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LongText Report for: 2XB6-pdb

Name Class
2XB6-pdb
HEADER    CELL ADHESION                           07-APR-10   2XB6              
TITLE     REVISITED CRYSTAL STRUCTURE OF NEUREXIN1BETA-NEUROLIGIN4              
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUROLIGIN-4, X-LINKED;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CHOLINESTERASE-LIKE DOMAIN, RESIDUES 43-619;               
COMPND   5 SYNONYM: NEUROLIGIN-4, NEUROLIGIN X, HNLX;                           
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: NEUREXIN-1-BETA;                                           
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 FRAGMENT: LNS DOMAIN, RESIDUES 80-258;                               
COMPND  11 SYNONYM: NEUREXIN I-BETA;                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  10 ORGANISM_COMMON: RAT;                                                
SOURCE  11 ORGANISM_TAXID: 10116;                                               
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_CELL_LINE: ROSETTA                                 
KEYWDS    ALPHA-BETA-HYDROLASE FOLD, AUTISM, CONFORMATIONAL REARRANGEMENT,      
KEYWDS   2 CELL ADHESION                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.LEONE,D.COMOLETTI,G.FERRACCI,S.CONROD,S.U.GARCIA,P.TAYLOR,Y.BOURNE, 
AUTHOR   2 P.MARCHOT                                                            
REVDAT   1   23-JUN-10 2XB6    0                                                
JRNL        AUTH   P.LEONE,D.COMOLETTI,G.FERRACCI,S.CONROD,S.U.GARCIA,P.TAYLOR, 
JRNL        AUTH 2 Y.BOURNE,P.MARCHOT                                           
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE EXQUISITE SELECTIVITY OF        
JRNL        TITL 2 NEUREXIN-NEUROLIGIN SYNAPTIC INTERACTIONS                    
JRNL        REF    EMBO J.                                    2010              
JRNL        REFN                   ESSN 1460-2075                               
JRNL        PMID   20543817                                                     
JRNL        DOI    10.1038/EMBOJ.2010.123                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.99                          
REMARK   3   NUMBER OF REFLECTIONS             : 68827                          
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3658                            
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) : 4984                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 265                          
REMARK   3   BIN FREE R VALUE                    : 0.351                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11176                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 195                                     
REMARK   3   SOLVENT ATOMS            : 349                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.92                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.65                                                 
REMARK   3    B22 (A**2) : -1.76                                                
REMARK   3    B33 (A**2) : -1.89                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.394         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.258         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.182         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.938        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11634 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  7785 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15758 ; 1.526 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 18926 ; 1.168 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1411 ; 6.254 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   540 ;36.224 ;24.481       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1804 ;16.316 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    54 ;21.426 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1717 ; 0.097 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12884 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2326 ; 0.002 ; 0.020       
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):  7070 ; 0.686 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2889 ; 0.096 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11409 ; 1.258 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4564 ; 2.119 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4349 ; 3.350 ; 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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 4                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     43       A      62      2                      
REMARK   3           1     B     43       B      62      2                      
REMARK   3           2     A     69       A     110      2                      
REMARK   3           2     B     69       B     110      2                      
REMARK   3           3     A    143       A     407      2                      
REMARK   3           3     B    143       B     407      2                      
REMARK   3           4     A    414       A     598      2                      
REMARK   3           4     B    414       B     598      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2852 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   2852 ;  0.04 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   3607 ;  0.08 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   3607 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):   2852 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):   2852 ;  0.09 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   3607 ;  0.09 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   3607 ;  0.09 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C     82       C     101      2                      
REMARK   3           1     D     82       D     101      2                      
REMARK   3           2     C    105       C     131      2                      
REMARK   3           2     D    105       D     131      2                      
REMARK   3           3     C    137       C     258      2                      
REMARK   3           3     D    137       D     258      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    C    (A):    812 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    D    (A):    812 ;  0.03 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  2    C    (A):   1026 ;  0.10 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    D    (A):   1026 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      2    C (A**2):    812 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      2    D (A**2):    812 ;  0.08 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    C (A**2):   1026 ;  0.07 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    D (A**2):   1026 ;  0.07 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 5                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    43        A   110                          
REMARK   3    RESIDUE RANGE :   A   143        A   291                          
REMARK   3    RESIDUE RANGE :   A   340        A   373                          
REMARK   3    RESIDUE RANGE :   A   449        A   472                          
REMARK   3    RESIDUE RANGE :   A   561        A   582                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.6510 -48.2130 -33.8390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1366 T22:   0.1308                                     
REMARK   3      T33:   0.0513 T12:   0.0788                                     
REMARK   3      T13:   0.0202 T23:  -0.0471                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8677 L22:   2.1851                                     
REMARK   3      L33:   1.0805 L12:  -0.0293                                     
REMARK   3      L13:  -0.1306 L23:   0.0574                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1192 S12:   0.1391 S13:  -0.1969                       
REMARK   3      S21:  -0.0518 S22:   0.0834 S23:  -0.0076                       
REMARK   3      S31:   0.2347 S32:   0.0694 S33:   0.0358                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   111        A   142                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.6490 -48.2790 -13.8690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4129 T22:   0.3160                                     
REMARK   3      T33:   0.0665 T12:   0.0488                                     
REMARK   3      T13:  -0.0452 T23:   0.0603                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8328 L22:   8.9121                                     
REMARK   3      L33:   2.2703 L12:  -3.6763                                     
REMARK   3      L13:  -0.8490 L23:   0.3688                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2549 S12:  -0.3116 S13:   0.0024                       
