GenomeNet

Database: PDB
Entry: 3RL7
LinkDB: 3RL7
Original site: 3RL7 
HEADER    MEMBRANE PROTEIN/SIGNALING PROTEIN      19-APR-11   3RL7              
TITLE     CRYSTAL STRUCTURE OF HDLG1-PDZ1 COMPLEXED WITH APC                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DISKS LARGE HOMOLOG 1;                                     
COMPND   3 CHAIN: B, A, C, D, E, F;                                             
COMPND   4 FRAGMENT: UNP RESIDUES 220-317;                                      
COMPND   5 SYNONYM: SYNAPSE-ASSOCIATED PROTEIN 97, SAP-97, SAP97, HDLG;         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 11-MER PEPTIDE FROM ADENOMATOUS POLYPOSIS COLI PROTEIN;    
COMPND   9 CHAIN: G, H, I, J, K, L;                                             
COMPND  10 SYNONYM: APC-C11;                                                    
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: DLG1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS              
KEYWDS    PDZ-LIGAND COMPLEX, MEMBRANE PROTEIN-SIGNALING PROTEIN COMPLEX        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.ZHANG,H.LI,G.WU                                                     
REVDAT   2   21-DEC-16 3RL7    1       TITLE                                    
REVDAT   1   14-DEC-11 3RL7    0                                                
JRNL        AUTH   Z.ZHANG,H.LI,L.CHEN,X.LU,J.ZHANG,P.XU,K.LIN,G.WU             
JRNL        TITL   MOLECULAR BASIS FOR THE RECOGNITION OF ADENOMATOUS POLYPOSIS 
JRNL        TITL 2 COLI BY THE DISCS LARGE 1 PROTEIN.                           
JRNL        REF    PLOS ONE                      V.   6 23507 2011              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   21858148                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0023507                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 28155                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1392                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1936                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.36                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 100                          
REMARK   3   BIN FREE R VALUE                    : 0.2770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4295                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 57                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 14.62000                                             
REMARK   3    B22 (A**2) : 14.62000                                             
REMARK   3    B33 (A**2) : -29.25000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.046         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.164         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.830        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.931                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4318 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5808 ; 0.970 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   548 ; 5.711 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   196 ;35.351 ;23.163       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   759 ;17.627 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;15.795 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   687 ; 0.066 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3189 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B A C D E F                     
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    225       B     309      4                      
REMARK   3           1     A    225       A     309      4                      
REMARK   3           1     C    225       C     309      4                      
REMARK   3           1     D    225       D     309      4                      
REMARK   3           1     E    225       E     309      4                      
REMARK   3           1     F    225       F     309      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    563 ; 0.490 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    563 ; 0.500 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    563 ; 0.470 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):    563 ; 0.420 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):    563 ; 0.440 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    F    (A):    563 ; 0.400 ; 0.500           
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 4                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.262                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : H+K, -K, -L                                     
REMARK   3      TWIN FRACTION : 0.239                                           
REMARK   3      TWIN DOMAIN   : 3                                               
REMARK   3      TWIN OPERATOR : -H, -K, L                                       
REMARK   3      TWIN FRACTION : 0.261                                           
REMARK   3      TWIN DOMAIN   : 4                                               
REMARK   3      TWIN OPERATOR : K, H, -L                                        
REMARK   3      TWIN FRACTION : 0.238                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 13                                         
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 :   B   219        B   310                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.9335 -20.6765  -4.7908              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0204 T22:   0.0221                                     
REMARK   3      T33:   0.0896 T12:   0.0161                                     
REMARK   3      T13:  -0.0116 T23:  -0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5291 L22:   2.8960                                     
REMARK   3      L33:   1.9234 L12:  -0.4846                                     
