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Database: PDB
Entry: 6FM2
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HEADER    STRUCTURAL PROTEIN                      30-JAN-18   6FM2              
TITLE     CARP DOMAIN OF MOUSE CYCLASE-ASSOCIATED PROTEIN 1 (CAP1) BOUND TO ADP-
TITLE    2 ACTIN                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACTIN, ALPHA SKELETAL MUSCLE;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALPHA-ACTIN-1;                                              
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: ADENYLYL CYCLASE-ASSOCIATED PROTEIN 1;                     
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: CAP 1;                                                      
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE   3 ORGANISM_COMMON: RABBIT;                                             
SOURCE   4 ORGANISM_TAXID: 9986;                                                
SOURCE   5 TISSUE: MUSCLE;                                                      
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   8 ORGANISM_COMMON: MOUSE;                                              
SOURCE   9 ORGANISM_TAXID: 10090;                                               
SOURCE  10 GENE: CAP1, CAP;                                                     
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  13 EXPRESSION_SYSTEM_VECTOR_TYPE: PCOOFY18;                             
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PPL974                                    
KEYWDS    COMPLEX, ACTIN CYTOSKELETON, NUCLEOTIDE EXCHANGE, ACTIN TURNOVER,     
KEYWDS   2 STRUCTURAL PROTEIN                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.M.KOTILA,K.KOGAN,P.LAPPALAINEN                                      
REVDAT   2   23-MAY-18 6FM2    1       JRNL                                     
REVDAT   1   16-MAY-18 6FM2    0                                                
JRNL        AUTH   T.KOTILA,K.KOGAN,G.ENKAVI,S.GUO,I.VATTULAINEN,B.L.GOODE,     
JRNL        AUTH 2 P.LAPPALAINEN                                                
JRNL        TITL   STRUCTURAL BASIS OF ACTIN MONOMER RE-CHARGING BY             
JRNL        TITL 2 CYCLASE-ASSOCIATED PROTEIN.                                  
JRNL        REF    NAT COMMUN                    V.   9  1892 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   29760438                                                     
JRNL        DOI    10.1038/S41467-018-04231-7                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 18983                          
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)  : 0.186                          
REMARK   3   R VALUE            (WORKING SET)  : 0.183                          
REMARK   3   FREE R VALUE                      : 0.234                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.800                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 912                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 10                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.95                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.93                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2738                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2430                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2600                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2370                   
REMARK   3   BIN FREE R VALUE                        : 0.3380                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.04                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 138                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4121                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 79                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 94.21                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 128.6                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -21.75110                                            
REMARK   3    B22 (A**2) : -21.75110                                            
REMARK   3    B33 (A**2) : 43.50220                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.380               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 1.420               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.318               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.734               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.310               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.922                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4229   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5737   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1486   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 109    