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Database: PDB
Entry: 3A7Q
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HEADER    SIGNALING PROTEIN                       01-OCT-09   3A7Q              
TITLE     STRUCTURAL BASIS FOR SPECIFIC RECOGNITION OF REELIN BY ITS RECEPTORS  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: REELIN;                                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: REPEAT 5-6 FRAGMENT, UNP RESIDUES 1948-2661;               
COMPND   5 SYNONYM: REELER PROTEIN;                                             
COMPND   6 EC: 3.4.21.-;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 8;        
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: LA1 MODULE, UNP RESIDUES 42-83;                            
COMPND  13 SYNONYM: APOLIPOPROTEIN E RECEPTOR 2;                                
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: RELN;                                                          
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: LEC 3.2.8.1;                               
SOURCE  10 EXPRESSION_SYSTEM_CELL_LINE: CHO CELLS;                              
SOURCE  11 EXPRESSION_SYSTEM_TISSUE: OVARY;                                     
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1;                                 
SOURCE  14 MOL_ID: 2;                                                           
SOURCE  15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  16 ORGANISM_COMMON: HUMAN;                                              
SOURCE  17 ORGANISM_TAXID: 9606;                                                
SOURCE  18 GENE: APOER2;                                                        
SOURCE  19 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  21 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  22 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  23 EXPRESSION_SYSTEM_PLASMID: PGEX-3T                                   
KEYWDS    SIGNALING PROTEIN                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.YASUI,T.NOGI,J.TAKAGI                                               
REVDAT   2   13-JUL-11 3A7Q    1       VERSN                                    
REVDAT   1   23-MAR-10 3A7Q    0                                                
JRNL        AUTH   N.YASUI,T.NOGI,J.TAKAGI                                      
JRNL        TITL   STRUCTURAL BASIS FOR SPECIFIC RECOGNITION OF REELIN BY ITS   
JRNL        TITL 2 RECEPTORS                                                    
JRNL        REF    STRUCTURE                     V.  18   320 2010              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   20223215                                                     
JRNL        DOI    10.1016/J.STR.2010.01.010                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 20837                          
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) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.296                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1135                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1554                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.45                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2550                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 87                           
REMARK   3   BIN FREE R VALUE                    : 0.3010                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5696                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 76                                      
REMARK   3   SOLVENT ATOMS            : 19                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 56.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.85000                                             
REMARK   3    B22 (A**2) : -1.77000                                             
REMARK   3    B33 (A**2) : 2.67000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -4.93000                                             
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): 0.418         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.301         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.323        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.924                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.866                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5974 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8116 ; 1.229 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   719 ; 6.875 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   289 ;32.980 ;23.875       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   910 ;15.832 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    38 ;16.151 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   867 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4612 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2471 ; 0.207 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4035 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   227 ; 0.145 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     6 ; 0.161 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    74 ; 0.197 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.121 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3697 ; 0.378 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5784 ; 0.642 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2634 ; 0.927 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2332 ; 1.459 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1953        A  2131                          