REMARK   3      L13:  -0.3016 L23:   0.2908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0299 S12:  -0.0750 S13:   0.1031                       
REMARK   3      S21:   0.0140 S22:  -0.0605 S23:   0.0742                       
REMARK   3      S31:  -0.1888 S32:  -0.1785 S33:   0.0306                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   220        A   309                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.2540 -14.0352  17.3585              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0625 T22:   0.0198                                     
REMARK   3      T33:   0.1008 T12:   0.0024                                     
REMARK   3      T13:   0.0067 T23:  -0.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1150 L22:   2.5338                                     
REMARK   3      L33:   1.4180 L12:  -0.1768                                     
REMARK   3      L13:   0.1477 L23:  -0.5302                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0654 S12:   0.1098 S13:   0.1254                       
REMARK   3      S21:  -0.0198 S22:  -0.0065 S23:   0.1000                       
REMARK   3      S31:  -0.2470 S32:  -0.0706 S33:   0.0719                       
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   220        C   310                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.2270  10.2524  17.5968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1208 T22:   0.0901                                     
REMARK   3      T33:   0.1508 T12:  -0.0179                                     
REMARK   3      T13:  -0.0204 T23:  -0.0101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3604 L22:   0.9317                                     
REMARK   3      L33:   1.5987 L12:   0.1804                                     
REMARK   3      L13:  -0.7445 L23:  -0.6754                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0024 S12:   0.0260 S13:   0.1605                       
REMARK   3      S21:  -0.1055 S22:  -0.0355 S23:  -0.1640                       
REMARK   3      S31:  -0.1545 S32:   0.2308 S33:   0.0379                       
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   219        D   310                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.4146  -9.9981  -4.4952              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0174 T22:   0.0840                                     
REMARK   3      T33:   0.1169 T12:   0.0245                                     
REMARK   3      T13:   0.0066 T23:  -0.0217                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0541 L22:   2.0543                                     
REMARK   3      L33:   1.4955 L12:  -0.1665                                     
REMARK   3      L13:   0.2862 L23:  -0.5508                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0120 S12:  -0.0558 S13:  -0.1331                       
REMARK   3      S21:   0.0905 S22:  -0.0102 S23:  -0.1313                       
REMARK   3      S31:   0.0335 S32:   0.1382 S33:  -0.0018                       
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   220        E   310                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.7038  25.0949  -5.1159              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1695 T22:   0.1849                                     
REMARK   3      T33:   0.2223 T12:   0.0197                                     
REMARK   3      T13:   0.0151 T23:  -0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2062 L22:   0.3906                                     
REMARK   3      L33:   0.6876 L12:   0.6538                                     
REMARK   3      L13:   0.0044 L23:  -0.1069                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0782 S12:  -0.1068 S13:   0.0292                       
REMARK   3      S21:   0.0366 S22:  -0.0545 S23:   0.0680                       
REMARK   3      S31:   0.1049 S32:  -0.1981 S33:  -0.0236                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   219        F   309                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.7962  13.9165  17.1066              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0933 T22:   0.0300                                     
REMARK   3      T33:   0.1702 T12:  -0.0191                                     
REMARK   3      T13:  -0.0191 T23:   0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9063 L22:   1.8144                                     
REMARK   3      L33:   1.4194 L12:   0.0238                                     
REMARK   3      L13:  -0.1709 L23:   0.2457                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0384 S12:   0.1449 S13:  -0.1292                       
REMARK   3      S21:  -0.0879 S22:  -0.0072 S23:  -0.0367                       
REMARK   3      S31:   0.0584 S32:  -0.0146 S33:   0.0456                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G  2837        G  2843                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.2039  -4.4242  24.7910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5134 T22:   0.1646                                     
REMARK   3      T33:   0.4323 T12:   0.1851                                     
REMARK   3      T13:  -0.0324 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9684 L22:   5.2514                                     
REMARK   3      L33:   0.1977 L12:  -0.9454                                     
REMARK   3      L13:  -0.1801 L23:   0.9709                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7099 S12:  -0.3347 S13:   0.0641                       
REMARK   3      S21:   0.2620 S22:   0.7311 S23:   0.5295                       