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 618    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4229   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 1      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 576    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4904   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.22                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.86                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.62                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|5 - A|36 }                                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -33.1586    7.5032    9.1121           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.6545 T22:   -0.8977                                    
REMARK   3     T33:   -0.6080 T12:    0.0929                                    
REMARK   3     T13:    0.2390 T23:   -0.1037                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.5144 L22:    1.2182                                    
REMARK   3     L33:    5.0285 L12:   -2.2069                                    
REMARK   3     L13:   -1.4946 L23:    0.7983                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.7719 S12:    0.5988 S13:   -0.7004                     
REMARK   3     S21:   -0.2599 S22:   -0.2422 S23:    0.3771                     
REMARK   3     S31:    0.9768 S32:   -0.5241 S33:    1.0141                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|37 - A|53 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  -44.7676   31.4313   11.2000           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    1.1029 T22:   -0.4753                                    
REMARK   3     T33:   -0.2995 T12:    0.2736                                    
REMARK   3     T13:   -0.5167 T23:   -0.0126                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.3330 L22:    4.5139                                    
REMARK   3     L33:   11.9664 L12:   -5.9214                                    
REMARK   3     L13:   -7.4917 L23:    1.4986                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.9823 S12:    0.6640 S13:   -0.5035                     
REMARK   3     S21:    0.0088 S22:    0.5132 S23:    0.5799                     
REMARK   3     S31:    0.4980 S32:   -1.3641 S33:    0.4691                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|54 - A|68 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  -33.9413   26.8077    4.6654           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.8285 T22:   -0.6512                                    
REMARK   3     T33:   -0.7196 T12:    0.0767                                    
REMARK   3     T13:   -0.1122 T23:    0.0566                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    9.0463 L22:    2.3486                                    
REMARK   3     L33:    8.7953 L12:   -7.4374                                    
REMARK   3     L13:    8.1714 L23:   -3.4585                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0560 S12:    0.6727 S13:    0.3199                     
REMARK   3     S21:   -0.3021 S22:    0.0109 S23:   -1.0843                     
REMARK   3     S31:   -0.3579 S32:    0.3947 S33:    0.0450                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { A|69 - A|107 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -38.4361   13.3749   13.3157           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.4891 T22:   -0.6733                                    
REMARK   3     T33:   -0.5378 T12:    0.1071                                    
REMARK   3     T13:    0.0276 T23:   -0.1031                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6697 L22:    4.8433                                    
REMARK   3     L33:    6.5838 L12:   -1.7719                                    
REMARK   3     L13:   -0.7196 L23:    0.3148                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.7210 S12:    0.4262 S13:   -0.4969                     
REMARK   3     S21:   -0.6482 S22:    0.0835 S23:    0.6341                     
REMARK   3     S31:    0.0890 S32:   -0.8958 S33:    0.6375                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { A|108 - A|175 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -28.7830    7.1223   23.8142           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.3570 T22:   -0.8471                                    
REMARK   3     T33:   -0.5476 T12:    0.3178                                    
REMARK   3     T13:    0.3929 T23:    0.0704                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.1177 L22:    1.8068                                    
REMARK   3     L33:    2.8960 L12:    1.1881                                    
REMARK   3     L13:   -1.1987 L23:    0.2352                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.8389 S12:   -0.1380 S13:   -0.5976                     
