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LongText Report for: 7cee-pdb

Name Class
7cee-pdb
HEADER    CELL ADHESION                           23-JUN-20   7CEE              
TITLE     CRYSTAL STRUCTURE OF MOUSE NEUROLIGIN-3                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUROLIGIN-3;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GLIOTACTIN HOMOLOG;                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: NLGN3;                                                         
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F                                 
KEYWDS    SYNAPSE ORGANIZATION, TRANS-SYNAPTIC COMPLEX, ESTERASE DOMAIN, CELL   
KEYWDS   2 ADHESION                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.YAMAGATA,T.YOSHIDA,T.SHIROSHIMA,A.MAEDA,S.FUKAI                     
REVDAT   1   24-FEB-21 7CEE    0                                                
JRNL        AUTH   T.YOSHIDA,A.YAMAGATA,A.IMAI,J.KIM,H.IZUMI,T.SHIROSHIMA,      
JRNL        AUTH 2 A.MAEDA,S.IWASAWA-OKAMOTO,K.AZECHI,F.OSAKA,T.SAITO,          
JRNL        AUTH 3 K.MAENAKA,T.SHIMADA,Y.FUKATA,M.FUKATA,Y.KOSHIDAKA,K.TAKAO,   
JRNL        AUTH 4 S.TANAKA,S.OKABE,K.TABUCHI,T.UEMURA,M.MISHINA,H.MORI,S.FUKAI 
JRNL        TITL   NON-CANONICAL INTERACTION BETWEEN NEUROLIGIN 3 AND PROTEIN   
JRNL        TITL 2 TYROSINE PHOSPHATASE DELTA UNDERLIES AUTISM-RELATED          
JRNL        TITL 3 PHENOTYPES                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.76 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.76                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.66                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.430                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 50376                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2501                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.6640 -  7.2337    1.00     2899   162  0.1837 0.2036        
REMARK   3     2  7.2337 -  5.7443    1.00     2762   172  0.1888 0.1839        
REMARK   3     3  5.7443 -  5.0190    1.00     2756   133  0.1699 0.2175        
REMARK   3     4  5.0190 -  4.5604    1.00     2735   134  0.1609 0.1931        
REMARK   3     5  4.5604 -  4.2338    1.00     2708   150  0.1664 0.2134        
REMARK   3     6  4.2338 -  3.9843    1.00     2685   153  0.1823 0.2219        
REMARK   3     7  3.9843 -  3.7848    0.99     2652   170  0.2042 0.2681        
REMARK   3     8  3.7848 -  3.6201    0.99     2673   134  0.2167 0.2885        
REMARK   3     9  3.6201 -  3.4808    0.99     2691   111  0.2317 0.2596        
REMARK   3    10  3.4808 -  3.3607    0.99     2699   118  0.2356 0.2565        
REMARK   3    11  3.3607 -  3.2556    0.99     2685   110  0.2415 0.2999        
REMARK   3    12  3.2556 -  3.1626    0.99     2650   122  0.2699 0.2902        
REMARK   3    13  3.1626 -  3.0793    0.98     2620   145  0.2927 0.3242        
REMARK   3    14  3.0793 -  3.0042    0.98     2612   142  0.3174 0.3608        
REMARK   3    15  3.0042 -  2.9359    0.98     2621   145  0.3299 0.3900        
REMARK   3    16  2.9359 -  2.8735    0.98     2581   132  0.3496 0.3882        
REMARK   3    17  2.8735 -  2.8160    0.98     2645   151  0.3663 0.4044        
REMARK   3    18  2.8160 -  2.7630    0.84     2201   117  0.3790 0.3877        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.760           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 55.71                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           8692                                  
REMARK   3   ANGLE     :  0.871          11878                                  
REMARK   3   CHIRALITY :  0.045           1297                                  
REMARK   3   PLANARITY :  0.004           1547                                  
REMARK   3   DIHEDRAL  : 13.792           3106                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  41.5403  13.8112 -10.5651              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5600 T22:   0.5819                                     
REMARK   3      T33:   0.5394 T12:   0.0115                                     
REMARK   3      T13:  -0.0480 T23:  -0.0504                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5988 L22:   0.0812                                     
REMARK   3      L33:   1.1163 L12:  -0.0363                                     
REMARK   3      L13:  -1.2903 L23:   0.1352                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0287 S12:   0.1898 S13:   0.0452                       
REMARK   3      S21:  -0.0630 S22:  -0.0066 S23:   0.0001                       
REMARK   3      S31:  -0.0314 S32:  -0.0852 S33:  -0.0001                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND SEGID A                         
REMARK   3     SELECTION          : CHAIN B AND SEGID B                         
REMARK   3     ATOM PAIRS NUMBER  : 5038                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7CEE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUN-20.                  
