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Database: PDB
Entry: 3LW8
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HEADER    SIGNALING PROTEIN/RHOA-BINDING PROTEIN  23-FEB-10   3LW8              
TITLE     SHIGELLA IPGB2 IN COMPLEX WITH HUMAN RHOA, GDP AND MG2+ (COMPLEX A)   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSFORMING PROTEIN RHOA;                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 2-181;                                            
COMPND   5 SYNONYM: H12;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: IPGB2;                                                     
COMPND   9 CHAIN: E, F, G, H;                                                   
COMPND  10 SYNONYM: IPGB2, PROBABLY SECRETED BY THE MXI-SPA SECRETION MACHINERY;
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RHOA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: TUNER (DE3);                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-28C;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: SHIGELLA FLEXNERI;                              
SOURCE  13 ORGANISM_TAXID: 623;                                                 
SOURCE  14 GENE: IPGB2;                                                         
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: TUNER (DE3);                               
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PET-M 41                                  
KEYWDS    IPGB2, RHOA, GTPASE, GEF, GEF-GTPASE-COMPLEX, WXXXE, TTSS EFFECTOR    
KEYWDS   2 PROTEIN, BACTERIAL GEF, CYTOSKELETON DYNAMICS, SIGNALING PROTEIN-    
KEYWDS   3 RHOA-BINDING PROTEIN COMPLEX                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.U.KLINK,S.BARDEN,T.V.HEIDLER,C.BORCHERS,M.LADWEIN,T.E.B.STRADAL,    
AUTHOR   2 K.ROTTNER,D.W.HEINZ                                                  
REVDAT   3   13-JUL-11 3LW8    1       VERSN                                    
REVDAT   2   02-JUN-10 3LW8    1       JRNL                                     
REVDAT   1   31-MAR-10 3LW8    0                                                
JRNL        AUTH   B.U.KLINK,S.BARDEN,T.V.HEIDLER,C.BORCHERS,M.LADWEIN,         
JRNL        AUTH 2 T.E.B.STRADAL,K.ROTTNER,D.W.HEINZ                            
JRNL        TITL   STRUCTURE OF SHIGELLA IPGB2 IN COMPLEX WITH HUMAN RHOA:      
JRNL        TITL 2 IMPLICATIONS FOR THE MECHANISM OF BACTERIAL GEF-MIMICRY      
JRNL        REF    J.BIOL.CHEM.                  V. 285 17197 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20363740                                                     
JRNL        DOI    10.1074/JBC.M110.107953                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 133481                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6674                            
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) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9262                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.74                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 487                          
REMARK   3   BIN FREE R VALUE                    : 0.3150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11613                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 116                                     
REMARK   3   SOLVENT ATOMS            : 1766                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 26.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.45000                                             
REMARK   3    B22 (A**2) : 1.47000                                              
REMARK   3    B33 (A**2) : -1.08000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.29000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.146         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.103         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.155         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12362 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16731 ; 1.423 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1562 ; 5.217 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   586 ;34.973 ;24.778       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2397 ;15.150 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    85 ;17.979 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1846 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9237 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7479 ; 0.777 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12205 ; 1.361 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4883 ; 2.153 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4480 ; 3.450 ; 4.500       
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  : 12                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -3        A   181                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.4300  17.5740  55.8340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0569 T22:   0.0426                                     
REMARK   3      T33:   0.0942 T12:  -0.0214                                     
REMARK   3      T13:  -0.0183 T23:   0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9110 L22:   0.9612                                     
REMARK   3      L33:   1.1603 L12:  -0.4133                                     
REMARK   3      L13:  -0.2653 L23:   0.2582                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0296 S12:   0.0022 S13:  -0.1513                       
REMARK   3      S21:  -0.0450 S22:  -0.0048 S23:   0.0997                       
REMARK   3      S31:   0.1370 S32:  -0.1462 S33:   0.0345                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    -3        B   179                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7110  -0.8890   6.6360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0824 T22:   0.0995                                     
REMARK   3      T33:   0.0302 T12:  -0.0097                                     
REMARK   3      T13:   0.0127 T23:  -0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3949 L22:   0.9215                                     
REMARK   3      L33:   2.1794 L12:   0.5448                                     
REMARK   3      L13:  -0.7419 L23:  -0.5832                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0051 S12:  -0.1060 S13:   0.0779                       
REMARK   3      S21:  -0.1235 S22:  -0.0435 S23:   0.0336                       