REMARK   3      S21:   0.7633 S22:   0.2077 S23:  -0.1458                       
REMARK   3      S31:   0.2486 S32:   0.3539 S33:   0.0472                       
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 :   A   292        A   339                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.5160 -49.8200 -21.9420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2798 T22:   0.4205                                     
REMARK   3      T33:   0.4133 T12:   0.1487                                     
REMARK   3      T13:  -0.2030 T23:   0.0855                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8499 L22:   4.2387                                     
REMARK   3      L33:   2.6840 L12:  -2.2195                                     
REMARK   3      L13:   0.0437 L23:   1.5424                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0390 S12:  -0.0187 S13:  -0.0044                       
REMARK   3      S21:   0.6717 S22:   0.0700 S23:  -0.8997                       
REMARK   3      S31:   0.1678 S32:   0.5960 S33:  -0.0309                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   374        A   448                          
REMARK   3    RESIDUE RANGE :   A   583        A   598                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.7100 -20.3850 -17.1530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1045 T22:   0.0861                                     
REMARK   3      T33:   0.0828 T12:   0.0411                                     
REMARK   3      T13:  -0.0616 T23:  -0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3039 L22:   3.1141                                     
REMARK   3      L33:   3.8428 L12:  -0.1031                                     
REMARK   3      L13:  -0.5910 L23:  -1.0419                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0424 S12:  -0.0156 S13:   0.0518                       
REMARK   3      S21:   0.2893 S22:  -0.0685 S23:  -0.4499                       
REMARK   3      S31:  -0.1581 S32:   0.2895 S33:   0.0260                       
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   473        A   560                          
REMARK   3    ORIGIN FOR THE GROUP (A): -53.2040 -39.8760 -23.1820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1009 T22:   0.0729                                     
REMARK   3      T33:   0.1379 T12:   0.0642                                     
REMARK   3      T13:   0.0514 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5832 L22:   2.7114                                     
REMARK   3      L33:   1.8373 L12:   0.6813                                     
REMARK   3      L13:  -0.1308 L23:   0.6205                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0657 S12:   0.0773 S13:  -0.1365                       
REMARK   3      S21:   0.2694 S22:   0.0750 S23:   0.4495                       
REMARK   3      S31:   0.1682 S32:   0.0103 S33:  -0.0093                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 5                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    34        B   110                          
REMARK   3    RESIDUE RANGE :   B   143        B   291                          
REMARK   3    RESIDUE RANGE :   B   340        B   373                          
REMARK   3    RESIDUE RANGE :   B   449        B   472                          
REMARK   3    RESIDUE RANGE :   B   561        B   582                          
REMARK   3    ORIGIN FOR THE GROUP (A): -47.1860  24.9220 -16.9640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0474 T22:   0.0809                                     
REMARK   3      T33:   0.0315 T12:  -0.0403                                     
REMARK   3      T13:   0.0101 T23:   0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5307 L22:   2.4984                                     
REMARK   3      L33:   0.8918 L12:  -0.4025                                     
REMARK   3      L13:  -0.1708 L23:   0.5099                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0221 S12:  -0.0703 S13:   0.0026                       
REMARK   3      S21:   0.1068 S22:   0.0125 S23:   0.1510                       
REMARK   3      S31:   0.0388 S32:   0.0388 S33:   0.0095                       
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 :   B   111        B   142                          
REMARK   3    ORIGIN FOR THE GROUP (A): -40.2220  25.1390 -36.3780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5743 T22:   0.2862                                     
REMARK   3      T33:   0.1736 T12:   0.1211                                     
REMARK   3      T13:  -0.0779 T23:  -0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7280 L22:  10.1590                                     
REMARK   3      L33:   3.2198 L12:   1.9833                                     
REMARK   3      L13:   0.8325 L23:   1.2748                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0619 S12:   0.1130 S13:  -0.1108                       
REMARK   3      S21:  -1.2939 S22:  -0.1239 S23:  -0.0065                       
REMARK   3      S31:  -0.1539 S32:  -0.0522 S33:   0.0620                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   292        B   339                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.0900  29.7520 -27.4180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1226 T22:   0.2573                                     
REMARK   3      T33:   0.3721 T12:  -0.0760                                     
REMARK   3      T13:   0.1745 T23:  -0.0168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2097 L22:   5.8176                                     
REMARK   3      L33:   3.0583 L12:   1.5336                                     
REMARK   3      L13:   0.3729 L23:   1.1735                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0866 S12:   0.1897 S13:  -0.0174                       
REMARK   3      S21:  -0.5682 S22:   0.2364 S23:  -1.3049                       
REMARK   3      S31:  -0.1139 S32:   0.4488 S33:  -0.3230                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   374        B   448                          
REMARK   3    RESIDUE RANGE :   B   583        B   598                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.7310  -2.3030 -32.9240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0703 T22:   0.0930                                     
REMARK   3      T33:   0.0906 T12:   0.0136                                     
REMARK   3      T13:   0.0495 T23:   0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1698 L22:   4.4958                                     
REMARK   3      L33:   2.8292 L12:   0.3234                                     
REMARK   3      L13:   0.4454 L23:   0.1277                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0680 S12:   0.1737 S13:  -0.0960                       
REMARK   3      S21:  -0.2269 S22:   0.0215 S23:  -0.5271                       
REMARK   3      S31:   0.0868 S32:   0.2318 S33:  -0.0895                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   473        B   560                          
REMARK   3    ORIGIN FOR THE GROUP (A): -57.5500  13.7280 -28.0590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0722 T22:   0.1414                                     
REMARK   3      T33:   0.2123 T12:  -0.0314                                     
REMARK   3      T13:  -0.0695 T23:  -0.0311                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4663 L22:   3.9117                                     
REMARK   3      L33:   2.4171 L12:  -1.2081                                     
REMARK   3      L13:  -0.7684 L23:   0.1664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1444 S12:   0.1858 S13:  -0.1050                       
REMARK   3      S21:  -0.3544 S22:  -0.2103 S23:   0.8329                       
REMARK   3      S31:  -0.0628 S32:  -0.2349 S33:   0.0659                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    82        C    94                          
REMARK   3    RESIDUE RANGE :   C   226        C   258                          
REMARK   3    ORIGIN FOR THE GROUP (A): -48.8910 -39.7950 -73.0700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2256 T22:   0.6761                                     
REMARK   3      T33:   0.3293 T12:  -0.1249                                     
REMARK   3      T13:  -0.1702 T23:  -0.0736                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5024 L22:   5.2605                                     
REMARK   3      L33:   7.3594 L12:   0.0344                                     
REMARK   3      L13:   1.0783 L23:   1.8325                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1586 S12:  -0.0104 S13:  -0.3051                       
REMARK   3      S21:  -0.6232 S22:  -0.4322 S23:   1.2689                       
