GenomeNet

Database: PDB
Entry: 3RL8
LinkDB: 3RL8
Original site: 3RL8 
HEADER    MEMBRANE PROTEIN/SIGNALING PROTEIN      19-APR-11   3RL8              
TITLE     CRYSTAL STRUCTURE OF HDLG1-PDZ2 COMPLEXED WITH APC                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DISKS LARGE HOMOLOG 1;                                     
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 FRAGMENT: UNP RESIDUES 315-410;                                      
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: F;                                                            
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 3RL8    1       TITLE                                    
REVDAT   1   14-DEC-11 3RL8    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.    2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 30711                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1545                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2108                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.29                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 126                          
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3507                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 286                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.51000                                             
REMARK   3    B22 (A**2) : 0.37000                                              
REMARK   3    B33 (A**2) : 2.05000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.23000                                             
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): 0.198         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.139         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.851        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3576 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4819 ; 1.306 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   469 ; 5.954 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   126 ;40.406 ;26.905       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   675 ;15.885 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   569 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2552 ; 0.005 ; 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):  2312 ; 0.449 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3714 ; 0.842 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1264 ; 1.508 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1103 ; 2.529 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E                       
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    317       A     405      4                      
REMARK   3           1     B    317       B     405      4                      
REMARK   3           1     C    317       C     405      4                      
REMARK   3           1     D    317       D     405      4                      
REMARK   3           1     E    317       E     405      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    653 ; 0.570 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    653 ; 0.550 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    653 ; 0.750 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):    653 ; 0.450 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):    653 ; 0.370 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    653 ; 1.000 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    653 ; 0.960 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    C (A**2):    653 ; 0.790 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    D (A**2):    653 ; 0.620 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    E (A**2):    653 ; 0.520 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   316        A   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.4883   5.4581  42.0125              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1693 T22:   0.0260                                     
REMARK   3      T33:   0.1462 T12:  -0.0048                                     
REMARK   3      T13:  -0.0487 T23:  -0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0496 L22:   3.2562                                     
REMARK   3      L33:   1.6170 L12:  -0.6752                                     
REMARK   3      L13:  -1.1211 L23:  -0.0178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0203 S12:   0.2372 S13:  -0.1639                       
REMARK   3      S21:  -0.2210 S22:   0.0673 S23:   0.2234                       
REMARK   3      S31:   0.2861 S32:   0.0381 S33:  -0.0470                       
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   316        B   405                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.0523   6.0989  41.1407              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1177 T22:   0.0206                                     