REMARK   3      S31:  -0.1570 S32:   0.2134 S33:   0.0385                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    -3        C   181                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7200  -0.4620  55.9010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0730 T22:   0.0391                                     
REMARK   3      T33:   0.0826 T12:  -0.0189                                     
REMARK   3      T13:   0.0147 T23:  -0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9321 L22:   1.0643                                     
REMARK   3      L33:   1.0506 L12:  -0.2854                                     
REMARK   3      L13:   0.1276 L23:  -0.3483                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0298 S12:  -0.0309 S13:   0.1426                       
REMARK   3      S21:  -0.0572 S22:  -0.0162 S23:  -0.1139                       
REMARK   3      S31:  -0.1112 S32:   0.0865 S33:   0.0461                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D   181                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.9350  17.4830   6.3290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0598 T22:   0.1477                                     
REMARK   3      T33:   0.0320 T12:  -0.0334                                     
REMARK   3      T13:  -0.0093 T23:   0.0463                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0936 L22:   1.2751                                     
REMARK   3      L33:   1.7201 L12:  -0.0085                                     
REMARK   3      L13:   0.3121 L23:   0.4025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0772 S12:  -0.0133 S13:  -0.1250                       
REMARK   3      S21:  -0.1461 S22:  -0.0773 S23:  -0.0159                       
REMARK   3      S31:   0.1997 S32:  -0.1422 S33:   0.0001                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    12        E    70                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4730  36.2180  33.0420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0365 T22:   0.1036                                     
REMARK   3      T33:   0.0705 T12:  -0.0266                                     
REMARK   3      T13:   0.0243 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7204 L22:   1.3607                                     
REMARK   3      L33:   2.5542 L12:  -0.3341                                     
REMARK   3      L13:   0.6444 L23:   0.4220                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0084 S12:  -0.0219 S13:   0.1088                       
REMARK   3      S21:   0.0885 S22:  -0.0390 S23:   0.0247                       
REMARK   3      S31:  -0.0859 S32:   0.0425 S33:   0.0306                       
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 :   E    71        E   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3070  28.5820  21.4590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0851 T22:   0.1096                                     
REMARK   3      T33:   0.0688 T12:  -0.0205                                     
REMARK   3      T13:   0.0097 T23:  -0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7670 L22:   0.6501                                     
REMARK   3      L33:   0.7090 L12:  -0.2362                                     
REMARK   3      L13:   0.0649 L23:   0.1216                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0372 S12:   0.1568 S13:  -0.0075                       
REMARK   3      S21:  -0.0604 S22:  -0.0199 S23:  -0.0780                       
REMARK   3      S31:   0.0336 S32:  -0.0194 S33:  -0.0172                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F    12        F    69                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3230  38.2000  80.7810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0933 T22:   0.2583                                     
REMARK   3      T33:   0.0764 T12:   0.1245                                     
REMARK   3      T13:  -0.0616 T23:  -0.1151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5052 L22:   2.9909                                     
REMARK   3      L33:   1.6972 L12:  -0.5205                                     
REMARK   3      L13:   0.3358 L23:   0.0655                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2119 S12:  -0.2976 S13:   0.1454                       
REMARK   3      S21:   0.1065 S22:   0.3221 S23:  -0.2459                       
REMARK   3      S31:  -0.1274 S32:   0.0941 S33:  -0.1102                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F    70        F   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.4440  30.1570  69.1320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0630 T22:   0.0878                                     
REMARK   3      T33:   0.1069 T12:  -0.0089                                     
REMARK   3      T13:  -0.0102 T23:   0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8483 L22:   0.5937                                     
REMARK   3      L33:   0.7419 L12:  -0.7344                                     
REMARK   3      L13:   0.0602 L23:   0.1037                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0079 S12:  -0.2714 S13:  -0.0361                       
REMARK   3      S21:  -0.0088 S22:   0.0957 S23:  -0.0663                       
REMARK   3      S31:   0.0095 S32:   0.0789 S33:  -0.0879                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G    12        G    71                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.6910 -19.7010  32.8910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0289 T22:   0.0954                                     
REMARK   3      T33:   0.0764 T12:  -0.0189                                     
REMARK   3      T13:  -0.0073 T23:   0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2879 L22:   1.3407                                     
REMARK   3      L33:   2.5377 L12:  -0.2215                                     
REMARK   3      L13:  -0.3614 L23:  -0.4198                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0234 S12:  -0.0316 S13:  -0.1021                       
REMARK   3      S21:   0.0342 S22:  -0.0142 S23:   0.1110                       
REMARK   3      S31:   0.1210 S32:  -0.0330 S33:  -0.0093                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G    72        G   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.8300 -11.5760  21.9880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0836 T22:   0.0966                                     
REMARK   3      T33:   0.0575 T12:  -0.0096                                     