REMARK   3    RESIDUE RANGE :   A  4001        A  4001                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.8971  -2.4211   5.5661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2733 T22:  -0.1680                                     
REMARK   3      T33:  -0.3190 T12:  -0.0155                                     
REMARK   3      T13:   0.0519 T23:  -0.0089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5497 L22:   6.3559                                     
REMARK   3      L33:   3.4678 L12:  -0.2880                                     
REMARK   3      L13:   1.8424 L23:  -0.1662                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1098 S12:  -0.2466 S13:   0.0810                       
REMARK   3      S21:  -0.0028 S22:  -0.0588 S23:  -0.0583                       
REMARK   3      S31:  -0.1083 S32:   0.0153 S33:   0.1686                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  2132        A  2165                          
REMARK   3    RESIDUE RANGE :   A  3001        A  3001                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.1302  16.2989  16.4798              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2594 T22:  -0.0115                                     
REMARK   3      T33:   0.2722 T12:   0.0568                                     
REMARK   3      T13:  -0.2194 T23:  -0.2479                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.0174 L22:   0.4218                                     
REMARK   3      L33:  12.4298 L12:  -2.2515                                     
REMARK   3      L13:   9.7769 L23:  -1.8271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.3610 S12:  -1.0949 S13:   1.5449                       
REMARK   3      S21:   0.2301 S22:   0.1071 S23:  -0.0005                       
REMARK   3      S31:  -0.7173 S32:   0.0073 S33:   1.2539                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  2166        A  2319                          
REMARK   3    RESIDUE RANGE :   A  4002        A  4002                          
REMARK   3    RESIDUE RANGE :   A  3002        A  3004                          
REMARK   3    RESIDUE RANGE :   A  6001        A  6001                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0161  -1.4843  16.7991              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1638 T22:  -0.1494                                     
REMARK   3      T33:  -0.0791 T12:  -0.0186                                     
REMARK   3      T13:  -0.0623 T23:   0.0247                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1253 L22:   5.4448                                     
REMARK   3      L33:   4.9103 L12:  -2.0471                                     
REMARK   3      L13:   1.8076 L23:   1.8874                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3012 S12:   0.1522 S13:  -0.7750                       
REMARK   3      S21:  -0.1278 S22:  -0.1314 S23:   0.2365                       
REMARK   3      S31:   0.1972 S32:   0.1189 S33:  -0.1699                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  2320        A  2480                          
REMARK   3    RESIDUE RANGE :   A  4003        A  4003                          
REMARK   3    RESIDUE RANGE :   A  4005        A  4005                          
REMARK   3    RESIDUE RANGE :   A  6002        A  6002                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.7028   2.8320  39.2105              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1513 T22:  -0.0523                                     
REMARK   3      T33:  -0.2457 T12:  -0.0050                                     
REMARK   3      T13:   0.0569 T23:  -0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8891 L22:   4.3154                                     
REMARK   3      L33:   3.6962 L12:   0.7891                                     
REMARK   3      L13:   0.6743 L23:  -1.3123                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1439 S12:   0.1682 S13:  -0.0692                       
REMARK   3      S21:  -0.1108 S22:   0.1401 S23:  -0.2591                       
REMARK   3      S31:   0.1181 S32:   0.2565 S33:   0.0037                       
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 :   A  2481        A  2515                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.5795  18.2298  55.2556              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0691 T22:   0.0057                                     
REMARK   3      T33:  -0.1419 T12:   0.0779                                     
REMARK   3      T13:   0.0854 T23:  -0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  18.5747 L22:   4.1113                                     
REMARK   3      L33:  16.0162 L12:   2.4350                                     
REMARK   3      L13:  13.4372 L23:   4.4924                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2580 S12:  -0.8184 S13:   0.8081                       
REMARK   3      S21:   0.1376 S22:  -0.0385 S23:   0.1684                       
REMARK   3      S31:  -0.4700 S32:  -0.2609 S33:   0.2965                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  2516        A  2662                          
REMARK   3    RESIDUE RANGE :   A  4004        A  4004                          
REMARK   3    RESIDUE RANGE :   A  3005        A  3005                          