REMARK   3     S21:   -0.3454 S22:    0.1386 S23:    0.2106                     
REMARK   3     S31:    1.1608 S32:    0.0124 S33:    0.7003                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { A|176 - A|224 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -12.1428   22.6176    6.3785           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.4000 T22:   -0.7644                                    
REMARK   3     T33:   -0.6483 T12:   -0.0023                                    
REMARK   3     T13:    0.4102 T23:   -0.0089                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.1587 L22:    5.4026                                    
REMARK   3     L33:    6.9385 L12:    0.4700                                    
REMARK   3     L13:   -3.5389 L23:   -0.7246                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0515 S12:   -0.5743 S13:    0.1978                     
REMARK   3     S21:   -0.8624 S22:    0.4035 S23:   -0.4151                     
REMARK   3     S31:   -1.3262 S32:    1.0116 S33:   -0.3520                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { A|225 - A|237 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):    5.4335   18.8513    2.9478           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.4129 T22:    0.3153                                    
REMARK   3     T33:   -0.1599 T12:   -0.2145                                    
REMARK   3     T13:    0.4914 T23:   -0.0142                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9899 L22:    5.6035                                    
REMARK   3     L33:    0.0061 L12:   -0.0364                                    
REMARK   3     L13:  -13.6095 L23:    4.3987                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0850 S12:   -0.0570 S13:    0.2874                     
REMARK   3     S21:   -0.0240 S22:    0.2385 S23:   -0.6300                     
REMARK   3     S31:    0.0178 S32:    0.7924 S33:   -0.1535                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { A|238 - A|334 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   -7.9159   11.9405   16.6488           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1511 T22:   -0.4574                                    
REMARK   3     T33:   -0.5608 T12:    0.4483                                    
REMARK   3     T13:    0.4235 T23:    0.0907                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9194 L22:    1.3032                                    
REMARK   3     L33:    8.2334 L12:    1.6827                                    
REMARK   3     L13:   -2.6705 L23:   -0.1182                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.6454 S12:   -0.5652 S13:   -0.4262                     
REMARK   3     S21:   -0.4591 S22:    0.2710 S23:   -0.6096                     
REMARK   3     S31:    0.2714 S32:    1.8853 S33:    0.3744                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: { A|335 - A|375 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -36.7180    0.2126   21.6919           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.5089 T22:   -1.0482                                    
REMARK   3     T33:   -0.5610 T12:    0.0524                                    
REMARK   3     T13:    0.4269 T23:    0.0047                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.6741 L22:    1.6108                                    
REMARK   3     L33:    4.7306 L12:   -0.0215                                    
REMARK   3     L13:   -0.3528 L23:    0.7319                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.3696 S12:   -0.1184 S13:   -1.0905                     
REMARK   3     S21:   -0.1925 S22:   -0.3209 S23:    0.3776                     
REMARK   3     S31:    1.1191 S32:   -0.8599 S33:    0.6905                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: { B|317 - B|333 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -37.6273   -7.5406   40.6596           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.9751 T22:   -0.8674                                    
REMARK   3     T33:   -0.2147 T12:    0.3632                                    
REMARK   3     T13:    0.7319 T23:    0.3321                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -3.6919 L22:    5.2231                                    
REMARK   3     L33:    3.7214 L12:    3.4576                                    
REMARK   3     L13:   -1.5061 L23:    3.9324                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.4312 S12:   -0.0690 S13:   -0.2489                     
REMARK   3     S21:   -0.4758 S22:   -0.8098 S23:    0.4433                     
REMARK   3     S31:    0.2909 S32:   -1.1105 S33:    0.3786                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: { B|334 - B|374 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -32.1380   -2.3017   45.1177           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.6253 T22:   -0.6933                                    