REMARK   3      S31:   0.5279 S32:  -2.1467 S33:   0.2736                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    95        C   225                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.3610 -35.9570 -67.5880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1012 T22:   0.0415                                     
REMARK   3      T33:   0.0153 T12:   0.0516                                     
REMARK   3      T13:   0.0092 T23:  -0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1095 L22:   2.1241                                     
REMARK   3      L33:   5.1635 L12:  -0.4755                                     
REMARK   3      L13:   0.4291 L23:   0.9428                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0542 S12:  -0.1965 S13:   0.1272                       
REMARK   3      S21:  -0.2889 S22:  -0.0966 S23:  -0.0130                       
REMARK   3      S31:  -0.2631 S32:  -0.2852 S33:   0.1508                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    82        D    94                          
REMARK   3    RESIDUE RANGE :   D   226        D   258                          
REMARK   3    ORIGIN FOR THE GROUP (A): -53.9330  14.0850  23.0370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5329 T22:   0.6732                                     
REMARK   3      T33:   0.2155 T12:   0.0447                                     
REMARK   3      T13:   0.2287 T23:   0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1556 L22:   3.6317                                     
REMARK   3      L33:   5.2497 L12:   1.1355                                     
REMARK   3      L13:  -0.0338 L23:   0.9011                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0612 S12:  -0.2685 S13:   0.3991                       
REMARK   3      S21:   0.9896 S22:  -0.1412 S23:   0.8523                       
REMARK   3      S31:   0.1926 S32:  -1.3859 S33:   0.2024                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    95        D   225                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.1940  13.4850  17.0370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3937 T22:   0.1903                                     
REMARK   3      T33:   0.0634 T12:   0.0453                                     
REMARK   3      T13:  -0.0309 T23:   0.0418                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8800 L22:   2.5722                                     
REMARK   3      L33:   6.3891 L12:   0.8563                                     
REMARK   3      L13:  -0.0984 L23:   0.9868                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0475 S12:  -0.0337 S13:  -0.0385                       
REMARK   3      S21:   0.5652 S22:   0.0663 S23:  -0.3119                       
REMARK   3      S31:   0.2603 S32:  -0.1673 S33:  -0.0188                       
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2XB6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-APR-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-43565.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9834                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 315R)                 
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72526                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.60                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.00                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.7                                
REMARK 200  R MERGE                    (I) : 0.10                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.70                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.55                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.80                               
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: PDB ENTRY 2WQZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.0                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES PH6.3,10% PEG 20000,           
REMARK 280  2MM CACL2                                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       68.15350            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       99.38950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       68.15350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       99.38950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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     ASP A   -12                                                      
REMARK 465     TYR A   -11                                                      
REMARK 465     LYS A   -10                                                      
REMARK 465     ASP A    -9                                                      
REMARK 465     ASP A    -8                                                      
REMARK 465     ASP A    -7                                                      
REMARK 465     ASP A    -6                                                      
REMARK 465     LYS A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     ALA A    -3                                                      
REMARK 465     ALA A    -2                                                      
REMARK 465     PRO A    63                                                      
REMARK 465     ASN A    64                                                      
REMARK 465     GLU A    65                                                      
REMARK 465     ILE A    66                                                      
REMARK 465     ASP A   157                                                      
REMARK 465     ASP A   158                                                      
REMARK 465     ILE A   159                                                      
REMARK 465     HIS A   160                                                      
REMARK 465     ASP A   161                                                      
REMARK 465     GLN A   162                                                      
REMARK 465     ASN A   163                                                      
REMARK 465     PRO A   541                                                      
REMARK 465     GLN A   542                                                      
REMARK 465     ASP A   543                                                      
REMARK 465     THR A   544                                                      
REMARK 465     LYS A   545                                                      
REMARK 465     PHE A   546                                                      
REMARK 465     ILE A   547                                                      
REMARK 465     HIS A   548                                                      
REMARK 465     THR A   549                                                      
REMARK 465     LYS A   550                                                      
REMARK 465     PRO A   551                                                      
REMARK 465     ASN A   552                                                      
REMARK 465     ARG A   553                                                      
REMARK 465     PHE A   554                                                      
REMARK 465     GLU A   555                                                      
REMARK 465     GLU A   556                                                      
REMARK 465     ASN A   599                                                      
REMARK 465     LEU A   600                                                      
REMARK 465     ASN A   601                                                      
REMARK 465     GLU A   602                                                      
REMARK 465     ILE A   603                                                      
REMARK 465     PHE A   604                                                      
REMARK 465     GLN A   605                                                      
REMARK 465     TYR A   606                                                      
REMARK 465     VAL A   607                                                      
REMARK 465     SER A   608                                                      
REMARK 465     THR A   609                                                      
REMARK 465     THR A   610                                                      
REMARK 465     THR A   611                                                      
REMARK 465     LYS A   612                                                      
REMARK 465     VAL A   613                                                      
REMARK 465     PRO A   614                                                      
REMARK 465     PRO A   615                                                      
REMARK 465     PRO A   616                                                      
REMARK 465     ASP A   617                                                      