REMARK   3    RESIDUE RANGE :   A  6003        A  6003                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.4629   2.6871  53.2275              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1891 T22:  -0.1482                                     
REMARK   3      T33:  -0.2249 T12:  -0.0140                                     
REMARK   3      T13:   0.0381 T23:  -0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2941 L22:   5.2803                                     
REMARK   3      L33:   2.6328 L12:  -2.5332                                     
REMARK   3      L13:   1.2399 L23:   0.8147                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0148 S12:   0.0050 S13:   0.0996                       
REMARK   3      S21:   0.1137 S22:   0.1310 S23:  -0.4109                       
REMARK   3      S31:   0.0698 S32:   0.0227 S33:  -0.1162                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    47        B    81                          
REMARK   3    RESIDUE RANGE :   B  5001        B  5001                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.1376 -21.1302  52.1721              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1412 T22:  -0.0349                                     
REMARK   3      T33:   0.0948 T12:   0.0006                                     
REMARK   3      T13:   0.0394 T23:  -0.0662                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0956 L22:  13.0205                                     
REMARK   3      L33:   8.8147 L12:  -2.2281                                     
REMARK   3      L13:  -2.7718 L23:  -6.5080                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5985 S12:  -0.1761 S13:  -0.8078                       
REMARK   3      S21:   0.4643 S22:   0.3075 S23:   1.4342                       
REMARK   3      S31:  -0.0553 S32:  -0.2475 S33:   0.2910                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3A7Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-OCT-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB028916.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-OCT-06                          
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               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL44XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.90                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : BRUKER DIP-6040                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21990                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.930                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : 0.07400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.37400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2E26                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 36-38% MPD, 21-25% PEG 1000, 100MM       
REMARK 280  HEPES-NA PH7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       46.92200            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A  1946                                                      
REMARK 465     ARG A  1947                                                      
REMARK 465     ASP A  1948                                                      
REMARK 465     GLY A  1949                                                      
REMARK 465     ASN A  1950                                                      
REMARK 465     ASN A  1951                                                      
REMARK 465     LEU A  1952                                                      
REMARK 465     SER A  1987                                                      
REMARK 465     LYS A  1988                                                      
REMARK 465     GLY A  1989                                                      
REMARK 465     ALA A  1990                                                      
REMARK 465     PRO A  1991                                                      
REMARK 465     GLU A  1992                                                      
REMARK 465     GLU A  1993                                                      
REMARK 465     TYR A  2060                                                      
REMARK 465     HIS A  2061                                                      
REMARK 465     SER A  2062                                                      
REMARK 465     SER A  2063                                                      
REMARK 465     SER A  2064                                                      
REMARK 465     LEU A  2065                                                      
REMARK 465     VAL A  2066                                                      
REMARK 465     SER A  2067                                                      
REMARK 465     SER A  2068                                                      
REMARK 465     LEU A  2069                                                      
REMARK 465     CYS A  2070                                                      
REMARK 465     SER A  2071                                                      
REMARK 465     THR A  2072                                                      
REMARK 465     GLU A  2073                                                      
REMARK 465     GLN A  2177                                                      
REMARK 465     LEU A  2178                                                      
REMARK 465     GLU A  2179                                                      
REMARK 465     SER A  2180                                                      
