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LongText Report for: 5ojk-pdb

Name Class
5ojk-pdb
HEADER    CELL ADHESION                           21-JUL-17   5OJK              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN NEUROLIGIN 1 CHOLINESTERASE DOMAIN     
TITLE    2 CONTAINING SPLICED SEQUENCE B (SSB) (NL1(-A+B))                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUROLIGIN-1,NEUROLIGIN-1;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NLGN1, KIAA1070;                                               
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-/-;                        
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PHLSEC                                    
KEYWDS    NEUROLIGIN-NEUREXIN, SYNAPTIC ORGANIZER PROTEIN, SPLICED SEQUENCE B,  
KEYWDS   2 CELL ADHESION                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.ELEGHEERT,A.R.ARICESCU                                            
REVDAT   1   23-AUG-17 5OJK    0                                                
JRNL        AUTH   J.ELEGHEERT,V.CVETKOVSKA,A.J.CLAYTON,C.HEROVEN,              
JRNL        AUTH 2 K.M.VENNEKENS,S.N.SMUKOWSKI,M.C.REGAN,W.JIA,A.C.SMITH,       
JRNL        AUTH 3 H.FURUKAWA,J.N.SAVAS,J.DE WIT,J.BEGBIE,A.M.CRAIG,            
JRNL        AUTH 4 A.R.ARICESCU                                                 
JRNL        TITL   STRUCTURAL MECHANISM FOR MODULATION OF SYNAPTIC              
JRNL        TITL 2 NEUROLIGIN-NEUREXIN SIGNALING BY MDGA PROTEINS               
JRNL        REF    NEURON                        V.  95   896 2017              
JRNL        REFN                   ISSN 0896-6273                               
JRNL        DOI    10.1016/J.NEURON.2017.07.040                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_2044)                                    
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 51.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 40739                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.238                           
REMARK   3   R VALUE            (WORKING SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.920                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2005                            
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 51.7126 -  6.1428    0.92     2826   158  0.2366 0.2718        
REMARK   3     2  6.1428 -  4.8769    0.95     2788   144  0.2128 0.2473        
REMARK   3     3  4.8769 -  4.2608    0.95     2767   140  0.1921 0.2152        
REMARK   3     4  4.2608 -  3.8713    0.96     2745   135  0.2057 0.2605        
REMARK   3     5  3.8713 -  3.5939    0.97     2779   136  0.2183 0.2856        
REMARK   3     6  3.5939 -  3.3821    0.97     2746   152  0.2425 0.2592        
REMARK   3     7  3.3821 -  3.2127    0.97     2765   135  0.2437 0.2943        
REMARK   3     8  3.2127 -  3.0729    0.97     2749   141  0.2548 0.3151        
REMARK   3     9  3.0729 -  2.9546    0.98     2767   146  0.2555 0.2965        
REMARK   3    10  2.9546 -  2.8527    0.97     2773   139  0.2573 0.3356        
REMARK   3    11  2.8527 -  2.7635    0.98     2735   148  0.2794 0.3133        
REMARK   3    12  2.7635 -  2.6845    0.98     2762   144  0.2939 0.3436        
REMARK   3    13  2.6845 -  2.6138    0.98     2712   147  0.3209 0.3438        
REMARK   3    14  2.6138 -  2.5501    0.98     2820   140  0.3331 0.3658        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 0.90                                          
REMARK   3   SHRINKAGE RADIUS   : 0.70                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.460           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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           8714                                  
REMARK   3   ANGLE     :  0.782          11891                                  
REMARK   3   CHIRALITY :  0.036           1296                                  
REMARK   3   PLANARITY :  0.003           1549                                  
REMARK   3   DIHEDRAL  : 10.509           5109                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5OJK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200005899.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JAN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96860                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40826                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 51.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.500                              
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: 3BIX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M KSCN, 0.1M BIS-TRIS PROPANE PH      
REMARK 280  8.5, 20% W/V PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
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,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.02500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      107.17000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.02500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      107.17000            
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: 3300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 13.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 852  LIES ON A SPECIAL POSITION.                          
