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Database: PDB
Entry: 1T44
LinkDB: 1T44
Original site: 1T44 
HEADER    STRUCTURAL PROTEIN                      28-APR-04   1T44              
TITLE     STRUCTURAL BASIS OF ACTIN SEQUESTRATION BY THYMOSIN-B4: IMPLICATIONS  
TITLE    2 FOR ARP2/3 ACTIVATION                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHIMERA OF GELSOLIN DOMAIN 1 AND C-TERMINAL DOMAIN OF      
COMPND   3 THYMOSIN BETA-4;                                                     
COMPND   4 CHAIN: G;                                                            
COMPND   5 FRAGMENT: CHIMERA OF GELSOLIN DOMAIN 1 (RESIDUES 28-152) FROM HUMAN  
COMPND   6 AND C-TERMINAL DOMAIN OF THYMOSIN BETA-4 FROM MOUSE (RESIDUES 153-   
COMPND   7 171);                                                                
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: ACTIN, ALPHA;                                              
COMPND  11 CHAIN: A;                                                            
COMPND  12 SYNONYM: ALPHA-ACTIN 1                                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, MUS MUSCULUS;                     
SOURCE   3 ORGANISM_COMMON: HUMAN, HOUSE MOUSE;                                 
SOURCE   4 ORGANISM_TAXID: 9606, 10090;                                         
SOURCE   5 STRAIN: ,;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE  10 ORGANISM_COMMON: RABBIT;                                             
SOURCE  11 ORGANISM_TAXID: 9986;                                                
SOURCE  12 TISSUE: SKELETAL MUSCLE                                              
KEYWDS    STRUCTURAL PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.IROBI,A.H.AGUDA,M.LARSSON,L.D.BURTNICK,R.C.ROBINSON                 
REVDAT   5   23-AUG-23 1T44    1       REMARK SEQADV LINK                       
REVDAT   4   23-AUG-17 1T44    1       SOURCE                                   
REVDAT   3   24-FEB-09 1T44    1       VERSN                                    
REVDAT   2   21-SEP-04 1T44    1       JRNL                                     
REVDAT   1   07-SEP-04 1T44    0                                                
JRNL        AUTH   E.IROBI,A.H.AGUDA,M.LARSSON,C.GUERIN,H.L.YIN,L.D.BURTNICK,   
JRNL        AUTH 2 L.BLANCHOIN,R.C.ROBINSON                                     
JRNL        TITL   STRUCTURAL BASIS OF ACTIN SEQUESTRATION BY THYMOSIN-BETA4:   
JRNL        TITL 2 IMPLICATIONS FOR WH2 PROTEINS.                               
JRNL        REF    EMBO J.                       V.  23  3599 2004              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   15329672                                                     
JRNL        DOI    10.1038/SJ.EMBOJ.7600372                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 39223                          
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) : 0.147                           
REMARK   3   R VALUE            (WORKING SET) : 0.144                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2079                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2890                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 140                          
REMARK   3   BIN FREE R VALUE                    : 0.1960                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3959                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 427                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.14000                                              
REMARK   3    B22 (A**2) : -0.42000                                             
REMARK   3    B33 (A**2) : -0.66000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.35000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.134         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.085         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.957         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4082 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  3627 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5535 ; 1.434 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8473 ; 0.868 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   499 ; 5.574 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   603 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4512 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   809 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   784 ; 0.203 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4127 ; 0.245 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2242 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   304 ; 0.162 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    15 ; 0.078 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     3 ; 0.068 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    42 ; 0.252 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.106 ; 0.200       