REMARK   3      S31:   0.0375 S32:   0.1517 S33:  -0.0213                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H  2838        H  2842                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.3639 -14.9696 -13.2771              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1256 T22:   0.1059                                     
REMARK   3      T33:   0.1591 T12:   0.0326                                     
REMARK   3      T13:   0.0038 T23:   0.0729                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  45.0916 L22:  11.7035                                     
REMARK   3      L33:   5.1781 L12: -20.0296                                     
REMARK   3      L13:  -2.2454 L23:   4.7680                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0646 S12:   0.5250 S13:   0.5925                       
REMARK   3      S21:  -0.2953 S22:  -0.2809 S23:   0.0123                       
REMARK   3      S31:  -0.4323 S32:  -0.0879 S33:   0.3455                       
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 :   I  2838        I  2842                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6409 -16.6215 -12.6454              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3287 T22:   0.3267                                     
REMARK   3      T33:   0.3198 T12:   0.2890                                     
REMARK   3      T13:   0.0623 T23:  -0.0435                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4241 L22:   0.4983                                     
REMARK   3      L33:   1.7010 L12:   1.3845                                     
REMARK   3      L13:  -2.7064 L23:  -0.8981                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0093 S12:   0.4637 S13:  -0.0304                       
REMARK   3      S21:  -0.1364 S22:   0.0014 S23:  -0.0484                       
REMARK   3      S31:   0.0996 S32:  -0.1715 S33:  -0.0107                       
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 :   J  2838        J  2843                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8651  16.4425  25.6511              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1518 T22:   0.3016                                     
REMARK   3      T33:   0.2215 T12:  -0.0255                                     
REMARK   3      T13:  -0.0550 T23:   0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4303 L22:  18.1425                                     
REMARK   3      L33:   2.1424 L12:   6.2029                                     
REMARK   3      L13:  -1.1484 L23:   1.4106                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0530 S12:   0.0004 S13:   0.4492                       
REMARK   3      S21:   0.1835 S22:   0.2187 S23:   0.5457                       
REMARK   3      S31:   0.0443 S32:   0.1085 S33:  -0.2717                       
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 :   K  2839        K  2843                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.2660  22.0446 -13.1611              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4609 T22:   0.4134                                     
REMARK   3      T33:   0.4387 T12:   0.0265                                     
REMARK   3      T13:  -0.1761 T23:  -0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  37.1340 L22:   0.4031                                     
REMARK   3      L33:   7.3546 L12:  -3.8429                                     
REMARK   3      L13:  16.5157 L23:  -1.7162                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4566 S12:  -0.5165 S13:   1.2392                       
REMARK   3      S21:  -0.0008 S22:  -0.0013 S23:  -0.0933                       
REMARK   3      S31:  -0.1277 S32:  -0.2249 S33:   0.4579                       
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 :   L  2839        L  2842                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.1279   5.3842  25.3685              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1478 T22:   0.1248                                     
REMARK   3      T33:   0.9509 T12:   0.1153                                     
REMARK   3      T13:   0.8198 T23:   0.0614                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6724 L22:   0.5029                                     
REMARK   3      L33:  39.1222 L12:  -1.1537                                     
REMARK   3      L13:  10.2173 L23:  -4.3957                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1860 S12:  -0.2053 S13:  -0.0893                       
REMARK   3      S21:  -0.0435 S22:   0.0239 S23:   0.1049                       
REMARK   3      S31:   1.2237 S32:  -0.7424 S33:  -0.2099                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    54                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.4371  -2.7116   4.8052              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0815 T22:   0.0832                                     
REMARK   3      T33:   0.0746 T12:   0.0081                                     
REMARK   3      T13:  -0.0245 T23:   0.0133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1761 L22:   0.0464                                     
REMARK   3      L33:   0.0131 L12:  -0.0794                                     
REMARK   3      L13:  -0.0212 L23:  -0.0004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0335 S12:   0.1115 S13:  -0.0070                       
REMARK   3      S21:   0.0115 S22:  -0.0479 S23:  -0.0047                       
REMARK   3      S31:  -0.0318 S32:  -0.0095 S33:   0.0145                       
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 : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 3RL7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-APR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065069.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-10                          