REMARK   3      T13:   0.0110 T23:   0.0237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3515 L22:   0.7450                                     
REMARK   3      L33:   0.9723 L12:  -0.1731                                     
REMARK   3      L13:  -0.0823 L23:  -0.0865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0337 S12:   0.1173 S13:   0.0588                       
REMARK   3      S21:  -0.0835 S22:  -0.0653 S23:   0.0347                       
REMARK   3      S31:   0.0242 S32:  -0.0862 S33:   0.0316                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    13        H    61                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.4680 -23.9140  80.3210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0733 T22:   0.1150                                     
REMARK   3      T33:   0.1003 T12:   0.0156                                     
REMARK   3      T13:   0.0164 T23:   0.0499                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0089 L22:   2.6720                                     
REMARK   3      L33:   3.0085 L12:  -0.3432                                     
REMARK   3      L13:  -0.4906 L23:  -0.1455                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1331 S12:  -0.0856 S13:  -0.0154                       
REMARK   3      S21:   0.0424 S22:   0.1073 S23:   0.1417                       
REMARK   3      S31:   0.0741 S32:  -0.0129 S33:   0.0258                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    62        H   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.6850 -12.0330  70.2030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0965 T22:   0.0738                                     
REMARK   3      T33:   0.0817 T12:   0.0018                                     
REMARK   3      T13:   0.0125 T23:   0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4057 L22:   0.6670                                     
REMARK   3      L33:   0.8413 L12:  -0.4157                                     
REMARK   3      L13:   0.0411 L23:  -0.0858                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0395 S12:  -0.0973 S13:   0.0556                       
REMARK   3      S21:   0.0230 S22:   0.0380 S23:   0.0644                       
REMARK   3      S31:  -0.0707 S32:  -0.1034 S33:   0.0015                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 U VALUES : RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 3LW8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-MAR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057807.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.873                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 133487                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.210                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.1100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1S1C, PARTIALLY REFINED STRUCTURE OF       
REMARK 200  FREE IPGB2                                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 3350, PH 7.5, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
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       50.80000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: 2170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 2500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: 2580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
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 D    -3                                                      
REMARK 465     PRO D    -2                                                      
REMARK 465     LEU D    -1                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     GLY E    -3                                                      
REMARK 465     ALA E    -2                                                      
REMARK 465     MET E    -1                                                      
REMARK 465     ASP E     0                                                      
REMARK 465     MET E     1                                                      
REMARK 465     LEU E     2                                                      
REMARK 465     GLY E     3                                                      
REMARK 465     THR E     4                                                      
REMARK 465     SER E     5                                                      
REMARK 465     PHE E     6                                                      
REMARK 465     ASN E     7                                                      
REMARK 465     GLY F    -3                                                      
REMARK 465     ALA F    -2                                                      
REMARK 465     MET F    -1                                                      
REMARK 465     ASP F     0                                                      
REMARK 465     MET F     1                                                      
REMARK 465     LEU F     2                                                      
REMARK 465     GLY F     3                                                      
REMARK 465     THR F     4                                                      
REMARK 465     SER F     5                                                      
REMARK 465     PHE F     6                                                      
REMARK 465     ASN F     7                                                      
REMARK 465     GLY G    -3                                                      
REMARK 465     ALA G    -2                                                      
REMARK 465     MET G    -1                                                      
REMARK 465     ASP G     0                                                      
REMARK 465     MET G     1                                                      
REMARK 465     LEU G     2                                                      
REMARK 465     GLY G     3                                                      
REMARK 465     THR G     4                                                      
REMARK 465     SER G     5                                                      
REMARK 465     PHE G     6                                                      
REMARK 465     ASN G     7                                                      
REMARK 465     GLY H    -3                                                      
REMARK 465     ALA H    -2                                                      
REMARK 465     MET H    -1                                                      
REMARK 465     ASP H     0                                                      