REMARK   3      T33:   0.1418 T12:   0.0181                                     
REMARK   3      T13:  -0.0063 T23:   0.0230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.3171 L22:   4.4867                                     
REMARK   3      L33:   1.2439 L12:   1.4452                                     
REMARK   3      L13:   1.6766 L23:   0.3877                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0882 S12:   0.3217 S13:   0.3777                       
REMARK   3      S21:   0.0684 S22:   0.0426 S23:  -0.2013                       
REMARK   3      S31:  -0.2369 S32:  -0.0518 S33:   0.0457                       
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   316        C   410                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.2410   8.7956  63.8628              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1804 T22:   0.2566                                     
REMARK   3      T33:   0.1221 T12:  -0.0156                                     
REMARK   3      T13:   0.0185 T23:   0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2474 L22:   2.6480                                     
REMARK   3      L33:   5.6620 L12:  -0.0316                                     
REMARK   3      L13:   1.5558 L23:  -0.0373                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0438 S12:  -0.6426 S13:  -0.1395                       
REMARK   3      S21:   0.1881 S22:   0.0046 S23:   0.1983                       
REMARK   3      S31:   0.1636 S32:  -0.4782 S33:  -0.0484                       
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   316        D   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.0424  20.1692  79.7109              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1507 T22:   0.3888                                     
REMARK   3      T33:   0.1554 T12:   0.0221                                     
REMARK   3      T13:  -0.0051 T23:  -0.0482                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.0597 L22:   4.0904                                     
REMARK   3      L33:   3.9069 L12:   0.9363                                     
REMARK   3      L13:   2.2009 L23:   1.5415                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0115 S12:  -0.9700 S13:   0.3414                       
REMARK   3      S21:   0.1897 S22:  -0.1347 S23:  -0.1176                       
REMARK   3      S31:  -0.0119 S32:  -0.0352 S33:   0.1232                       
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   316        E   405                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.1057  20.7229  79.1349              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2144 T22:   0.4815                                     
REMARK   3      T33:   0.3167 T12:   0.0145                                     
REMARK   3      T13:   0.0204 T23:  -0.0461                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  19.4618 L22:   1.5905                                     
REMARK   3      L33:   4.6954 L12:   1.2878                                     
REMARK   3      L13:  -2.6299 L23:   0.1915                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0960 S12:  -0.0081 S13:   0.7736                       
REMARK   3      S21:  -0.1065 S22:   0.2362 S23:   0.3158                       
REMARK   3      S31:   0.1088 S32:   0.0045 S33:  -0.1402                       
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  2838        F  2843                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.1838  -4.0696  48.9956              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3883 T22:   0.2755                                     
REMARK   3      T33:   0.3986 T12:   0.0947                                     
REMARK   3      T13:  -0.1830 T23:   0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  46.3981 L22:  50.4297                                     
REMARK   3      L33:  32.8998 L12: -33.7563                                     
REMARK   3      L13:  17.2550 L23:  -0.2484                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6677 S12:  -0.6898 S13:  -1.1980                       
REMARK   3      S21:   2.8535 S22:   1.5932 S23:  -1.6130                       
REMARK   3      S31:   1.4764 S32:   1.8893 S33:  -0.9255                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A   286                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.5764  10.3953  55.8690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3355 T22:   0.2545                                     
REMARK   3      T33:   0.3235 T12:   0.0127                                     
REMARK   3      T13:  -0.0131 T23:   0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3384 L22:   0.2511                                     
REMARK   3      L33:   0.3011 L12:   0.0411                                     