REMARK   3     T33:   -0.4790 T12:    0.6520                                    
REMARK   3     T13:    0.6395 T23:    0.3625                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.2832 L22:    4.1824                                    
REMARK   3     L33:    4.3794 L12:   -2.4309                                    
REMARK   3     L13:    2.0000 L23:    0.0299                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.6325 S12:   -0.4558 S13:   -0.4965                     
REMARK   3     S21:    0.6316 S22:   -0.0063 S23:    0.1128                     
REMARK   3     S31:    1.8223 S32:   -0.1409 S33:    0.6388                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: { B|375 - B|388 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -28.5724    3.7825   46.0270           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.5485 T22:   -0.2302                                    
REMARK   3     T33:   -0.5007 T12:    0.8660                                    
REMARK   3     T13:    0.4925 T23:    0.3977                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.9636 L22:   -0.6323                                    
REMARK   3     L33:    1.9313 L12:    0.0064                                    
REMARK   3     L13:   -9.1422 L23:    3.2686                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0125 S12:   -0.3108 S13:   -0.3090                     
REMARK   3     S21:   -0.0512 S22:   -0.3783 S23:   -0.1720                     
REMARK   3     S31:    1.1576 S32:   -0.6075 S33:    0.3658                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: { B|389 - B|394 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -37.2069    9.7412   40.8973           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1715 T22:   -0.5388                                    
REMARK   3     T33:   -0.3936 T12:    0.4136                                    
REMARK   3     T13:    0.2909 T23:    0.0223                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -1.8980 L22:   11.2904                                    
REMARK   3     L33:    0.1780 L12:    0.3457                                    
REMARK   3     L13:  -10.1421 L23:   -0.5125                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0998 S12:   -0.3166 S13:    0.4731                     
REMARK   3     S21:    0.1151 S22:   -0.3146 S23:    0.2038                     
REMARK   3     S31:   -0.2385 S32:   -0.5058 S33:    0.2148                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: { B|395 - B|436 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -27.7284   12.1228   46.1279           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0335 T22:   -0.3568                                    
REMARK   3     T33:   -0.6080 T12:    0.7482                                    
REMARK   3     T13:    0.2149 T23:    0.2520                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.3617 L22:    3.6697                                    
REMARK   3     L33:   10.1541 L12:    0.5130                                    
REMARK   3     L13:    0.8667 L23:   -1.0780                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1164 S12:   -0.6010 S13:   -0.4805                     
REMARK   3     S21:   -0.1769 S22:   -0.6027 S23:    0.1574                     
REMARK   3     S31:    1.1288 S32:    0.6787 S33:    0.7192                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: { B|437 - B|455 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -25.5918   18.1870   54.1024           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1388 T22:   -0.1037                                    
REMARK   3     T33:   -0.6381 T12:    0.7737                                    
REMARK   3     T13:    0.1176 T23:    0.2300                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -0.1052 L22:    3.0068                                    
REMARK   3     L33:   10.9278 L12:    1.5501                                    
REMARK   3     L13:    0.8704 L23:    6.7072                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0347 S12:   -0.5095 S13:    0.0006                     
REMARK   3     S21:    0.3481 S22:    0.0741 S23:   -0.5200                     
REMARK   3     S31:   -0.3031 S32:    0.9176 S33:   -0.0394                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: { B|456 - B|473 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -28.0748   33.4571   34.3243           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2917 T22:   -0.6209                                    
REMARK   3     T33:   -0.5303 T12:    0.3868                                    
REMARK   3     T13:   -0.1914 T23:   -0.0561                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   11.7509 L22:    9.8081                                    