REMARK 465     MET A   618                                                      
REMARK 465     THR A   619                                                      
REMARK 465     ASP B   -12                                                      
REMARK 465     TYR B   -11                                                      
REMARK 465     ASP B   157                                                      
REMARK 465     ASP B   158                                                      
REMARK 465     ILE B   159                                                      
REMARK 465     HIS B   160                                                      
REMARK 465     ASP B   161                                                      
REMARK 465     GLN B   162                                                      
REMARK 465     ASN B   163                                                      
REMARK 465     SER B   164                                                      
REMARK 465     PRO B   541                                                      
REMARK 465     GLN B   542                                                      
REMARK 465     ASP B   543                                                      
REMARK 465     THR B   544                                                      
REMARK 465     LYS B   545                                                      
REMARK 465     PHE B   546                                                      
REMARK 465     ILE B   547                                                      
REMARK 465     HIS B   548                                                      
REMARK 465     THR B   549                                                      
REMARK 465     LYS B   550                                                      
REMARK 465     PRO B   551                                                      
REMARK 465     ASN B   552                                                      
REMARK 465     ARG B   553                                                      
REMARK 465     PHE B   554                                                      
REMARK 465     GLU B   555                                                      
REMARK 465     GLU B   556                                                      
REMARK 465     ASN B   599                                                      
REMARK 465     LEU B   600                                                      
REMARK 465     ASN B   601                                                      
REMARK 465     GLU B   602                                                      
REMARK 465     ILE B   603                                                      
REMARK 465     PHE B   604                                                      
REMARK 465     GLN B   605                                                      
REMARK 465     TYR B   606                                                      
REMARK 465     VAL B   607                                                      
REMARK 465     SER B   608                                                      
REMARK 465     THR B   609                                                      
REMARK 465     THR B   610                                                      
REMARK 465     THR B   611                                                      
REMARK 465     LYS B   612                                                      
REMARK 465     VAL B   613                                                      
REMARK 465     PRO B   614                                                      
REMARK 465     PRO B   615                                                      
REMARK 465     PRO B   616                                                      
REMARK 465     ASP B   617                                                      
REMARK 465     MET B   618                                                      
REMARK 465     THR B   619                                                      
REMARK 465     GLY C    80                                                      
REMARK 465     GLY C    81                                                      
REMARK 465     GLY D    80                                                      
REMARK 465     GLY D    81                                                      
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   OE2  GLU B   411     OD1  ASP B   414              1.86            
REMARK 500   O6   NAG A   700     O    HOH A  2124              1.94            
REMARK 500   ND2  ASN B   102     O5   NAG B   700              2.04            
REMARK 500   O    LEU D   135     O    HOH D  2005              2.13            
REMARK 500   O    LEU B   593     O    HIS B   596              2.14            
REMARK 500   ND2  ASN A   102     C2   NAG A   700              2.15            
REMARK 500   O    LEU A   593     O    HIS A   596              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ALA A  -1   C     GLN A  44   N       0.155                       
REMARK 500    VAL A 238   CB    VAL A 238   CG1    -0.171                       
REMARK 500    VAL A 238   CB    VAL A 238   CG2    -0.162                       
REMARK 500    VAL B 238   CB    VAL B 238   CG1    -0.195                       
REMARK 500    VAL B 238   CB    VAL B 238   CG2    -0.195                       
REMARK 500    ARG C 197   CZ    ARG C 197   NH1    -0.214                       
REMARK 500    ARG D 197   CZ    ARG D 197   NH1    -0.207                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 231   CB  -  CG  -  CD1 ANGL. DEV. =  10.3 DEGREES          
REMARK 500    MET A 501   CB  -  CG  -  SD  ANGL. DEV. =  30.2 DEGREES          
REMARK 500    LEU B 440   CB  -  CG  -  CD1 ANGL. DEV. =  12.9 DEGREES          
REMARK 500    MET B 501   CB  -  CG  -  SD  ANGL. DEV. =  31.8 DEGREES          
REMARK 500    ARG C 197   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.8 DEGREES          
REMARK 500    ARG C 197   NE  -  CZ  -  NH2 ANGL. DEV. =  13.0 DEGREES          
REMARK 500    ARG D 197   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500    ARG D 197   NE  -  CZ  -  NH2 ANGL. DEV. =  13.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A 103       67.45   -119.92                                   
REMARK 500    GLU A 116      120.80    -38.50                                   
REMARK 500    ARG A 117      -24.53    103.42                                   
REMARK 500    CYS A 146       16.45   -143.72                                   
REMARK 500    LYS A 165      114.16   -164.58                                   
REMARK 500    SER A 176       10.74   -140.16                                   
REMARK 500    TYR A 177      -14.55     74.90                                   
REMARK 500    CYS A 306       69.41   -100.87                                   
REMARK 500    GLU A 411     -163.15   -124.69                                   
REMARK 500    ASP A 429       50.14   -164.51                                   
REMARK 500    SER A 487      120.24    -35.61                                   
REMARK 500    LEU A 597       29.96     90.59                                   
REMARK 500    ASP B  -9      -42.77    173.99                                   
REMARK 500    ASP B  -8      -24.90    -22.61                                   
REMARK 500    ASP B  -7      -49.26     94.39                                   
REMARK 500    GLU B 116      -40.84    102.83                                   
REMARK 500    CYS B 146       13.35   -144.22                                   
REMARK 500    TYR B 177      -15.44     74.34                                   
REMARK 500    CYS B 306       69.10   -102.31                                   
REMARK 500    ASP B 347      -60.17   -124.50                                   
REMARK 500    TYR B 407       44.01   -141.13                                   
REMARK 500    GLU B 411     -156.70   -159.89                                   
REMARK 500    ASP B 429       52.98   -162.97                                   
REMARK 500    TRP B 449      -50.78   -121.59                                   
REMARK 500    HIS B 475      153.89    179.85                                   
REMARK 500    SER B 487      121.37    -38.61                                   
REMARK 500    LEU B 597       30.15     95.27                                   
REMARK 500    ASP C 104       34.60   -152.27                                   
REMARK 500    THR C 156      -85.82    -97.82                                   
REMARK 500    ASP C 190     -123.14     51.92                                   
REMARK 500    SER D 132      164.03    -47.72                                   
REMARK 500    THR D 156      -88.17    -93.13                                   
REMARK 500    ASN D 165      -39.74   -131.05                                   
REMARK 500    ASN D 169       57.44    -97.27                                   