REMARK   3      L13:  -0.1060 L23:   0.0232                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0026 S12:  -0.3100 S13:   0.0105                       
REMARK   3      S21:   0.0264 S22:  -0.0271 S23:   0.0087                       
REMARK   3      S31:  -0.0142 S32:  -0.0245 S33:   0.0297                       
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 3RL8 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 RCSB065070.                                      
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   : 30730                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 85.380                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21600                            
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   (%): 52.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
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 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       26.25100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   306                                                      
REMARK 465     GLY A   307                                                      
REMARK 465     HIS A   308                                                      
REMARK 465     HIS A   309                                                      
REMARK 465     HIS A   310                                                      
REMARK 465     HIS A   311                                                      
REMARK 465     HIS A   312                                                      
REMARK 465     HIS A   313                                                      
REMARK 465     MET A   314                                                      
REMARK 465     GLU A   315                                                      
REMARK 465     MET A   410                                                      
REMARK 465     MET B   306                                                      
REMARK 465     GLY B   307                                                      
REMARK 465     HIS B   308                                                      
REMARK 465     HIS B   309                                                      
REMARK 465     HIS B   310                                                      
REMARK 465     HIS B   311                                                      
REMARK 465     HIS B   312                                                      
REMARK 465     HIS B   313                                                      
REMARK 465     MET B   314                                                      
REMARK 465     GLU B   315                                                      
REMARK 465     THR B   406                                                      
REMARK 465     SER B   407                                                      
REMARK 465     MET B   408                                                      
REMARK 465     TYR B   409                                                      
REMARK 465     MET B   410                                                      
REMARK 465     MET C   306                                                      
REMARK 465     GLY C   307                                                      
REMARK 465     HIS C   308                                                      
REMARK 465     HIS C   309                                                      
REMARK 465     HIS C   310                                                      
REMARK 465     HIS C   311                                                      
REMARK 465     HIS C   312                                                      
REMARK 465     HIS C   313                                                      
REMARK 465     MET C   314                                                      
REMARK 465     GLU C   315                                                      
REMARK 465     MET D   306                                                      
REMARK 465     GLY D   307                                                      
REMARK 465     HIS D   308                                                      
REMARK 465     HIS D   309                                                      
REMARK 465     HIS D   310                                                      
REMARK 465     HIS D   311                                                      
REMARK 465     HIS D   312                                                      
REMARK 465     HIS D   313                                                      
REMARK 465     MET D   314                                                      
REMARK 465     GLU D   315                                                      
REMARK 465     MET D   410                                                      
REMARK 465     MET E   306                                                      
