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Database: PDB
Entry: 5Z8X
LinkDB: 5Z8X
Original site: 5Z8X 
HEADER    CELL ADHESION                           01-FEB-18   5Z8X              
TITLE     CRYSTAL STRUCTURE OF HUMAN LRRTM2                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUCINE-RICH REPEAT TRANSMEMBRANE NEURONAL PROTEIN 2;      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: LEUCINE-RICH REPEAT NEURONAL 2 PROTEIN;                     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LRRTM2, KIAA0416, LRRN2;                                       
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F                                
KEYWDS    SYNAPSE, LEUCINE-RICH REPEAT, SYNAPTIC ORGANIZER, CELL ADHESION       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.YAMAGATA,S.FUKAI                                                    
REVDAT   3   29-JUL-20 5Z8X    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE                                     
REVDAT   2   31-OCT-18 5Z8X    1       TITLE  COMPND                            
REVDAT   1   10-OCT-18 5Z8X    0                                                
JRNL        AUTH   A.YAMAGATA,S.GOTO-ITO,Y.SATO,T.SHIROSHIMA,A.MAEDA,           
JRNL        AUTH 2 M.WATANABE,T.SAITOH,K.MAENAKA,T.TERADA,T.YOSHIDA,T.UEMURA,   
JRNL        AUTH 3 S.FUKAI                                                      
JRNL        TITL   STRUCTURAL INSIGHTS INTO MODULATION AND SELECTIVITY OF       
JRNL        TITL 2 TRANSSYNAPTIC NEUREXIN-LRRTM INTERACTION.                    
JRNL        REF    NAT COMMUN                    V.   9  3964 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   30262834                                                     
JRNL        DOI    10.1038/S41467-018-06333-8                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.15 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) : 3.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.43                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.500                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 47760                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2397                            
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 49.4354 -  8.0884    0.99     2926   154  0.1766 0.1997        
REMARK   3     2  8.0884 -  6.4245    0.99     2786   148  0.2012 0.2126        
REMARK   3     3  6.4245 -  5.6137    0.99     2763   150  0.1996 0.2403        
REMARK   3     4  5.6137 -  5.1010    0.99     2773   149  0.1776 0.2125        
REMARK   3     5  5.1010 -  4.7357    0.99     2719   153  0.1628 0.1797        
REMARK   3     6  4.7357 -  4.4567    0.98     2717   144  0.1690 0.2166        
REMARK   3     7  4.4567 -  4.2336    0.98     2760   114  0.1834 0.2124        
REMARK   3     8  4.2336 -  4.0494    0.98     2706   147  0.1889 0.2255        
REMARK   3     9  4.0494 -  3.8936    0.98     2696   135  0.1797 0.2110        
REMARK   3    10  3.8936 -  3.7593    0.97     2637   147  0.1985 0.2247        
REMARK   3    11  3.7593 -  3.6417    0.97     2667   137  0.2127 0.2494        
REMARK   3    12  3.6417 -  3.5377    0.95     2623   143  0.2266 0.2479        
REMARK   3    13  3.5377 -  3.4446    0.95     2560   149  0.2565 0.2814        
REMARK   3    14  3.4446 -  3.3606    0.94     2578   147  0.2673 0.3040        
REMARK   3    15  3.3606 -  3.2842    0.92     2534   140  0.2827 0.2970        
REMARK   3    16  3.2842 -  3.2143    0.91     2475   117  0.2868 0.2804        
REMARK   3    17  3.2143 -  3.1500    0.89     2443   123  0.3006 0.3350        
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)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.560           
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      :  0.011          11028                                  
REMARK   3   ANGLE     :  1.147          14928                                  
REMARK   3   CHIRALITY :  0.059           1708                                  
REMARK   3   PLANARITY :  0.005           1872                                  
REMARK   3   DIHEDRAL  : 12.836           3984                                  
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):  -8.5937  86.9882  -1.9881              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4332 T22:   0.3852                                     
REMARK   3      T33:   0.4235 T12:   0.0047                                     
REMARK   3      T13:  -0.0143 T23:   0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3662 L22:   0.1348                                     
REMARK   3      L33:   0.1231 L12:  -0.0197                                     
REMARK   3      L13:  -0.0955 L23:  -0.0052                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0113 S12:   0.0384 S13:   0.0822                       
REMARK   3      S21:  -0.0460 S22:  -0.0085 S23:   0.0575                       
REMARK   3      S31:   0.0251 S32:  -0.0824 S33:  -0.0000                       
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 5Z8X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300006678.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
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 PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48031                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.150                              