REMARK 465     ARG A  2663                                                      
REMARK 465     LEU A  2664                                                      
REMARK 465     GLU A  2665                                                      
REMARK 465     ASN A  2666                                                      
REMARK 465     LEU A  2667                                                      
REMARK 465     TYR A  2668                                                      
REMARK 465     PHE A  2669                                                      
REMARK 465     GLN A  2670                                                      
REMARK 465     GLY B    40                                                      
REMARK 465     SER B    41                                                      
REMARK 465     GLY B    42                                                      
REMARK 465     PRO B    43                                                      
REMARK 465     ALA B    44                                                      
REMARK 465     LYS B    45                                                      
REMARK 465     GLU B    46                                                      
REMARK 465     PRO B    82                                                      
REMARK 465     LYS B    83                                                      
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 A2186    CG   SD   CE                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN A  2569     C2   NAG A  3005              2.11            
REMARK 500   ND2  ASN A  2317     C2   NAG A  3004              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A1962       25.39     44.03                                   
REMARK 500    PHE A1964       56.15   -155.59                                   
REMARK 500    PRO A1984       57.56    -63.57                                   
REMARK 500    PRO A2057      178.36    -56.74                                   
REMARK 500    SER A2078       49.91    -76.33                                   
REMARK 500    GLU A2135       15.98     52.79                                   
REMARK 500    TYR A2138       15.87     52.96                                   
REMARK 500    ASN A2145        5.76     56.41                                   
REMARK 500    PRO A2158        1.98    -61.10                                   
REMARK 500    LYS A2165      107.26    -50.13                                   
REMARK 500    PHE A2174       11.67     59.18                                   
REMARK 500    ASN A2272       18.98    -62.83                                   
REMARK 500    SER A2289       56.77   -163.98                                   
REMARK 500    SER A2298      141.71   -172.96                                   
REMARK 500    HIS A2339       57.62   -143.07                                   
REMARK 500    CYS A2348       40.90     70.62                                   
REMARK 500    ALA A2385     -133.62    -86.19                                   
REMARK 500    ASP A2414      102.93    -51.64                                   
REMARK 500    PRO A2417       28.37    -59.93                                   
REMARK 500    GLU A2421      -19.62    -41.38                                   
REMARK 500    ASP A2484       -7.48     72.25                                   
REMARK 500    MET A2485       31.85     70.56                                   
REMARK 500    ALA A2548      -67.19   -108.12                                   
REMARK 500    SER A2556       17.67   -144.86                                   
REMARK 500    CYS A2559     -117.34   -113.42                                   
REMARK 500    LEU A2585      -70.63   -111.93                                   
REMARK 500    ALA A2636       82.62   -152.19                                   
REMARK 500    ASP B  50       18.46    -69.54                                   
REMARK 500    GLU B  57      -15.79     77.59                                   
REMARK 500    LEU B  73       -0.69     87.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A1961   O                                                      
REMARK 620 2 ASP A1963   OD2  73.5                                              
REMARK 620 3 SER A1995   O    95.2  97.2                                        
REMARK 620 4 ASP A2125   OD1  83.6 157.0  86.9                                  
REMARK 620 5 ASP A2125   OD2 133.2 152.6  76.9  50.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A2173   O                                                      
REMARK 620 2 GLU A2175   OE2  78.1                                              
REMARK 620 3 ASN A2202   O    85.1  79.1                                        
REMARK 620 4 ASP A2310   OD1  78.6 156.3  94.9                                  
REMARK 620 5 ASP A2310   OD2 134.9 145.7  93.0  56.7                            
REMARK 620 6 HOH A6001   O   155.2  77.8  84.6 124.8  68.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A2327   O                                                      
REMARK 620 2 THR A2351   O   140.3                                              
REMARK 620 3 ASP A2353   O    79.5 100.4                                        
REMARK 620 4 ASP A2474   OD1  79.0 138.9  98.4                                  
REMARK 620 5 ASP A2474   OD2 132.1  87.5  91.5  55.7                            
REMARK 620 6 HOH A6002   O   101.5  74.6 173.4  88.2  92.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A4004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A2522   O                                                      