REMARK 465     GLY E   307                                                      
REMARK 465     HIS E   308                                                      
REMARK 465     HIS E   309                                                      
REMARK 465     HIS E   310                                                      
REMARK 465     HIS E   311                                                      
REMARK 465     HIS E   312                                                      
REMARK 465     HIS E   313                                                      
REMARK 465     MET E   314                                                      
REMARK 465     GLU E   315                                                      
REMARK 465     THR E   406                                                      
REMARK 465     SER E   407                                                      
REMARK 465     MET E   408                                                      
REMARK 465     TYR E   409                                                      
REMARK 465     MET E   410                                                      
REMARK 465     ARG F  2833                                                      
REMARK 465     HIS F  2834                                                      
REMARK 465     SER F  2835                                                      
REMARK 465     GLY F  2836                                                      
REMARK 465     SER F  2837                                                      
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 C 410    CG   SD   CE                                        
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    ASN A 339       56.83   -143.85                                   
REMARK 500    ASN A 375     -127.02     49.84                                   
REMARK 500    ASN A 393       41.99    -79.16                                   
REMARK 500    SER A 395     -149.27   -103.59                                   
REMARK 500    ASN B 339       49.43   -151.57                                   
REMARK 500    ASN C 339       47.23   -144.26                                   
REMARK 500    TYR C 409       -8.52     82.09                                   
REMARK 500    ASN D 339       51.14   -140.83                                   
REMARK 500    ASN D 376       -6.14     74.59                                   
REMARK 500    SER D 407     -154.70   -106.63                                   
REMARK 500    ASN E 339       56.52   -141.28                                   
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 A 254        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH A 266        DISTANCE =  6.54 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3RL7   RELATED DB: PDB                                   
DBREF  3RL8 A  315   410  UNP    Q12959   DLG1_HUMAN     315    410             
DBREF  3RL8 B  315   410  UNP    Q12959   DLG1_HUMAN     315    410             
DBREF  3RL8 C  315   410  UNP    Q12959   DLG1_HUMAN     315    410             
DBREF  3RL8 D  315   410  UNP    Q12959   DLG1_HUMAN     315    410             
DBREF  3RL8 E  315   410  UNP    Q12959   DLG1_HUMAN     315    410             
DBREF  3RL8 F 2833  2843  UNP    P25054   APC_HUMAN     2833   2843             
SEQADV 3RL8 MET A  306  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 GLY A  307  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS A  308  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS A  309  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS A  310  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS A  311  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS A  312  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS A  313  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 MET A  314  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 MET B  306  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 GLY B  307  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS B  308  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS B  309  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS B  310  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS B  311  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS B  312  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS B  313  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 MET B  314  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 MET C  306  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 GLY C  307  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS C  308  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS C  309  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS C  310  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS C  311  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS C  312  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS C  313  