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     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.29100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 5A5C                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 3350, 0.1 M AMMONIUM SULFATE,    
REMARK 280  0.1 M SODIUM MALONATE, PH 5.0, VAPOR DIFFUSION, SITTING DROP,       
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      129.71700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      129.71700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       45.34550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      120.47950            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       45.34550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      120.47950            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      129.71700            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       45.34550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      120.47950            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      129.71700            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       45.34550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      120.47950            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN A   362                                                      
REMARK 465     LEU A   363                                                      
REMARK 465     SER A   364                                                      
REMARK 465     THR A   365                                                      
REMARK 465     THR A   366                                                      
REMARK 465     VAL A   367                                                      
REMARK 465     THR A   368                                                      
REMARK 465     VAL A   369                                                      
REMARK 465     MET A   370                                                      
REMARK 465     ALA A   371                                                      
REMARK 465     THR A   372                                                      
REMARK 465     THR A   373                                                      
REMARK 465     HIS A   374                                                      
REMARK 465     HIS A   375                                                      
REMARK 465     HIS A   376                                                      
REMARK 465     HIS A   377                                                      
REMARK 465     HIS A   378                                                      
REMARK 465     HIS A   379                                                      
REMARK 465     ASN B   362                                                      
REMARK 465     LEU B   363                                                      
REMARK 465     SER B   364                                                      
REMARK 465     THR B   365                                                      
REMARK 465     THR B   366                                                      
REMARK 465     VAL B   367                                                      
REMARK 465     THR B   368                                                      
REMARK 465     VAL B   369                                                      
REMARK 465     MET B   370                                                      
REMARK 465     ALA B   371                                                      
REMARK 465     THR B   372                                                      
REMARK 465     THR B   373                                                      
REMARK 465     HIS B   374                                                      
REMARK 465     HIS B   375                                                      
REMARK 465     HIS B   376                                                      
REMARK 465     HIS B   377                                                      
REMARK 465     HIS B   378                                                      
REMARK 465     HIS B   379                                                      
REMARK 465     ASN C   362                                                      
REMARK 465     LEU C   363                                                      
REMARK 465     SER C   364                                                      
REMARK 465     THR C   365                                                      
REMARK 465     THR C   366                                                      
REMARK 465     VAL C   367                                                      
REMARK 465     THR C   368                                                      
REMARK 465     VAL C   369                                                      
REMARK 465     MET C   370                                                      
REMARK 465     ALA C   371                                                      
REMARK 465     THR C   372                                                      
REMARK 465     THR C   373                                                      
REMARK 465     HIS C   374                                                      
REMARK 465     HIS C   375                                                      
REMARK 465     HIS C   376                                                      
REMARK 465     HIS C   377                                                      
REMARK 465     HIS C   378                                                      
REMARK 465     HIS C   379                                                      