REMARK 620 2 ASN A2524   OD1  70.8                                              
REMARK 620 3 SER A2549   O   161.8  95.6                                        
REMARK 620 4 LEU A2551   O    99.2  96.2  94.1                                  
REMARK 620 5 ASP A2657   OD1 123.8 163.5  68.4  89.2                            
REMARK 620 6 ASP A2657   OD2  69.6 139.9 121.5  95.6  54.3                      
REMARK 620 7 HOH A6003   O    91.0  83.4  75.1 169.1  88.4  91.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B5001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP B  64   O                                                      
REMARK 620 2 ASP B  67   OD2  82.9                                              
REMARK 620 3 ASP B  69   O   168.8  85.9                                        
REMARK 620 4 ASP B  71   OD2  94.8  90.6  84.5                                  
REMARK 620 5 ASP B  77   OD2 108.0 168.3  83.1  84.5                            
REMARK 620 6 GLU B  78   OE2  97.9  80.1  80.9 163.3 101.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A4005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A2399   OE2                                                    
REMARK 620 2 HIS A2460   ND1 128.4                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 4001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 4002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 4003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 4004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 4005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 5001                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE IS BASED ON REFERENCE 1, 2, 3, 5 AND 12 IN THE          
REMARK 999 DATABASE UNIPROTKB/SWISS-PROT Q14114 (LRP8_HUMAN). D46E IS NATURAL   
REMARK 999 VARIENT OF LRP8_HUMAN.                                               
DBREF  3A7Q A 1948  2661  UNP    Q60841   RELN_MOUSE    1948   2661             
DBREF  3A7Q B   42    83  UNP    Q14114   LRP8_HUMAN      42     83             
SEQADV 3A7Q GLY A 1946  UNP  Q60841              EXPRESSION TAG                 
SEQADV 3A7Q ARG A 1947  UNP  Q60841              EXPRESSION TAG                 
SEQADV 3A7Q ALA A 2101  UNP  Q60841    CYS  2101 ENGINEERED                     
SEQADV 3A7Q SER A 2662  UNP  Q60841              EXPRESSION TAG                 
SEQADV 3A7Q ARG A 2663  UNP  Q60841              EXPRESSION TAG                 
SEQADV 3A7Q LEU A 2664  UNP  Q60841              EXPRESSION TAG                 
SEQADV 3A7Q GLU A 2665  UNP  Q60841              EXPRESSION TAG                 
SEQADV 3A7Q ASN A 2666  UNP  Q60841              EXPRESSION TAG                 
SEQADV 3A7Q LEU A 2667  UNP  Q60841              EXPRESSION TAG                 
SEQADV 3A7Q TYR A 2668  UNP  Q60841              EXPRESSION TAG                 
SEQADV 3A7Q PHE A 2669  UNP  Q60841              EXPRESSION TAG                 
SEQADV 3A7Q GLN A 2670  UNP  Q60841              EXPRESSION TAG                 
SEQADV 3A7Q GLY B   40  UNP  Q14114              EXPRESSION TAG                 
SEQADV 3A7Q SER B   41  UNP  Q14114              EXPRESSION TAG                 
SEQADV 3A7Q GLU B   46  UNP  Q14114    ASP    46 SEE REMARK 999                 
SEQRES   1 A  725  GLY ARG ASP GLY ASN ASN LEU ASN ASN PRO VAL LEU LEU          
SEQRES   2 A  725  LEU ASP THR PHE ASP PHE GLY PRO ARG GLU ASP ASN TRP          
SEQRES   3 A  725  PHE PHE TYR PRO GLY GLY ASN ILE GLY LEU TYR CYS PRO          
SEQRES   4 A  725  TYR SER SER LYS GLY ALA PRO GLU GLU ASP SER ALA MET          
SEQRES   5 A  725  VAL PHE VAL SER ASN GLU VAL GLY GLU HIS SER ILE THR          
SEQRES   6 A  725  THR ARG ASP LEU SER VAL ASN GLU ASN THR ILE ILE GLN          
SEQRES   7 A  725  PHE GLU ILE ASN VAL GLY CYS SER THR ASP SER SER SER          
SEQRES   8 A  725  ALA ASP PRO VAL ARG LEU GLU PHE SER ARG ASP PHE GLY          
SEQRES   9 A  725  ALA THR TRP HIS LEU LEU LEU PRO LEU CYS TYR HIS SER          
SEQRES  10 A  725  SER SER LEU VAL SER SER LEU CYS SER THR GLU HIS HIS          
SEQRES  11 A  725  PRO SER SER THR TYR TYR ALA GLY THR THR GLN GLY TRP          
SEQRES  12 A  725  ARG ARG GLU VAL VAL HIS PHE GLY LYS LEU HIS LEU ALA          
SEQRES  13 A  725  GLY SER VAL ARG PHE ARG TRP TYR GLN GLY PHE TYR PRO          
SEQRES  14 A  725  ALA GLY SER GLN PRO VAL THR TRP ALA ILE ASP ASN VAL          
SEQRES  15 A  725  TYR ILE GLY PRO GLN CYS GLU GLU MET CYS TYR GLY HIS          
SEQRES  16 A  725  GLY SER CYS ILE ASN GLY THR LYS CYS ILE CYS ASP PRO          
SEQRES  17 A  725  GLY TYR SER GLY PRO THR CYS LYS ILE SER THR LYS ASN          
SEQRES  18 A  725  PRO ASP PHE LEU LYS ASP ASP PHE GLU GLY GLN LEU GLU          
SEQRES  19 A  725  SER ASP ARG PHE LEU LEU MET SER GLY GLY LYS PRO SER          
SEQRES  20 A  725  ARG LYS CYS GLY ILE LEU SER SER GLY ASN ASN LEU PHE          
SEQRES  21 A  725  PHE ASN GLU ASP GLY LEU ARG MET LEU VAL THR ARG ASP          
SEQRES  22 A  725  LEU ASP LEU SER HIS ALA ARG PHE VAL GLN PHE PHE MET          
SEQRES  23 A  725  ARG LEU GLY CYS GLY LYS GLY VAL PRO ASP PRO ARG SER          
SEQRES  24 A  725  GLN PRO VAL LEU LEU GLN TYR SER LEU ASN GLY GLY LEU          
SEQRES  25 A  725  SER TRP SER LEU LEU GLN GLU PHE LEU PHE SER ASN SER          
SEQRES  26 A  725  SER ASN VAL GLY ARG TYR ILE ALA LEU GLU MET PRO LEU          
SEQRES  27 A  725  LYS ALA ARG SER GLY SER THR ARG LEU ARG TRP TRP GLN          
SEQRES  28 A  725  PRO SER GLU ASN GLY HIS PHE TYR SER PRO TRP VAL ILE          