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               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97916                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28225                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.010                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1ZOK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M NA2HPO4, 0.9M KH2PO4, PH 7.5,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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 APPLY THE FOLLOWING TO CHAINS: A, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, J                                  
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 APPLY THE FOLLOWING TO CHAINS: D, I                                  
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: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, K                                  
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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, L                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET B   211                                                      
REMARK 465     GLY B   212                                                      
REMARK 465     HIS B   213                                                      
REMARK 465     HIS B   214                                                      
REMARK 465     HIS B   215                                                      
REMARK 465     HIS B   216                                                      
REMARK 465     HIS B   217                                                      
REMARK 465     HIS B   218                                                      
REMARK 465     ILE B   247                                                      
REMARK 465     GLY B   248                                                      
REMARK 465     ASP B   249                                                      
REMARK 465     LYS B   311                                                      
REMARK 465     PRO B   312                                                      
REMARK 465     VAL B   313                                                      
REMARK 465     SER B   314                                                      
REMARK 465     GLU B   315                                                      
REMARK 465     LYS B   316                                                      
REMARK 465     ILE B   317                                                      
REMARK 465     MET A   211                                                      
REMARK 465     GLY A   212                                                      
REMARK 465     HIS A   213                                                      
REMARK 465     HIS A   214                                                      
REMARK 465     HIS A   215                                                      
REMARK 465     HIS A   216                                                      
REMARK 465     HIS A   217                                                      
REMARK 465     HIS A   218                                                      
REMARK 465     MET A   219                                                      
REMARK 465     ARG A   310                                                      
REMARK 465     LYS A   311                                                      
REMARK 465     PRO A   312                                                      
REMARK 465     VAL A   313                                                      
REMARK 465     SER A   314                                                      
REMARK 465     GLU A   315                                                      
REMARK 465     LYS A   316                                                      
REMARK 465     ILE A   317                                                      
REMARK 465     MET C   211                                                      
REMARK 465     GLY C   212                                                      
REMARK 465     HIS C   213                                                      
REMARK 465     HIS C   214                                                      
REMARK 465     HIS C   215                                                      
REMARK 465     HIS C   216                                                      
REMARK 465     HIS C   217                                                      
REMARK 465     HIS C   218                                                      
REMARK 465     MET C   219                                                      
REMARK 465     HIS C   246                                                      
REMARK 465     ILE C   247                                                      
REMARK 465     GLY C   248                                                      
REMARK 465     ASP C   249                                                      
REMARK 465     LYS C   311                                                      
REMARK 465     PRO C   312                                                      
REMARK 465     VAL C   313                                                      
REMARK 465     SER C   314                                                      
REMARK 465     GLU C   315                                                      
REMARK 465     LYS C   316                                                      
REMARK 465     ILE C   317                                                      
REMARK 465     MET D   211                                                      
REMARK 465     GLY D   212                                                      
REMARK 465     HIS D   213                                                      
REMARK 465     HIS D   214                                                      
REMARK 465     HIS D   215                                                      