REMARK   3     L33:    0.0000 L12:    1.0600                                    
REMARK   3     L13:   10.4869 L23:    7.8223                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2483 S12:   -0.7723 S13:    0.2786                     
REMARK   3     S21:    0.0080 S22:    0.7396 S23:   -0.3237                     
REMARK   3     S31:   -0.6853 S32:    0.4104 S33:   -0.4913                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6FM2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200007320.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-SEP-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0-8.3                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19109                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.340                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.37100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: 1K4Z, 3TPQ                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, 0.2 M LICL, 20% (W/V)    
REMARK 280  PEG8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
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   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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      151.12567            
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      302.25133            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      226.68850            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      377.81417            
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       75.56283            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      151.12567            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      302.25133            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      377.81417            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      226.68850            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       75.56283            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12640 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.500000  0.866025  0.000000      -36.91650            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000       63.94125            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       75.56283            
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     ASP A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     GLY B   474                                                      
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    THR A   6      108.55    -44.04                                   
REMARK 500    MET A  44       42.96    -88.83                                   
REMARK 500    GLN A  49      112.68     13.80                                   
REMARK 500    ASP A  51      145.12    -25.06                                   
REMARK 500    GLU A  72      -39.13    -36.03                                   
REMARK 500    PHE A  90      -74.70    -65.08                                   
REMARK 500    ALA A 181     -146.78   -152.37                                   
REMARK 500    GLN A 263       76.18   -119.65                                   
REMARK 500    THR A 303        9.31    -68.22                                   
REMARK 500    THR A 351       34.80    -90.54                                   
REMARK 500    GLU A 364      -61.57    -93.96                                   
REMARK 500    CYS A 374       62.40   -111.73                                   
REMARK 500    ASN B 335       65.01     71.31                                   
REMARK 500    ASP B 382      -86.15    -86.33                                   
REMARK 500    LYS B 421       -4.27    -54.85                                   
REMARK 500    SER B 423       21.89    -72.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 402   O2B                                                    
REMARK 620 2 HOH A 506   O    71.7                                              
REMARK 620 3 HOH A 528   O    81.3  81.7                                        
REMARK 620 4 HOH A 504   O    76.5  83.8 156.4                                  
REMARK 620 5 HOH A 527   O    87.9 154.3 111.1  76.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 402                 
DBREF  6FM2 A    1   375  UNP    P68135   ACTS_RABIT       3    377             
DBREF  6FM2 B  317   474  UNP    P40124   CAP1_MOUSE     317    474             
SEQRES   1 A  375  ASP GLU ASP GLU THR THR ALA LEU VAL CYS ASP ASN GLY          
SEQRES   2 A  375  SER GLY LEU VAL LYS ALA GLY PHE ALA GLY ASP ASP ALA          
SEQRES   3 A  375  PRO ARG ALA VAL PHE PRO SER ILE VAL GLY ARG PRO ARG          
SEQRES   4 A  375  HIS GLN GLY VAL MET VAL GLY MET GLY GLN LYS ASP SER          
SEQRES   5 A  375  TYR VAL GLY ASP GLU ALA GLN SER LYS ARG GLY ILE LEU          