REMARK 500    ASP D 190     -120.19     50.57                                   
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 C1296  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE C 236   O                                                      
REMARK 620 2 ASP C 137   OD2  88.4                                              
REMARK 620 3 ASN C 238   OD1  81.3  80.5                                        
REMARK 620 4 HOH C2012   O   171.6  83.2  97.7                                  
REMARK 620 5 VAL C 154   O    90.0  92.9 169.2  89.8                            
REMARK 620 6 HOH A2060   O    96.7 167.3  88.8  91.6  98.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D1289  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN D 238   OD1                                                    
REMARK 620 2 ASP D 137   OD2  83.5                                              
REMARK 620 3 HOH B2096   O    92.5 174.0                                        
REMARK 620 4 VAL D 154   O   170.1  91.4  93.2                                  
REMARK 620 5 ILE D 236   O    81.4  86.5  97.4  89.9                            
REMARK 620 6 HOH D2006   O   101.2  82.6  93.8  86.5 168.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1599                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1599                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES C1289                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1290                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1291                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1292                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1293                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1294                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C1296                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA D1289                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1C4R   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF THE LIGAND-BINDING DOMAIN                          
REMARK 900  OF NEUREXIN 1BETA: REGULATION OF LNS DOMAIN                         
REMARK 900   FUNCTION BY ALTERNATIVE SPLICING                                   
REMARK 900 RELATED ID: 2VH8   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL ANALYSIS OF THE SYNAPTIC PROTEIN                         
REMARK 900  NEUROLIGIN AND ITS BETA-NEUREXIN COMPLEX:                           
REMARK 900  DETERMINANTS FOR FOLDING AND CELL ADHESION                          
REMARK 900 RELATED ID: 2WQZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SYNAPTIC PROTEIN                               
REMARK 900  NEUROLIGIN-4 IN COMPLEX WITH NEUREXIN-BETA                          
REMARK 900  1: ALTERNATIVE REFINEMENT                                           
REMARK 999                                                                      
REMARK 999 R561K IS A SPONTANEOUS MUTAGENESIS OF CDNA CLONE                     
DBREF  2XB6 A   44   619  UNP    Q8N0W4   NLGNX_HUMAN     44    619             
DBREF  2XB6 B   44   619  UNP    Q8N0W4   NLGNX_HUMAN     44    619             
DBREF  2XB6 C   80   288  UNP    Q63373   NRX1B_RAT       80    258             
DBREF  2XB6 D   80   288  UNP    Q63373   NRX1B_RAT       80    258             
SEQADV 2XB6 ASP A  -12  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 TYR A  -11  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 LYS A  -10  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ASP A   -9  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ASP A   -8  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ASP A   -7  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ASP A   -6  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 LYS A   -5  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 LEU A   -4  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ALA A   -3  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ALA A   -2  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ALA A   -1  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ASP B  -12  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 TYR B  -11  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 LYS B  -10  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ASP B   -9  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ASP B   -8  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ASP B   -7  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ASP B   -6  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 LYS B   -5  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 LEU B   -4  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ALA B   -3  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ALA B   -2  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ALA B   -1  UNP  Q8N0W4              EXPRESSION TAG                 
SEQADV 2XB6 ARG A  561  UNP  Q8N0W4    LYS   561 CLONING ARTIFACT               
SEQADV 2XB6 ARG B  561  UNP  Q8N0W4    LYS   561 CLONING ARTIFACT               
SEQRES   1 A  588  ASP TYR LYS ASP ASP ASP ASP LYS LEU ALA ALA ALA GLN          
SEQRES   2 A  588  TYR PRO VAL VAL ASN THR ASN TYR GLY LYS ILE ARG GLY          
SEQRES   3 A  588  LEU ARG THR PRO LEU PRO ASN GLU ILE LEU GLY PRO VAL          
SEQRES   4 A  588  GLU GLN TYR LEU GLY VAL PRO TYR ALA SER PRO PRO THR          
SEQRES   5 A  588  GLY GLU ARG ARG PHE GLN PRO PRO GLU PRO PRO SER SER          
SEQRES   6 A  588  TRP THR GLY ILE ARG ASN THR THR GLN PHE ALA ALA VAL          
SEQRES   7 A  588  CYS PRO GLN HIS LEU ASP GLU ARG SER LEU LEU HIS ASP          
SEQRES   8 A  588  MET LEU PRO ILE TRP PHE THR ALA ASN LEU ASP THR LEU          
SEQRES   9 A  588  MET THR TYR VAL GLN ASP GLN ASN GLU ASP CYS LEU TYR          
SEQRES  10 A  588  LEU ASN ILE TYR VAL PRO THR GLU ASP ASP ILE HIS ASP          
SEQRES  11 A  588  GLN ASN SER LYS LYS PRO VAL MET VAL TYR ILE HIS GLY          
SEQRES  12 A  588  GLY SER TYR MET GLU GLY THR GLY ASN MET ILE ASP GLY          
SEQRES  13 A  588  SER ILE LEU ALA SER TYR GLY ASN VAL ILE VAL ILE THR          
SEQRES  14 A  588  ILE ASN TYR ARG LEU GLY ILE LEU GLY PHE LEU SER THR          
SEQRES  15 A  588  GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU LEU ASP          
SEQRES  16 A  588  GLN ILE GLN ALA LEU ARG TRP ILE GLU GLU ASN VAL GLY          
SEQRES  17 A  588  ALA PHE GLY GLY ASP PRO LYS ARG VAL THR ILE PHE GLY          
SEQRES  18 A  588  SER GLY ALA GLY ALA SER CYS VAL SER LEU LEU THR LEU          
SEQRES  19 A  588  SER HIS TYR SER GLU GLY LEU PHE GLN LYS ALA ILE ILE          
SEQRES  20 A  588  GLN SER GLY THR ALA LEU SER SER TRP ALA VAL ASN TYR          
SEQRES  21 A  588  GLN PRO ALA LYS TYR THR ARG ILE LEU ALA ASP LYS VAL          
SEQRES  22 A  588  GLY CYS ASN MET LEU ASP THR THR ASP MET VAL GLU CYS          
SEQRES  23 A  588  LEU ARG ASN LYS ASN TYR LYS GLU LEU ILE GLN GLN THR          
SEQRES  24 A  588  ILE THR PRO ALA THR TYR HIS ILE ALA PHE GLY PRO VAL          
SEQRES  25 A  588  ILE ASP GLY ASP VAL ILE PRO ASP ASP PRO GLN ILE LEU          
SEQRES  26 A  588  MET GLU GLN GLY GLU PHE LEU ASN TYR ASP ILE MET LEU          
SEQRES  27 A  588  GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL ASP GLY          
SEQRES  28 A  588  ILE VAL ASP ASN GLU ASP GLY VAL THR PRO ASN ASP PHE          
SEQRES  29 A  588  ASP PHE SER VAL SER ASN PHE VAL ASP ASN LEU TYR GLY          
SEQRES  30 A  588  TYR PRO GLU GLY LYS ASP THR LEU ARG GLU THR ILE LYS          
SEQRES  31 A  588  PHE MET TYR THR ASP TRP ALA ASP LYS GLU ASN PRO GLU          
SEQRES  32 A  588  THR ARG ARG LYS THR LEU VAL ALA LEU PHE THR ASP HIS          
SEQRES  33 A  588  GLN TRP VAL ALA PRO ALA VAL ALA THR ALA ASP LEU HIS          
SEQRES  34 A  588  ALA GLN TYR GLY SER PRO THR TYR PHE TYR ALA PHE TYR          
SEQRES  35 A  588  HIS HIS CYS GLN SER GLU MET LYS PRO SER TRP ALA ASP          
SEQRES  36 A  588  SER ALA HIS GLY ASP GLU VAL PRO TYR VAL PHE GLY ILE          
SEQRES  37 A  588  PRO MET ILE GLY PRO THR GLU LEU PHE SER CYS ASN PHE          
SEQRES  38 A  588  SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL MET THR          
SEQRES  39 A  588  TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO ASN GLN          
SEQRES  40 A  588  PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR LYS PRO          
SEQRES  41 A  588  ASN ARG PHE GLU GLU VAL ALA TRP SER ARG TYR ASN PRO          
SEQRES  42 A  588  LYS ASP GLN LEU TYR LEU HIS ILE GLY LEU LYS PRO ARG          
SEQRES  43 A  588  VAL ARG ASP HIS TYR ARG ALA THR LYS VAL ALA PHE TRP          
SEQRES  44 A  588  LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU ASN GLU ILE          
SEQRES  45 A  588  PHE GLN TYR VAL SER THR THR THR LYS VAL PRO PRO PRO          
SEQRES  46 A  588  ASP MET THR                                                  
SEQRES   1 B  588  ASP TYR LYS ASP ASP ASP ASP LYS LEU ALA ALA ALA GLN          
SEQRES   2 B  588  TYR PRO VAL VAL ASN THR ASN TYR GLY LYS ILE ARG GLY          