SEQRES  29 A  725  ASP GLN ILE LEU ILE GLY GLY ASN ILE SER GLY ASN THR          
SEQRES  30 A  725  VAL LEU GLU ASP ASP PHE SER THR LEU ASP SER ARG LYS          
SEQRES  31 A  725  TRP LEU LEU HIS PRO GLY GLY THR LYS MET PRO VAL CYS          
SEQRES  32 A  725  GLY SER THR GLY ASP ALA LEU VAL PHE ILE GLU LYS ALA          
SEQRES  33 A  725  SER THR ARG TYR VAL VAL THR THR ASP ILE ALA VAL ASN          
SEQRES  34 A  725  GLU ASP SER PHE LEU GLN ILE ASP PHE ALA ALA SER CYS          
SEQRES  35 A  725  SER VAL THR ASP SER CYS TYR ALA ILE GLU LEU GLU TYR          
SEQRES  36 A  725  SER VAL ASP LEU GLY LEU SER TRP HIS PRO LEU VAL ARG          
SEQRES  37 A  725  ASP CYS LEU PRO THR ASN VAL GLU CYS SER ARG TYR HIS          
SEQRES  38 A  725  LEU GLN ARG ILE LEU VAL SER ASP THR PHE ASN LYS TRP          
SEQRES  39 A  725  THR ARG ILE THR LEU PRO LEU PRO SER TYR THR ARG SER          
SEQRES  40 A  725  GLN ALA THR ARG PHE ARG TRP HIS GLN PRO ALA PRO PHE          
SEQRES  41 A  725  ASP LYS GLN GLN THR TRP ALA ILE ASP ASN VAL TYR ILE          
SEQRES  42 A  725  GLY ASP GLY CYS LEU ASP MET CYS SER GLY HIS GLY ARG          
SEQRES  43 A  725  CYS VAL GLN GLY SER CYS VAL CYS ASP GLU GLN TRP GLY          
SEQRES  44 A  725  GLY LEU TYR CYS ASP GLU PRO GLU THR SER LEU PRO THR          
SEQRES  45 A  725  GLN LEU LYS ASP ASN PHE ASN ARG ALA PRO SER ASN GLN          
SEQRES  46 A  725  ASN TRP LEU THR VAL SER GLY GLY LYS LEU SER THR VAL          
SEQRES  47 A  725  CYS GLY ALA VAL ALA SER GLY LEU ALA LEU HIS PHE SER          
SEQRES  48 A  725  GLY GLY CYS SER ARG LEU LEU VAL THR VAL ASP LEU ASN          
SEQRES  49 A  725  LEU THR ASN ALA GLU PHE ILE GLN PHE TYR PHE MET TYR          
SEQRES  50 A  725  GLY CYS LEU ILE THR PRO SER ASN ARG ASN GLN GLY VAL          
SEQRES  51 A  725  LEU LEU GLU TYR SER VAL ASN GLY GLY ILE THR TRP ASN          
SEQRES  52 A  725  LEU LEU MET GLU ILE PHE TYR ASP GLN TYR SER LYS PRO          
SEQRES  53 A  725  GLY PHE VAL ASN ILE LEU LEU PRO PRO ASP ALA LYS GLU          
SEQRES  54 A  725  ILE ALA THR ARG PHE ARG TRP TRP GLN PRO ARG HIS ASP          
SEQRES  55 A  725  GLY LEU ASP GLN ASN ASP TRP ALA ILE ASP ASN VAL LEU          
SEQRES  56 A  725  ILE SER ARG LEU GLU ASN LEU TYR PHE GLN                      
SEQRES   1 B   44  GLY SER GLY PRO ALA LYS GLU CYS GLU LYS ASP GLN PHE          
SEQRES   2 B   44  GLN CYS ARG ASN GLU ARG CYS ILE PRO SER VAL TRP ARG          
SEQRES   3 B   44  CYS ASP GLU ASP ASP ASP CYS LEU ASP HIS SER ASP GLU          
SEQRES   4 B   44  ASP ASP CYS PRO LYS                                          
MODRES 3A7Q ASN A 2145  ASN  GLYCOSYLATION SITE                                 
MODRES 3A7Q ASN A 2269  ASN  GLYCOSYLATION SITE                                 
MODRES 3A7Q ASN A 2317  ASN  GLYCOSYLATION SITE                                 
MODRES 3A7Q ASN A 2569  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A3001      14                                                       
HET    NAG  A3002      14                                                       
HET    NAG  A3003      14                                                       
HET    NAG  A3004      14                                                       
HET    NAG  A3005      14                                                       
HET     CA  A4001       1                                                       
HET     CA  A4002       1                                                       
HET     CA  A4003       1                                                       
HET     CA  A4004       1                                                       
HET     ZN  A4005       1                                                       
HET     CA  B5001       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CA CALCIUM ION                                                      
HETNAM      ZN ZINC ION                                                         
FORMUL   3  NAG    5(C8 H15 N O6)                                               
FORMUL   7   CA    5(CA 2+)                                                     
FORMUL  11   ZN    ZN 2+                                                        
FORMUL  13  HOH   *19(H2 O)                                                     
HELIX    1   1 ARG A 1967  ASP A 1969  5                                   3    
HELIX    2   2 HIS A 2094  HIS A 2099  1                                   6    
HELIX    3   3 CYS A 2133  GLY A 2139  5                                   7    
HELIX    4   4 PRO A 2282  ARG A 2286  5                                   5    
HELIX    5   5 PRO A 2447  ARG A 2451  5                                   5    
HELIX    6   6 CYS A 2482  GLY A 2488  5                                   7    
HELIX    7   7 ASN A 2590  GLY A 2594  5                                   5    
HELIX    8   8 PRO A 2629  LYS A 2633  5                                   5    
HELIX    9   9 VAL B   63  ARG B   65  5                                   3    
SHEET    1   A 4 LEU A1958  ASP A1960  0                                        
SHEET    2   A 4 TRP A2122  PRO A2131 -1  O  ILE A2129   N  LEU A1958           
SHEET    3   A 4 ALA A1996  PHE A1999 -1  N  PHE A1999   O  TRP A2122           
SHEET    4   A 4 GLY A1977  GLY A1980 -1  N  ASN A1978   O  VAL A1998           
SHEET    1   B 4 LEU A1958  ASP A1960  0                                        
SHEET    2   B 4 TRP A2122  PRO A2131 -1  O  ILE A2129   N  LEU A1958           
SHEET    3   B 4 THR A2020  VAL A2028 -1  N  GLN A2023   O  TYR A2128           