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):  2494 ; 0.969 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4025 ; 1.629 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1588 ; 2.950 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1510 ; 4.545 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     6        A    32                          
REMARK   3    RESIDUE RANGE :   A    71        A   136                          
REMARK   3    RESIDUE RANGE :   A   337        A   375                          
REMARK   3    RESIDUE RANGE :   A   700        A   700                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2700  -8.4420  23.0340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0634 T22:   0.1292                                     
REMARK   3      T33:   0.1194 T12:  -0.0043                                     
REMARK   3      T13:   0.0115 T23:  -0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5605 L22:   1.1180                                     
REMARK   3      L33:   1.1494 L12:   0.1648                                     
REMARK   3      L13:  -0.2891 L23:   0.1821                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0190 S12:  -0.0111 S13:  -0.0442                       
REMARK   3      S21:  -0.0277 S22:   0.0356 S23:  -0.1174                       
REMARK   3      S31:   0.0297 S32:   0.0954 S33:  -0.0166                       
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 :   A    33        A    70                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5280   1.1990   3.7080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0516 T22:   0.1358                                     
REMARK   3      T33:   0.0745 T12:  -0.0136                                     
REMARK   3      T13:   0.0600 T23:  -0.0263                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4305 L22:   8.0116                                     
REMARK   3      L33:   2.9583 L12:   1.4418                                     
REMARK   3      L13:  -0.6866 L23:  -1.3148                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1536 S12:   0.1717 S13:   0.0814                       
REMARK   3      S21:  -0.1824 S22:  -0.0247 S23:  -0.3562                       
REMARK   3      S31:   0.0883 S32:   0.2529 S33:  -0.1289                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   137        A   180                          
REMARK   3    RESIDUE RANGE :   A   274        A   336                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.5150  -0.4510  22.7710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0833 T22:   0.1425                                     
REMARK   3      T33:   0.1016 T12:  -0.0118                                     
REMARK   3      T13:   0.0025 T23:   0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8275 L22:   0.7237                                     
REMARK   3      L33:   1.2282 L12:  -0.0942                                     
REMARK   3      L13:   0.0683 L23:  -0.1121                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0133 S12:   0.0317 S13:   0.0173                       
REMARK   3      S21:  -0.0227 S22:   0.0288 S23:   0.0389                       
REMARK   3      S31:   0.0466 S32:  -0.0964 S33:  -0.0155                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   181        A   273                          
REMARK   3    RESIDUE RANGE :   A   900        A   900                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.7810  13.5290   3.1250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1104 T22:   0.1341                                     
REMARK   3      T33:   0.0662 T12:  -0.0016                                     
REMARK   3      T13:   0.0049 T23:   0.0351                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9088 L22:   1.1919                                     
REMARK   3      L33:   1.0628 L12:  -0.1035                                     
REMARK   3      L13:  -0.3906 L23:  -0.3899                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0332 S12:   0.0584 S13:   0.0367                       
REMARK   3      S21:  -0.1388 S22:  -0.0017 S23:  -0.0331                       
REMARK   3      S31:  -0.0100 S32:  -0.0762 S33:  -0.0315                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G    28        G   152                          
REMARK   3    RESIDUE RANGE :   G   701        G   702                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.8120  -1.7860  47.4380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1344 T22:   0.1038                                     
REMARK   3      T33:   0.0792 T12:   0.0056                                     
REMARK   3      T13:   0.0027 T23:   0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6797 L22:   1.5906                                     
REMARK   3      L33:   0.9111 L12:   0.4544                                     