SEQRES   3 B  588  LEU ARG THR PRO LEU PRO ASN GLU ILE LEU GLY PRO VAL          
SEQRES   4 B  588  GLU GLN TYR LEU GLY VAL PRO TYR ALA SER PRO PRO THR          
SEQRES   5 B  588  GLY GLU ARG ARG PHE GLN PRO PRO GLU PRO PRO SER SER          
SEQRES   6 B  588  TRP THR GLY ILE ARG ASN THR THR GLN PHE ALA ALA VAL          
SEQRES   7 B  588  CYS PRO GLN HIS LEU ASP GLU ARG SER LEU LEU HIS ASP          
SEQRES   8 B  588  MET LEU PRO ILE TRP PHE THR ALA ASN LEU ASP THR LEU          
SEQRES   9 B  588  MET THR TYR VAL GLN ASP GLN ASN GLU ASP CYS LEU TYR          
SEQRES  10 B  588  LEU ASN ILE TYR VAL PRO THR GLU ASP ASP ILE HIS ASP          
SEQRES  11 B  588  GLN ASN SER LYS LYS PRO VAL MET VAL TYR ILE HIS GLY          
SEQRES  12 B  588  GLY SER TYR MET GLU GLY THR GLY ASN MET ILE ASP GLY          
SEQRES  13 B  588  SER ILE LEU ALA SER TYR GLY ASN VAL ILE VAL ILE THR          
SEQRES  14 B  588  ILE ASN TYR ARG LEU GLY ILE LEU GLY PHE LEU SER THR          
SEQRES  15 B  588  GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU LEU ASP          
SEQRES  16 B  588  GLN ILE GLN ALA LEU ARG TRP ILE GLU GLU ASN VAL GLY          
SEQRES  17 B  588  ALA PHE GLY GLY ASP PRO LYS ARG VAL THR ILE PHE GLY          
SEQRES  18 B  588  SER GLY ALA GLY ALA SER CYS VAL SER LEU LEU THR LEU          
SEQRES  19 B  588  SER HIS TYR SER GLU GLY LEU PHE GLN LYS ALA ILE ILE          
SEQRES  20 B  588  GLN SER GLY THR ALA LEU SER SER TRP ALA VAL ASN TYR          
SEQRES  21 B  588  GLN PRO ALA LYS TYR THR ARG ILE LEU ALA ASP LYS VAL          
SEQRES  22 B  588  GLY CYS ASN MET LEU ASP THR THR ASP MET VAL GLU CYS          
SEQRES  23 B  588  LEU ARG ASN LYS ASN TYR LYS GLU LEU ILE GLN GLN THR          
SEQRES  24 B  588  ILE THR PRO ALA THR TYR HIS ILE ALA PHE GLY PRO VAL          
SEQRES  25 B  588  ILE ASP GLY ASP VAL ILE PRO ASP ASP PRO GLN ILE LEU          
SEQRES  26 B  588  MET GLU GLN GLY GLU PHE LEU ASN TYR ASP ILE MET LEU          
SEQRES  27 B  588  GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL ASP GLY          
SEQRES  28 B  588  ILE VAL ASP ASN GLU ASP GLY VAL THR PRO ASN ASP PHE          
SEQRES  29 B  588  ASP PHE SER VAL SER ASN PHE VAL ASP ASN LEU TYR GLY          
SEQRES  30 B  588  TYR PRO GLU GLY LYS ASP THR LEU ARG GLU THR ILE LYS          
SEQRES  31 B  588  PHE MET TYR THR ASP TRP ALA ASP LYS GLU ASN PRO GLU          
SEQRES  32 B  588  THR ARG ARG LYS THR LEU VAL ALA LEU PHE THR ASP HIS          
SEQRES  33 B  588  GLN TRP VAL ALA PRO ALA VAL ALA THR ALA ASP LEU HIS          
SEQRES  34 B  588  ALA GLN TYR GLY SER PRO THR TYR PHE TYR ALA PHE TYR          
SEQRES  35 B  588  HIS HIS CYS GLN SER GLU MET LYS PRO SER TRP ALA ASP          
SEQRES  36 B  588  SER ALA HIS GLY ASP GLU VAL PRO TYR VAL PHE GLY ILE          
SEQRES  37 B  588  PRO MET ILE GLY PRO THR GLU LEU PHE SER CYS ASN PHE          
SEQRES  38 B  588  SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL MET THR          
SEQRES  39 B  588  TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO ASN GLN          
SEQRES  40 B  588  PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR LYS PRO          
SEQRES  41 B  588  ASN ARG PHE GLU GLU VAL ALA TRP SER ARG TYR ASN PRO          
SEQRES  42 B  588  LYS ASP GLN LEU TYR LEU HIS ILE GLY LEU LYS PRO ARG          
SEQRES  43 B  588  VAL ARG ASP HIS TYR ARG ALA THR LYS VAL ALA PHE TRP          
SEQRES  44 B  588  LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU ASN GLU ILE          
SEQRES  45 B  588  PHE GLN TYR VAL SER THR THR THR LYS VAL PRO PRO PRO          
SEQRES  46 B  588  ASP MET THR                                                  
SEQRES   1 C  179  GLY GLY HIS ALA GLY THR THR TYR ILE PHE SER LYS GLY          
SEQRES   2 C  179  GLY GLY GLN ILE THR TYR LYS TRP PRO PRO ASN ASP ARG          
SEQRES   3 C  179  PRO SER THR ARG ALA ASP ARG LEU ALA ILE GLY PHE SER          
SEQRES   4 C  179  THR VAL GLN LYS GLU ALA VAL LEU VAL ARG VAL ASP SER          
SEQRES   5 C  179  SER SER GLY LEU GLY ASP TYR LEU GLU LEU HIS ILE HIS          
SEQRES   6 C  179  GLN GLY LYS ILE GLY VAL LYS PHE ASN VAL GLY THR ASP          
SEQRES   7 C  179  ASP ILE ALA ILE GLU GLU SER ASN ALA ILE ILE ASN ASP          
SEQRES   8 C  179  GLY LYS TYR HIS VAL VAL ARG PHE THR ARG SER GLY GLY          
SEQRES   9 C  179  ASN ALA THR LEU GLN VAL ASP SER TRP PRO VAL ILE GLU          
SEQRES  10 C  179  ARG TYR PRO ALA GLY ARG GLN LEU THR ILE PHE ASN SER          
SEQRES  11 C  179  GLN ALA THR ILE ILE ILE GLY GLY LYS GLU GLN GLY GLN          
SEQRES  12 C  179  PRO PHE GLN GLY GLN LEU SER GLY LEU TYR TYR ASN GLY          
SEQRES  13 C  179  LEU LYS VAL LEU ASN MET ALA ALA GLU ASN ASP ALA ASN          
SEQRES  14 C  179  ILE ALA ILE VAL GLY ASN VAL ARG LEU VAL                      
SEQRES   1 D  179  GLY GLY HIS ALA GLY THR THR TYR ILE PHE SER LYS GLY          
SEQRES   2 D  179  GLY GLY GLN ILE THR TYR LYS TRP PRO PRO ASN ASP ARG          
SEQRES   3 D  179  PRO SER THR ARG ALA ASP ARG LEU ALA ILE GLY PHE SER          
SEQRES   4 D  179  THR VAL GLN LYS GLU ALA VAL LEU VAL ARG VAL ASP SER          
SEQRES   5 D  179  SER SER GLY LEU GLY ASP TYR LEU GLU LEU HIS ILE HIS          
SEQRES   6 D  179  GLN GLY LYS ILE GLY VAL LYS PHE ASN VAL GLY THR ASP          
SEQRES   7 D  179  ASP ILE ALA ILE GLU GLU SER ASN ALA ILE ILE ASN ASP          
SEQRES   8 D  179  GLY LYS TYR HIS VAL VAL ARG PHE THR ARG SER GLY GLY          
SEQRES   9 D  179  ASN ALA THR LEU GLN VAL ASP SER TRP PRO VAL ILE GLU          
SEQRES  10 D  179  ARG TYR PRO ALA GLY ARG GLN LEU THR ILE PHE ASN SER          
SEQRES  11 D  179  GLN ALA THR ILE ILE ILE GLY GLY LYS GLU GLN GLY GLN          
SEQRES  12 D  179  PRO PHE GLN GLY GLN LEU SER GLY LEU TYR TYR ASN GLY          
SEQRES  13 D  179  LEU LYS VAL LEU ASN MET ALA ALA GLU ASN ASP ALA ASN          
SEQRES  14 D  179  ILE ALA ILE VAL GLY ASN VAL ARG LEU VAL                      
HET    NAG  A 700      14                                                       
HET    NAG  A 701      14                                                       
HET    EDO  A1599       4                                                       
HET    EDO  A1600       4                                                       
HET    EDO  A1601       4                                                       
HET    EDO  A1602       4                                                       
HET    EDO  A1603       4                                                       
HET    EDO  A1604       4                                                       
HET    EDO  A1605       4                                                       
HET    EDO  A1606       4                                                       
HET    EDO  A1607       4                                                       
HET    EDO  A1608       4                                                       
HET     CL  A1609       1                                                       
HET     CL  A1610       1                                                       
HET    NAG  B 700      14                                                       
HET    NAG  B 701      14                                                       
HET    EDO  B1599       4                                                       
HET    EDO  B1600       4                                                       
HET    EDO  B1601       4                                                       
HET    EDO  B1602       4                                                       
HET    EDO  B1603       4                                                       
HET    EDO  B1604       4                                                       
HET    EDO  B1605       4                                                       
HET    EDO  B1606       4                                                       
HET    EDO  B1607       4                                                       
HET    EDO  B1608       4                                                       
HET    EDO  B1609       4                                                       
HET    EDO  B1610       4                                                       
HET    EDO  B1611       4                                                       
HET    EDO  B1612       4                                                       
HET     CL  B1613       1                                                       
HET     CL  B1614       1                                                       
HET     CL  B1615       1                                                       
HET    MES  C1289      12                                                       
HET    EDO  C1290       4                                                       
HET    EDO  C1291       4                                                       
HET    EDO  C1292       4                                                       
HET    EDO  C1293       4                                                       