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     GLU A    43                                                      
REMARK 465     THR A    44                                                      
REMARK 465     GLY A    45                                                      
REMARK 465     GLN A    46                                                      
REMARK 465     LYS A    47                                                      
REMARK 465     LEU A    48                                                      
REMARK 465     ASP A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     VAL A    51                                                      
REMARK 465     GLY A   124                                                      
REMARK 465     GLU A   180                                                      
REMARK 465     ASP A   181                                                      
REMARK 465     ASP A   182                                                      
REMARK 465     ILE A   183                                                      
REMARK 465     ARG A   184                                                      
REMARK 465     ASP A   185                                                      
REMARK 465     SER A   186                                                      
REMARK 465     GLU A   444                                                      
REMARK 465     VAL A   573                                                      
REMARK 465     PRO A   574                                                      
REMARK 465     GLN A   575                                                      
REMARK 465     ASP A   576                                                      
REMARK 465     THR A   577                                                      
REMARK 465     LYS A   578                                                      
REMARK 465     PHE A   579                                                      
REMARK 465     ILE A   580                                                      
REMARK 465     HIS A   581                                                      
REMARK 465     THR A   582                                                      
REMARK 465     LYS A   583                                                      
REMARK 465     PRO A   584                                                      
REMARK 465     ASN A   585                                                      
REMARK 465     ARG A   586                                                      
REMARK 465     PHE A   587                                                      
REMARK 465     GLU A   588                                                      
REMARK 465     GLU A   589                                                      
REMARK 465     ASN A   632                                                      
REMARK 465     LEU A   633                                                      
REMARK 465     ASN A   634                                                      
REMARK 465     ASP A   635                                                      
REMARK 465     ARG A   636                                                      
REMARK 465     THR A   637                                                      
REMARK 465     LYS A   638                                                      
REMARK 465     HIS A   639                                                      
REMARK 465     HIS A   640                                                      
REMARK 465     HIS A   641                                                      
REMARK 465     HIS A   642                                                      
REMARK 465     HIS A   643                                                      
REMARK 465     HIS A   644                                                      
REMARK 465     GLU B    43                                                      
REMARK 465     THR B    44                                                      
REMARK 465     GLY B    45                                                      
REMARK 465     GLN B    46                                                      