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 MET C  314  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 MET D  306  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 GLY D  307  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS D  308  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS D  309  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS D  310  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS D  311  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS D  312  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS D  313  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 MET D  314  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 MET E  306  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 GLY E  307  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS E  308  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS E  309  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS E  310  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS E  311  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS E  312  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 HIS E  313  UNP  Q12959              EXPRESSION TAG                 
SEQADV 3RL8 MET E  314  UNP  Q12959              EXPRESSION TAG                 
SEQRES   1 A  105  MET GLY HIS HIS HIS HIS HIS HIS MET GLU LYS ILE MET          
SEQRES   2 A  105  GLU ILE LYS LEU ILE LYS GLY PRO LYS GLY LEU GLY PHE          
SEQRES   3 A  105  SER ILE ALA GLY GLY VAL GLY ASN GLN HIS ILE PRO GLY          
SEQRES   4 A  105  ASP ASN SER ILE TYR VAL THR LYS ILE ILE GLU GLY GLY          
SEQRES   5 A  105  ALA ALA HIS LYS ASP GLY LYS LEU GLN ILE GLY ASP LYS          
SEQRES   6 A  105  LEU LEU ALA VAL ASN ASN VAL CYS LEU GLU GLU VAL THR          
SEQRES   7 A  105  HIS GLU GLU ALA VAL THR ALA LEU LYS ASN THR SER ASP          
SEQRES   8 A  105  PHE VAL TYR LEU LYS VAL ALA LYS PRO THR SER MET TYR          
SEQRES   9 A  105  MET                                                          
SEQRES   1 B  105  MET GLY HIS HIS HIS HIS HIS HIS MET GLU LYS ILE MET          
SEQRES   2 B  105  GLU ILE LYS LEU ILE LYS GLY PRO LYS GLY LEU GLY PHE          
SEQRES   3 B  105  SER ILE ALA GLY GLY VAL GLY ASN GLN HIS ILE PRO GLY          
SEQRES   4 B  105  ASP ASN SER ILE TYR VAL THR LYS ILE ILE GLU GLY GLY          
SEQRES   5 B  105  ALA ALA HIS LYS ASP GLY LYS LEU GLN ILE GLY ASP LYS          
SEQRES   6 B  105  LEU LEU ALA VAL ASN ASN VAL CYS LEU GLU GLU VAL THR          
SEQRES   7 B  105  HIS GLU GLU ALA VAL THR ALA LEU LYS ASN THR SER ASP          
SEQRES   8 B  105  PHE VAL TYR LEU LYS VAL ALA LYS PRO THR SER MET TYR          
SEQRES   9 B  105  MET                                                          
SEQRES   1 C  105  MET GLY HIS HIS HIS HIS HIS HIS MET GLU LYS ILE MET          
SEQRES   2 C  105  GLU ILE LYS LEU ILE LYS GLY PRO LYS GLY LEU GLY PHE          
SEQRES   3 C  105  SER ILE ALA GLY GLY VAL GLY ASN GLN HIS ILE PRO GLY          
SEQRES   4 C  105  ASP ASN SER ILE TYR VAL THR LYS ILE ILE GLU GLY GLY          
SEQRES   5 C  105  ALA ALA HIS LYS ASP GLY LYS LEU GLN ILE GLY ASP LYS          
SEQRES   6 C  105  LEU LEU ALA VAL ASN ASN VAL CYS LEU GLU GLU VAL THR          
SEQRES   7 C  105  HIS GLU GLU ALA VAL THR ALA LEU LYS ASN THR SER ASP          
SEQRES   8 C  105  PHE VAL TYR LEU LYS VAL ALA LYS PRO THR SER MET TYR          
SEQRES   9 C  105  MET                                                          
SEQRES   1 D  105  MET GLY HIS HIS HIS HIS HIS HIS MET GLU LYS ILE MET          
SEQRES   2 D  105  GLU ILE LYS LEU ILE LYS GLY PRO LYS GLY LEU GLY PHE          
SEQRES   3 D  105  SER ILE ALA GLY GLY VAL GLY ASN GLN HIS ILE PRO GLY          
SEQRES   4 D  105  ASP ASN SER ILE TYR VAL THR LYS ILE ILE GLU GLY GLY          
SEQRES   5 D  105  ALA ALA HIS LYS ASP GLY LYS LEU GLN ILE GLY ASP LYS          
SEQRES   6 D  105  LEU LEU ALA VAL ASN ASN VAL CYS LEU GLU GLU VAL THR          
SEQRES   7 D  105  HIS GLU GLU ALA VAL THR ALA LEU LYS ASN THR SER ASP          
SEQRES   8 D  105  PHE VAL TYR LEU LYS VAL ALA LYS PRO THR SER MET TYR          
SEQRES   9 D  105  MET                                                          
SEQRES   1 E  105  MET GLY HIS HIS HIS HIS HIS HIS MET GLU LYS ILE MET          
SEQRES   2 E  105  GLU ILE LYS LEU ILE LYS GLY PRO LYS GLY LEU GLY PHE          
SEQRES   3 E  105  SER ILE ALA GLY GLY VAL GLY ASN GLN HIS ILE PRO GLY          
SEQRES   4 E  105  ASP ASN SER ILE TYR VAL THR LYS ILE ILE GLU GLY GLY          
SEQRES   5 E  105  ALA ALA HIS LYS ASP GLY LYS LEU GLN ILE GLY ASP LYS          
SEQRES   6 E  105  LEU LEU ALA VAL ASN ASN VAL CYS LEU GLU GLU VAL THR          
SEQRES   7 E  105  HIS GLU GLU ALA VAL THR ALA LEU LYS ASN THR SER ASP          
SEQRES   8 E  105  PHE VAL TYR LEU LYS VAL ALA LYS PRO THR SER MET TYR          
SEQRES   9 E  105  MET                                                          