REMARK 465     HIS D   216                                                      
REMARK 465     HIS D   217                                                      
REMARK 465     HIS D   218                                                      
REMARK 465     LYS D   311                                                      
REMARK 465     PRO D   312                                                      
REMARK 465     VAL D   313                                                      
REMARK 465     SER D   314                                                      
REMARK 465     GLU D   315                                                      
REMARK 465     LYS D   316                                                      
REMARK 465     ILE D   317                                                      
REMARK 465     MET E   211                                                      
REMARK 465     GLY E   212                                                      
REMARK 465     HIS E   213                                                      
REMARK 465     HIS E   214                                                      
REMARK 465     HIS E   215                                                      
REMARK 465     HIS E   216                                                      
REMARK 465     HIS E   217                                                      
REMARK 465     HIS E   218                                                      
REMARK 465     MET E   219                                                      
REMARK 465     THR E   242                                                      
REMARK 465     ASP E   243                                                      
REMARK 465     ASN E   244                                                      
REMARK 465     PRO E   245                                                      
REMARK 465     HIS E   246                                                      
REMARK 465     ILE E   247                                                      
REMARK 465     GLY E   248                                                      
REMARK 465     ASP E   249                                                      
REMARK 465     ASP E   250                                                      
REMARK 465     LYS E   311                                                      
REMARK 465     PRO E   312                                                      
REMARK 465     VAL E   313                                                      
REMARK 465     SER E   314                                                      
REMARK 465     GLU E   315                                                      
REMARK 465     LYS E   316                                                      
REMARK 465     ILE E   317                                                      
REMARK 465     MET F   211                                                      
REMARK 465     GLY F   212                                                      
REMARK 465     HIS F   213                                                      
REMARK 465     HIS F   214                                                      
REMARK 465     HIS F   215                                                      
REMARK 465     HIS F   216                                                      
REMARK 465     HIS F   217                                                      
REMARK 465     HIS F   218                                                      
REMARK 465     ARG F   310                                                      
REMARK 465     LYS F   311                                                      
REMARK 465     PRO F   312                                                      
REMARK 465     VAL F   313                                                      
REMARK 465     SER F   314                                                      
REMARK 465     GLU F   315                                                      
REMARK 465     LYS F   316                                                      
REMARK 465     ILE F   317                                                      
REMARK 465     ARG G  2833                                                      
REMARK 465     HIS G  2834                                                      
REMARK 465     SER G  2835                                                      
REMARK 465     GLY G  2836                                                      
REMARK 465     ARG H  2833                                                      
REMARK 465     HIS H  2834                                                      
REMARK 465     SER H  2835                                                      
REMARK 465     GLY H  2836                                                      
REMARK 465     SER H  2837                                                      
REMARK 465     VAL H  2843                                                      
REMARK 465     ARG I  2833                                                      
REMARK 465     HIS I  2834                                                      
REMARK 465     SER I  2835                                                      
REMARK 465     GLY I  2836                                                      
REMARK 465     SER I  2837                                                      
REMARK 465     VAL I  2843                                                      
REMARK 465     ARG J  2833                                                      
REMARK 465     HIS J  2834                                                      
REMARK 465     SER J  2835                                                      
REMARK 465     GLY J  2836                                                      
REMARK 465     SER J  2837                                                      
REMARK 465     ARG K  2833                                                      