REMARK 465     LYS B    47                                                      
REMARK 465     LEU B    48                                                      
REMARK 465     ASP B    49                                                      
REMARK 465     ASP B    50                                                      
REMARK 465     VAL B    51                                                      
REMARK 465     GLY B   124                                                      
REMARK 465     GLU B   180                                                      
REMARK 465     ASP B   181                                                      
REMARK 465     ASP B   182                                                      
REMARK 465     ILE B   183                                                      
REMARK 465     ARG B   184                                                      
REMARK 465     ASP B   185                                                      
REMARK 465     SER B   186                                                      
REMARK 465     GLY B   187                                                      
REMARK 465     GLU B   444                                                      
REMARK 465     GLN B   575                                                      
REMARK 465     ASP B   576                                                      
REMARK 465     THR B   577                                                      
REMARK 465     LYS B   578                                                      
REMARK 465     PHE B   579                                                      
REMARK 465     ILE B   580                                                      
REMARK 465     HIS B   581                                                      
REMARK 465     THR B   582                                                      
REMARK 465     LYS B   583                                                      
REMARK 465     PRO B   584                                                      
REMARK 465     ASN B   585                                                      
REMARK 465     ARG B   586                                                      
REMARK 465     PHE B   587                                                      
REMARK 465     GLU B   588                                                      
REMARK 465     GLU B   589                                                      
REMARK 465     HIS B   631                                                      
REMARK 465     ASN B   632                                                      
REMARK 465     LEU B   633                                                      
REMARK 465     ASN B   634                                                      
REMARK 465     ASP B   635                                                      
REMARK 465     ARG B   636                                                      
REMARK 465     THR B   637                                                      
REMARK 465     LYS B   638                                                      
REMARK 465     HIS B   639                                                      
REMARK 465     HIS B   640                                                      
REMARK 465     HIS B   641                                                      
REMARK 465     HIS B   642                                                      
REMARK 465     HIS B   643                                                      
REMARK 465     HIS B   644                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 125    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 126    CG   CD1  CD2                                       
REMARK 470     TYR A 442    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 446    CG   CD   CE   NZ                                   
REMARK 470     ARG A 450    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 598    CG   CD   CE   NZ                                   
REMARK 470     LYS A 608    CG   CD   CE   NZ                                   
REMARK 470     ASP B 123    CG   OD1  OD2                                       