SEQRES   6 A  375  THR LEU LYS TYR PRO ILE GLU HIC GLY ILE ILE THR ASN          
SEQRES   7 A  375  TRP ASP ASP MET GLU LYS ILE TRP HIS HIS THR PHE TYR          
SEQRES   8 A  375  ASN GLU LEU ARG VAL ALA PRO GLU GLU HIS PRO THR LEU          
SEQRES   9 A  375  LEU THR GLU ALA PRO LEU ASN PRO LYS ALA ASN ARG GLU          
SEQRES  10 A  375  LYS MET THR GLN ILE MET PHE GLU THR PHE ASN VAL PRO          
SEQRES  11 A  375  ALA MET TYR VAL ALA ILE GLN ALA VAL LEU SER LEU TYR          
SEQRES  12 A  375  ALA SER GLY ARG THR THR GLY ILE VAL LEU ASP SER GLY          
SEQRES  13 A  375  ASP GLY VAL THR HIS ASN VAL PRO ILE TYR GLU GLY TYR          
SEQRES  14 A  375  ALA LEU PRO HIS ALA ILE MET ARG LEU ASP LEU ALA GLY          
SEQRES  15 A  375  ARG ASP LEU THR ASP TYR LEU MET LYS ILE LEU THR GLU          
SEQRES  16 A  375  ARG GLY TYR SER PHE VAL THR THR ALA GLU ARG GLU ILE          
SEQRES  17 A  375  VAL ARG ASP ILE LYS GLU LYS LEU CYS TYR VAL ALA LEU          
SEQRES  18 A  375  ASP PHE GLU ASN GLU MET ALA THR ALA ALA SER SER SER          
SEQRES  19 A  375  SER LEU GLU LYS SER TYR GLU LEU PRO ASP GLY GLN VAL          
SEQRES  20 A  375  ILE THR ILE GLY ASN GLU ARG PHE ARG CYS PRO GLU THR          
SEQRES  21 A  375  LEU PHE GLN PRO SER PHE ILE GLY MET GLU SER ALA GLY          
SEQRES  22 A  375  ILE HIS GLU THR THR TYR ASN SER ILE MET LYS CYS ASP          
SEQRES  23 A  375  ILE ASP ILE ARG LYS ASP LEU TYR ALA ASN ASN VAL MET          
SEQRES  24 A  375  SER GLY GLY THR THR MET TYR PRO GLY ILE ALA ASP ARG          
SEQRES  25 A  375  MET GLN LYS GLU ILE THR ALA LEU ALA PRO SER THR MET          
SEQRES  26 A  375  LYS ILE LYS ILE ILE ALA PRO PRO GLU ARG LYS TYR SER          
SEQRES  27 A  375  VAL TRP ILE GLY GLY SER ILE LEU ALA SER LEU SER THR          
SEQRES  28 A  375  PHE GLN GLN MET TRP ILE THR LYS GLN GLU TYR ASP GLU          
SEQRES  29 A  375  ALA GLY PRO SER ILE VAL HIS ARG LYS CYS PHE                  
SEQRES   1 B  158  GLU PRO ALA LEU LEU GLU LEU GLU GLY LYS LYS TRP ARG          
SEQRES   2 B  158  VAL GLU ASN GLN GLU ASN VAL SER ASN LEU VAL ILE ASP          
SEQRES   3 B  158  ASP THR GLU LEU LYS GLN VAL ALA TYR ILE TYR LYS CYS          
SEQRES   4 B  158  VAL ASN THR THR LEU GLN ILE LYS GLY LYS ILE ASN SER          
SEQRES   5 B  158  ILE THR VAL ASP ASN CYS LYS LYS LEU GLY LEU VAL PHE          
SEQRES   6 B  158  ASP ASP VAL VAL GLY ILE VAL GLU ILE ILE ASN SER ARG          
SEQRES   7 B  158  ASP VAL LYS VAL GLN VAL MET GLY LYS VAL PRO THR ILE          
SEQRES   8 B  158  SER ILE ASN LYS THR ASP GLY CYS HIS ALA TYR LEU SER          
SEQRES   9 B  158  LYS ASN SER LEU ASP CYS GLU ILE VAL SER ALA LYS SER          
SEQRES  10 B  158  SER GLU MET ASN VAL LEU ILE PRO THR GLU GLY GLY ASP          
SEQRES  11 B  158  PHE ASN GLU PHE PRO VAL PRO GLU GLN PHE LYS THR LEU          
SEQRES  12 B  158  TRP ASN GLY GLN LYS LEU VAL THR THR VAL THR GLU ILE          
SEQRES  13 B  158  ALA GLY                                                      
MODRES 6FM2 HIC A   73  HIS  MODIFIED RESIDUE                                   
HET    HIC  A  73      11                                                       
HET     MG  A 401       1                                                       
HET    ADP  A 402      27                                                       
HETNAM     HIC 4-METHYL-HISTIDINE                                               
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   1  HIC    C7 H11 N3 O2                                                 
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  ADP    C10 H15 N5 O10 P2                                            
FORMUL   5  HOH   *79(H2 O)                                                     
HELIX    1 AA1 GLY A   55  LYS A   61  1                                   7    
HELIX    2 AA2 ASN A   78  ASN A   92  1                                  15    
HELIX    3 AA3 ALA A   97  HIS A  101  5                                   5    
HELIX    4 AA4 PRO A  112  ASN A  128  1                                  17    
HELIX    5 AA5 GLN A  137  SER A  145  1                                   9    
HELIX    6 AA6 PRO A  172  ILE A  175  5                                   4    
HELIX    7 AA7 ALA A  181  THR A  194  1                                  14    
HELIX    8 AA8 THR A  202  CYS A  217  1                                  16    
HELIX    9 AA9 ASP A  222  SER A  233  1                                  12    
HELIX   10 AB1 ASN A  252  CYS A  257  1                                   6    
HELIX   11 AB2 PRO A  258  LEU A  261  5                                   4    
HELIX   12 AB3 GLN A  263  ILE A  267  5                                   5    
HELIX   13 AB4 GLY A  273  CYS A  285  1                                  13    
HELIX   14 AB5 ILE A  289  ASN A  296  1                                   8    
HELIX   15 AB6 GLY A  301  MET A  305  5                                   5    
HELIX   16 AB7 GLY A  308  ALA A  321  1                                  14    
