  211  MET GLY MET GLU GLU ARG THR ILE THR ILE GLU ILE PRO          
SEQRES   2 D  211  GLU VAL LEU LYS LYS GLN LEU GLU ASP ASP CYS TYR TYR          
SEQRES   3 D  211  ILE ASN ARG ARG LYS ARG LEU VAL LYS LEU PRO CYS GLN          
SEQRES   4 D  211  THR ASN ILE ILE THR ILE LEU GLU SER TYR VAL LYS HIS          
SEQRES   5 D  211  PHE ALA ILE ASN ALA ALA PHE SER ALA ASN GLU ARG PRO          
SEQRES   6 D  211  ARG HIS HIS HIS VAL MET PRO HIS ALA ASN MET ASN VAL          
SEQRES   7 D  211  HIS TYR ILE PRO ALA GLU LYS ASN VAL ASP LEU CYS LYS          
SEQRES   8 D  211  GLU MET VAL ASP GLY LEU ARG ILE THR PHE ASP TYR THR          
SEQRES   9 D  211  LEU PRO LEU VAL LEU LEU TYR PRO TYR GLU GLN ALA GLN          
SEQRES  10 D  211  TYR LYS LYS VAL THR SER SER LYS TYR ASP ILE PRO PRO          
SEQRES  11 D  211  THR THR GLU PHE ASP GLN PRO PRO PRO PRO SER TYR ILE          
SEQRES  12 D  211  TYR GLY ALA GLN HIS LEU LEU ARG LEU PHE VAL LYS LEU          
SEQRES  13 D  211  PRO GLU ILE LEU GLY LYS MET SER PHE SER GLU LYS ASN          
SEQRES  14 D  211  LEU LYS ALA LEU LEU LYS HIS PHE ASP LEU PHE LEU ARG          
SEQRES  15 D  211  PHE LEU ALA GLU TYR HIS ASP ASP PHE PHE PRO GLU SER          
SEQRES  16 D  211  ALA TYR VAL ALA ALA CYS GLU ALA HIS TYR SER THR LYS          
SEQRES  17 D  211  ASN PRO ARG                                                  
SEQRES   1 E   56  GLY ALA MET GLY ILE GLN GLU SER GLU PRO GLU VAL THR          
SEQRES   2 E   56  SER PHE PHE PRO GLU PRO ASP ASP VAL GLU SER LEU LEU          
SEQRES   3 E   56  ILE THR PRO PHE LEU PRO VAL VAL ALA PHE GLY ARG PRO          
SEQRES   4 E   56  LEU PRO LYS LEU ALA PRO GLN ASN PHE GLU LEU PRO TRP          
SEQRES   5 E   56  LEU ASP GLU ARG                                              
SEQRES   1 F   56  GLY ALA MET GLY ILE GLN GLU SER GLU PRO GLU VAL THR          
SEQRES   2 F   56  SER PHE PHE PRO GLU PRO ASP ASP VAL GLU SER LEU LEU          
SEQRES   3 F   56  ILE THR PRO PHE LEU PRO VAL VAL ALA PHE GLY ARG PRO          
SEQRES   4 F   56  LEU PRO LYS LEU ALA PRO GLN ASN PHE GLU LEU PRO TRP          
SEQRES   5 F   56  LEU ASP GLU ARG                                              
SEQRES   1 G   56  GLY ALA MET GLY ILE GLN GLU SER GLU PRO GLU VAL THR          
SEQRES   2 G   56  SER PHE PHE PRO GLU PRO ASP ASP VAL GLU SER LEU LEU          
SEQRES   3 G   56  ILE THR PRO PHE LEU PRO VAL VAL ALA PHE GLY ARG PRO          
SEQRES   4 G   56  LEU PRO LYS LEU ALA PRO GLN ASN PHE GLU LEU PRO TRP          
SEQRES   5 G   56  LEU ASP GLU ARG                                              
SEQRES   1 H   56  GLY ALA MET GLY ILE GLN GLU SER GLU PRO GLU VAL THR          
SEQRES   2 H   56  SER PHE PHE PRO GLU PRO ASP ASP VAL GLU SER LEU LEU          
SEQRES   3 H   56  ILE THR PRO PHE LEU PRO VAL VAL ALA PHE GLY ARG PRO          
SEQRES   4 H   56  LEU PRO LYS LEU ALA PRO GLN ASN PHE GLU LEU PRO TRP          
SEQRES   5 H   56  LEU ASP GLU ARG                                              
HELIX    1   1 PRO A  177  ARG A  193  1                                  17    
HELIX    2   2 ASN A  205  PHE A  223  1                                  19    
HELIX    3   3 ASN A  250  LEU A  273  1                                  24    
HELIX    4   4 TYR A  275  TYR A  277  5                                   3    
HELIX    5   5 GLU A  278  SER A  288  1                                  11    
HELIX    6   6 PRO A  446  ILE A  450  5                                   5    
HELIX    7   7 GLY A  452  MET A  470  1                                  19    
HELIX    8   8 SER A  473  TYR A  494  1                                  22    
HELIX    9   9 TYR A  494  PHE A  499  1                                   6    
HELIX   10  10 PRO A  500  SER A  502  5                                   3    
HELIX   11  11 PRO B  177  ARG B  193  1                                  17    
HELIX   12  12 ASN B  205  PHE B  223  1                                  19    
HELIX   13  13 ASN B  250  LEU B  273  1                                  24    
HELIX   14  14 TYR B  275  TYR B  277  5                                   3    
HELIX   15  15 GLU B  278  SER B  288  1                                  11    
HELIX   16  16 PRO B  446  ILE B  450  5                                   5    
HELIX   17  17 GLY B  452  MET B  470  1                                  19    
HELIX   18  18 SER B  473  TYR B  494  1                                  22    
HELIX   19  19 TYR B  494  PHE B  499  1                                   6    
HELIX   20  20 PRO B  500  SER B  502  5                                   3    
HELIX   21  21 PRO C  177  ARG C  193  1                                  17    