REMARK 470     ARG B 125    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 126    CG   CD1  CD2                                       
REMARK 470     TYR B 442    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 446    CG   CD   CE   NZ                                   
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   O    ASN A    71     O    HOH A   801              2.15            
REMARK 500   NH1  ARG B   331     O    VAL B   341              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP A   152     NH2  ARG B   297     4655     2.11            
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    ASP A 106     -150.18   -103.27                                   
REMARK 500    ALA A 110       73.05   -112.86                                   
REMARK 500    TYR A 201       -7.34     73.71                                   
REMARK 500    ASP A 380      -79.90   -127.39                                   
REMARK 500    TYR A 457       43.14   -107.07                                   
REMARK 500    TRP A 482      -52.87   -121.36                                   
REMARK 500    PRO A 499      104.01    -56.21                                   
REMARK 500    ALA A 520      109.59    -57.18                                   
REMARK 500    LYS A 612     -158.54   -111.71                                   
REMARK 500    ASP B 106     -150.74   -101.25                                   
REMARK 500    ALA B 110       73.87   -111.95                                   
REMARK 500    PRO B 127       87.70    -69.06                                   
REMARK 500    TYR B 201       -7.96     73.74                                   
REMARK 500    ASP B 380      -78.53   -129.30                                   
REMARK 500    TYR B 457       41.73   -107.36                                   
REMARK 500    TRP B 482      -52.73   -121.11                                   
REMARK 500    PRO B 499      103.75    -56.41                                   
REMARK 500    ALA B 520      109.60    -56.71                                   
REMARK 500    PHE B 541       79.84   -115.77                                   
REMARK 500    PRO B 569        0.06    -66.66                                   
REMARK 500    LYS B 612     -158.74   -111.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 854        DISTANCE =  5.90 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 701 bound   
REMARK 800  to ASN A 109                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 701 bound   
REMARK 800  to ASN B 109                                                        
DBREF  5OJK A   46   181  UNP    Q8N2Q7   NLGN1_HUMAN     46    164             
DBREF  5OJK A  182   635  UNP    Q8N2Q7   NLGN1_HUMAN    182    635             
DBREF  5OJK B   46   181  UNP    Q8N2Q7   NLGN1_HUMAN     46    164             
DBREF  5OJK B  182   635  UNP    Q8N2Q7   NLGN1_HUMAN    182    635             
SEQADV 5OJK GLU A   43  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK THR A   44  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK GLY A   45  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK ARG A  636  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK THR A  637  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK LYS A  638  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK HIS A  639  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK HIS A  640  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK HIS A  641  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK HIS A  642  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK HIS A  643  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK HIS A  644  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK GLU B   43  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK THR B   44  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK GLY B   45  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK ARG B  636  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK THR B  637  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK LYS B  638  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK HIS B  639  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK HIS B  640  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK HIS B  641  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK HIS B  642  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK HIS B  643  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQADV 5OJK HIS B  644  UNP  Q8N2Q7              EXPRESSION TAG                 