REMARK 100 THE DEPOSITION ID IS D_1300017476.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50446                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.760                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 7.700                              
REMARK 200  R MERGE                    (I) : 0.11100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 4.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.76                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 3BIX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 3350, 0.2 M AMMONIUM CHLORIDE,   
REMARK 280  0.1 M MES-NA, PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       32.92100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.97500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       83.57100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.97500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.92100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       83.57100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ALA A    36                                                      
REMARK 465     PRO A    37                                                      
REMARK 465     GLU A   148                                                      
REMARK 465     ASP A   149                                                      
REMARK 465     GLY A   150                                                      
REMARK 465     SER A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     ALA A   153                                                      
REMARK 465     LYS A   154                                                      
REMARK 465     LYS A   155                                                      
REMARK 465     GLN A   156                                                      
REMARK 465     GLY A   157                                                      
REMARK 465     GLU A   158                                                      
REMARK 465     ASP A   159                                                      
REMARK 465     LEU A   160                                                      
REMARK 465     ALA A   161                                                      
REMARK 465     ASP A   162                                                      
REMARK 465     ASN A   163                                                      
REMARK 465     ASP A   164                                                      
REMARK 465     GLY A   165                                                      
REMARK 465     ASP A   166                                                      
REMARK 465     GLU A   167                                                      
REMARK 465     ASP A   168                                                      
REMARK 465     GLU A   169                                                      
REMARK 465     ASP A   170                                                      
REMARK 465     ILE A   171                                                      
REMARK 465     ARG A   172                                                      
REMARK 465     ASP A   173                                                      
REMARK 465     THR A   555                                                      
REMARK 465     LYS A   556                                                      
REMARK 465     PHE A   557                                                      
REMARK 465     ILE A   558                                                      
REMARK 465     HIS A   559                                                      
REMARK 465     THR A   560                                                      
REMARK 465     LYS A   561                                                      
REMARK 465     ALA A   562                                                      
REMARK 465     ASN A   563                                                      
REMARK 465     ARG A   564                                                      
REMARK 465     PHE A   565                                                      
REMARK 465     GLU A   566                                                      
REMARK 465     GLU A   567                                                      
REMARK 465     LEU A   611                                                      
REMARK 465     HIS A   612                                                      
REMARK 465     ASP A   613                                                      
REMARK 465     MET A   614                                                      
REMARK 465     PHE A   615                                                      
REMARK 465     HIS A   616                                                      
REMARK 465     TYR A   617                                                      
REMARK 465     THR A   618                                                      
REMARK 465     SER A   619                                                      
REMARK 465     THR A   620                                                      
REMARK 465     THR A   621                                                      
REMARK 465     THR A   622                                                      
REMARK 465     LYS A   623                                                      
REMARK 465     VAL A   624                                                      
REMARK 465     PRO A   625                                                      
REMARK 465     PRO A   626                                                      
REMARK 465     PRO A   627                                                      
REMARK 465     ASP A   628                                                      