REMARK 465     MET H     1                                                      
REMARK 465     LEU H     2                                                      
REMARK 465     GLY H     3                                                      
REMARK 465     THR H     4                                                      
REMARK 465     SER H     5                                                      
REMARK 465     PHE H     6                                                      
REMARK 465     ASN H     7                                                      
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   NE2  GLN B    52     O    HOH B   200              1.88            
REMARK 500   N    ASN A   109     O    HOH A  1681              1.95            
REMARK 500   NH1  ARG C    68     OD2  ASP H    65              2.00            
REMARK 500   NH1  ARG G    95     O    HOH G  1741              2.01            
REMARK 500   OG   SER D    85     OD1  ASP D    87              2.08            
REMARK 500   O    HOH D  1425     O    HOH D  1872              2.14            
REMARK 500   O    HOH E   997     O    HOH E  1751              2.16            
REMARK 500   OE1  GLN G   116     O    HOH G  1852              2.16            
REMARK 500   OE1  GLN G   116     O    HOH G  1880              2.17            
REMARK 500   NH2  ARG E    95     O    HOH E   996              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH C  1298     O    HOH E   871     2646     2.13            
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 F 158   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP H  80   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  98      -54.14   -125.16                                   
REMARK 500    ASP B  49       48.05     39.84                                   
REMARK 500    ASN B 109       -2.79     71.16                                   
REMARK 500    LYS B 164       -7.45     76.95                                   
REMARK 500    LYS D  98      -55.10   -120.78                                   
REMARK 500    LYS D 135      -14.88     79.11                                   
REMARK 500    LYS D 164       -4.41     79.97                                   
REMARK 500    SER E  87       54.90     38.13                                   
REMARK 500    ALA E 115      -58.53   -131.39                                   
REMARK 500    VAL E 165      -58.11   -120.87                                   
REMARK 500    ALA F 115      -54.00   -131.59                                   
REMARK 500    ALA G 115      -61.23   -136.23                                   
REMARK 500    VAL H  69      -36.37   -132.73                                   
REMARK 500    ALA H 115      -60.90   -126.68                                   
REMARK 500    VAL H 165      -58.07   -120.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    TYR F 167        24.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1143        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH A1736        DISTANCE =  5.52 ANGSTROMS                       
REMARK 525    HOH C1035        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH D1610        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH E1149        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH E1583        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH G1672        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH H1649        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH H1778        DISTANCE =  6.32 ANGSTROMS                       
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 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP A 201   O2B                                                    
REMARK 620 2 THR A  19   OG1  94.8                                              
REMARK 620 3 HOH A1844   O    95.9  88.3                                        
REMARK 620 4 HOH A1739   O    85.2  87.6 175.8                                  
REMARK 620 5 HOH A1676   O   170.6  91.9  90.8  88.6                            
REMARK 620 6 HOH A1337   O    91.3 173.8  90.9  93.1  82.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP C 201   O2B                                                    
REMARK 620 2 THR C  19   OG1  90.6                                              
REMARK 620 3 HOH C1738   O    94.0  85.0                                        
REMARK 620 4 HOH C1853   O    89.7  93.7 176.1                                  
REMARK 620 5 HOH C 210   O   176.9  90.8  88.8  87.5                            
REMARK 620 6 HOH C1675   O    91.9 174.5  89.9  91.2  86.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP B 201   O3B                                                    
REMARK 620 2 THR B  19   OG1  99.8                                              
REMARK 620 3 HOH B1677   O    98.0  89.3                                        
REMARK 620 4 HOH B1851   O   169.9  89.9  85.0                                  
REMARK 620 5 HOH B1740   O    93.8  91.5 167.9  83.0                            
REMARK 620 6 HOH B 810   O    89.0 170.9  87.2  81.5  90.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP D 201   O2B                                                    
REMARK 620 2 THR D  19   OG1  93.9                                              
REMARK 620 3 HOH D 841   O    89.8  88.7                                        
REMARK 620 4 HOH D1742   O    91.7 173.1  95.3                                  
REMARK 620 5 HOH D1470   O    98.6  84.4 169.4  90.8                            
REMARK 620 6 HOH D1678   O   170.1  91.4  82.0  83.7  90.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 301                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3LWN   RELATED DB: PDB                                   
REMARK 900 IPGB2 IN COMPLEX WITH HUMAN RHOA (COMPLEX B)                         
REMARK 900 RELATED ID: 3LXR   RELATED DB: PDB                                   
REMARK 900 IPGB2 IN COMPLEX WITH HUMAN RHOA (COMPLEX C)                         
REMARK 900 RELATED ID: 3LYQ   RELATED DB: PDB                                   
REMARK 900 IPGB2, APO FORM                                                      
DBREF  3LW8 A    2   181  UNP    P61586   RHOA_HUMAN       2    181             
DBREF  3LW8 B    2   181  UNP    P61586   RHOA_HUMAN       2    181             
DBREF  3LW8 C    2   181  UNP    P61586   RHOA_HUMAN       2    181             
DBREF  3LW8 D    2   181  UNP    P61586   RHOA_HUMAN       2    181             
DBREF  3LW8 E    1   188  UNP    Q9AJW7   Q9AJW7_SHIFL     1    188             