SEQRES   1 A  585  GLU THR GLY GLN LYS LEU ASP ASP VAL ASP PRO LEU VAL          
SEQRES   2 A  585  ALA THR ASN PHE GLY LYS ILE ARG GLY ILE LYS LYS GLU          
SEQRES   3 A  585  LEU ASN ASN GLU ILE LEU GLY PRO VAL ILE GLN PHE LEU          
SEQRES   4 A  585  GLY VAL PRO TYR ALA ALA PRO PRO THR GLY GLU ARG ARG          
SEQRES   5 A  585  PHE GLN PRO PRO GLU PRO PRO SER PRO TRP SER ASP ILE          
SEQRES   6 A  585  ARG ASN ALA THR GLN PHE ALA PRO VAL CYS PRO GLN ASN          
SEQRES   7 A  585  ILE ILE ASP GLY ARG LEU PRO GLU VAL MET LEU PRO VAL          
SEQRES   8 A  585  TRP PHE THR ASN ASN LEU ASP VAL VAL SER SER TYR VAL          
SEQRES   9 A  585  GLN ASP GLN SER GLU ASP CYS LEU TYR LEU ASN ILE TYR          
SEQRES  10 A  585  VAL PRO THR GLU ASP ASP ILE ARG ASP SER GLY GLY PRO          
SEQRES  11 A  585  LYS PRO VAL MET VAL TYR ILE HIS GLY GLY SER TYR MET          
SEQRES  12 A  585  GLU GLY THR GLY ASN LEU TYR ASP GLY SER VAL LEU ALA          
SEQRES  13 A  585  SER TYR GLY ASN VAL ILE VAL ILE THR VAL ASN TYR ARG          
SEQRES  14 A  585  LEU GLY VAL LEU GLY PHE LEU SER THR GLY ASP GLN ALA          
SEQRES  15 A  585  ALA LYS GLY ASN TYR GLY LEU LEU ASP LEU ILE GLN ALA          
SEQRES  16 A  585  LEU ARG TRP THR SER GLU ASN ILE GLY PHE PHE GLY GLY          
SEQRES  17 A  585  ASP PRO LEU ARG ILE THR VAL PHE GLY SER GLY ALA GLY          
SEQRES  18 A  585  GLY SER CYS VAL ASN LEU LEU THR LEU SER HIS TYR SER          
SEQRES  19 A  585  GLU GLY ASN ARG TRP SER ASN SER THR LYS GLY LEU PHE          
SEQRES  20 A  585  GLN ARG ALA ILE ALA GLN SER GLY THR ALA LEU SER SER          
SEQRES  21 A  585  TRP ALA VAL SER PHE GLN PRO ALA LYS TYR ALA ARG MET          
SEQRES  22 A  585  LEU ALA THR LYS VAL GLY CYS ASN VAL SER ASP THR VAL          
SEQRES  23 A  585  GLU LEU VAL GLU CYS LEU GLN LYS LYS PRO TYR LYS GLU          
SEQRES  24 A  585  LEU VAL ASP GLN ASP ILE GLN PRO ALA ARG TYR HIS ILE          
SEQRES  25 A  585  ALA PHE GLY PRO VAL ILE ASP GLY ASP VAL ILE PRO ASP          
SEQRES  26 A  585  ASP PRO GLN ILE LEU MET GLU GLN GLY GLU PHE LEU ASN          
SEQRES  27 A  585  TYR ASP ILE MET LEU GLY VAL ASN GLN GLY GLU GLY LEU          
SEQRES  28 A  585  LYS PHE VAL GLU ASN ILE VAL ASP SER ASP ASP GLY ILE          
SEQRES  29 A  585  SER ALA SER ASP PHE ASP PHE ALA VAL SER ASN PHE VAL          
SEQRES  30 A  585  ASP ASN LEU TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU          
SEQRES  31 A  585  ARG GLU THR ILE LYS PHE MET TYR THR ASP TRP ALA ASP          
SEQRES  32 A  585  ARG HIS ASN PRO GLU THR ARG ARG LYS THR LEU LEU ALA          
SEQRES  33 A  585  LEU PHE THR ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA          
SEQRES  34 A  585  THR ALA ASP LEU HIS SER ASN PHE GLY SER PRO THR TYR          
SEQRES  35 A  585  PHE TYR ALA PHE TYR HIS HIS CYS GLN THR ASP GLN VAL          
SEQRES  36 A  585  PRO ALA TRP ALA ASP ALA ALA HIS GLY ASP GLU VAL PRO          
SEQRES  37 A  585  TYR VAL LEU GLY ILE PRO MET ILE GLY PRO THR GLU LEU          
SEQRES  38 A  585  PHE PRO CYS ASN PHE SER LYS ASN ASP VAL MET LEU SER          
SEQRES  39 A  585  ALA VAL VAL MET THR TYR TRP THR ASN PHE ALA LYS THR          
SEQRES  40 A  585  GLY ASP PRO ASN GLN PRO VAL PRO GLN ASP THR LYS PHE          
SEQRES  41 A  585  ILE HIS THR LYS PRO ASN ARG PHE GLU GLU VAL ALA TRP          
SEQRES  42 A  585  THR ARG TYR SER GLN LYS ASP GLN LEU TYR LEU HIS ILE          
SEQRES  43 A  585  GLY LEU LYS PRO ARG VAL LYS GLU HIS TYR ARG ALA ASN          
SEQRES  44 A  585  LYS VAL ASN LEU TRP LEU GLU LEU VAL PRO HIS LEU HIS          
SEQRES  45 A  585  ASN LEU ASN ASP ARG THR LYS HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  585  GLU THR GLY GLN LYS LEU ASP ASP VAL ASP PRO LEU VAL          
SEQRES   2 B  585  ALA THR ASN PHE GLY LYS ILE ARG GLY ILE LYS LYS GLU          