REMARK 465     THR A   629                                                      
REMARK 465     THR A   630                                                      
REMARK 465     HIS A   631                                                      
REMARK 465     SER A   632                                                      
REMARK 465     SER A   633                                                      
REMARK 465     HIS A   634                                                      
REMARK 465     ILE A   635                                                      
REMARK 465     THR A   636                                                      
REMARK 465     ARG A   637                                                      
REMARK 465     ARG A   638                                                      
REMARK 465     PRO A   639                                                      
REMARK 465     ASN A   640                                                      
REMARK 465     GLY A   641                                                      
REMARK 465     LYS A   642                                                      
REMARK 465     THR A   643                                                      
REMARK 465     TRP A   644                                                      
REMARK 465     SER A   645                                                      
REMARK 465     THR A   646                                                      
REMARK 465     LYS A   647                                                      
REMARK 465     ARG A   648                                                      
REMARK 465     PRO A   649                                                      
REMARK 465     ALA A   650                                                      
REMARK 465     ILE A   651                                                      
REMARK 465     SER A   652                                                      
REMARK 465     PRO A   653                                                      
REMARK 465     ALA A   654                                                      
REMARK 465     TYR A   655                                                      
REMARK 465     SER A   656                                                      
REMARK 465     ASN A   657                                                      
REMARK 465     GLU A   658                                                      
REMARK 465     ASN A   659                                                      
REMARK 465     ALA A   660                                                      
REMARK 465     PRO A   661                                                      
REMARK 465     GLY A   662                                                      
REMARK 465     SER A   663                                                      
REMARK 465     TRP A   664                                                      
REMARK 465     ASN A   665                                                      
REMARK 465     GLY A   666                                                      
REMARK 465     ASP A   667                                                      
REMARK 465     GLN A   668                                                      
REMARK 465     ASP A   669                                                      
REMARK 465     ALA A   670                                                      
REMARK 465     GLY A   671                                                      
REMARK 465     PRO A   672                                                      
REMARK 465     LEU A   673                                                      
REMARK 465     LEU A   674                                                      
REMARK 465     VAL A   675                                                      
REMARK 465     GLU A   676                                                      
REMARK 465     ASN A   677                                                      
REMARK 465     PRO A   678                                                      
REMARK 465     ARG A   679                                                      
REMARK 465     ASP A   680                                                      
REMARK 465     TYR A   681                                                      
REMARK 465     SER A   682                                                      
REMARK 465     THR A   683                                                      
REMARK 465     GLU A   684                                                      
REMARK 465     HIS A   685                                                      
REMARK 465     HIS A   686                                                      
REMARK 465     HIS A   687                                                      
REMARK 465     HIS A   688                                                      
REMARK 465     HIS A   689                                                      
REMARK 465     HIS A   690                                                      
REMARK 465     ALA B    36                                                      
REMARK 465     PRO B    37                                                      
REMARK 465     GLU B   148                                                      
REMARK 465     ASP B   149                                                      
REMARK 465     GLY B   150                                                      
REMARK 465     SER B   151                                                      
REMARK 465     GLY B   152                                                      
REMARK 465     ALA B   153                                                      