HELIX   17 AB8 PRO A  332  LYS A  336  5                                   5    
HELIX   18 AB9 TYR A  337  LEU A  349  1                                  13    
HELIX   19 AC1 SER A  350  GLN A  353  5                                   4    
HELIX   20 AC2 LYS A  359  GLY A  366  1                                   8    
HELIX   21 AC3 SER A  368  CYS A  374  1                                   7    
HELIX   22 AC4 ASN B  422  CYS B  426  5                                   5    
SHEET    1 AA1 6 ALA A  29  PRO A  32  0                                        
SHEET    2 AA1 6 LEU A  16  PHE A  21 -1  N  ALA A  19   O  ALA A  29           
SHEET    3 AA1 6 LEU A   8  ASN A  12 -1  N  ASP A  11   O  LYS A  18           
SHEET    4 AA1 6 THR A 103  GLU A 107  1  O  LEU A 104   N  LEU A   8           
SHEET    5 AA1 6 ALA A 131  ILE A 136  1  O  TYR A 133   N  LEU A 105           
SHEET    6 AA1 6 ILE A 357  THR A 358 -1  O  ILE A 357   N  MET A 132           
SHEET    1 AA2 3 TYR A  53  VAL A  54  0                                        
SHEET    2 AA2 3 VAL A  35  PRO A  38 -1  N  GLY A  36   O  TYR A  53           
SHEET    3 AA2 3 LEU A  65  LYS A  68 -1  O  LYS A  68   N  VAL A  35           
SHEET    1 AA3 3 TYR A 169  ALA A 170  0                                        
SHEET    2 AA3 3 THR A 160  TYR A 166 -1  N  TYR A 166   O  TYR A 169           
SHEET    3 AA3 3 MET A 176  LEU A 178 -1  O  LEU A 178   N  THR A 160           
SHEET    1 AA4 5 TYR A 169  ALA A 170  0                                        
SHEET    2 AA4 5 THR A 160  TYR A 166 -1  N  TYR A 166   O  TYR A 169           
SHEET    3 AA4 5 GLY A 150  SER A 155 -1  N  ASP A 154   O  HIS A 161           
SHEET    4 AA4 5 ASN A 297  SER A 300  1  O  VAL A 298   N  LEU A 153           
SHEET    5 AA4 5 ILE A 329  ILE A 330  1  O  ILE A 330   N  ASN A 297           
SHEET    1 AA5 2 LYS A 238  GLU A 241  0                                        
SHEET    2 AA5 2 VAL A 247  ILE A 250 -1  O  ILE A 248   N  TYR A 240           
SHEET    1 AA6 7 LEU B 320  GLU B 324  0                                        
SHEET    2 AA6 7 LYS B 327  GLU B 331 -1  O  GLU B 331   N  LEU B 320           
SHEET    3 AA6 7 VAL B 349  TYR B 353  1  O  TYR B 351   N  TRP B 328           
SHEET    4 AA6 7 ILE B 369  ASP B 372  1  O  ASP B 372   N  ILE B 352           
SHEET    5 AA6 7 ILE B 387  ILE B 391  1  O  ILE B 391   N  VAL B 371           
SHEET    6 AA6 7 THR B 406  ASN B 410  1  O  SER B 408   N  ILE B 390           
SHEET    7 AA6 7 GLU B 427  ALA B 431  1  O  VAL B 429   N  ILE B 409           
SHEET    1 AA7 7 LEU B 339  ILE B 341  0                                        
SHEET    2 AA7 7 THR B 359  ILE B 366  1  O  LYS B 363   N  ILE B 341           
SHEET    3 AA7 7 GLY B 378  VAL B 384  1  O  GLY B 378   N  LEU B 360           
SHEET    4 AA7 7 ARG B 394  VAL B 400  1  O  LYS B 397   N  LEU B 379           
SHEET    5 AA7 7 ASP B 413  TYR B 418  1  O  HIS B 416   N  VAL B 398           
SHEET    6 AA7 7 SER B 434  PRO B 441  1  O  LEU B 439   N  ALA B 417           
SHEET    7 AA7 7 PHE B 447  PRO B 451 -1  O  ASN B 448   N  ILE B 440           
SHEET    1 AA8 2 PHE B 456  TRP B 460  0                                        
SHEET    2 AA8 2 LEU B 465  VAL B 469 -1  O  THR B 468   N  LYS B 457           
LINK         C   GLU A  72                 N   HIC A  73     1555   1555  1.34  
LINK         C   HIC A  73                 N   GLY A  74     1555   1555  1.32  
LINK        MG    MG A 401                 O2B ADP A 402     1555   1555  2.57  
LINK        MG    MG A 401                 O   HOH A 506     1555   1555  1.94  
LINK        MG    MG A 401                 O   HOH A 528     1555   1555  2.17  
LINK        MG    MG A 401                 O   HOH A 504     1555   1555  2.05  
LINK        MG    MG A 401                 O   HOH A 527     1555   1555  2.35  
SITE     1 AC1  5 ADP A 402  HOH A 504  HOH A 506  HOH A 527                    
SITE     2 AC1  5 HOH A 528                                                     
SITE     1 AC2 22 GLY A  13  SER A  14  GLY A  15  LEU A  16                    
SITE     2 AC2 22 LYS A  18  GLY A 156  ASP A 157  GLY A 182                    
SITE     3 AC2 22 ARG A 210  LYS A 213  GLU A 214  GLY A 301                    
SITE     4 AC2 22 GLY A 302  THR A 303  MET A 305  TYR A 306                    
SITE     5 AC2 22 LYS A 336   MG A 401  HOH A 504  HOH A 506                    
SITE     6 AC2 22 HOH A 513  HOH A 527                                          
CRYST1   73.833   73.833  453.377  90.00  90.00 120.00 P 61 2 2     12          
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      0.013544  0.007820  0.000000        0.00000                         
SCALE2      0.000000  0.015639  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002206        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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