SEQRES   3 B  585  LEU ASN ASN GLU ILE LEU GLY PRO VAL ILE GLN PHE LEU          
SEQRES   4 B  585  GLY VAL PRO TYR ALA ALA PRO PRO THR GLY GLU ARG ARG          
SEQRES   5 B  585  PHE GLN PRO PRO GLU PRO PRO SER PRO TRP SER ASP ILE          
SEQRES   6 B  585  ARG ASN ALA THR GLN PHE ALA PRO VAL CYS PRO GLN ASN          
SEQRES   7 B  585  ILE ILE ASP GLY ARG LEU PRO GLU VAL MET LEU PRO VAL          
SEQRES   8 B  585  TRP PHE THR ASN ASN LEU ASP VAL VAL SER SER TYR VAL          
SEQRES   9 B  585  GLN ASP GLN SER GLU ASP CYS LEU TYR LEU ASN ILE TYR          
SEQRES  10 B  585  VAL PRO THR GLU ASP ASP ILE ARG ASP SER GLY GLY PRO          
SEQRES  11 B  585  LYS PRO VAL MET VAL TYR ILE HIS GLY GLY SER TYR MET          
SEQRES  12 B  585  GLU GLY THR GLY ASN LEU TYR ASP GLY SER VAL LEU ALA          
SEQRES  13 B  585  SER TYR GLY ASN VAL ILE VAL ILE THR VAL ASN TYR ARG          
SEQRES  14 B  585  LEU GLY VAL LEU GLY PHE LEU SER THR GLY ASP GLN ALA          
SEQRES  15 B  585  ALA LYS GLY ASN TYR GLY LEU LEU ASP LEU ILE GLN ALA          
SEQRES  16 B  585  LEU ARG TRP THR SER GLU ASN ILE GLY PHE PHE GLY GLY          
SEQRES  17 B  585  ASP PRO LEU ARG ILE THR VAL PHE GLY SER GLY ALA GLY          
SEQRES  18 B  585  GLY SER CYS VAL ASN LEU LEU THR LEU SER HIS TYR SER          
SEQRES  19 B  585  GLU GLY ASN ARG TRP SER ASN SER THR LYS GLY LEU PHE          
SEQRES  20 B  585  GLN ARG ALA ILE ALA GLN SER GLY THR ALA LEU SER SER          
SEQRES  21 B  585  TRP ALA VAL SER PHE GLN PRO ALA LYS TYR ALA ARG MET          
SEQRES  22 B  585  LEU ALA THR LYS VAL GLY CYS ASN VAL SER ASP THR VAL          
SEQRES  23 B  585  GLU LEU VAL GLU CYS LEU GLN LYS LYS PRO TYR LYS GLU          
SEQRES  24 B  585  LEU VAL ASP GLN ASP ILE GLN PRO ALA ARG TYR HIS ILE          
SEQRES  25 B  585  ALA PHE GLY PRO VAL ILE ASP GLY ASP VAL ILE PRO ASP          
SEQRES  26 B  585  ASP PRO GLN ILE LEU MET GLU GLN GLY GLU PHE LEU ASN          
SEQRES  27 B  585  TYR ASP ILE MET LEU GLY VAL ASN GLN GLY GLU GLY LEU          
SEQRES  28 B  585  LYS PHE VAL GLU ASN ILE VAL ASP SER ASP ASP GLY ILE          
SEQRES  29 B  585  SER ALA SER ASP PHE ASP PHE ALA VAL SER ASN PHE VAL          
SEQRES  30 B  585  ASP ASN LEU TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU          
SEQRES  31 B  585  ARG GLU THR ILE LYS PHE MET TYR THR ASP TRP ALA ASP          
SEQRES  32 B  585  ARG HIS ASN PRO GLU THR ARG ARG LYS THR LEU LEU ALA          
SEQRES  33 B  585  LEU PHE THR ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA          
SEQRES  34 B  585  THR ALA ASP LEU HIS SER ASN PHE GLY SER PRO THR TYR          
SEQRES  35 B  585  PHE TYR ALA PHE TYR HIS HIS CYS GLN THR ASP GLN VAL          
SEQRES  36 B  585  PRO ALA TRP ALA ASP ALA ALA HIS GLY ASP GLU VAL PRO          
SEQRES  37 B  585  TYR VAL LEU GLY ILE PRO MET ILE GLY PRO THR GLU LEU          
SEQRES  38 B  585  PHE PRO CYS ASN PHE SER LYS ASN ASP VAL MET LEU SER          
SEQRES  39 B  585  ALA VAL VAL MET THR TYR TRP THR ASN PHE ALA LYS THR          
SEQRES  40 B  585  GLY ASP PRO ASN GLN PRO VAL PRO GLN ASP THR LYS PHE          
SEQRES  41 B  585  ILE HIS THR LYS PRO ASN ARG PHE GLU GLU VAL ALA TRP          
SEQRES  42 B  585  THR ARG TYR SER GLN LYS ASP GLN LEU TYR LEU HIS ILE          
SEQRES  43 B  585  GLY LEU LYS PRO ARG VAL LYS GLU HIS TYR ARG ALA ASN          
SEQRES  44 B  585  LYS VAL ASN LEU TRP LEU GLU LEU VAL PRO HIS LEU HIS          
SEQRES  45 B  585  ASN LEU ASN ASP ARG THR LYS HIS HIS HIS HIS HIS HIS          
HET    NAG  A 701      14                                                       
HET    PGE  A 702      10                                                       
HET    PGE  A 703      10                                                       
HET    NAG  B 701      14                                                       
HET    PGE  B 702      10                                                       
HET    PGE  B 703      10                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     PGE TRIETHYLENE GLYCOL                                               
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   4  PGE    4(C6 H14 O4)                                                 