REMARK 465     LYS B   154                                                      
REMARK 465     LYS B   155                                                      
REMARK 465     GLN B   156                                                      
REMARK 465     GLY B   157                                                      
REMARK 465     GLU B   158                                                      
REMARK 465     ASP B   159                                                      
REMARK 465     LEU B   160                                                      
REMARK 465     ALA B   161                                                      
REMARK 465     ASP B   162                                                      
REMARK 465     ASN B   163                                                      
REMARK 465     ASP B   164                                                      
REMARK 465     GLY B   165                                                      
REMARK 465     ASP B   166                                                      
REMARK 465     GLU B   167                                                      
REMARK 465     ASP B   168                                                      
REMARK 465     GLU B   169                                                      
REMARK 465     ASP B   170                                                      
REMARK 465     ILE B   171                                                      
REMARK 465     ARG B   172                                                      
REMARK 465     ASP B   173                                                      
REMARK 465     SER B   174                                                      
REMARK 465     THR B   555                                                      
REMARK 465     LYS B   556                                                      
REMARK 465     PHE B   557                                                      
REMARK 465     ILE B   558                                                      
REMARK 465     HIS B   559                                                      
REMARK 465     THR B   560                                                      
REMARK 465     LYS B   561                                                      
REMARK 465     ALA B   562                                                      
REMARK 465     ASN B   563                                                      
REMARK 465     ARG B   564                                                      
REMARK 465     PHE B   565                                                      
REMARK 465     GLU B   566                                                      
REMARK 465     GLU B   567                                                      
REMARK 465     LEU B   611                                                      
REMARK 465     HIS B   612                                                      
REMARK 465     ASP B   613                                                      
REMARK 465     MET B   614                                                      
REMARK 465     PHE B   615                                                      
REMARK 465     HIS B   616                                                      
REMARK 465     TYR B   617                                                      
REMARK 465     THR B   618                                                      
REMARK 465     SER B   619                                                      
REMARK 465     THR B   620                                                      
REMARK 465     THR B   621                                                      
REMARK 465     THR B   622                                                      
REMARK 465     LYS B   623                                                      
REMARK 465     VAL B   624                                                      
REMARK 465     PRO B   625                                                      
REMARK 465     PRO B   626                                                      
REMARK 465     PRO B   627                                                      
REMARK 465     ASP B   628                                                      
REMARK 465     THR B   629                                                      
REMARK 465     THR B   630                                                      
REMARK 465     HIS B   631                                                      
REMARK 465     SER B   632                                                      
REMARK 465     SER B   633                                                      
REMARK 465     HIS B   634                                                      
REMARK 465     ILE B   635                                                      
REMARK 465     THR B   636                                                      
REMARK 465     ARG B   637                                                      
REMARK 465     ARG B   638                                                      
REMARK 465     PRO B   639                                                      
REMARK 465     ASN B   640                                                      
REMARK 465     GLY B   641                                                      
REMARK 465     LYS B   642                                                      
REMARK 465     THR B   643                                                      
REMARK 465     TRP B   644                                                      
REMARK 465     SER B   645                                                      
REMARK 465     THR B   646                                                      
REMARK 465     LYS B   647                                                      