HET    EDO  C1294       4                                                       
HET    EDO  C1295       4                                                       
HET     CA  C1296       1                                                       
HET     CA  D1289       1                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CA CALCIUM ION                                                      
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     NAG NAG                                                              
FORMUL   5   CL    5(CL 1-)                                                     
FORMUL   8  NAG    4(C8 H15 N O6)                                               
FORMUL  14   CA    2(CA 2+)                                                     
FORMUL  16  MES    C6 H13 N O4 S                                                
FORMUL  17  EDO    30(C2 H6 O2)                                                 
FORMUL  47  HOH   *349(H2 O)                                                    
HELIX    1   1 THR A   83  ARG A   87  5                                   5    
HELIX    2   2 LEU A  120  LEU A  124  5                                   5    
HELIX    3   3 PRO A  125  ASN A  131  1                                   7    
HELIX    4   4 ASN A  131  GLN A  140  1                                  10    
HELIX    5   5 THR A  181  ILE A  185  5                                   5    
HELIX    6   6 GLY A  187  ASN A  195  1                                   9    
HELIX    7   7 LEU A  205  LEU A  211  1                                   7    
HELIX    8   8 ASN A  221  VAL A  238  1                                  18    
HELIX    9   9 GLY A  239  PHE A  241  5                                   3    
HELIX   10  10 GLY A  254  THR A  264  1                                  11    
HELIX   11  11 LEU A  265  GLU A  270  5                                   6    
HELIX   12  12 GLN A  292  GLY A  305  1                                  14    
HELIX   13  13 ASP A  310  LYS A  321  1                                  12    
HELIX   14  14 ASN A  322  GLN A  328  1                                   7    
HELIX   15  15 ASP A  352  GLN A  359  1                                   8    
HELIX   16  16 GLY A  376  ASP A  381  5                                   6    
HELIX   17  17 THR A  391  TYR A  407  1                                  17    
HELIX   18  18 GLY A  412  TYR A  424  1                                  13    
HELIX   19  19 ASN A  432  TRP A  449  1                                  18    
HELIX   20  20 TRP A  449  TYR A  463  1                                  15    
HELIX   21  21 GLU A  492  PHE A  497  1                                   6    
HELIX   22  22 GLY A  498  ILE A  502  5                                   5    
HELIX   23  23 SER A  513  GLY A  534  1                                  22    
HELIX   24  24 ARG A  583  GLU A  592  1                                  10    
HELIX   25  25 ASP B   -6  TYR B   45  1                                   8    
HELIX   26  26 THR B   83  ARG B   87  5                                   5    
HELIX   27  27 LEU B  120  LEU B  124  5                                   5    
HELIX   28  28 PRO B  125  ALA B  130  1                                   6    
HELIX   29  29 ASN B  131  MET B  136  1                                   6    
HELIX   30  30 THR B  181  ILE B  185  5                                   5    
HELIX   31  31 GLY B  187  ASN B  195  1                                   9    
HELIX   32  32 LEU B  205  LEU B  211  1                                   7    
HELIX   33  33 ASN B  221  VAL B  238  1                                  18    
HELIX   34  34 GLY B  239  PHE B  241  5                                   3    
HELIX   35  35 GLY B  254  THR B  264  1                                  11    
HELIX   36  36 LEU B  265  GLU B  270  5                                   6    
HELIX   37  37 GLN B  292  GLY B  305  1                                  14    
HELIX   38  38 ASP B  310  LYS B  321  1                                  12    
HELIX   39  39 ASN B  322  GLN B  328  1                                   7    
HELIX   40  40 ASP B  352  GLN B  359  1                                   8    
HELIX   41  41 GLY B  376  ASP B  381  5                                   6    
HELIX   42  42 THR B  391  TYR B  407  1                                  17    
HELIX   43  43 GLY B  412  TYR B  424  1                                  13    
HELIX   44  44 ASN B  432  TRP B  449  1                                  18    
HELIX   45  45 TRP B  449  TYR B  463  1                                  15    
HELIX   46  46 GLU B  492  PHE B  497  1                                   6    
HELIX   47  47 GLY B  498  ILE B  502  5                                   5    
HELIX   48  48 SER B  513  GLY B  534  1                                  22    
HELIX   49  49 ARG B  583  GLU B  592  1                                  10    
HELIX   50  50 PRO C  101  ARG C  105  5                                   5    
HELIX   51  51 LYS C  267  GLU C  274  1                                   8    
HELIX   52  52 LYS D  267  GLU D  274  1                                   8    
SHEET    1  AA 3 VAL A  47  THR A  50  0                                        
SHEET    2  AA 3 GLY A  53  ARG A  56 -1  O  GLY A  53   N  THR A  50           
SHEET    3  AA 3 ILE A 100  ASN A 102  1  O  ARG A 101   N  ARG A  56           
SHEET    1  AB11 LEU A  58  THR A  60  0                                        
SHEET    2  AB11 VAL A  70  PRO A  77 -1  O  VAL A  70   N  THR A  60           
SHEET    3  AB11 TYR A 148  PRO A 154 -1  O  LEU A 149   N  VAL A  76           
SHEET    4  AB11 ILE A 197  ILE A 201 -1  O  VAL A 198   N  TYR A 152           
SHEET    5  AB11 LYS A 166  ILE A 172  1  O  PRO A 167   N  ILE A 197           
SHEET    6  AB11 GLY A 243  SER A 253  1  N  ASP A 244   O  LYS A 166           
SHEET    7  AB11 LYS A 275  GLN A 279  1  O  LYS A 275   N  ILE A 250           
SHEET    8  AB11 ASP A 366  ASN A 372  1  O  ASP A 366   N  ALA A 276           
SHEET    9  AB11 THR A 467  PHE A 472  1  O  TYR A 468   N  LEU A 369           
SHEET   10  AB11 LEU A 568  ILE A 572  1  O  LEU A 570   N  ALA A 471           
SHEET   11  AB11 ARG A 577  ASP A 580 -1  O  ARG A 577   N  HIS A 571           
SHEET    1  BA 3 VAL B  47  THR B  50  0                                        
SHEET    2  BA 3 GLY B  53  ARG B  56 -1  O  GLY B  53   N  THR B  50           
SHEET    3  BA 3 ILE B 100  ASN B 102  1  O  ARG B 101   N  ARG B  56           
SHEET    1  BB11 LEU B  58  THR B  60  0                                        
SHEET    2  BB11 VAL B  70  PRO B  77 -1  O  VAL B  70   N  THR B  60           
SHEET    3  BB11 TYR B 148  PRO B 154 -1  O  LEU B 149   N  VAL B  76           
SHEET    4  BB11 ILE B 197  ILE B 201 -1  O  VAL B 198   N  TYR B 152           
SHEET    5  BB11 LYS B 166  ILE B 172  1  O  PRO B 167   N  ILE B 197           
SHEET    6  BB11 GLY B 243  SER B 253  1  N  ASP B 244   O  LYS B 166           
SHEET    7  BB11 LYS B 275  GLN B 279  1  O  LYS B 275   N  ILE B 250           
SHEET    8  BB11 ASP B 366  ASN B 372  1  O  ASP B 366   N  ALA B 276           
SHEET    9  BB11 THR B 467  PHE B 472  1  O  TYR B 468   N  LEU B 369           
SHEET   10  BB11 LEU B 568  ILE B 572  1  O  LEU B 570   N  ALA B 471           
SHEET   11  BB11 ARG B 577  ASP B 580 -1  O  ARG B 577   N  HIS B 571           
SHEET    1  BC 2 GLN B 477  SER B 478  0                                        
SHEET    2  BC 2 CYS B 510  ASN B 511 -1  O  ASN B 511   N  GLN B 477           
SHEET    1  CA 7 ILE C 159  GLU C 162  0                                        
SHEET    2  CA 7 LYS C 147  ASN C 153 -1  O  VAL C 150   N  ILE C 161           
SHEET    3  CA 7 TYR C 138  HIS C 144  1  O  TYR C 138   N  ASN C 153           
SHEET    4  CA 7 GLU C 123  SER C 131  1  O  ALA C 124   N  ILE C 143           
SHEET    5  CA 7 GLN C 240  ILE C 245  1  N  ALA C 241   O  ASP C 130           
SHEET    6  CA 7 THR C  86  LYS C  99 -1  O  ILE C  96   N  ILE C 245           
SHEET    7  CA 7 ILE C 279  ARG C 286 -1  O  ALA C 280   N  THR C  97           
SHEET    1  CB11 ILE C 159  GLU C 162  0                                        
SHEET    2  CB11 LYS C 147  ASN C 153 -1  O  VAL C 150   N  ILE C 161           
SHEET    3  CB11 TYR C 138  HIS C 144  1  O  TYR C 138   N  ASN C 153           
SHEET    4  CB11 GLU C 123  SER C 131  1  O  ALA C 124   N  ILE C 143           
SHEET    5  CB11 GLN C 240  ILE C 245  1  N  ALA C 241   O  ASP C 130           
SHEET    6  CB11 THR C  86  LYS C  99 -1  O  ILE C  96   N  ILE C 245           
SHEET    7  CB11 GLY C 256  TYR C 263 -1  O  GLY C 256   N  PHE C  89           
SHEET    8  CB11 ALA C 110  SER C 118 -1  O  ALA C 114   N  TYR C 262           
SHEET    9  CB11 HIS C 174  SER C 181 -1  O  HIS C 174   N  PHE C 117           
SHEET   10  CB11 ASN C 184  VAL C 189 -1  O  ASN C 184   N  SER C 181           