FORMUL   9  HOH   *109(H2 O)                                                    
HELIX    1 AA1 THR A   90  ARG A   94  5                                   5    
HELIX    2 AA2 PRO A  132  ASN A  138  1                                   7    
HELIX    3 AA3 ASN A  138  TYR A  145  1                                   8    
HELIX    4 AA4 THR A  205  TYR A  209  5                                   5    
HELIX    5 AA5 GLY A  211  ASN A  219  1                                   9    
HELIX    6 AA6 LEU A  229  LEU A  235  1                                   7    
HELIX    7 AA7 ASN A  245  ILE A  262  1                                  18    
HELIX    8 AA8 GLY A  263  PHE A  265  5                                   3    
HELIX    9 AA9 GLY A  278  LEU A  289  1                                  12    
HELIX   10 AB1 SER A  290  GLU A  294  5                                   5    
HELIX   11 AB2 GLN A  325  VAL A  337  1                                  13    
HELIX   12 AB3 ASP A  343  GLN A  352  1                                  10    
HELIX   13 AB4 PRO A  355  ASP A  361  1                                   7    
HELIX   14 AB5 ASP A  385  GLN A  392  1                                   8    
HELIX   15 AB6 GLY A  409  GLU A  414  1                                   6    
HELIX   16 AB7 SER A  424  TYR A  440  1                                  17    
HELIX   17 AB8 LYS A  446  TYR A  457  1                                  12    
HELIX   18 AB9 ASP A  459  ARG A  463  5                                   5    
HELIX   19 AC1 ASN A  465  TRP A  482  1                                  18    
HELIX   20 AC2 TRP A  482  PHE A  496  1                                  15    
HELIX   21 AC3 GLU A  525  GLY A  531  1                                   7    
HELIX   22 AC4 GLY A  531  GLY A  536  1                                   6    
HELIX   23 AC5 SER A  546  GLY A  567  1                                  22    
HELIX   24 AC6 ARG A  616  GLU A  625  1                                  10    
HELIX   25 AC7 GLU A  625  LEU A  630  1                                   6    
HELIX   26 AC8 THR B   90  ARG B   94  5                                   5    
HELIX   27 AC9 PRO B  132  ASN B  138  1                                   7    
HELIX   28 AD1 ASN B  138  TYR B  145  1                                   8    
HELIX   29 AD2 THR B  205  TYR B  209  5                                   5    
HELIX   30 AD3 GLY B  211  ASN B  219  1                                   9    
HELIX   31 AD4 LEU B  229  LEU B  235  1                                   7    
HELIX   32 AD5 ASN B  245  ILE B  262  1                                  18    
HELIX   33 AD6 GLY B  263  PHE B  265  5                                   3    
HELIX   34 AD7 GLY B  278  LEU B  289  1                                  12    
HELIX   35 AD8 SER B  290  GLU B  294  5                                   5    
HELIX   36 AD9 GLN B  325  VAL B  337  1                                  13    
HELIX   37 AE1 ASP B  343  GLN B  352  1                                  10    
HELIX   38 AE2 PRO B  355  ASP B  361  1                                   7    
HELIX   39 AE3 ASP B  385  GLN B  392  1                                   8    
HELIX   40 AE4 GLY B  409  GLU B  414  1                                   6    
HELIX   41 AE5 SER B  424  TYR B  440  1                                  17    
HELIX   42 AE6 LYS B  446  TYR B  457  1                                  12    
HELIX   43 AE7 ASP B  459  ARG B  463  5                                   5    
HELIX   44 AE8 ASN B  465  TRP B  482  1                                  18    
HELIX   45 AE9 TRP B  482  PHE B  496  1                                  15    
HELIX   46 AF1 GLU B  525  GLY B  531  1                                   7    
HELIX   47 AF2 GLY B  531  GLY B  536  1                                   6    
HELIX   48 AF3 SER B  546  GLY B  567  1                                  22    
HELIX   49 AF4 ARG B  616  GLU B  625  1                                  10    
HELIX   50 AF5 GLU B  625  LEU B  630  1                                   6    