REMARK 465     ARG B   648                                                      
REMARK 465     PRO B   649                                                      
REMARK 465     ALA B   650                                                      
REMARK 465     ILE B   651                                                      
REMARK 465     SER B   652                                                      
REMARK 465     PRO B   653                                                      
REMARK 465     ALA B   654                                                      
REMARK 465     TYR B   655                                                      
REMARK 465     SER B   656                                                      
REMARK 465     ASN B   657                                                      
REMARK 465     GLU B   658                                                      
REMARK 465     ASN B   659                                                      
REMARK 465     ALA B   660                                                      
REMARK 465     PRO B   661                                                      
REMARK 465     GLY B   662                                                      
REMARK 465     SER B   663                                                      
REMARK 465     TRP B   664                                                      
REMARK 465     ASN B   665                                                      
REMARK 465     GLY B   666                                                      
REMARK 465     ASP B   667                                                      
REMARK 465     GLN B   668                                                      
REMARK 465     ASP B   669                                                      
REMARK 465     ALA B   670                                                      
REMARK 465     GLY B   671                                                      
REMARK 465     PRO B   672                                                      
REMARK 465     LEU B   673                                                      
REMARK 465     LEU B   674                                                      
REMARK 465     VAL B   675                                                      
REMARK 465     GLU B   676                                                      
REMARK 465     ASN B   677                                                      
REMARK 465     PRO B   678                                                      
REMARK 465     ARG B   679                                                      
REMARK 465     ASP B   680                                                      
REMARK 465     TYR B   681                                                      
REMARK 465     SER B   682                                                      
REMARK 465     THR B   683                                                      
REMARK 465     GLU B   684                                                      
REMARK 465     HIS B   685                                                      
REMARK 465     HIS B   686                                                      
REMARK 465     HIS B   687                                                      
REMARK 465     HIS B   688                                                      
REMARK 465     HIS B   689                                                      
REMARK 465     HIS B   690                                                      
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   OD1  ASN B    95     OG1  THR B    97              2.13            
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    SER A 187       16.94   -149.63                                   
REMARK 500    TYR A 188       -8.34     78.01                                   
REMARK 500    PHE A 221       11.38   -142.37                                   
REMARK 500    ASP A 226     -153.37   -138.10                                   
REMARK 500    ARG A 258       72.91   -112.77                                   
REMARK 500    ASP A 358      -78.39   -114.83                                   
REMARK 500    ASP A 440       65.29   -157.03                                   
REMARK 500    TRP A 460      -59.03   -121.15                                   
REMARK 500    PRO A 520       13.58    -68.66                                   
REMARK 500    SER B 187       17.01   -150.17                                   
REMARK 500    TYR B 188       -7.91     78.90                                   
REMARK 500    PHE B 221       11.29   -142.98                                   
REMARK 500    ASP B 226     -153.15   -138.75                                   
REMARK 500    ARG B 258       72.84   -112.85                                   
REMARK 500    ASP B 358      -78.11   -114.58                                   
REMARK 500    ASP B 440       64.49   -156.96                                   
REMARK 500    TRP B 460      -58.62   -121.33                                   
REMARK 500    PRO B 520       14.36    -68.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7CEE A   36   684  UNP    Q8BYM5   NLGN3_MOUSE     36    684             
DBREF  7CEE B   36   684  UNP    Q8BYM5   NLGN3_MOUSE     36    684             
SEQADV 7CEE HIS A  685  UNP  Q8BYM5              EXPRESSION TAG                 
SEQADV 7CEE HIS A  686  UNP  Q8BYM5              EXPRESSION TAG                 
SEQADV 7CEE HIS A  687  UNP  Q8BYM5              EXPRESSION TAG                 
SEQADV 7CEE HIS A  688  UNP  Q8BYM5              EXPRESSION TAG                 
SEQADV 7CEE HIS A  689  UNP  Q8BYM5              EXPRESSION TAG                 
SEQADV 7CEE HIS A  690  UNP  Q8BYM5              EXPRESSION TAG                 