SEQRES   1 F   11  ARG HIS SER GLY SER TYR LEU VAL THR SER VAL                  
FORMUL   7  HOH   *286(H2 O)                                                    
HELIX    1   1 GLY A  357  GLY A  363  1                                   7    
HELIX    2   2 THR A  383  ASN A  393  1                                  11    
HELIX    3   3 GLY B  357  GLY B  363  1                                   7    
HELIX    4   4 THR B  383  ASN B  393  1                                  11    
HELIX    5   5 GLY C  357  GLY C  363  1                                   7    
HELIX    6   6 THR C  383  ASN C  393  1                                  11    
HELIX    7   7 GLY D  357  GLY D  363  1                                   7    
HELIX    8   8 THR D  383  ASN D  393  1                                  11    
HELIX    9   9 GLY E  357  GLY E  363  1                                   7    
HELIX   10  10 THR E  383  ASN E  393  1                                  11    
SHEET    1   A 5 ILE A 317  ILE A 323  0                                        
SHEET    2   A 5 PHE A 397  ALA A 403 -1  O  LEU A 400   N  ILE A 320           
SHEET    3   A 5 LYS A 370  VAL A 374 -1  N  LYS A 370   O  ALA A 403           
SHEET    4   A 5 ILE A 348  ILE A 353 -1  N  ILE A 348   O  LEU A 371           
SHEET    5   A 5 PHE A 331  GLY A 335 -1  N  ALA A 334   O  TYR A 349           
SHEET    1   B 4 ILE A 317  ILE A 323  0                                        
SHEET    2   B 4 PHE A 397  ALA A 403 -1  O  LEU A 400   N  ILE A 320           
SHEET    3   B 4 LYS A 370  VAL A 374 -1  N  LYS A 370   O  ALA A 403           
SHEET    4   B 4 VAL A 377  CYS A 378 -1  O  VAL A 377   N  VAL A 374           
SHEET    1   C 5 ILE B 317  ILE B 323  0                                        
SHEET    2   C 5 PHE B 397  ALA B 403 -1  O  LEU B 400   N  ILE B 320           
SHEET    3   C 5 LYS B 370  VAL B 374 -1  N  LEU B 372   O  LYS B 401           
SHEET    4   C 5 ILE B 348  ILE B 353 -1  N  ILE B 348   O  LEU B 371           
SHEET    5   C 5 PHE B 331  GLY B 335 -1  N  ALA B 334   O  TYR B 349           
SHEET    1   D 4 ILE B 317  ILE B 323  0                                        
SHEET    2   D 4 PHE B 397  ALA B 403 -1  O  LEU B 400   N  ILE B 320           
SHEET    3   D 4 LYS B 370  VAL B 374 -1  N  LEU B 372   O  LYS B 401           
SHEET    4   D 4 VAL B 377  CYS B 378 -1  O  VAL B 377   N  VAL B 374           
SHEET    1   E 5 ILE C 317  ILE C 323  0                                        
SHEET    2   E 5 PHE C 397  ALA C 403 -1  O  VAL C 402   N  MET C 318           
SHEET    3   E 5 LYS C 370  VAL C 374 -1  N  LEU C 372   O  LYS C 401           
SHEET    4   E 5 ILE C 348  ILE C 353 -1  N  ILE C 348   O  LEU C 371           
SHEET    5   E 5 PHE C 331  GLY C 335 -1  N  ALA C 334   O  TYR C 349           
SHEET    1   F 4 ILE C 317  ILE C 323  0                                        
SHEET    2   F 4 PHE C 397  ALA C 403 -1  O  VAL C 402   N  MET C 318           
SHEET    3   F 4 LYS C 370  VAL C 374 -1  N  LEU C 372   O  LYS C 401           
SHEET    4   F 4 VAL C 377  CYS C 378 -1  O  VAL C 377   N  VAL C 374           
SHEET    1   G 5 ILE D 317  ILE D 323  0                                        
SHEET    2   G 5 PHE D 397  ALA D 403 -1  O  LEU D 400   N  ILE D 320           
SHEET    3   G 5 LYS D 370  VAL D 374 -1  N  LEU D 372   O  LYS D 401           
SHEET    4   G 5 ILE D 348  ILE D 353 -1  N  ILE D 348   O  LEU D 371           
SHEET    5   G 5 PHE D 331  GLY D 335 -1  N  ALA D 334   O  TYR D 349           
SHEET    1   H 4 ILE D 317  ILE D 323  0                                        
SHEET    2   H 4 PHE D 397  ALA D 403 -1  O  LEU D 400   N  ILE D 320           
SHEET    3   H 4 LYS D 370  VAL D 374 -1  N  LEU D 372   O  LYS D 401           
SHEET    4   H 4 VAL D 377  CYS D 378 -1  O  VAL D 377   N  VAL D 374           
SHEET    1   I 5 ILE E 317  ILE E 323  0                                        
SHEET    2   I 5 PHE E 397  ALA E 403 -1  O  LEU E 400   N  ILE E 320           
SHEET    3   I 5 LYS E 370  VAL E 374 -1  N  LEU E 372   O  LYS E 401           
SHEET    4   I 5 ILE E 348  ILE E 353 -1  N  ILE E 348   O  LEU E 371           
SHEET    5   I 5 PHE E 331  GLY E 335 -1  N  ALA E 334   O  TYR E 349           
SHEET    1   J 4 ILE E 317  ILE E 323  0                                        
SHEET    2   J 4 PHE E 397  ALA E 403 -1  O  LEU E 400   N  ILE E 320           
SHEET    3   J 4 LYS E 370  VAL E 374 -1  N  LEU E 372   O  LYS E 401           
SHEET    4   J 4 VAL E 377  CYS E 378 -1  O  VAL E 377   N  VAL E 374           
CRYST1   67.806   52.502   87.426  90.00 102.42  90.00 P 1 21 1     10          
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      0.014748  0.000000  0.003247        0.00000                         
SCALE2      0.000000  0.019047  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011712        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system