REMARK   3      L13:  -0.2006 L23:  -0.0675                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0099 S12:  -0.0591 S13:  -0.0098                       
REMARK   3      S21:   0.1737 S22:   0.0096 S23:   0.0193                       
REMARK   3      S31:   0.0130 S32:   0.0458 S33:  -0.0195                       
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   153        G   171                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.5960  12.6590   3.6640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0940 T22:   0.0756                                     
REMARK   3      T33:   0.1570 T12:   0.0203                                     
REMARK   3      T13:   0.0962 T23:   0.0520                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0654 L22:   0.9998                                     
REMARK   3      L33:  32.7026 L12:   0.3132                                     
REMARK   3      L13:  -1.0000 L23:  -4.8265                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1943 S12:   0.1473 S13:   0.3959                       
REMARK   3      S21:   0.0083 S22:  -0.0160 S23:  -0.2443                       
REMARK   3      S31:  -0.0383 S32:   0.3091 S33:  -0.1783                       
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 :   A   901        A  1175                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.0040   1.3470  25.0510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1027 T22:   0.1280                                     
REMARK   3      T33:   0.1012 T12:  -0.0148                                     
REMARK   3      T13:  -0.0028 T23:   0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0662 L22:   0.2688                                     
REMARK   3      L33:   0.3065 L12:  -0.0219                                     
REMARK   3      L13:  -0.1275 L23:  -0.0315                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0024 S12:   0.0201 S13:   0.0092                       
REMARK   3      S21:   0.0119 S22:   0.0066 S23:  -0.0100                       
REMARK   3      S31:   0.0121 S32:  -0.0104 S33:  -0.0090                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1T44 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000022287.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
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                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0052                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39223                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.11400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1P8Z                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM ACETATE, CALCIUM        
REMARK 280  CHLORIDE, PH 6.5, MICROBATCH, TEMPERATURE 293K                      
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       34.66750            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, A                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY G    25                                                      
REMARK 465     SER G    26                                                      
REMARK 465     HIS G    27                                                      
REMARK 465     ARG A    39                                                      
REMARK 465     HIS A    40                                                      
REMARK 465     GLN A    41                                                      
REMARK 465     GLY A    42                                                      
REMARK 465     VAL A    43                                                      
REMARK 465     MET A    44                                                      
REMARK 465     VAL A    45                                                      
REMARK 465     GLY A    46                                                      
REMARK 465     MET A    47                                                      
REMARK 465     GLY A    48                                                      
REMARK 465     GLN A    49                                                      
REMARK 465     LYS A    50                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLN G   171     O    HOH G   749              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  51   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG A 147   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG A 147   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ASP A 222   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A 256   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG A 256   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU G 112       30.42    -86.37                                   
REMARK 500    PHE G 125       27.13   -141.50                                   
REMARK 500    LYS G 157       77.47   -101.83                                   
REMARK 500    ALA A 181     -159.45   -151.97                                   