DBREF  3LW8 F    1   188  UNP    Q9AJW7   Q9AJW7_SHIFL     1    188             
DBREF  3LW8 G    1   188  UNP    Q9AJW7   Q9AJW7_SHIFL     1    188             
DBREF  3LW8 H    1   188  UNP    Q9AJW7   Q9AJW7_SHIFL     1    188             
SEQADV 3LW8 GLY A   -3  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 PRO A   -2  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 LEU A   -1  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 GLY A    0  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 SER A    1  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 GLY B   -3  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 PRO B   -2  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 LEU B   -1  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 GLY B    0  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 SER B    1  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 GLY C   -3  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 PRO C   -2  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 LEU C   -1  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 GLY C    0  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 SER C    1  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 GLY D   -3  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 PRO D   -2  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 LEU D   -1  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 GLY D    0  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 SER D    1  UNP  P61586              EXPRESSION TAG                 
SEQADV 3LW8 GLY E   -3  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LW8 ALA E   -2  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LW8 MET E   -1  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LW8 ASP E    0  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LW8 GLY F   -3  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LW8 ALA F   -2  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LW8 MET F   -1  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LW8 ASP F    0  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LW8 GLY G   -3  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LW8 ALA G   -2  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LW8 MET G   -1  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LW8 ASP G    0  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LW8 GLY H   -3  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LW8 ALA H   -2  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LW8 MET H   -1  UNP  Q9AJW7              EXPRESSION TAG                 
SEQADV 3LW8 ASP H    0  UNP  Q9AJW7              EXPRESSION TAG                 
SEQRES   1 A  185  GLY PRO LEU GLY SER ALA ALA ILE ARG LYS LYS LEU VAL          
SEQRES   2 A  185  ILE VAL GLY ASP GLY ALA CYS GLY LYS THR CYS LEU LEU          
SEQRES   3 A  185  ILE VAL PHE SER LYS ASP GLN PHE PRO GLU VAL TYR VAL          
SEQRES   4 A  185  PRO THR VAL PHE GLU ASN TYR VAL ALA ASP ILE GLU VAL          
SEQRES   5 A  185  ASP GLY LYS GLN VAL GLU LEU ALA LEU TRP ASP THR ALA          
SEQRES   6 A  185  GLY GLN GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR          
SEQRES   7 A  185  PRO ASP THR ASP VAL ILE LEU MET CYS PHE SER ILE ASP          
SEQRES   8 A  185  SER PRO ASP SER LEU GLU ASN ILE PRO GLU LYS TRP THR          
SEQRES   9 A  185  PRO GLU VAL LYS HIS PHE CYS PRO ASN VAL PRO ILE ILE          
SEQRES  10 A  185  LEU VAL GLY ASN LYS LYS ASP LEU ARG ASN ASP GLU HIS          
SEQRES  11 A  185  THR ARG ARG GLU LEU ALA LYS MET LYS GLN GLU PRO VAL          
SEQRES  12 A  185  LYS PRO GLU GLU GLY ARG ASP MET ALA ASN ARG ILE GLY          
SEQRES  13 A  185  ALA PHE GLY TYR MET GLU CYS SER ALA LYS THR LYS ASP          
SEQRES  14 A  185  GLY VAL ARG GLU VAL PHE GLU MET ALA THR ARG ALA ALA          
SEQRES  15 A  185  LEU GLN ALA                                                  
SEQRES   1 B  185  GLY PRO LEU GLY SER ALA ALA ILE ARG LYS LYS LEU VAL          
SEQRES   2 B  185  ILE VAL GLY ASP GLY ALA CYS GLY LYS THR CYS LEU LEU          
SEQRES   3 B  185  ILE VAL PHE SER LYS ASP GLN PHE PRO GLU VAL TYR VAL          
SEQRES   4 B  185  PRO THR VAL PHE GLU ASN TYR VAL ALA ASP ILE GLU VAL          
SEQRES   5 B  185  ASP GLY LYS GLN VAL GLU LEU ALA LEU TRP ASP THR ALA          
SEQRES   6 B  185  GLY GLN GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR          
SEQRES   7 B  185  PRO ASP THR ASP VAL ILE LEU MET CYS PHE SER ILE ASP          
SEQRES   8 B  185  SER PRO ASP SER LEU GLU ASN ILE PRO GLU LYS TRP THR          
SEQRES   9 B  185  PRO GLU VAL LYS HIS PHE CYS PRO ASN VAL PRO ILE ILE          
SEQRES  10 B  185  LEU VAL GLY ASN LYS LYS ASP LEU ARG ASN ASP GLU HIS          
SEQRES  11 B  185  THR ARG ARG GLU LEU ALA LYS MET LYS GLN GLU PRO VAL          
SEQRES  12 B  185  LYS PRO GLU GLU GLY ARG ASP MET ALA ASN ARG ILE GLY          
SEQRES  13 B  185  ALA PHE GLY TYR MET GLU CYS SER ALA LYS THR LYS ASP          
SEQRES  14 B  185  GLY VAL ARG GLU VAL PHE GLU MET ALA THR ARG ALA ALA          
SEQRES  15 B  185  LEU GLN ALA                                                  
SEQRES   1 C  185  GLY PRO LEU GLY SER ALA ALA ILE ARG LYS LYS LEU VAL          
SEQRES   2 C  185  ILE VAL GLY ASP GLY ALA CYS GLY LYS THR CYS LEU LEU          
SEQRES   3 C  185  ILE VAL PHE SER LYS ASP GLN PHE PRO GLU VAL TYR VAL          
SEQRES   4 C  185  PRO THR VAL PHE GLU ASN TYR VAL ALA ASP ILE GLU VAL          
SEQRES   5 C  185  ASP GLY LYS GLN VAL GLU LEU ALA LEU TRP ASP THR ALA          
SEQRES   6 C  185  GLY GLN GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR          
SEQRES   7 C  185  PRO ASP THR ASP VAL ILE LEU MET CYS PHE SER ILE ASP          
SEQRES   8 C  185  SER PRO ASP SER LEU GLU ASN ILE PRO GLU LYS TRP THR          
SEQRES   9 C  185  PRO GLU VAL LYS HIS PHE CYS PRO ASN VAL PRO ILE ILE          
SEQRES  10 C  185  LEU VAL GLY ASN LYS LYS ASP LEU ARG ASN ASP GLU HIS          
SEQRES  11 C  185  THR ARG ARG GLU LEU ALA LYS MET LYS GLN GLU PRO VAL          
SEQRES  12 C  185  LYS PRO GLU GLU GLY ARG ASP MET ALA ASN ARG ILE GLY          
SEQRES  13 C  185  ALA PHE GLY TYR MET GLU CYS SER ALA LYS THR LYS ASP          
SEQRES  14 C  185  GLY VAL ARG GLU VAL PHE GLU MET ALA THR ARG ALA ALA          
SEQRES  15 C  185  LEU GLN ALA                                                  
SEQRES   1 D  185  GLY PRO LEU GLY SER ALA ALA ILE ARG LYS LYS LEU VAL          
SEQRES   2 D  185  ILE VAL GLY ASP GLY ALA CYS GLY LYS THR CYS LEU LEU          
SEQRES   3 D  185  ILE VAL PHE SER LYS ASP GLN PHE PRO GLU VAL TYR VAL          
SEQRES   4 D  185  PRO THR VAL PHE GLU ASN TYR VAL ALA ASP ILE GLU VAL          