REMARK 465     HIS K  2834                                                      
REMARK 465     SER K  2835                                                      
REMARK 465     GLY K  2836                                                      
REMARK 465     SER K  2837                                                      
REMARK 465     TYR K  2838                                                      
REMARK 465     ARG L  2833                                                      
REMARK 465     HIS L  2834                                                      
REMARK 465     SER L  2835                                                      
REMARK 465     GLY L  2836                                                      
REMARK 465     SER L  2837                                                      
REMARK 465     TYR L  2838                                                      
REMARK 465     VAL L  2843                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MET B 219    CG   SD   CE                                        
REMARK 470     TYR C 220    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR H2838    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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    PRO B 245      118.89    -37.77                                   
REMARK 500    ASN B 273      -11.34     91.24                                   
REMARK 500    ASN B 280     -110.79     54.12                                   
REMARK 500    ASN A 273       -1.39     88.04                                   
REMARK 500    ASN A 280     -117.33     50.56                                   
REMARK 500    ASN C 273       -5.24     94.95                                   
REMARK 500    ASN C 280     -108.58     52.22                                   
REMARK 500    SER D 232       56.96   -114.28                                   
REMARK 500    ASN D 273       -3.49     90.83                                   
REMARK 500    ASN D 280     -113.95     48.63                                   
REMARK 500    ASN E 273       -6.59     89.55                                   
REMARK 500    ASN E 280     -105.76     52.11                                   
REMARK 500    TYR F 220     -166.66    -78.07                                   
REMARK 500    SER F 232       52.58   -110.71                                   
REMARK 500    ALA F 239     -167.98   -118.48                                   
REMARK 500    HIS F 246       38.87   -149.80                                   
REMARK 500    ILE F 247     -130.80     63.81                                   
REMARK 500    ASP F 249      166.59    133.30                                   
REMARK 500    ASN F 273       -6.65     90.31                                   
REMARK 500    ASN F 280     -107.73     57.78                                   
REMARK 500    ASP F 286       52.83   -110.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3RL8   RELATED DB: PDB                                   
DBREF  3RL7 B  220   317  UNP    Q12959   DLG1_HUMAN     220    317             
DBREF  3RL7 A  220   317  UNP    Q12959   DLG1_HUMAN     220    317             
DBREF  3RL7 C  220   317  UNP    Q12959   DLG1_HUMAN     220    317             
DBREF  3RL7 D  220   317  UNP    Q12959   DLG1_HUMAN     220    317             
DBREF  3RL7 E  220   317  UNP    Q12959   DLG1_HUMAN     220    317             
DBREF  3RL7 F  220   317  UNP    Q12959   DLG1_HUMAN     220    317             
DBREF  3RL7 G 2833  2843  UNP    P25054   APC_HUMAN     2833   2843             
DBREF  3RL7 H 2833  2843  UNP    P25054   APC_HUMAN     2833   2843             
DBREF  3RL7 I 2833  2843  UNP    P25054   APC_HUMAN     2833   2843             
DBREF  3RL7 J 2833  2843  UNP    P25054   APC_HUMAN     2833   2843             
DBREF  3RL7 K 2833  2843  UNP    P25054   APC_HUMAN     2833   2843             
DBREF  3RL7 L 2833  2843  UNP    P25054   APC_HUMAN     2833   2843             
SEQADV 3RL7 MET B  211  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 GLY B  212  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS B  213  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS B  214  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS B  215  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS B  216  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS B  217  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS B  218  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 MET B  219  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 MET A  211  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 GLY A  212  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS A  213  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS A  214  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS A  215  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS A  216  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS A  217  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS A  218  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 MET A  219  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 MET C  211  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 GLY C  212  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS C  213  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS C  214  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS C  215  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS C  216  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS C  217  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS C  218  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 MET C  219  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 MET D  211  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 GLY D  212  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS D  213  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS D  214  