SEQADV 7CEE HIS B  685  UNP  Q8BYM5              EXPRESSION TAG                 
SEQADV 7CEE HIS B  686  UNP  Q8BYM5              EXPRESSION TAG                 
SEQADV 7CEE HIS B  687  UNP  Q8BYM5              EXPRESSION TAG                 
SEQADV 7CEE HIS B  688  UNP  Q8BYM5              EXPRESSION TAG                 
SEQADV 7CEE HIS B  689  UNP  Q8BYM5              EXPRESSION TAG                 
SEQADV 7CEE HIS B  690  UNP  Q8BYM5              EXPRESSION TAG                 
SEQRES   1 A  655  ALA PRO ALA PRO THR VAL ASN THR HIS PHE GLY LYS LEU          
SEQRES   2 A  655  ARG GLY ALA ARG VAL PRO LEU PRO SER GLU ILE LEU GLY          
SEQRES   3 A  655  PRO VAL ASP GLN TYR LEU GLY VAL PRO TYR ALA ALA PRO          
SEQRES   4 A  655  PRO ILE GLY GLU LYS ARG PHE LEU PRO PRO GLU PRO PRO          
SEQRES   5 A  655  PRO SER TRP SER GLY ILE ARG ASN ALA THR HIS PHE PRO          
SEQRES   6 A  655  PRO VAL CYS PRO GLN ASN ILE HIS THR ALA VAL PRO GLU          
SEQRES   7 A  655  VAL MET LEU PRO VAL TRP PHE THR ALA ASN LEU ASP ILE          
SEQRES   8 A  655  VAL ALA THR TYR ILE GLN GLU PRO ASN GLU ASP CYS LEU          
SEQRES   9 A  655  TYR LEU ASN VAL TYR VAL PRO THR GLU ASP GLY SER GLY          
SEQRES  10 A  655  ALA LYS LYS GLN GLY GLU ASP LEU ALA ASP ASN ASP GLY          
SEQRES  11 A  655  ASP GLU ASP GLU ASP ILE ARG ASP SER GLY ALA LYS PRO          
SEQRES  12 A  655  VAL MET VAL TYR ILE HIS GLY GLY SER TYR MET GLU GLY          
SEQRES  13 A  655  THR GLY ASN MET ILE ASP GLY SER VAL LEU ALA SER TYR          
SEQRES  14 A  655  GLY ASN VAL ILE VAL ILE THR LEU ASN TYR ARG VAL GLY          
SEQRES  15 A  655  VAL LEU GLY PHE LEU SER THR GLY ASP GLN ALA ALA LYS          
SEQRES  16 A  655  GLY ASN TYR GLY LEU LEU ASP GLN ILE GLN ALA LEU ARG          
SEQRES  17 A  655  TRP VAL SER GLU ASN ILE ALA PHE PHE GLY GLY ASP PRO          
SEQRES  18 A  655  ARG ARG ILE THR VAL PHE GLY SER GLY ILE GLY ALA SER          
SEQRES  19 A  655  CYS VAL SER LEU LEU THR LEU SER HIS HIS SER GLU GLY          
SEQRES  20 A  655  LEU PHE GLN ARG ALA ILE ILE GLN SER GLY SER ALA LEU          
SEQRES  21 A  655  SER SER TRP ALA VAL ASN TYR GLN PRO VAL LYS TYR THR          
SEQRES  22 A  655  SER LEU LEU ALA ASP LYS VAL GLY CYS ASN VAL LEU ASP          
SEQRES  23 A  655  THR VAL ASP MET VAL ASP CYS LEU ARG GLN LYS SER ALA          
SEQRES  24 A  655  LYS GLU LEU VAL GLU GLN ASP ILE GLN PRO ALA ARG TYR          
SEQRES  25 A  655  HIS VAL ALA PHE GLY PRO VAL ILE ASP GLY ASP VAL ILE          
SEQRES  26 A  655  PRO ASP ASP PRO GLU ILE LEU MET GLU GLN GLY GLU PHE          
SEQRES  27 A  655  LEU ASN TYR ASP ILE MET LEU GLY VAL ASN GLN GLY GLU          
SEQRES  28 A  655  GLY LEU LYS PHE VAL GLU GLY VAL VAL ASP PRO GLU ASP          
SEQRES  29 A  655  GLY VAL SER GLY THR ASP PHE ASP TYR SER VAL SER ASN          
SEQRES  30 A  655  PHE VAL ASP ASN LEU TYR GLY TYR PRO GLU GLY LYS ASP          
SEQRES  31 A  655  THR LEU ARG GLU THR ILE LYS PHE MET TYR THR ASP TRP          
SEQRES  32 A  655  ALA ASP ARG ASP ASN PRO GLU THR ARG ARG LYS THR LEU          
SEQRES  33 A  655  VAL ALA LEU PHE THR ASP HIS GLN TRP VAL GLU PRO SER          
SEQRES  34 A  655  VAL VAL THR ALA ASP LEU HIS ALA ARG TYR GLY SER PRO          
SEQRES  35 A  655  THR TYR PHE TYR ALA PHE TYR HIS HIS CYS GLN SER LEU          
SEQRES  36 A  655  MET LYS PRO ALA TRP SER ASP ALA ALA HIS GLY ASP GLU          
SEQRES  37 A  655  VAL PRO TYR VAL PHE GLY VAL PRO MET VAL GLY PRO THR          
SEQRES  38 A  655  ASP LEU PHE PRO CYS ASN PHE SER LYS ASN ASP VAL MET          
SEQRES  39 A  655  LEU SER ALA VAL VAL MET THR TYR TRP THR ASN PHE ALA          
SEQRES  40 A  655  LYS THR GLY ASP PRO ASN LYS PRO VAL PRO GLN ASP THR          
SEQRES  41 A  655  LYS PHE ILE HIS THR LYS ALA ASN ARG PHE GLU GLU VAL          
SEQRES  42 A  655  ALA TRP SER LYS TYR ASN PRO ARG ASP GLN LEU TYR LEU          
SEQRES  43 A  655  HIS ILE GLY LEU LYS PRO ARG VAL ARG ASP HIS TYR ARG          
SEQRES  44 A  655  ALA THR LYS VAL ALA PHE TRP LYS HIS LEU VAL PRO HIS          
SEQRES  45 A  655  LEU TYR ASN LEU HIS ASP MET PHE HIS TYR THR SER THR          
SEQRES  46 A  655  THR THR LYS VAL PRO PRO PRO ASP THR THR HIS SER SER          
SEQRES  47 A  655  HIS ILE THR ARG ARG PRO ASN GLY LYS THR TRP SER THR          
SEQRES  48 A  655  LYS ARG PRO ALA ILE SER PRO ALA TYR SER ASN GLU ASN          
SEQRES  49 A  655  ALA PRO GLY SER TRP ASN GLY ASP GLN ASP ALA GLY PRO          
SEQRES  50 A  655  LEU LEU VAL GLU ASN PRO ARG ASP TYR SER THR GLU HIS          
SEQRES  51 A  655  HIS HIS HIS HIS HIS                                          
SEQRES   1 B  655  ALA PRO ALA PRO THR VAL ASN THR HIS PHE GLY LYS LEU          
SEQRES   2 B  655  ARG GLY ALA ARG VAL PRO LEU PRO SER GLU ILE LEU GLY          
SEQRES   3 B  655  PRO VAL ASP GLN TYR LEU GLY VAL PRO TYR ALA ALA PRO          
SEQRES   4 B  655  PRO ILE GLY GLU LYS ARG PHE LEU PRO PRO GLU PRO PRO          
SEQRES   5 B  655  PRO SER TRP SER GLY ILE ARG ASN ALA THR HIS PHE PRO          
SEQRES   6 B  655  PRO VAL CYS PRO GLN ASN ILE HIS THR ALA VAL PRO GLU          
SEQRES   7 B  655  VAL MET LEU PRO VAL TRP PHE THR ALA ASN LEU ASP ILE          
SEQRES   8 B  655  VAL ALA THR TYR ILE GLN GLU PRO ASN GLU ASP CYS LEU          
SEQRES   9 B  655  TYR LEU ASN VAL TYR VAL PRO THR GLU ASP GLY SER GLY          
SEQRES  10 B  655  ALA LYS LYS GLN GLY GLU ASP LEU ALA ASP ASN ASP GLY          
SEQRES  11 B  655  ASP GLU ASP GLU ASP ILE ARG ASP SER GLY ALA LYS PRO          
SEQRES  12 B  655  VAL MET VAL TYR ILE HIS GLY GLY SER TYR MET GLU GLY          
SEQRES  13 B  655  THR GLY ASN MET ILE ASP GLY SER VAL LEU ALA SER TYR          