REMARK 500    ASN A 296       55.73   -141.84                                   
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                              CA G 702  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY G  65   O                                                      
REMARK 620 2 ASP G  66   OD2  79.8                                              
REMARK 620 3 GLU G  97   OE2 121.7  86.2                                        
REMARK 620 4 GLU G  97   OE1  75.4 100.1  51.8                                  
REMARK 620 5 VAL G 145   O   149.9  88.5  84.7 134.4                            
REMARK 620 6 HOH G 704   O    80.1 100.6 158.1 144.4  74.8                      
REMARK 620 7 HOH G 730   O   103.5 170.0  84.1  72.1  92.7  89.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G 701  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G 109   OD1                                                    
REMARK 620 2 ASP G 109   OD2  49.1                                              
REMARK 620 3 GLY G 114   O    70.9 119.2                                        
REMARK 620 4 ALA G 116   O    79.4  83.7  95.8                                  
REMARK 620 5 HOH G 712   O    78.6  72.9  88.2 154.9                            
REMARK 620 6 HOH G 724   O   137.1 140.9  77.1 132.6  72.4                      
REMARK 620 7 HOH G 729   O   138.0 152.3  80.0  74.0 130.9  58.5                
REMARK 620 8 GLU A 167   OE1 131.0  81.9 156.3  97.4  88.1  79.5  84.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 700  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP A 900   O2B                                                    
REMARK 620 2 ATP A 900   O3G  80.1                                              
REMARK 620 3 HOH A 909   O   171.1  91.2                                        
REMARK 620 4 HOH A 911   O    94.0  77.7  82.4                                  
REMARK 620 5 HOH A 915   O    95.6  70.3  82.9 144.4                            
REMARK 620 6 HOH A 918   O    91.2 134.1  96.2 148.1  65.8                      
REMARK 620 7 HOH A 970   O    86.8 152.1 100.3  78.7 136.0  70.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 700                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA G 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA G 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 900                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1P8Z   RELATED DB: PDB                                   
REMARK 900 A HYBRID OF THIS PROTEIN WITH THE C-TERMINAL HALF OF THYMOSIN B4     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 FUSION OF GELSOLIN DOMAIN 1 FROM HUMAN WITH                          
REMARK 999 C-TERMINAL DOMAIN OF THYMOSIN B4 FROM MOUSE                          
REMARK 999 (SEQUENCE:ETQEKNPLPSKETIEQEKQ)                                       
DBREF  1T44 G   28   152  UNP    P06396   GELS_HUMAN      55    179             
DBREF  1T44 G  153   171  UNP    P20065   TYB4_MOUSE      28     46             
DBREF  1T44 A    6   375  UNP    P02568   ACTS_HUMAN       8    377             
SEQADV 1T44 GLY G   25  UNP  P06396              CLONING ARTIFACT               
SEQADV 1T44 SER G   26  UNP  P06396              CLONING ARTIFACT               
SEQADV 1T44 HIS G   27  UNP  P06396              CLONING ARTIFACT               
SEQRES   1 G  147  GLY SER HIS GLU HIS PRO GLU PHE LEU LYS ALA GLY LYS          
SEQRES   2 G  147  GLU PRO GLY LEU GLN ILE TRP ARG VAL GLU LYS PHE ASP          
SEQRES   3 G  147  LEU VAL PRO VAL PRO THR ASN LEU TYR GLY ASP PHE PHE          
SEQRES   4 G  147  THR GLY ASP ALA TYR VAL ILE LEU LYS THR VAL GLN LEU          
SEQRES   5 G  147  ARG ASN GLY ASN LEU GLN TYR ASP LEU HIS TYR TRP LEU          
SEQRES   6 G  147  GLY ASN GLU CYS SER GLN ASP GLU SER GLY ALA ALA ALA          
SEQRES   7 G  147  ILE PHE THR VAL GLN LEU ASP ASP TYR LEU ASN GLY ARG          
SEQRES   8 G  147  ALA VAL GLN HIS ARG GLU VAL GLN GLY PHE GLU SER ALA          
SEQRES   9 G  147  THR PHE LEU GLY TYR PHE LYS SER GLY LEU LYS TYR LYS          
SEQRES  10 G  147  LYS GLY GLY VAL ALA SER GLY PHE LYS HIS VAL GLU THR          
SEQRES  11 G  147  GLN GLU LYS ASN PRO LEU PRO SER LYS GLU THR ILE GLU          
SEQRES  12 G  147  GLN GLU LYS GLN                                              
SEQRES   1 A  370  THR ALA LEU VAL CYS ASP ASN GLY SER GLY LEU VAL LYS          
SEQRES   2 A  370  ALA GLY PHE ALA GLY ASP ASP ALA PRO ARG ALA VAL PHE          
SEQRES   3 A  370  PRO SER ILE VAL GLY ARG PRO ARG HIS GLN GLY VAL MET          
SEQRES   4 A  370  VAL GLY MET GLY GLN LYS ASP SER TYR VAL GLY ASP GLU          
SEQRES   5 A  370  ALA GLN SER LYS ARG GLY ILE LEU THR LEU LYS TYR PRO          
SEQRES   6 A  370  ILE GLU HIS GLY ILE ILE THR ASN TRP ASP ASP MET GLU          
SEQRES   7 A  370  LYS ILE TRP HIS HIS THR PHE TYR ASN GLU LEU ARG VAL          
SEQRES   8 A  370  ALA PRO GLU GLU HIS PRO THR LEU LEU THR GLU ALA PRO          