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS D  215  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS D  216  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS D  217  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS D  218  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 MET D  219  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 MET E  211  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 GLY E  212  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS E  213  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS E  214  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS E  215  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS E  216  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS E  217  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS E  218  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 MET E  219  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 MET F  211  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 GLY F  212  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS F  213  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS F  214  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS F  215  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS F  216  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS F  217  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 HIS F  218  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL7 MET F  219  UNP  Q12959              EXPRESSION TAG                 
SEQRES   1 B  107  MET GLY HIS HIS HIS HIS HIS HIS MET TYR GLU TYR GLU          
SEQRES   2 B  107  GLU ILE THR LEU GLU ARG GLY ASN SER GLY LEU GLY PHE          
SEQRES   3 B  107  SER ILE ALA GLY GLY THR ASP ASN PRO HIS ILE GLY ASP          
SEQRES   4 B  107  ASP SER SER ILE PHE ILE THR LYS ILE ILE THR GLY GLY          
SEQRES   5 B  107  ALA ALA ALA GLN ASP GLY ARG LEU ARG VAL ASN ASP CYS          
SEQRES   6 B  107  ILE LEU ARG VAL ASN GLU VAL ASP VAL ARG ASP VAL THR          
SEQRES   7 B  107  HIS SER LYS ALA VAL GLU ALA LEU LYS GLU ALA GLY SER          
SEQRES   8 B  107  ILE VAL ARG LEU TYR VAL LYS ARG ARG LYS PRO VAL SER          
SEQRES   9 B  107  GLU LYS ILE                                                  
SEQRES   1 A  107  MET GLY HIS HIS HIS HIS HIS HIS MET TYR GLU TYR GLU          
SEQRES   2 A  107  GLU ILE THR LEU GLU ARG GLY ASN SER GLY LEU GLY PHE          
SEQRES   3 A  107  SER ILE ALA GLY GLY THR ASP ASN PRO HIS ILE GLY ASP          
SEQRES   4 A  107  ASP SER SER ILE PHE ILE THR LYS ILE ILE THR GLY GLY          
SEQRES   5 A  107  ALA ALA ALA GLN ASP GLY ARG LEU ARG VAL ASN ASP CYS          
SEQRES   6 A  107  ILE LEU ARG VAL ASN GLU VAL ASP VAL ARG ASP VAL THR          
SEQRES   7 A  107  HIS SER LYS ALA VAL GLU ALA LEU LYS GLU ALA GLY SER          
SEQRES   8 A  107  ILE VAL ARG LEU TYR VAL LYS ARG ARG LYS PRO VAL SER          
SEQRES   9 A  107  GLU LYS ILE                                                  
SEQRES   1 C  107  MET GLY HIS HIS HIS HIS HIS HIS MET TYR GLU TYR GLU          
SEQRES   2 C  107  GLU ILE THR LEU GLU ARG GLY ASN SER GLY LEU GLY PHE          
SEQRES   3 C  107  SER ILE ALA GLY GLY THR ASP ASN PRO HIS ILE GLY ASP          
SEQRES   4 C  107  ASP SER SER ILE PHE ILE THR LYS ILE ILE THR GLY GLY          
SEQRES   5 C  107  ALA ALA ALA GLN ASP GLY ARG LEU ARG VAL ASN ASP CYS          
SEQRES   6 C  107  ILE LEU ARG VAL ASN GLU VAL ASP VAL ARG ASP VAL THR          
SEQRES   7 C  107  HIS SER LYS ALA VAL GLU ALA LEU LYS GLU ALA GLY SER          
SEQRES   8 C  107  ILE VAL ARG LEU TYR VAL LYS ARG ARG LYS PRO VAL SER          
SEQRES   9 C  107  GLU LYS ILE                                                  
SEQRES   1 D  107  MET GLY HIS HIS HIS HIS HIS HIS MET TYR GLU TYR GLU          
SEQRES   2 D  107  GLU ILE THR LEU GLU ARG GLY ASN SER GLY LEU GLY PHE          
SEQRES   3 D  107  SER ILE ALA GLY GLY THR ASP ASN PRO HIS ILE GLY ASP          
SEQRES   4 D  107  ASP SER SER ILE PHE ILE THR LYS ILE ILE THR GLY GLY          
SEQRES   5 D  107  ALA ALA ALA GLN ASP GLY ARG LEU ARG VAL ASN ASP CYS          
SEQRES   6 D  107  ILE LEU ARG VAL ASN GLU VAL ASP VAL ARG ASP VAL THR          
SEQRES   7 D  107  HIS SER LYS ALA VAL GLU ALA LEU LYS GLU ALA GLY SER          
SEQRES   8 D  107  ILE VAL ARG LEU TYR VAL LYS ARG ARG LYS PRO VAL SER          
SEQRES   9 D  107  GLU LYS ILE                                                  
SEQRES   1 E  107  MET GLY HIS HIS HIS HIS HIS HIS MET TYR GLU TYR GLU          
SEQRES   2 E  107  GLU ILE THR LEU GLU ARG GLY ASN SER GLY LEU GLY PHE          
SEQRES   3 E  107  SER ILE ALA GLY GLY THR ASP ASN PRO HIS ILE GLY ASP          
SEQRES   4 E  107  ASP SER SER ILE PHE ILE THR LYS ILE ILE THR GLY GLY          
SEQRES   5 E  107  ALA ALA ALA GLN ASP GLY ARG LEU ARG VAL ASN ASP CYS          
SEQRES   6 E  107  ILE LEU ARG VAL ASN GLU VAL ASP VAL ARG ASP VAL THR          
SEQRES   7 E  107  HIS SER LYS ALA VAL GLU ALA LEU LYS GLU ALA GLY SER          
SEQRES   8 E  107  ILE VAL ARG LEU TYR VAL LYS ARG ARG LYS PRO VAL SER          
SEQRES   9 E  107  GLU LYS ILE                                                  
SEQRES   1 F  107  MET GLY HIS HIS HIS HIS HIS HIS MET TYR GLU TYR GLU          
SEQRES   2 F  107  GLU ILE THR LEU GLU ARG GLY ASN SER GLY LEU GLY PHE          
SEQRES   3 F  107  SER ILE ALA GLY GLY THR ASP ASN PRO HIS ILE GLY ASP          
SEQRES   4 F  107  ASP SER SER ILE PHE ILE THR LYS ILE ILE THR GLY GLY          
SEQRES   5 F  107  ALA ALA ALA GLN ASP GLY ARG LEU ARG VAL ASN ASP CYS          
SEQRES   6 F  107  ILE LEU ARG VAL ASN GLU VAL ASP VAL ARG ASP VAL THR          
SEQRES   7 F  107  HIS SER LYS ALA VAL GLU ALA LEU LYS GLU ALA GLY SER          
SEQRES   8 F  107  ILE VAL ARG LEU TYR VAL LYS ARG ARG LYS PRO VAL SER          
SEQRES   9 F  107  GLU LYS ILE                                                  