SHEET    4   B 4 ARG A2089  VAL A2093 -1  O  VAL A2093   N  ILE A2022           
SHEET    1   C 5 TRP A1971  PHE A1973  0                                        
SHEET    2   C 5 GLY A2005  THR A2011 -1  O  THR A2010   N  PHE A1973           
SHEET    3   C 5 GLY A2102  TYR A2113 -1  O  GLY A2111   N  HIS A2007           
SHEET    4   C 5 SER A2035  SER A2045 -1  N  ARG A2041   O  TYR A2109           
SHEET    5   C 5 HIS A2053  LEU A2054 -1  O  HIS A2053   N  PHE A2044           
SHEET    1   D 4 LEU A2014  VAL A2016  0                                        
SHEET    2   D 4 GLY A2102  TYR A2113 -1  O  VAL A2104   N  LEU A2014           
SHEET    3   D 4 SER A2035  SER A2045 -1  N  ARG A2041   O  TYR A2109           
SHEET    4   D 4 THR A2079  ALA A2082 -1  O  TYR A2080   N  VAL A2040           
SHEET    1   E 2 GLY A2141  ILE A2144  0                                        
SHEET    2   E 2 LYS A2148  CYS A2151 -1  O  ILE A2150   N  SER A2142           
SHEET    1   F 2 TYR A2155  SER A2156  0                                        
SHEET    2   F 2 ILE A2162  SER A2163 -1  O  ILE A2162   N  SER A2156           
SHEET    1   G 4 LEU A2170  ASP A2172  0                                        
SHEET    2   G 4 TRP A2307  GLY A2315 -1  O  ILE A2314   N  LEU A2170           
SHEET    3   G 4 ASN A2203  PHE A2206 -1  N  LEU A2204   O  ILE A2309           
SHEET    4   G 4 LYS A2190  SER A2192 -1  N  SER A2192   O  ASN A2203           
SHEET    1   H 4 LEU A2170  ASP A2172  0                                        
SHEET    2   H 4 TRP A2307  GLY A2315 -1  O  ILE A2314   N  LEU A2170           
SHEET    3   H 4 PHE A2226  LEU A2233 -1  N  PHE A2230   O  ASP A2310           
SHEET    4   H 4 ARG A2275  GLU A2280 -1  O  LEU A2279   N  VAL A2227           
SHEET    1   I 5 PHE A2183  SER A2187  0                                        
SHEET    2   I 5 ARG A2212  THR A2216 -1  O  MET A2213   N  SER A2187           
SHEET    3   I 5 ARG A2291  GLN A2296 -1  O  LEU A2292   N  THR A2216           
SHEET    4   I 5 VAL A2247  SER A2252 -1  N  LEU A2248   O  TRP A2295           
SHEET    5   I 5 SER A2260  PHE A2265 -1  O  LEU A2262   N  LEU A2249           
SHEET    1   J 4 LEU A2324  ASP A2326  0                                        
SHEET    2   J 4 TRP A2471  GLY A2479 -1  O  VAL A2476   N  ASP A2326           
SHEET    3   J 4 ALA A2354  PHE A2357 -1  N  PHE A2357   O  TRP A2471           
SHEET    4   J 4 THR A2343  MET A2345 -1  N  MET A2345   O  ALA A2354           
SHEET    1   K 4 LEU A2324  ASP A2326  0                                        
SHEET    2   K 4 TRP A2471  GLY A2479 -1  O  VAL A2476   N  ASP A2326           
SHEET    3   K 4 PHE A2378  ALA A2384 -1  N  GLN A2380   O  TYR A2477           
SHEET    4   K 4 THR A2440  PRO A2445 -1  O  LEU A2444   N  LEU A2379           
SHEET    1   L 5 TRP A2336  LEU A2338  0                                        
SHEET    2   L 5 ARG A2364  THR A2368 -1  O  VAL A2367   N  LEU A2338           
SHEET    3   L 5 ARG A2456  GLN A2461 -1  O  PHE A2457   N  THR A2368           
SHEET    4   L 5 ALA A2395  SER A2401 -1  N  GLU A2399   O  ARG A2458           
SHEET    5   L 5 HIS A2409  PRO A2410 -1  O  HIS A2409   N  TYR A2400           
SHEET    1   M 5 TRP A2336  LEU A2338  0                                        
SHEET    2   M 5 ARG A2364  THR A2368 -1  O  VAL A2367   N  LEU A2338           
SHEET    3   M 5 ARG A2456  GLN A2461 -1  O  PHE A2457   N  THR A2368           
SHEET    4   M 5 ALA A2395  SER A2401 -1  N  GLU A2399   O  ARG A2458           
SHEET    5   M 5 LEU A2431  VAL A2432 -1  O  LEU A2431   N  ILE A2396           
SHEET    1   N 2 GLY A2490  CYS A2492  0                                        
SHEET    2   N 2 CYS A2497  CYS A2499 -1  O  VAL A2498   N  ARG A2491           
SHEET    1   O 2 TRP A2503  GLY A2504  0                                        
SHEET    2   O 2 GLU A2510  PRO A2511 -1  O  GLU A2510   N  GLY A2504           
SHEET    1   P 4 LEU A2519  ASP A2521  0                                        
SHEET    2   P 4 TRP A2654  SER A2662 -1  O  ILE A2661   N  LEU A2519           
SHEET    3   P 4 ALA A2552  PHE A2555 -1  N  PHE A2555   O  TRP A2654           
SHEET    4   P 4 GLY A2538  SER A2541 -1  N  LYS A2539   O  HIS A2554           
SHEET    1   Q 4 LEU A2519  ASP A2521  0                                        
SHEET    2   Q 4 TRP A2654  SER A2662 -1  O  ILE A2661   N  LEU A2519           
SHEET    3   Q 4 PHE A2575  TYR A2582 -1  N  GLN A2577   O  LEU A2660           
SHEET    4   Q 4 GLY A2622  LEU A2627 -1  O  GLY A2622   N  PHE A2580           
SHEET    1   R 5 TRP A2532  SER A2536  0                                        
SHEET    2   R 5 ARG A2561  THR A2565 -1  O  LEU A2562   N  SER A2536           
SHEET    3   R 5 ARG A2638  GLN A2643 -1  O  TRP A2641   N  LEU A2563           
SHEET    4   R 5 VAL A2595  SER A2600 -1  N  SER A2600   O  ARG A2638           
SHEET    5   R 5 ASN A2608  ILE A2613 -1  O  LEU A2610   N  LEU A2597           
SHEET    1   S 2 GLN B  51  GLN B  53  0                                        
SHEET    2   S 2 CYS B  59  PRO B  61 -1  O  ILE B  60   N  PHE B  52           
SSBOND   1 CYS A 1983    CYS A 2030                          1555   1555  2.05  
SSBOND   2 CYS A 2133    CYS A 2143                          1555   1555  2.08  
SSBOND   3 CYS A 2137    CYS A 2149                          1555   1555  2.05  
SSBOND   4 CYS A 2151    CYS A 2160                          1555   1555  2.04  
SSBOND   5 CYS A 2195    CYS A 2235                          1555   1555  2.03  
SSBOND   6 CYS A 2348    CYS A 2387                          1555   1555  2.04  