REMARK 465     ASN D   362                                                      
REMARK 465     LEU D   363                                                      
REMARK 465     SER D   364                                                      
REMARK 465     THR D   365                                                      
REMARK 465     THR D   366                                                      
REMARK 465     VAL D   367                                                      
REMARK 465     THR D   368                                                      
REMARK 465     VAL D   369                                                      
REMARK 465     MET D   370                                                      
REMARK 465     ALA D   371                                                      
REMARK 465     THR D   372                                                      
REMARK 465     THR D   373                                                      
REMARK 465     HIS D   374                                                      
REMARK 465     HIS D   375                                                      
REMARK 465     HIS D   376                                                      
REMARK 465     HIS D   377                                                      
REMARK 465     HIS D   378                                                      
REMARK 465     HIS D   379                                                      
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    ARG D   157     OG   SER D   182              2.13            
REMARK 500   O    ARG B   157     OG   SER B   182              2.14            
REMARK 500   NH2  ARG C   332     OE2  GLU C   334              2.15            
REMARK 500   O    ARG A   157     OG   SER A   182              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   NH1  ARG C   192     OE2  GLU D   249     4565     2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  35   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  42     -109.68   -141.75                                   
REMARK 500    CYS A  47       53.59   -113.86                                   
REMARK 500    ASN A  71     -167.30   -116.22                                   
REMARK 500    LEU A 108       59.11    -95.98                                   
REMARK 500    GLN A 144       43.40   -101.23                                   
REMARK 500    LEU A 156       58.32   -108.75                                   
REMARK 500    ASN A 191     -157.55   -123.68                                   
REMARK 500    ASN A 215     -146.31   -108.63                                   
REMARK 500    ASN A 239     -149.43   -106.82                                   
REMARK 500    ASN A 263     -153.79    -95.41                                   
REMARK 500    LEU A 270        6.55    -69.92                                   
REMARK 500    ASN A 287     -166.01   -115.26                                   
REMARK 500    LEU A 300       66.36   -104.21                                   
REMARK 500    LEU A 312       52.87   -109.85                                   
REMARK 500    SER A 316     -163.15   -121.55                                   
REMARK 500    LYS B  42     -108.84   -143.74                                   
REMARK 500    CYS B  47       54.55   -113.45                                   
REMARK 500    ASN B  71     -167.88   -115.47                                   
REMARK 500    LEU B 108       58.11    -93.80                                   
REMARK 500    ASN B 119     -166.52   -129.02                                   
REMARK 500    GLN B 144       44.07   -103.21                                   
REMARK 500    LEU B 156       61.81   -111.16                                   
REMARK 500    SER B 168       30.45    -98.09                                   
REMARK 500    ASN B 191     -159.51   -126.34                                   
REMARK 500    LEU B 204       46.11   -102.33                                   
REMARK 500    ASN B 215     -147.99   -109.15                                   
REMARK 500    ASN B 239     -151.45   -107.40                                   
REMARK 500    ASN B 263     -157.09    -94.10                                   
REMARK 500    ASN B 287     -166.83   -114.26                                   
REMARK 500    LEU B 300       65.23   -102.79                                   
REMARK 500    LEU B 312       51.48   -109.12                                   
REMARK 500    SER B 316     -164.87   -123.32                                   
REMARK 500    LYS C  42     -106.01   -142.01                                   
REMARK 500    CYS C  47       57.86   -113.04                                   
REMARK 500    ASN C  71     -167.66   -114.99                                   
REMARK 500    LEU C 108       59.07    -97.36                                   
REMARK 500    ASN C 119     -168.79   -128.69                                   
REMARK 500    GLN C 144       41.29   -103.87                                   
REMARK 500    LEU C 156       61.48   -111.56                                   
REMARK 500    SER C 168       30.98    -98.94                                   
REMARK 500    ASN C 191     -158.77   -124.97                                   
REMARK 500    LEU C 204       47.55   -102.59                                   
REMARK 500    ASN C 215     -147.05   -108.25                                   
REMARK 500    ASN C 239     -150.72   -105.66                                   