SEQRES   1 G   11  ARG HIS SER GLY SER TYR LEU VAL THR SER VAL                  
SEQRES   1 H   11  ARG HIS SER GLY SER TYR LEU VAL THR SER VAL                  
SEQRES   1 I   11  ARG HIS SER GLY SER TYR LEU VAL THR SER VAL                  
SEQRES   1 J   11  ARG HIS SER GLY SER TYR LEU VAL THR SER VAL                  
SEQRES   1 K   11  ARG HIS SER GLY SER TYR LEU VAL THR SER VAL                  
SEQRES   1 L   11  ARG HIS SER GLY SER TYR LEU VAL THR SER VAL                  
FORMUL  13  HOH   *57(H2 O)                                                     
HELIX    1   1 GLY B  262  GLY B  268  1                                   7    
HELIX    2   2 THR B  288  ALA B  299  1                                  12    
HELIX    3   3 GLY A  262  GLY A  268  1                                   7    
HELIX    4   4 THR A  288  GLU A  298  1                                  11    
HELIX    5   5 GLY C  262  GLY C  268  1                                   7    
HELIX    6   6 THR C  288  GLU C  298  1                                  11    
HELIX    7   7 GLY D  262  GLY D  268  1                                   7    
HELIX    8   8 THR D  288  ALA D  299  1                                  12    
HELIX    9   9 GLY E  262  GLY E  268  1                                   7    
HELIX   10  10 THR E  288  ALA E  299  1                                  12    
HELIX   11  11 GLY F  262  GLY F  268  1                                   7    
HELIX   12  12 THR F  288  ALA F  299  1                                  12    
SHEET    1   A 4 GLU B 221  GLU B 228  0                                        
SHEET    2   A 4 ILE B 302  ARG B 309 -1  O  VAL B 303   N  LEU B 227           
SHEET    3   A 4 CYS B 275  VAL B 279 -1  N  LEU B 277   O  TYR B 306           
SHEET    4   A 4 VAL B 282  ASP B 283 -1  O  VAL B 282   N  VAL B 279           
SHEET    1   B 3 PHE B 254  ILE B 258  0                                        
SHEET    2   B 3 PHE B 236  ALA B 239 -1  N  ALA B 239   O  PHE B 254           
SHEET    3   B 3 VAL H2840  THR H2841 -1  O  THR H2841   N  ILE B 238           
SHEET    1   C 4 GLU A 221  GLU A 228  0                                        
SHEET    2   C 4 ILE A 302  ARG A 309 -1  O  LEU A 305   N  ILE A 225           
SHEET    3   C 4 CYS A 275  VAL A 279 -1  N  LEU A 277   O  TYR A 306           
SHEET    4   C 4 VAL A 282  ASP A 283 -1  O  VAL A 282   N  VAL A 279           
SHEET    1   D 3 PHE A 254  ILE A 258  0                                        
SHEET    2   D 3 PHE A 236  ALA A 239 -1  N  ALA A 239   O  PHE A 254           
SHEET    3   D 3 VAL G2840  SER G2842 -1  O  THR G2841   N  ILE A 238           
SHEET    1   E 4 GLU C 221  GLU C 228  0                                        
SHEET    2   E 4 ILE C 302  ARG C 309 -1  O  LEU C 305   N  ILE C 225           
SHEET    3   E 4 CYS C 275  VAL C 279 -1  N  LEU C 277   O  TYR C 306           
SHEET    4   E 4 VAL C 282  ASP C 283 -1  O  VAL C 282   N  VAL C 279           
SHEET    1   F 6 GLU C 221  GLU C 228  0                                        
SHEET    2   F 6 ILE C 302  ARG C 309 -1  O  LEU C 305   N  ILE C 225           
SHEET    3   F 6 CYS C 275  VAL C 279 -1  N  LEU C 277   O  TYR C 306           
SHEET    4   F 6 ILE C 253  ILE C 258 -1  N  ILE C 253   O  ILE C 276           
SHEET    5   F 6 PHE C 236  ALA C 239 -1  N  ALA C 239   O  PHE C 254           
SHEET    6   F 6 THR J2841  SER J2842 -1  O  THR J2841   N  ILE C 238           
SHEET    1   G 4 GLU D 221  GLU D 228  0                                        
SHEET    2   G 4 ILE D 302  ARG D 309 -1  O  LEU D 305   N  ILE D 225           
SHEET    3   G 4 CYS D 275  VAL D 279 -1  N  LEU D 277   O  TYR D 306           
SHEET    4   G 4 VAL D 282  ASP D 283 -1  O  VAL D 282   N  VAL D 279           
SHEET    1   H 2 PHE D 236  ALA D 239  0                                        
SHEET    2   H 2 PHE D 254  ILE D 258 -1  O  PHE D 254   N  ALA D 239           
SHEET    1   I 4 GLU E 221  GLU E 228  0                                        
SHEET    2   I 4 ILE E 302  ARG E 309 -1  O  VAL E 303   N  LEU E 227           
SHEET    3   I 4 CYS E 275  VAL E 279 -1  N  LEU E 277   O  TYR E 306           
SHEET    4   I 4 VAL E 282  ASP E 283 -1  O  VAL E 282   N  VAL E 279           
SHEET    1   J 6 GLU E 221  GLU E 228  0                                        
SHEET    2   J 6 ILE E 302  ARG E 309 -1  O  VAL E 303   N  LEU E 227           
SHEET    3   J 6 CYS E 275  VAL E 279 -1  N  LEU E 277   O  TYR E 306           
SHEET    4   J 6 ILE E 253  ILE E 258 -1  N  ILE E 253   O  ILE E 276           
SHEET    5   J 6 PHE E 236  ALA E 239 -1  N  SER E 237   O  LYS E 257           
SHEET    6   J 6 THR K2841  VAL K2843 -1  O  VAL K2843   N  PHE E 236           
SHEET    1   K 5 GLU F 221  GLU F 228  0                                        
SHEET    2   K 5 ILE F 302  ARG F 309 -1  O  LEU F 305   N  ILE F 225           
SHEET    3   K 5 CYS F 275  VAL F 279 -1  N  LEU F 277   O  TYR F 306           
SHEET    4   K 5 ILE F 253  ILE F 258 -1  N  ILE F 253   O  ILE F 276           
SHEET    5   K 5 PHE F 236  ALA F 239 -1  N  ALA F 239   O  PHE F 254           
SHEET    1   L 4 GLU F 221  GLU F 228  0                                        
SHEET    2   L 4 ILE F 302  ARG F 309 -1  O  LEU F 305   N  ILE F 225           
SHEET    3   L 4 CYS F 275  VAL F 279 -1  N  LEU F 277   O  TYR F 306           
SHEET    4   L 4 VAL F 282  ASP F 283 -1  O  VAL F 282   N  VAL F 279           
CISPEP   1 ASP F  249    ASP F  250          0         4.41                     
CRYST1  105.627  105.627   50.830  90.00  90.00 120.00 P 3          18          
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      0.009467  0.005466  0.000000        0.00000                         
SCALE2      0.000000  0.010932  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019673        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system