SEQRES   5 D  185  ASP GLY LYS GLN VAL GLU LEU ALA LEU TRP ASP THR ALA          
SEQRES   6 D  185  GLY GLN GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR          
SEQRES   7 D  185  PRO ASP THR ASP VAL ILE LEU MET CYS PHE SER ILE ASP          
SEQRES   8 D  185  SER PRO ASP SER LEU GLU ASN ILE PRO GLU LYS TRP THR          
SEQRES   9 D  185  PRO GLU VAL LYS HIS PHE CYS PRO ASN VAL PRO ILE ILE          
SEQRES  10 D  185  LEU VAL GLY ASN LYS LYS ASP LEU ARG ASN ASP GLU HIS          
SEQRES  11 D  185  THR ARG ARG GLU LEU ALA LYS MET LYS GLN GLU PRO VAL          
SEQRES  12 D  185  LYS PRO GLU GLU GLY ARG ASP MET ALA ASN ARG ILE GLY          
SEQRES  13 D  185  ALA PHE GLY TYR MET GLU CYS SER ALA LYS THR LYS ASP          
SEQRES  14 D  185  GLY VAL ARG GLU VAL PHE GLU MET ALA THR ARG ALA ALA          
SEQRES  15 D  185  LEU GLN ALA                                                  
SEQRES   1 E  192  GLY ALA MET ASP MET LEU GLY THR SER PHE ASN ASN PHE          
SEQRES   2 E  192  GLY ILE SER LEU SER HIS LYS ARG TYR PHE SER GLY LYS          
SEQRES   3 E  192  VAL ASP GLU ILE ILE ARG CYS THR MET GLY LYS ARG ILE          
SEQRES   4 E  192  VAL LYS ILE SER SER THR LYS ILE ASN THR SER ILE LEU          
SEQRES   5 E  192  SER SER VAL SER GLU GLN ILE GLY GLU ASN ILE THR ASP          
SEQRES   6 E  192  TRP LYS ASN ASP GLU LYS LYS VAL TYR VAL SER ARG VAL          
SEQRES   7 E  192  VAL ASN GLN CYS ILE ASP LYS PHE CYS ALA GLU HIS SER          
SEQRES   8 E  192  ARG LYS ILE GLY ASP ASN LEU ARG LYS GLN ILE PHE LYS          
SEQRES   9 E  192  GLN VAL GLU LYS ASP TYR ARG ILE SER LEU ASP ILE ASN          
SEQRES  10 E  192  ALA ALA GLN SER SER ILE ASN HIS LEU VAL SER GLY SER          
SEQRES  11 E  192  SER TYR PHE LYS LYS LYS MET ASP GLU LEU CYS GLU GLY          
SEQRES  12 E  192  MET ASN ARG SER VAL LYS ASN ASP THR THR SER ASN VAL          
SEQRES  13 E  192  ALA ASN LEU ILE SER ASP GLN PHE PHE GLU LYS ASN VAL          
SEQRES  14 E  192  GLN TYR ILE ASP LEU LYS LYS LEU ARG GLY ASN MET SER          
SEQRES  15 E  192  ASP TYR ILE THR ASN LEU GLU SER PRO PHE                      
SEQRES   1 F  192  GLY ALA MET ASP MET LEU GLY THR SER PHE ASN ASN PHE          
SEQRES   2 F  192  GLY ILE SER LEU SER HIS LYS ARG TYR PHE SER GLY LYS          
SEQRES   3 F  192  VAL ASP GLU ILE ILE ARG CYS THR MET GLY LYS ARG ILE          
SEQRES   4 F  192  VAL LYS ILE SER SER THR LYS ILE ASN THR SER ILE LEU          
SEQRES   5 F  192  SER SER VAL SER GLU GLN ILE GLY GLU ASN ILE THR ASP          
SEQRES   6 F  192  TRP LYS ASN ASP GLU LYS LYS VAL TYR VAL SER ARG VAL          
SEQRES   7 F  192  VAL ASN GLN CYS ILE ASP LYS PHE CYS ALA GLU HIS SER          
SEQRES   8 F  192  ARG LYS ILE GLY ASP ASN LEU ARG LYS GLN ILE PHE LYS          
SEQRES   9 F  192  GLN VAL GLU LYS ASP TYR ARG ILE SER LEU ASP ILE ASN          
SEQRES  10 F  192  ALA ALA GLN SER SER ILE ASN HIS LEU VAL SER GLY SER          
SEQRES  11 F  192  SER TYR PHE LYS LYS LYS MET ASP GLU LEU CYS GLU GLY          
SEQRES  12 F  192  MET ASN ARG SER VAL LYS ASN ASP THR THR SER ASN VAL          
SEQRES  13 F  192  ALA ASN LEU ILE SER ASP GLN PHE PHE GLU LYS ASN VAL          
SEQRES  14 F  192  GLN TYR ILE ASP LEU LYS LYS LEU ARG GLY ASN MET SER          
SEQRES  15 F  192  ASP TYR ILE THR ASN LEU GLU SER PRO PHE                      
SEQRES   1 G  192  GLY ALA MET ASP MET LEU GLY THR SER PHE ASN ASN PHE          
SEQRES   2 G  192  GLY ILE SER LEU SER HIS LYS ARG TYR PHE SER GLY LYS          
SEQRES   3 G  192  VAL ASP GLU ILE ILE ARG CYS THR MET GLY LYS ARG ILE          
SEQRES   4 G  192  VAL LYS ILE SER SER THR LYS ILE ASN THR SER ILE LEU          
SEQRES   5 G  192  SER SER VAL SER GLU GLN ILE GLY GLU ASN ILE THR ASP          
SEQRES   6 G  192  TRP LYS ASN ASP GLU LYS LYS VAL TYR VAL SER ARG VAL          
SEQRES   7 G  192  VAL ASN GLN CYS ILE ASP LYS PHE CYS ALA GLU HIS SER          
SEQRES   8 G  192  ARG LYS ILE GLY ASP ASN LEU ARG LYS GLN ILE PHE LYS          
SEQRES   9 G  192  GLN VAL GLU LYS ASP TYR ARG ILE SER LEU ASP ILE ASN          
SEQRES  10 G  192  ALA ALA GLN SER SER ILE ASN HIS LEU VAL SER GLY SER          
SEQRES  11 G  192  SER TYR PHE LYS LYS LYS MET ASP GLU LEU CYS GLU GLY          
SEQRES  12 G  192  MET ASN ARG SER VAL LYS ASN ASP THR THR SER ASN VAL          
SEQRES  13 G  192  ALA ASN LEU ILE SER ASP GLN PHE PHE GLU LYS ASN VAL          
SEQRES  14 G  192  GLN TYR ILE ASP LEU LYS LYS LEU ARG GLY ASN MET SER          
SEQRES  15 G  192  ASP TYR ILE THR ASN LEU GLU SER PRO PHE                      
SEQRES   1 H  192  GLY ALA MET ASP MET LEU GLY THR SER PHE ASN ASN PHE          
SEQRES   2 H  192  GLY ILE SER LEU SER HIS LYS ARG TYR PHE SER GLY LYS          
SEQRES   3 H  192  VAL ASP GLU ILE ILE ARG CYS THR MET GLY LYS ARG ILE          
SEQRES   4 H  192  VAL LYS ILE SER SER THR LYS ILE ASN THR SER ILE LEU          
SEQRES   5 H  192  SER SER VAL SER GLU GLN ILE GLY GLU ASN ILE THR ASP          
SEQRES   6 H  192  TRP LYS ASN ASP GLU LYS LYS VAL TYR VAL SER ARG VAL          
SEQRES   7 H  192  VAL ASN GLN CYS ILE ASP LYS PHE CYS ALA GLU HIS SER          
SEQRES   8 H  192  ARG LYS ILE GLY ASP ASN LEU ARG LYS GLN ILE PHE LYS          
SEQRES   9 H  192  GLN VAL GLU LYS ASP TYR ARG ILE SER LEU ASP ILE ASN          
SEQRES  10 H  192  ALA ALA GLN SER SER ILE ASN HIS LEU VAL SER GLY SER          
SEQRES  11 H  192  SER TYR PHE LYS LYS LYS MET ASP GLU LEU CYS GLU GLY          
SEQRES  12 H  192  MET ASN ARG SER VAL LYS ASN ASP THR THR SER ASN VAL          
SEQRES  13 H  192  ALA ASN LEU ILE SER ASP GLN PHE PHE GLU LYS ASN VAL          
SEQRES  14 H  192  GLN TYR ILE ASP LEU LYS LYS LEU ARG GLY ASN MET SER          
SEQRES  15 H  192  ASP TYR ILE THR ASN LEU GLU SER PRO PHE                      
HET    GDP  A 201      28                                                       
HET     MG  A 301       1                                                       
HET    GDP  B 201      28                                                       
HET     MG  B 301       1                                                       
HET    GDP  C 201      28                                                       
HET     MG  C 301       1                                                       
HET    GDP  D 201      28                                                       
HET     MG  D 301       1                                                       
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   9  GDP    4(C10 H15 N5 O11 P2)                                         
FORMUL  10   MG    4(MG 2+)                                                     