HELIX   22  22 ASN C  205  PHE C  223  1                                  19    
HELIX   23  23 ASN C  250  LEU C  273  1                                  24    
HELIX   24  24 TYR C  275  TYR C  277  5                                   3    
HELIX   25  25 GLU C  278  SER C  288  1                                  11    
HELIX   26  26 PRO C  446  ILE C  450  5                                   5    
HELIX   27  27 GLY C  452  MET C  470  1                                  19    
HELIX   28  28 SER C  473  TYR C  494  1                                  22    
HELIX   29  29 TYR C  494  PHE C  499  1                                   6    
HELIX   30  30 PRO C  500  SER C  502  5                                   3    
HELIX   31  31 PRO D  177  ARG D  193  1                                  17    
HELIX   32  32 ASN D  205  PHE D  223  1                                  19    
HELIX   33  33 ASN D  250  LEU D  273  1                                  24    
HELIX   34  34 TYR D  275  TYR D  277  5                                   3    
HELIX   35  35 GLU D  278  SER D  288  1                                  11    
HELIX   36  36 PRO D  446  ILE D  450  5                                   5    
HELIX   37  37 GLY D  452  MET D  470  1                                  19    
HELIX   38  38 SER D  473  TYR D  494  1                                  22    
HELIX   39  39 TYR D  494  PHE D  499  1                                   6    
HELIX   40  40 PRO D  500  SER D  502  5                                   3    
SHEET    1  AA 2 LEU A 197  VAL A 198  0                                        
SHEET    2  AA 2 TYR A 504  VAL A 505 -1  O  VAL A 505   N  LEU A 197           
SHEET    1  BA 2 LEU B 197  VAL B 198  0                                        
SHEET    2  BA 2 TYR B 504  VAL B 505 -1  O  VAL B 505   N  LEU B 197           
SHEET    1  CA 2 LEU C 197  VAL C 198  0                                        
SHEET    2  CA 2 TYR C 504  VAL C 505 -1  O  VAL C 505   N  LEU C 197           
SHEET    1  DA 2 LEU D 197  VAL D 198  0                                        
SHEET    2  DA 2 TYR D 504  VAL D 505 -1  O  VAL D 505   N  LEU D 197           
SHEET    1  EA 2 VAL E 575  ALA E 576  0                                        
SHEET    2  EA 2 ARG E 579  PRO E 580 -1  O  ARG E 579   N  ALA E 576           
SHEET    1  FA 2 VAL F 575  ALA F 576  0                                        
SHEET    2  FA 2 ARG F 579  PRO F 580 -1  O  ARG F 579   N  ALA F 576           
SHEET    1  GA 2 VAL G 575  ALA G 576  0                                        
SHEET    2  GA 2 ARG G 579  PRO G 580 -1  O  ARG G 579   N  ALA G 576           
SHEET    1  HA 2 VAL H 575  ALA H 576  0                                        
SHEET    2  HA 2 ARG H 579  PRO H 580 -1  O  ARG H 579   N  ALA H 576           
CISPEP   1 LEU A  200    PRO A  201          0        -4.47                     
CISPEP   2 LEU B  200    PRO B  201          0        -4.29                     
CISPEP   3 LEU C  200    PRO C  201          0        -3.80                     
CISPEP   4 LEU D  200    PRO D  201          0        -3.72                     
CRYST1   76.230  127.270   79.680  90.00 118.46  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013118  0.000000  0.007111        0.00000                         
SCALE2      0.000000  0.007857  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014275        0.00000                         
MTRIX1   1  1.000000 -0.000190 -0.000180        0.08857    1                    
MTRIX2   1 -0.000190 -1.000000 -0.000060       -1.53947    1                    
MTRIX3   1 -0.000180  0.000060 -1.000000       70.05445    1                    
MTRIX1   2 -0.985880  0.004870  0.167410       -0.12480    1                    
MTRIX2   2 -0.006430  0.997740 -0.066880        7.97456    1                    
MTRIX3   2 -0.167360 -0.067010 -0.983620       70.28783    1                    
MTRIX1   3 -0.985370  0.004630  0.170340       -0.26853    1                    
MTRIX2   3  0.006450 -0.997900  0.064420       -9.47295    1                    
MTRIX3   3  0.170280  0.064570  0.983280       -0.25216    1                    
MTRIX1   4  1.000000  0.001720 -0.001580        0.06299    1                    
MTRIX2   4  0.001720 -1.000000  0.001610       -1.59342    1                    
MTRIX3   4 -0.001580 -0.001610 -1.000000       70.06078    1                    
MTRIX1   5  1.000000 -0.000470  0.001520        0.00417    1                    
MTRIX2   5 -0.000470 -1.000000 -0.001580       -1.50081    1                    
MTRIX3   5  0.001520  0.001580 -1.000000       70.04503    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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