SEQRES  14 B  655  GLY ASN VAL ILE VAL ILE THR LEU ASN TYR ARG VAL GLY          
SEQRES  15 B  655  VAL LEU GLY PHE LEU SER THR GLY ASP GLN ALA ALA LYS          
SEQRES  16 B  655  GLY ASN TYR GLY LEU LEU ASP GLN ILE GLN ALA LEU ARG          
SEQRES  17 B  655  TRP VAL SER GLU ASN ILE ALA PHE PHE GLY GLY ASP PRO          
SEQRES  18 B  655  ARG ARG ILE THR VAL PHE GLY SER GLY ILE GLY ALA SER          
SEQRES  19 B  655  CYS VAL SER LEU LEU THR LEU SER HIS HIS SER GLU GLY          
SEQRES  20 B  655  LEU PHE GLN ARG ALA ILE ILE GLN SER GLY SER ALA LEU          
SEQRES  21 B  655  SER SER TRP ALA VAL ASN TYR GLN PRO VAL LYS TYR THR          
SEQRES  22 B  655  SER LEU LEU ALA ASP LYS VAL GLY CYS ASN VAL LEU ASP          
SEQRES  23 B  655  THR VAL ASP MET VAL ASP CYS LEU ARG GLN LYS SER ALA          
SEQRES  24 B  655  LYS GLU LEU VAL GLU GLN ASP ILE GLN PRO ALA ARG TYR          
SEQRES  25 B  655  HIS VAL ALA PHE GLY PRO VAL ILE ASP GLY ASP VAL ILE          
SEQRES  26 B  655  PRO ASP ASP PRO GLU ILE LEU MET GLU GLN GLY GLU PHE          
SEQRES  27 B  655  LEU ASN TYR ASP ILE MET LEU GLY VAL ASN GLN GLY GLU          
SEQRES  28 B  655  GLY LEU LYS PHE VAL GLU GLY VAL VAL ASP PRO GLU ASP          
SEQRES  29 B  655  GLY VAL SER GLY THR ASP PHE ASP TYR SER VAL SER ASN          
SEQRES  30 B  655  PHE VAL ASP ASN LEU TYR GLY TYR PRO GLU GLY LYS ASP          
SEQRES  31 B  655  THR LEU ARG GLU THR ILE LYS PHE MET TYR THR ASP TRP          
SEQRES  32 B  655  ALA ASP ARG ASP ASN PRO GLU THR ARG ARG LYS THR LEU          
SEQRES  33 B  655  VAL ALA LEU PHE THR ASP HIS GLN TRP VAL GLU PRO SER          
SEQRES  34 B  655  VAL VAL THR ALA ASP LEU HIS ALA ARG TYR GLY SER PRO          
SEQRES  35 B  655  THR TYR PHE TYR ALA PHE TYR HIS HIS CYS GLN SER LEU          
SEQRES  36 B  655  MET LYS PRO ALA TRP SER ASP ALA ALA HIS GLY ASP GLU          
SEQRES  37 B  655  VAL PRO TYR VAL PHE GLY VAL PRO MET VAL GLY PRO THR          
SEQRES  38 B  655  ASP LEU PHE PRO CYS ASN PHE SER LYS ASN ASP VAL MET          
SEQRES  39 B  655  LEU SER ALA VAL VAL MET THR TYR TRP THR ASN PHE ALA          
SEQRES  40 B  655  LYS THR GLY ASP PRO ASN LYS PRO VAL PRO GLN ASP THR          
SEQRES  41 B  655  LYS PHE ILE HIS THR LYS ALA ASN ARG PHE GLU GLU VAL          
SEQRES  42 B  655  ALA TRP SER LYS TYR ASN PRO ARG ASP GLN LEU TYR LEU          
SEQRES  43 B  655  HIS ILE GLY LEU LYS PRO ARG VAL ARG ASP HIS TYR ARG          
SEQRES  44 B  655  ALA THR LYS VAL ALA PHE TRP LYS HIS LEU VAL PRO HIS          
SEQRES  45 B  655  LEU TYR ASN LEU HIS ASP MET PHE HIS TYR THR SER THR          
SEQRES  46 B  655  THR THR LYS VAL PRO PRO PRO ASP THR THR HIS SER SER          
SEQRES  47 B  655  HIS ILE THR ARG ARG PRO ASN GLY LYS THR TRP SER THR          
SEQRES  48 B  655  LYS ARG PRO ALA ILE SER PRO ALA TYR SER ASN GLU ASN          
SEQRES  49 B  655  ALA PRO GLY SER TRP ASN GLY ASP GLN ASP ALA GLY PRO          
SEQRES  50 B  655  LEU LEU VAL GLU ASN PRO ARG ASP TYR SER THR GLU HIS          
SEQRES  51 B  655  HIS HIS HIS HIS HIS                                          
HET    NAG  A1001      14                                                       
HET    NAG  A1002      14                                                       
HET    NAG  B1001      14                                                       
HET    NAG  B1002      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   7  HOH   *59(H2 O)                                                     
HELIX    1 AA1 ILE A   76  ARG A   80  5                                   5    
HELIX    2 AA2 PRO A  117  ALA A  122  1                                   6    
HELIX    3 AA3 ASN A  123  GLN A  132  1                                  10    
HELIX    4 AA4 THR A  192  ILE A  196  5                                   5    
HELIX    5 AA5 GLY A  198  ASN A  206  1                                   9    
HELIX    6 AA6 VAL A  216  LEU A  222  1                                   7    
HELIX    7 AA7 ASN A  232  ILE A  249  1                                  18    
HELIX    8 AA8 ALA A  250  PHE A  252  5                                   3    
HELIX    9 AA9 GLY A  265  LEU A  276  1                                  12    
HELIX   10 AB1 GLN A  303  VAL A  315  1                                  13    
HELIX   11 AB2 ASP A  321  LYS A  332  1                                  12    
HELIX   12 AB3 SER A  333  GLN A  340  1                                   8    
HELIX   13 AB4 ASP A  363  GLY A  371  1                                   9    
HELIX   14 AB5 GLU A  372  TYR A  376  5                                   5    
HELIX   15 AB6 GLY A  387  VAL A  395  5                                   9    
HELIX   16 AB7 SER A  402  GLY A  419  1                                  18    
HELIX   17 AB8 GLY A  423  TYR A  435  1                                  13    
HELIX   18 AB9 ASN A  443  TRP A  460  1                                  18    
HELIX   19 AC1 TRP A  460  ALA A  472  1                                  13    
HELIX   20 AC2 GLU A  503  PHE A  508  1                                   6    
HELIX   21 AC3 GLY A  509  VAL A  513  5                                   5    
HELIX   22 AC4 SER A  524  GLY A  545  1                                  22    
HELIX   23 AC5 ARG A  594  HIS A  603  1                                  10    
HELIX   24 AC6 HIS A  603  TYR A  609  1                                   7    
HELIX   25 AC7 ILE B   76  ARG B   80  5                                   5    
HELIX   26 AC8 PRO B  117  ALA B  122  1                                   6    
HELIX   27 AC9 ASN B  123  GLN B  132  1                                  10    
HELIX   28 AD1 THR B  192  ILE B  196  5                                   5    