FORMUL  17  HOH   *1766(H2 O)                                                   
HELIX    1   1 LEU A   -1  ALA A    3  5                                   5    
HELIX    2   2 GLY A   17  ASP A   28  1                                  12    
HELIX    3   3 GLN A   63  ASP A   67  5                                   5    
HELIX    4   4 LEU A   69  TYR A   74  5                                   6    
HELIX    5   5 SER A   88  LYS A   98  1                                  11    
HELIX    6   6 LYS A   98  CYS A  107  1                                  10    
HELIX    7   7 LYS A  118  ARG A  122  5                                   5    
HELIX    8   8 ASP A  124  MET A  134  1                                  11    
HELIX    9   9 LYS A  140  GLY A  152  1                                  13    
HELIX   10  10 GLY A  166  GLN A  180  1                                  15    
HELIX   11  11 GLY B   17  ASP B   28  1                                  12    
HELIX   12  12 GLN B   63  ASP B   67  5                                   5    
HELIX   13  13 LEU B   69  TYR B   74  5                                   6    
HELIX   14  14 SER B   88  LYS B   98  1                                  11    
HELIX   15  15 LYS B   98  CYS B  107  1                                  10    
HELIX   16  16 LYS B  118  ARG B  122  5                                   5    
HELIX   17  17 ASP B  124  LYS B  133  1                                  10    
HELIX   18  18 LYS B  140  ILE B  151  1                                  12    
HELIX   19  19 GLY B  166  ALA B  181  1                                  16    
HELIX   20  20 LEU C   -1  ALA C    3  5                                   5    
HELIX   21  21 GLY C   17  ASP C   28  1                                  12    
HELIX   22  22 GLN C   63  ASP C   67  5                                   5    
HELIX   23  23 LEU C   69  TYR C   74  5                                   6    
HELIX   24  24 SER C   88  LYS C   98  1                                  11    
HELIX   25  25 LYS C   98  CYS C  107  1                                  10    
HELIX   26  26 LYS C  118  ARG C  122  5                                   5    
HELIX   27  27 ASP C  124  MET C  134  1                                  11    
HELIX   28  28 LYS C  140  GLY C  152  1                                  13    
HELIX   29  29 GLY C  166  GLN C  180  1                                  15    
HELIX   30  30 GLY D   17  ASP D   28  1                                  12    
HELIX   31  31 GLN D   63  ASP D   67  5                                   5    
HELIX   32  32 LEU D   69  TYR D   74  5                                   6    
HELIX   33  33 SER D   88  LYS D   98  1                                  11    
HELIX   34  34 LYS D   98  CYS D  107  1                                  10    
HELIX   35  35 LYS D  118  ARG D  122  5                                   5    
HELIX   36  36 ASP D  124  LYS D  133  1                                  10    
HELIX   37  37 LYS D  140  ILE D  151  1                                  12    
HELIX   38  38 GLY D  166  GLN D  180  1                                  15    
HELIX   39  39 SER E   40  ILE E   55  1                                  16    
HELIX   40  40 ASN E   58  HIS E   86  1                                  29    
HELIX   41  41 GLY E   91  ARG E  107  1                                  17    
HELIX   42  42 SER E  117  SER E  126  1                                  10    
HELIX   43  43 SER E  126  CYS E  137  1                                  12    
HELIX   44  44 ASN E  141  VAL E  165  1                                  25    
HELIX   45  45 ASP E  169  ASN E  183  1                                  15    
HELIX   46  46 SER F   40  GLN F   54  1                                  15    
HELIX   47  47 ASN F   58  HIS F   86  1                                  29    
HELIX   48  48 GLY F   91  ARG F  107  1                                  17    
HELIX   49  49 SER F  117  GLY F  125  1                                   9    
HELIX   50  50 SER F  126  CYS F  137  1                                  12    
HELIX   51  51 ASN F  141  VAL F  165  1                                  25    
HELIX   52  52 ASP F  169  ASN F  183  1                                  15    
HELIX   53  53 SER G   40  ILE G   55  1                                  16    
HELIX   54  54 ASN G   58  SER G   87  1                                  30    
HELIX   55  55 GLY G   91  ARG G  107  1                                  17    
HELIX   56  56 SER G  117  SER G  126  1                                  10    
HELIX   57  57 SER G  126  GLU G  138  1                                  13    
HELIX   58  58 ASN G  141  VAL G  165  1                                  25    
HELIX   59  59 ASP G  169  ASN G  183  1                                  15    
HELIX   60  60 SER H   40  GLY H   56  1                                  17    
HELIX   61  61 ILE H   59  HIS H   86  1                                  28    
HELIX   62  62 GLY H   91  ARG H  107  1                                  17    
HELIX   63  63 SER H  117  GLY H  125  1                                   9    
HELIX   64  64 SER H  126  CYS H  137  1                                  12    
HELIX   65  65 ASN H  141  VAL H  165  1                                  25    
HELIX   66  66 ASP H  169  ASN H  183  1                                  15    
SHEET    1   A 6 TYR A  42  VAL A  48  0                                        
SHEET    2   A 6 LYS A  51  TRP A  58 -1  O  LEU A  57   N  TYR A  42           
SHEET    3   A 6 ARG A   5  GLY A  12  1  N  LEU A   8   O  ALA A  56           
SHEET    4   A 6 VAL A  79  SER A  85  1  O  CYS A  83   N  VAL A  11           
SHEET    5   A 6 ILE A 112  ASN A 117  1  O  ASN A 117   N  PHE A  84           
SHEET    6   A 6 GLY A 155  GLU A 158  1  O  GLY A 155   N  LEU A 114           
SHEET    1   B 6 TYR B  42  VAL B  48  0                                        
SHEET    2   B 6 LYS B  51  TRP B  58 -1  O  VAL B  53   N  ILE B  46           
SHEET    3   B 6 ILE B   4  GLY B  12  1  N  LEU B   8   O  ALA B  56           
SHEET    4   B 6 VAL B  79  SER B  85  1  O  LEU B  81   N  VAL B  11           
SHEET    5   B 6 ILE B 112  ASN B 117  1  O  ILE B 113   N  ILE B  80           
SHEET    6   B 6 GLY B 155  GLU B 158  1  O  GLY B 155   N  LEU B 114           
SHEET    1   C 6 TYR C  42  VAL C  48  0                                        
SHEET    2   C 6 LYS C  51  TRP C  58 -1  O  VAL C  53   N  ILE C  46           
SHEET    3   C 6 ARG C   5  GLY C  12  1  N  LEU C   8   O  ALA C  56           