SHEET   11  CB11 ILE C 195  ARG C 197 -1  O  ILE C 195   N  LEU C 187           
SHEET    1  CC 2 ILE C 279  ARG C 286  0                                        
SHEET    2  CC 2 THR C  86  LYS C  99 -1  O  ILE C  88   N  ARG C 286           
SHEET    1  DA 7 ILE D 159  GLU D 162  0                                        
SHEET    2  DA 7 LYS D 147  ASN D 153 -1  O  VAL D 150   N  ILE D 161           
SHEET    3  DA 7 TYR D 138  HIS D 144  1  O  TYR D 138   N  ASN D 153           
SHEET    4  DA 7 ALA D 124  SER D 131  1  O  ALA D 124   N  ILE D 143           
SHEET    5  DA 7 GLN D 240  ILE D 245  1  N  ALA D 241   O  ASP D 130           
SHEET    6  DA 7 THR D  86  LYS D  99 -1  O  ILE D  96   N  ILE D 245           
SHEET    7  DA 7 ILE D 279  ARG D 286 -1  O  ALA D 280   N  THR D  97           
SHEET    1  DB11 ILE D 159  GLU D 162  0                                        
SHEET    2  DB11 LYS D 147  ASN D 153 -1  O  VAL D 150   N  ILE D 161           
SHEET    3  DB11 TYR D 138  HIS D 144  1  O  TYR D 138   N  ASN D 153           
SHEET    4  DB11 ALA D 124  SER D 131  1  O  ALA D 124   N  ILE D 143           
SHEET    5  DB11 GLN D 240  ILE D 245  1  N  ALA D 241   O  ASP D 130           
SHEET    6  DB11 THR D  86  LYS D  99 -1  O  ILE D  96   N  ILE D 245           
SHEET    7  DB11 GLY D 256  TYR D 263 -1  O  GLY D 256   N  PHE D  89           
SHEET    8  DB11 ALA D 110  SER D 118 -1  O  ALA D 114   N  TYR D 262           
SHEET    9  DB11 HIS D 174  SER D 181 -1  O  HIS D 174   N  PHE D 117           
SHEET   10  DB11 ASN D 184  VAL D 189 -1  O  ASN D 184   N  SER D 181           
SHEET   11  DB11 ILE D 195  ARG D 197 -1  O  ILE D 195   N  LEU D 187           
SHEET    1  DC 2 ILE D 279  ARG D 286  0                                        
SHEET    2  DC 2 THR D  86  LYS D  99 -1  O  ILE D  88   N  ARG D 286           
SSBOND   1 CYS A  110    CYS A  146                          1555   1555  2.05  
SSBOND   2 CYS A  306    CYS A  317                          1555   1555  2.09  
SSBOND   3 CYS A  476    CYS A  510                          1555   1555  2.07  
SSBOND   4 CYS B  110    CYS B  146                          1555   1555  2.07  
SSBOND   5 CYS B  306    CYS B  317                          1555   1555  2.07  
SSBOND   6 CYS B  476    CYS B  510                          1555   1555  2.06  
LINK         ND2 ASN A 102                 C1  NAG A 700     1555   1555  1.44  
LINK         ND2 ASN A 511                 C1  NAG A 701     1555   1555  1.37  
LINK         ND2 ASN B 102                 C1  NAG B 700     1555   1555  1.39  
LINK         ND2 ASN B 511                 C1  NAG B 701     1555   1555  1.52  
LINK        CA    CA C1296                 O   ILE C 236     1555   1555  2.24  
LINK        CA    CA C1296                 OD2 ASP C 137     1555   1555  2.34  
LINK        CA    CA C1296                 OD1 ASN C 238     1555   1555  2.30  
LINK        CA    CA C1296                 O   HOH C2012     1555   1555  2.11  
LINK        CA    CA C1296                 O   VAL C 154     1555   1555  2.36  
LINK        CA    CA C1296                 O   HOH A2060     1555   1555  2.53  
LINK        CA    CA D1289                 OD2 ASP D 137     1555   1555  2.30  
LINK        CA    CA D1289                 O   HOH B2096     1555   1555  2.27  
LINK        CA    CA D1289                 O   VAL D 154     1555   1555  2.34  
LINK        CA    CA D1289                 O   ILE D 236     1555   1555  2.27  
LINK        CA    CA D1289                 O   HOH D2006     1555   1555  1.98  
LINK        CA    CA D1289                 OD1 ASN D 238     1555   1555  2.27  
CISPEP   1 PRO A  410    GLU A  411          0         2.93                     
SITE     1 AC1  4 ARG A  56  ASN A 102  HOH A2124  ASN D 165                    
SITE     1 AC2  1 ASN A 511                                                     
SITE     1 AC3  4 ARG A 232  GLU A 235  GLU A 270  LEU A 272                    
SITE     1 AC4  4 GLN A 292  PRO A 293  ALA A 294  LYS A 295                    
SITE     1 AC5  7 PHE A 106  ALA A 107  ALA A 108  VAL A 109                    
SITE     2 AC5  7 CYS A 146  ASN A 183  ASN A 202                               
SITE     1 AC6  4 ASN A 386  EDO A1608  GLN C 121  GLU C 123                    
SITE     1 AC7  4 THR A 391  PRO A 392  PRO A 433  ARG A 436                    
SITE     1 AC8  7 TYR A 569  ASP A 580  HIS A 581  TYR A 582                    
SITE     2 AC8  7 ARG A 583  HOH A2125  HOH A2126                               
SITE     1 AC9  6 ILE A 126  CYS A 476  MET A 480  LYS A 481                    
SITE     2 AC9  6 ASP A 491  PHE A 508                                          
SITE     1 BC1  4 THR A 137  TYR A 138  GLN A 140  ASP A 141                    
SITE     1 BC2  1 GLN A 373                                                     
SITE     1 BC3  5 GLY A 382  VAL A 384  EDO A1602  HOH A2129                    
SITE     2 BC3  5 LYS C 122                                                     
SITE     1 BC4  2 ARG A 583  THR A 585                                          
SITE     1 BC5  2 MET A 423  LYS A 586                                          
SITE     1 BC6  5 ILE B 100  ASN B 102  EDO B1609  HOH B2157                    
SITE     2 BC6  5 HOH B2158                                                     
SITE     1 BC7  1 ASN B 511                                                     
SITE     1 BC8  3 GLN B 292  ALA B 294  LYS B 295                               
SITE     1 BC9  7 VAL B 454  TYR B 562  GLN B 567  TYR B 569                    
SITE     2 BC9  7 HIS B 581  TYR B 582  HOH B2159                               
SITE     1 CC1  4 MET B 178  GLN B 329  THR B 330  ILE B 331                    
SITE     1 CC2  2 HIS B 447  LEU B 591                                          
SITE     1 CC3  2 ASP B  -8  LYS B  54                                          
SITE     1 CC4  3 GLU B 235  PRO B 245  GLY B 271                               
SITE     1 CC5  8 PHE B  88  GLN B  89  PRO B  90  GLN B 216                    
SITE     2 CC5  8 ALA B 217  LYS B 219  TYR B 222  HOH B2161                    
SITE     1 CC6  4 ASP B 122  TYR B 336  LYS B 378  PHE B 379                    
SITE     1 CC7  7 ASP B 122  LEU B 124  ILE B 126  GLU B 375                    
SITE     2 CC7  7 GLY B 376  LYS B 378  PHE B 444                               
SITE     1 CC8  2 ASP B 385  THR B 391                                          
SITE     1 CC9  2 TYR B  45  NAG B 700                                          
SITE     1 DC1  2 GLY B  84  ASN B 320                                          
SITE     1 DC2  5 LYS A 575  LEU B  62  ASN B  64  GLU B  65                    
SITE     2 DC2  5 LEU B  67                                                     
SITE     1 DC3  6 GLY B 174  GLY B 175  GLU B 179  GLY B 180                    
SITE     2 DC3  6 THR B 181  MET B 184                                          
SITE     1 DC4  3 ARG B 583  THR B 585  LYS B 586                               
SITE     1 DC5  2 MET B 423  LYS B 586                                          
SITE     1 DC6  1 GLU B 592                                                     
SITE     1 DC7  6 TRP B  97  THR B  98  ILE B 100  ARG B 101                    
SITE     2 DC7  6 GLU C 196  HOH C2038                                          
SITE     1 DC8  4 SER B  96  HOH B2024  VAL C 194  GLU C 196                    
SITE     1 DC9  3 LYS C 122  GLN C 145  ASN C 169                               
SITE     1 EC1  2 TYR C 173  ASP C 190                                          
SITE     1 EC2  3 ALA C 110  ASP C 111  ARG C 112                               
SITE     1 EC3  4 GLU B  85  GLY C 260  TYR C 262  EDO C1295                    
SITE     1 EC4  4 ALA C 114  TYR C 173  GLY C 260  EDO C1294                    
SITE     1 EC5  6 HOH A2060  ASP C 137  VAL C 154  ILE C 236                    
SITE     2 EC5  6 ASN C 238  HOH C2012                                          
SITE     1 EC6  6 HOH B2096  ASP D 137  VAL D 154  ILE D 236                    
SITE     2 EC6  6 ASN D 238  HOH D2006                                          
CRYST1  136.307  198.779   85.896  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007336  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005031  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011642        0.00000                         
TER    4183      HIS A 598                                                      
TER    8460      HIS B 598                                                      
TER    9820      VAL C 288                                                      
TER   11180      VAL D 288                                                      
MASTER      992    0   42   52   70    0   55    611720    4  220  120          
END                                                                             

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