HELIX   29 AD2 GLY B  198  ASN B  206  1                                   9    
HELIX   30 AD3 VAL B  216  LEU B  222  1                                   7    
HELIX   31 AD4 ASN B  232  ILE B  249  1                                  18    
HELIX   32 AD5 ALA B  250  PHE B  252  5                                   3    
HELIX   33 AD6 GLY B  265  LEU B  276  1                                  12    
HELIX   34 AD7 GLN B  303  VAL B  315  1                                  13    
HELIX   35 AD8 ASP B  321  LYS B  332  1                                  12    
HELIX   36 AD9 SER B  333  GLN B  340  1                                   8    
HELIX   37 AE1 ASP B  363  GLY B  371  1                                   9    
HELIX   38 AE2 GLU B  372  TYR B  376  5                                   5    
HELIX   39 AE3 GLY B  387  GLU B  392  1                                   6    
HELIX   40 AE4 GLY B  393  VAL B  395  5                                   3    
HELIX   41 AE5 SER B  402  GLY B  419  1                                  18    
HELIX   42 AE6 GLY B  423  TYR B  435  1                                  13    
HELIX   43 AE7 ASN B  443  TRP B  460  1                                  18    
HELIX   44 AE8 TRP B  460  ALA B  472  1                                  13    
HELIX   45 AE9 GLU B  503  PHE B  508  1                                   6    
HELIX   46 AF1 GLY B  509  VAL B  513  5                                   5    
HELIX   47 AF2 SER B  524  GLY B  545  1                                  22    
HELIX   48 AF3 ARG B  594  HIS B  603  1                                  10    
HELIX   49 AF4 HIS B  603  TYR B  609  1                                   7    
SHEET    1 AA1 3 THR A  40  THR A  43  0                                        
SHEET    2 AA1 3 GLY A  46  ARG A  49 -1  O  LEU A  48   N  VAL A  41           
SHEET    3 AA1 3 ILE A  93  ASN A  95  1  O  ARG A  94   N  ARG A  49           
SHEET    1 AA211 ALA A  51  VAL A  53  0                                        
SHEET    2 AA211 VAL A  63  PRO A  70 -1  O  GLN A  65   N  ALA A  51           
SHEET    3 AA211 TYR A 140  PRO A 146 -1  O  VAL A 145   N  ASP A  64           
SHEET    4 AA211 ILE A 208  LEU A 212 -1  O  THR A 211   N  ASN A 142           
SHEET    5 AA211 LYS A 177  ILE A 183  1  N  MET A 180   O  ILE A 208           
SHEET    6 AA211 GLY A 254  SER A 264  1  O  THR A 260   N  VAL A 181           
SHEET    7 AA211 ARG A 286  GLN A 290  1  O  ARG A 286   N  VAL A 261           
SHEET    8 AA211 ASP A 377  ASN A 383  1  O  MET A 379   N  ILE A 289           
SHEET    9 AA211 THR A 478  PHE A 483  1  O  PHE A 483   N  VAL A 382           
SHEET   10 AA211 LEU A 579  ILE A 583  1  O  LEU A 581   N  PHE A 480           
SHEET   11 AA211 ARG A 588  ASP A 591 -1  O  ARG A 590   N  TYR A 580           
SHEET    1 AA3 3 THR B  40  THR B  43  0                                        
SHEET    2 AA3 3 GLY B  46  ARG B  49 -1  O  LEU B  48   N  VAL B  41           
SHEET    3 AA3 3 ARG B  94  ASN B  95  1  O  ARG B  94   N  ARG B  49           
SHEET    1 AA411 ALA B  51  VAL B  53  0                                        
SHEET    2 AA411 VAL B  63  PRO B  70 -1  O  GLN B  65   N  ALA B  51           
SHEET    3 AA411 TYR B 140  PRO B 146 -1  O  VAL B 145   N  ASP B  64           
SHEET    4 AA411 ILE B 208  LEU B 212 -1  O  THR B 211   N  ASN B 142           
SHEET    5 AA411 LYS B 177  ILE B 183  1  N  MET B 180   O  ILE B 208           
SHEET    6 AA411 GLY B 254  SER B 264  1  O  THR B 260   N  VAL B 181           
SHEET    7 AA411 ARG B 286  GLN B 290  1  O  ARG B 286   N  VAL B 261           
SHEET    8 AA411 ASP B 377  ASN B 383  1  O  MET B 379   N  ILE B 289           
SHEET    9 AA411 THR B 478  PHE B 483  1  O  PHE B 483   N  VAL B 382           
SHEET   10 AA411 LEU B 579  ILE B 583  1  O  LEU B 581   N  PHE B 480           
SHEET   11 AA411 ARG B 588  ASP B 591 -1  O  ARG B 588   N  HIS B 582           
SSBOND   1 CYS A  103    CYS A  138                          1555   1555  2.03  
SSBOND   2 CYS A  317    CYS A  328                          1555   1555  2.03  
SSBOND   3 CYS A  487    CYS A  521                          1555   1555  2.03  
SSBOND   4 CYS B  103    CYS B  138                          1555   1555  2.03  
SSBOND   5 CYS B  317    CYS B  328                          1555   1555  2.03  
SSBOND   6 CYS B  487    CYS B  521                          1555   1555  2.03  
LINK         ND2 ASN A  95                 C1  NAG A1001     1555   1555  1.44  
LINK         ND2 ASN A 522                 C1  NAG A1002     1555   1555  1.45  
LINK         ND2 ASN B  95                 C1  NAG B1001     1555   1555  1.44  
LINK         ND2 ASN B 522                 C1  NAG B1002     1555   1555  1.45  
CISPEP   1 LYS A  549    PRO A  550          0         2.96                     
CISPEP   2 LYS B  549    PRO B  550          0         2.98                     
CRYST1   65.842  167.142  177.950  90.00  90.00  90.00 P 21 21 21    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      0.015188  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005983  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005620        0.00000                         
TER    4191      ASN A 610                                                      
TER    8376      ASN B 610                                                      
MASTER      526    0    4   49   28    0    0    6 8489    2   72  102          
END                                                                             

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Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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