SEQRES   9 A  370  LEU ASN PRO LYS ALA ASN ARG GLU LYS MET THR GLN ILE          
SEQRES  10 A  370  MET PHE GLU THR PHE ASN VAL PRO ALA MET TYR VAL ALA          
SEQRES  11 A  370  ILE GLN ALA VAL LEU SER LEU TYR ALA SER GLY ARG THR          
SEQRES  12 A  370  THR GLY ILE VAL LEU ASP SER GLY ASP GLY VAL THR HIS          
SEQRES  13 A  370  ASN VAL PRO ILE TYR GLU GLY TYR ALA LEU PRO HIS ALA          
SEQRES  14 A  370  ILE MET ARG LEU ASP LEU ALA GLY ARG ASP LEU THR ASP          
SEQRES  15 A  370  TYR LEU MET LYS ILE LEU THR GLU ARG GLY TYR SER PHE          
SEQRES  16 A  370  VAL THR THR ALA GLU ARG GLU ILE VAL ARG ASP ILE LYS          
SEQRES  17 A  370  GLU LYS LEU CYS TYR VAL ALA LEU ASP PHE GLU ASN GLU          
SEQRES  18 A  370  MET ALA THR ALA ALA SER SER SER SER LEU GLU LYS SER          
SEQRES  19 A  370  TYR GLU LEU PRO ASP GLY GLN VAL ILE THR ILE GLY ASN          
SEQRES  20 A  370  GLU ARG PHE ARG CYS PRO GLU THR LEU PHE GLN PRO SER          
SEQRES  21 A  370  PHE ILE GLY MET GLU SER ALA GLY ILE HIS GLU THR THR          
SEQRES  22 A  370  TYR ASN SER ILE MET LYS CYS ASP ILE ASP ILE ARG LYS          
SEQRES  23 A  370  ASP LEU TYR ALA ASN ASN VAL MET SER GLY GLY THR THR          
SEQRES  24 A  370  MET TYR PRO GLY ILE ALA ASP ARG MET GLN LYS GLU ILE          
SEQRES  25 A  370  THR ALA LEU ALA PRO SER THR MET LYS ILE LYS ILE ILE          
SEQRES  26 A  370  ALA PRO PRO GLU ARG LYS TYR SER VAL TRP ILE GLY GLY          
SEQRES  27 A  370  SER ILE LEU ALA SER LEU SER THR PHE GLN GLN MET TRP          
SEQRES  28 A  370  ILE THR LYS GLN GLU TYR ASP GLU ALA GLY PRO SER ILE          
SEQRES  29 A  370  VAL HIS ARG LYS CYS PHE                                      
HET     CA  G 701       1                                                       
HET     CA  G 702       1                                                       
HET     CA  A 700       1                                                       
HET    ATP  A 900      31                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   3   CA    3(CA 2+)                                                     
FORMUL   6  ATP    C10 H16 N5 O13 P3                                            
FORMUL   7  HOH   *427(H2 O)                                                    
HELIX    1   1 HIS G   29  ALA G   35  1                                   7    
HELIX    2   2 PRO G   55  TYR G   59  5                                   5    
HELIX    3   3 SER G   94  LEU G  112  1                                  19    
HELIX    4   4 SER G  127  GLY G  132  1                                   6    
HELIX    5   5 SER G  162  GLN G  171  1                                  10    
HELIX    6   6 GLY A   55  LYS A   61  1                                   7    
HELIX    7   7 ARG A   62  LEU A   65  5                                   4    
HELIX    8   8 ASN A   78  ASN A   92  1                                  15    
HELIX    9   9 ALA A   97  HIS A  101  5                                   5    
HELIX   10  10 PRO A  112  THR A  126  1                                  15    
HELIX   11  11 GLN A  137  SER A  145  1                                   9    
HELIX   12  12 PRO A  172  ILE A  175  5                                   4    
HELIX   13  13 ALA A  181  ARG A  196  1                                  16    
HELIX   14  14 THR A  202  CYS A  217  1                                  16    
HELIX   15  15 ASP A  222  SER A  233  1                                  12    
HELIX   16  16 ASN A  252  THR A  260  1                                   9    
HELIX   17  17 LEU A  261  PHE A  262  5                                   2    
HELIX   18  18 GLN A  263  GLY A  268  5                                   6    
HELIX   19  19 GLY A  273  LYS A  284  1                                  12    
HELIX   20  20 ASP A  286  ALA A  295  1                                  10    
HELIX   21  21 GLY A  301  MET A  305  5                                   5    
HELIX   22  22 GLY A  308  ALA A  321  1                                  14    
HELIX   23  23 GLU A  334  LYS A  336  5                                   3    
HELIX   24  24 TYR A  337  LEU A  349  1                                  13    
HELIX   25  25 SER A  350  GLN A  353  5                                   4    
HELIX   26  26 LYS A  359  GLY A  366  1                                   8    
HELIX   27  27 ILE A  369  CYS A  374  1                                   6    
SHEET    1   A 5 ASP G  50  PRO G  53  0                                        
SHEET    2   A 5 GLY G  40  GLU G  47 -1  N  ARG G  45   O  VAL G  52           
SHEET    3   A 5 ALA G  67  GLN G  75 -1  O  VAL G  69   N  TRP G  44           
SHEET    4   A 5 LEU G  81  LEU G  89 -1  O  GLN G  82   N  VAL G  74           
SHEET    5   A 5 VAL G 117  VAL G 122  1  O  GLU G 121   N  TYR G  87           
SHEET    1   B 2 ASP G  61  PHE G  63  0                                        
SHEET    2   B 2 LYS G 139  LYS G 141  1  O  LYS G 139   N  PHE G  62           