SSBOND   7 CYS A 2393    CYS A 2559                          1555   1555  2.06  
SSBOND   8 CYS A 2415    CYS A 2422                          1555   1555  2.03  
SSBOND   9 CYS A 2482    CYS A 2492                          1555   1555  2.04  
SSBOND  10 CYS A 2486    CYS A 2497                          1555   1555  2.07  
SSBOND  11 CYS A 2499    CYS A 2508                          1555   1555  2.05  
SSBOND  12 CYS A 2544    CYS A 2584                          1555   1555  2.02  
SSBOND  13 CYS B   47    CYS B   59                          1555   1555  2.05  
SSBOND  14 CYS B   54    CYS B   72                          1555   1555  2.03  
SSBOND  15 CYS B   66    CYS B   81                          1555   1555  2.04  
LINK         O   THR A1961                CA    CA A4001     1555   1555  2.41  
LINK         OD2 ASP A1963                CA    CA A4001     1555   1555  2.35  
LINK         O   SER A1995                CA    CA A4001     1555   1555  2.29  
LINK         OD1 ASP A2125                CA    CA A4001     1555   1555  2.49  
LINK         OD2 ASP A2125                CA    CA A4001     1555   1555  2.61  
LINK         O   ASP A2173                CA    CA A4002     1555   1555  2.59  
LINK         OE2 GLU A2175                CA    CA A4002     1555   1555  2.46  
LINK         O   ASN A2202                CA    CA A4002     1555   1555  2.34  
LINK         OD1 ASP A2310                CA    CA A4002     1555   1555  2.31  
LINK         OD2 ASP A2310                CA    CA A4002     1555   1555  2.32  
LINK         O   ASP A2327                CA    CA A4003     1555   1555  2.35  
LINK         O   THR A2351                CA    CA A4003     1555   1555  2.35  
LINK         O   ASP A2353                CA    CA A4003     1555   1555  2.33  
LINK         OD1 ASP A2474                CA    CA A4003     1555   1555  2.36  
LINK         OD2 ASP A2474                CA    CA A4003     1555   1555  2.34  
LINK         O   ASN A2522                CA    CA A4004     1555   1555  2.29  
LINK         OD1 ASN A2524                CA    CA A4004     1555   1555  2.98  
LINK         O   SER A2549                CA    CA A4004     1555   1555  2.31  
LINK         O   LEU A2551                CA    CA A4004     1555   1555  2.37  
LINK         OD1 ASP A2657                CA    CA A4004     1555   1555  2.36  
LINK         OD2 ASP A2657                CA    CA A4004     1555   1555  2.33  
LINK         O   TRP B  64                CA    CA B5001     1555   1555  2.17  
LINK         OD2 ASP B  67                CA    CA B5001     1555   1555  2.33  
LINK         O   ASP B  69                CA    CA B5001     1555   1555  2.33  
LINK         OD2 ASP B  71                CA    CA B5001     1555   1555  2.33  
LINK         OD2 ASP B  77                CA    CA B5001     1555   1555  2.32  
LINK         OE2 GLU B  78                CA    CA B5001     1555   1555  2.31  
LINK         ND2 ASN A2145                 C1  NAG A3001     1555   1555  1.44  
LINK         ND2 ASN A2269                 C1  NAG A3002     1555   1555  1.45  
LINK         ND2 ASN A2317                 C1  NAG A3004     1555   1555  1.45  
LINK         OE2 GLU A2399                ZN    ZN A4005     1555   1555  2.21  
LINK         ND1 HIS A2460                ZN    ZN A4005     1555   1555  2.27  
LINK         ND2 ASN A2569                 C1  NAG A3005     1555   1555  1.44  
LINK         O4  NAG A3002                 C1  NAG A3003     1555   1555  1.46  
LINK        CA    CA A4002                 O   HOH A6001     1555   1555  2.16  
LINK        CA    CA A4003                 O   HOH A6002     1555   1555  2.31  
LINK        CA    CA A4004                 O   HOH A6003     1555   1555  2.33  
CISPEP   1 ALA A 2463    PRO A 2464          0        -4.09                     
SITE     1 AC1  3 VAL A1956  ILE A2144  ASN A2145                               
SITE     1 AC2  3 TYR A1974  ASN A2269  NAG A3003                               
SITE     1 AC3  1 NAG A3002                                                     
SITE     1 AC4  3 ASP A2168  GLY A2316  ASN A2317                               
SITE     1 AC5  5 SER A2514  LEU A2515  ASN A2569  THR A2571                    
SITE     2 AC5  5 ASN A2572                                                     
SITE     1 AC6  5 THR A1961  ASP A1963  SER A1995  ASP A2125                    
SITE     2 AC6  5 ASN A2126                                                     
SITE     1 AC7  5 ASP A2173  GLU A2175  ASN A2202  ASP A2310                    
SITE     2 AC7  5 HOH A6001                                                     
SITE     1 AC8  5 ASP A2327  THR A2351  ASP A2353  ASP A2474                    
SITE     2 AC8  5 HOH A6002                                                     
SITE     1 AC9  6 ASN A2522  ASN A2524  SER A2549  LEU A2551                    
SITE     2 AC9  6 ASP A2657  HOH A6003                                          
SITE     1 BC1  3 GLU A2399  ARG A2458  HIS A2460                               
SITE     1 BC2  6 TRP B  64  ASP B  67  ASP B  69  ASP B  71                    
SITE     2 BC2  6 ASP B  77  GLU B  78                                          
CRYST1   56.980   93.844   73.456  90.00 107.41  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017550  0.000000  0.005503        0.00000                         
SCALE2      0.000000  0.010656  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014267        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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