SHEET    4   C 6 VAL C  79  SER C  85  1  O  CYS C  83   N  VAL C  11           
SHEET    5   C 6 ILE C 112  ASN C 117  1  O  ASN C 117   N  PHE C  84           
SHEET    6   C 6 GLY C 155  GLU C 158  1  O  MET C 157   N  LEU C 114           
SHEET    1   D 6 TYR D  42  VAL D  48  0                                        
SHEET    2   D 6 LYS D  51  TRP D  58 -1  O  LEU D  55   N  ALA D  44           
SHEET    3   D 6 ARG D   5  GLY D  12  1  N  LEU D   8   O  ALA D  56           
SHEET    4   D 6 VAL D  79  SER D  85  1  O  CYS D  83   N  VAL D  11           
SHEET    5   D 6 ILE D 112  ASN D 117  1  O  ASN D 117   N  PHE D  84           
SHEET    6   D 6 GLY D 155  GLU D 158  1  O  MET D 157   N  GLY D 116           
SHEET    1   E 3 PHE E   9  ARG E  17  0                                        
SHEET    2   E 3 VAL E  23  MET E  31 -1  O  THR E  30   N  GLY E  10           
SHEET    3   E 3 ARG E  34  SER E  39 -1  O  VAL E  36   N  CYS E  29           
SHEET    1   F 3 GLY F  10  ARG F  17  0                                        
SHEET    2   F 3 VAL F  23  MET F  31 -1  O  ASP F  24   N  LYS F  16           
SHEET    3   F 3 ARG F  34  SER F  39 -1  O  VAL F  36   N  CYS F  29           
SHEET    1   G 3 PHE G   9  ARG G  17  0                                        
SHEET    2   G 3 VAL G  23  MET G  31 -1  O  ARG G  28   N  SER G  12           
SHEET    3   G 3 ARG G  34  SER G  39 -1  O  VAL G  36   N  CYS G  29           
SHEET    1   H 3 PHE H   9  ARG H  17  0                                        
SHEET    2   H 3 VAL H  23  MET H  31 -1  O  ASP H  24   N  LYS H  16           
SHEET    3   H 3 ARG H  34  SER H  39 -1  O  VAL H  36   N  CYS H  29           
LINK         O2B GDP A 201                MG    MG A 301     1555   1555  1.97  
LINK         O2B GDP C 201                MG    MG C 301     1555   1555  1.97  
LINK         O3B GDP B 201                MG    MG B 301     1555   1555  1.97  
LINK         O2B GDP D 201                MG    MG D 301     1555   1555  1.98  
LINK         OG1 THR D  19                MG    MG D 301     1555   1555  2.05  
LINK         OG1 THR C  19                MG    MG C 301     1555   1555  2.06  
LINK         OG1 THR A  19                MG    MG A 301     1555   1555  2.12  
LINK         OG1 THR B  19                MG    MG B 301     1555   1555  2.12  
LINK        MG    MG B 301                 O   HOH B1677     1555   1555  1.98  
LINK        MG    MG C 301                 O   HOH C1738     1555   1555  2.07  
LINK        MG    MG C 301                 O   HOH C1853     1555   1555  2.07  
LINK        MG    MG A 301                 O   HOH A1844     1555   1555  2.10  
LINK        MG    MG B 301                 O   HOH B1851     1555   1555  2.11  
LINK        MG    MG A 301                 O   HOH A1739     1555   1555  2.11  
LINK        MG    MG A 301                 O   HOH A1676     1555   1555  2.15  
LINK        MG    MG B 301                 O   HOH B1740     1555   1555  2.15  
LINK        MG    MG C 301                 O   HOH C 210     1555   1555  2.16  
LINK        MG    MG D 301                 O   HOH D 841     1555   1555  2.18  
LINK        MG    MG D 301                 O   HOH D1742     1555   1555  2.18  
LINK        MG    MG D 301                 O   HOH D1470     1555   1555  2.20  
LINK        MG    MG C 301                 O   HOH C1675     1555   1555  2.21  
LINK        MG    MG D 301                 O   HOH D1678     1555   1555  2.22  
LINK        MG    MG A 301                 O   HOH A1337     1555   1555  2.24  
LINK        MG    MG B 301                 O   HOH B 810     1555   1555  2.34  
SITE     1 AC1 25 ALA A  15  CYS A  16  GLY A  17  LYS A  18                    
SITE     2 AC1 25 THR A  19  CYS A  20  PHE A  30  LYS A 118                    
SITE     3 AC1 25 ASP A 120  LEU A 121  SER A 160  ALA A 161                    
SITE     4 AC1 25 LYS A 162  HOH A 186  HOH A 188  HOH A 199                    
SITE     5 AC1 25 HOH A 210  HOH A 230   MG A 301  HOH A 432                    
SITE     6 AC1 25 HOH A 636  HOH A 867  HOH A1337  HOH A1739                    
SITE     7 AC1 25 HOH A1844                                                     
SITE     1 AC2  6 THR A  19  GDP A 201  HOH A1337  HOH A1676                    
SITE     2 AC2  6 HOH A1739  HOH A1844                                          
SITE     1 AC3 22 ASP B  13  ALA B  15  CYS B  16  GLY B  17                    
SITE     2 AC3 22 LYS B  18  THR B  19  CYS B  20  PHE B  30                    
SITE     3 AC3 22 LYS B 118  ASP B 120  LEU B 121  SER B 160                    
SITE     4 AC3 22 ALA B 161  LYS B 162  HOH B 183   MG B 301                    
SITE     5 AC3 22 HOH B 810  HOH B 927  HOH B1284  HOH B1380                    
SITE     6 AC3 22 HOH B1677  HOH B1740                                          
SITE     1 AC4  6 THR B  19  GDP B 201  HOH B 810  HOH B1677                    
SITE     2 AC4  6 HOH B1740  HOH B1851                                          
SITE     1 AC5 25 ALA C  15  CYS C  16  GLY C  17  LYS C  18                    
SITE     2 AC5 25 THR C  19  CYS C  20  PHE C  30  LYS C 118                    
SITE     3 AC5 25 ASP C 120  LEU C 121  SER C 160  ALA C 161                    
SITE     4 AC5 25 LYS C 162  HOH C 182  HOH C 183  HOH C 217                    
SITE     5 AC5 25 HOH C 224   MG C 301  HOH C 393  HOH C 409                    
SITE     6 AC5 25 HOH C 999  HOH C1548  HOH C1675  HOH C1738                    
SITE     7 AC5 25 HOH C1853                                                     
SITE     1 AC6  6 THR C  19  GDP C 201  HOH C 210  HOH C1675                    
SITE     2 AC6  6 HOH C1738  HOH C1853                                          
SITE     1 AC7 20 GLY D  14  ALA D  15  CYS D  16  GLY D  17                    
SITE     2 AC7 20 LYS D  18  THR D  19  CYS D  20  PHE D  30                    
SITE     3 AC7 20 LYS D 118  ASP D 120  LEU D 121  SER D 160                    
SITE     4 AC7 20 ALA D 161  LYS D 162  HOH D 183   MG D 301                    
SITE     5 AC7 20 HOH D 391  HOH D 841  HOH D1563  HOH D1742                    
SITE     1 AC8  6 THR D  19  GDP D 201  HOH D 841  HOH D1470                    
SITE     2 AC8  6 HOH D1678  HOH D1742                                          
CRYST1   82.590  101.600   97.030  90.00  96.43  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012108  0.000000  0.001364        0.00000                         
SCALE2      0.000000  0.009843  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010371        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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