SHEET    1 AA1 3 LEU A  54  THR A  57  0                                        
SHEET    2 AA1 3 GLY A  60  ARG A  63 -1  O  ILE A  62   N  VAL A  55           
SHEET    3 AA1 3 ILE A 107  ASN A 109  1  O  ARG A 108   N  LYS A  61           
SHEET    1 AA211 ILE A  65  LYS A  67  0                                        
SHEET    2 AA211 VAL A  77  PRO A  84 -1  O  GLN A  79   N  ILE A  65           
SHEET    3 AA211 TYR A 155  VAL A 160 -1  O  VAL A 160   N  ILE A  78           
SHEET    4 AA211 ILE A 221  VAL A 225 -1  O  THR A 224   N  ASN A 157           
SHEET    5 AA211 LYS A 190  TYR A 195  1  N  TYR A 195   O  ILE A 223           
SHEET    6 AA211 GLY A 267  SER A 277  1  O  THR A 273   N  VAL A 192           
SHEET    7 AA211 ARG A 308  GLN A 312  1  O  GLN A 312   N  GLY A 276           
SHEET    8 AA211 ASP A 399  ASN A 405  1  O  ASP A 399   N  ALA A 309           
SHEET    9 AA211 THR A 500  PHE A 505  1  O  PHE A 505   N  VAL A 404           
SHEET   10 AA211 LEU A 601  ILE A 605  1  O  LEU A 603   N  PHE A 502           
SHEET   11 AA211 ARG A 610  GLU A 613 -1  O  ARG A 610   N  HIS A 604           
SHEET    1 AA3 3 LEU B  54  THR B  57  0                                        
SHEET    2 AA3 3 GLY B  60  ARG B  63 -1  O  ILE B  62   N  VAL B  55           
SHEET    3 AA3 3 ILE B 107  ASN B 109  1  O  ARG B 108   N  LYS B  61           
SHEET    1 AA411 ILE B  65  LYS B  67  0                                        
SHEET    2 AA411 VAL B  77  PRO B  84 -1  O  GLN B  79   N  ILE B  65           
SHEET    3 AA411 TYR B 155  VAL B 160 -1  O  VAL B 160   N  ILE B  78           
SHEET    4 AA411 ILE B 221  VAL B 225 -1  O  THR B 224   N  ASN B 157           
SHEET    5 AA411 LYS B 190  TYR B 195  1  N  TYR B 195   O  ILE B 223           
SHEET    6 AA411 GLY B 267  SER B 277  1  O  THR B 273   N  VAL B 192           
SHEET    7 AA411 ARG B 308  GLN B 312  1  O  GLN B 312   N  GLY B 276           
SHEET    8 AA411 ASP B 399  ASN B 405  1  O  ASP B 399   N  ALA B 309           
SHEET    9 AA411 THR B 500  PHE B 505  1  O  PHE B 505   N  VAL B 404           
SHEET   10 AA411 LEU B 601  ILE B 605  1  O  LEU B 603   N  PHE B 502           
SHEET   11 AA411 ARG B 610  GLU B 613 -1  O  ARG B 610   N  HIS B 604           
SSBOND   1 CYS A  117    CYS A  153                          1555   1555  2.03  
SSBOND   2 CYS A  339    CYS A  350                          1555   1555  2.03  
SSBOND   3 CYS A  509    CYS A  543                          1555   1555  2.03  
SSBOND   4 CYS B  117    CYS B  153                          1555   1555  2.03  
SSBOND   5 CYS B  339    CYS B  350                          1555   1555  2.03  
SSBOND   6 CYS B  509    CYS B  543                          1555   1555  2.03  
LINK         ND2 ASN A 109                 C1  NAG A 701     1555   1555  1.44  
LINK         ND2 ASN B 109                 C1  NAG B 701     1555   1555  1.44  
CISPEP   1 VAL B  573    PRO B  574          0         2.36                     
SITE     1 AC1  2 GLN A 352  LYS A 353                                          
SITE     1 AC2  2 GLY A 238  ILE A 377                                          
SITE     1 AC3  3 TRP A 298  GLN B 352  LYS B 353                               
SITE     1 AC4  5 SER B 236  GLY B 238  LYS B 243  ILE B 377                    
SITE     2 AC4  5 ASP B 378                                                     
SITE     1 AC5  3 ARG A  63  ASN A 109  GLN B 240                               
SITE     1 AC6  3 GLN A 240  ARG B  63  ASN B 109                               
CRYST1   49.570  118.050  214.340  90.00  90.00  90.00 P 2 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      0.020173  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008471  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004665        0.00000                         
TER    4200      HIS A 631                                                      
TER    8408      LEU B 630                                                      
MASTER      443    0    6   50   28    0    7    6 8564    2   82   90          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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