SHEET    1   C 7 GLN G 155  GLU G 156  0                                        
SHEET    2   C 7 ALA A  29  PRO A  32  1  O  VAL A  30   N  GLN G 155           
SHEET    3   C 7 LEU A  16  PHE A  21 -1  N  VAL A  17   O  PHE A  31           
SHEET    4   C 7 LEU A   8  ASN A  12 -1  N  ASP A  11   O  LYS A  18           
SHEET    5   C 7 THR A 103  GLU A 107  1  O  LEU A 104   N  LEU A   8           
SHEET    6   C 7 ALA A 131  ILE A 136  1  O  TYR A 133   N  LEU A 105           
SHEET    7   C 7 ILE A 357  THR A 358 -1  O  ILE A 357   N  MET A 132           
SHEET    1   D 3 TYR A  53  VAL A  54  0                                        
SHEET    2   D 3 VAL A  35  ARG A  37 -1  N  GLY A  36   O  TYR A  53           
SHEET    3   D 3 THR A  66  LYS A  68 -1  O  THR A  66   N  ARG A  37           
SHEET    1   E 2 ILE A  71  GLU A  72  0                                        
SHEET    2   E 2 ILE A  75  ILE A  76 -1  O  ILE A  75   N  GLU A  72           
SHEET    1   F 3 TYR A 169  ALA A 170  0                                        
SHEET    2   F 3 THR A 160  TYR A 166 -1  N  TYR A 166   O  TYR A 169           
SHEET    3   F 3 MET A 176  LEU A 178 -1  O  LEU A 178   N  THR A 160           
SHEET    1   G 5 TYR A 169  ALA A 170  0                                        
SHEET    2   G 5 THR A 160  TYR A 166 -1  N  TYR A 166   O  TYR A 169           
SHEET    3   G 5 GLY A 150  SER A 155 -1  N  GLY A 150   O  ILE A 165           
SHEET    4   G 5 ASN A 297  SER A 300  1  O  SER A 300   N  LEU A 153           
SHEET    5   G 5 ILE A 329  ILE A 330  1  O  ILE A 330   N  ASN A 297           
SHEET    1   H 2 LYS A 238  GLU A 241  0                                        
SHEET    2   H 2 VAL A 247  ILE A 250 -1  O  ILE A 248   N  TYR A 240           
LINK         O   GLY G  65                CA    CA G 702     1555   1555  2.33  
LINK         OD2 ASP G  66                CA    CA G 702     1555   1555  2.34  
LINK         OE2 GLU G  97                CA    CA G 702     1555   1555  2.46  
LINK         OE1 GLU G  97                CA    CA G 702     1555   1555  2.53  
LINK         OD1 ASP G 109                CA    CA G 701     1555   1555  2.75  
LINK         OD2 ASP G 109                CA    CA G 701     1555   1555  2.36  
LINK         O   GLY G 114                CA    CA G 701     1555   1555  2.43  
LINK         O   ALA G 116                CA    CA G 701     1555   1555  2.31  
LINK         O   VAL G 145                CA    CA G 702     1555   1555  2.34  
LINK        CA    CA G 701                 O   HOH G 712     1555   1555  2.40  
LINK        CA    CA G 701                 O   HOH G 724     1555   1555  2.61  
LINK        CA    CA G 701                 O   HOH G 729     1555   1555  2.42  
LINK        CA    CA G 701                 OE1 GLU A 167     1555   1555  2.31  
LINK        CA    CA G 702                 O   HOH G 704     1555   1555  2.32  
LINK        CA    CA G 702                 O   HOH G 730     1555   1555  2.33  
LINK        CA    CA A 700                 O2B ATP A 900     1555   1555  2.30  
LINK        CA    CA A 700                 O3G ATP A 900     1555   1555  2.41  
LINK        CA    CA A 700                 O   HOH A 909     1555   1555  2.38  
LINK        CA    CA A 700                 O   HOH A 911     1555   1555  2.43  
LINK        CA    CA A 700                 O   HOH A 915     1555   1555  2.75  
LINK        CA    CA A 700                 O   HOH A 918     1555   1555  2.36  
LINK        CA    CA A 700                 O   HOH A 970     1555   1555  2.38  
SITE     1 AC1  6 ATP A 900  HOH A 909  HOH A 911  HOH A 915                    
SITE     2 AC1  6 HOH A 918  HOH A 970                                          
SITE     1 AC2  7 GLU A 167  ASP G 109  GLY G 114  ALA G 116                    
SITE     2 AC2  7 HOH G 712  HOH G 724  HOH G 729                               
SITE     1 AC3  6 GLY G  65  ASP G  66  GLU G  97  VAL G 145                    
SITE     2 AC3  6 HOH G 704  HOH G 730                                          
SITE     1 AC4 26 GLY A  13  SER A  14  GLY A  15  LEU A  16                    
SITE     2 AC4 26 LYS A  18  GLY A 156  ASP A 157  GLY A 158                    
SITE     3 AC4 26 VAL A 159  GLY A 182  ARG A 210  LYS A 213                    
SITE     4 AC4 26 GLU A 214  GLY A 301  GLY A 302  THR A 303                    
SITE     5 AC4 26 MET A 305  TYR A 306   CA A 700  HOH A 904                    
SITE     6 AC4 26 HOH A 911  HOH A 915  HOH A 949  HOH A 992                    
SITE     7 AC4 26 HOH A 999  HOH A1022                                          
CRYST1   56.850   69.335   80.233  90.00  94.93  90.00 P 1 21 1      2          
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      0.017590  0.000000  0.001517        0.00000                         
SCALE2      0.000000  0.014423  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012510        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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