REMARK 500    ASN C 263     -154.61    -94.51                                   
REMARK 500    LEU C 270        8.90    -69.94                                   
REMARK 500    ASN C 287     -164.97   -112.19                                   
REMARK 500    LEU C 300       67.32   -102.79                                   
REMARK 500    LEU C 312       52.83   -107.74                                   
REMARK 500    SER C 316     -162.54   -123.08                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      68 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5Z8X A   34   373  UNP    O43300   LRRT2_HUMAN     34    373             
DBREF  5Z8X B   34   373  UNP    O43300   LRRT2_HUMAN     34    373             
DBREF  5Z8X C   34   373  UNP    O43300   LRRT2_HUMAN     34    373             
DBREF  5Z8X D   34   373  UNP    O43300   LRRT2_HUMAN     34    373             
SEQADV 5Z8X LEU A   59  UNP  O43300    THR    59 ENGINEERED MUTATION            
SEQADV 5Z8X HIS A  374  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS A  375  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS A  376  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS A  377  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS A  378  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS A  379  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X LEU B   59  UNP  O43300    THR    59 ENGINEERED MUTATION            
SEQADV 5Z8X HIS B  374  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS B  375  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS B  376  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS B  377  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS B  378  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS B  379  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X LEU C   59  UNP  O43300    THR    59 ENGINEERED MUTATION            
SEQADV 5Z8X HIS C  374  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS C  375  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS C  376  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS C  377  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS C  378  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS C  379  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X LEU D   59  UNP  O43300    THR    59 ENGINEERED MUTATION            
SEQADV 5Z8X HIS D  374  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS D  375  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS D  376  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS D  377  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS D  378  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8X HIS D  379  UNP  O43300              EXPRESSION TAG                 
SEQRES   1 A  346  CYS PRO PRO LYS CYS ARG CYS GLU LYS LEU LEU PHE TYR          
SEQRES   2 A  346  CYS ASP SER GLN GLY PHE HIS SER VAL PRO ASN ALA LEU          
SEQRES   3 A  346  ASP LYS GLY SER LEU GLY LEU SER LEU ARG HIS ASN HIS          
SEQRES   4 A  346  ILE THR GLU LEU GLU ARG ASP GLN PHE ALA SER PHE SER          
SEQRES   5 A  346  GLN LEU THR TRP LEU HIS LEU ASP HIS ASN GLN ILE SER          
SEQRES   6 A  346  THR VAL LYS GLU ASP ALA PHE GLN GLY LEU TYR LYS LEU          
SEQRES   7 A  346  LYS GLU LEU ILE LEU SER SER ASN LYS ILE PHE TYR LEU          
SEQRES   8 A  346  PRO ASN THR THR PHE THR GLN LEU ILE ASN LEU GLN ASN          
SEQRES   9 A  346  LEU ASP LEU SER PHE ASN GLN LEU SER SER LEU HIS PRO          
SEQRES  10 A  346  GLU LEU PHE TYR GLY LEU ARG LYS LEU GLN THR LEU HIS          
SEQRES  11 A  346  LEU ARG SER ASN SER LEU ARG THR ILE PRO VAL ARG LEU          
SEQRES  12 A  346  PHE TRP ASP CYS ARG SER LEU GLU PHE LEU ASP LEU SER          
SEQRES  13 A  346  THR ASN ARG LEU ARG SER LEU ALA ARG ASN GLY PHE ALA          
SEQRES  14 A  346  GLY LEU ILE LYS LEU ARG GLU LEU HIS LEU GLU HIS ASN          
SEQRES  15 A  346  GLN LEU THR LYS ILE ASN PHE ALA HIS PHE LEU ARG LEU          
SEQRES  16 A  346  SER SER LEU HIS THR LEU PHE LEU GLN TRP ASN LYS ILE          
SEQRES  17 A  346  SER ASN LEU THR CYS GLY MET GLU TRP THR TRP GLY THR          
SEQRES  18 A  346  LEU GLU LYS LEU ASP LEU THR GLY ASN GLU ILE LYS ALA          
SEQRES  19 A  346  ILE ASP LEU THR VAL PHE GLU THR MET PRO ASN LEU LYS          
SEQRES  20 A  346  ILE LEU LEU MET ASP ASN ASN LYS LEU ASN SER LEU ASP          
SEQRES  21 A  346  SER LYS ILE LEU ASN SER LEU ARG SER LEU THR THR VAL          
SEQRES  22 A  346  GLY LEU SER GLY ASN LEU TRP GLU CYS SER ALA ARG ILE          
SEQRES  23 A  346  CYS ALA LEU ALA SER TRP LEU GLY SER PHE GLN GLY ARG          
SEQRES  24 A  346  TRP GLU HIS SER ILE LEU CYS HIS SER PRO ASP HIS THR          
SEQRES  25 A  346  GLN GLY GLU ASP ILE LEU ASP ALA VAL HIS GLY PHE GLN          
SEQRES  26 A  346  LEU CYS TRP ASN LEU SER THR THR VAL THR VAL MET ALA          
SEQRES  27 A  346  THR THR HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  346  CYS PRO PRO LYS CYS ARG CYS GLU LYS LEU LEU PHE TYR          
SEQRES   2 B  346  CYS ASP SER GLN GLY PHE HIS SER VAL PRO ASN ALA LEU          
SEQRES   3 B  346  ASP LYS GLY SER LEU GLY LEU SER LEU ARG HIS ASN HIS          
SEQRES   4 B  346  ILE THR GLU LEU GLU ARG ASP GLN PHE ALA SER PHE SER          
SEQRES   5 B  346  GLN LEU THR TRP LEU HIS LEU ASP HIS ASN GLN ILE SER          
SEQRES   6 B  346  THR VAL LYS GLU ASP ALA PHE GLN GLY LEU TYR LYS LEU          
SEQRES   7 B  346  LYS GLU LEU ILE LEU SER SER ASN LYS ILE PHE TYR LEU          
SEQRES   8 B  346  PRO ASN THR THR PHE THR GLN LEU ILE ASN LEU GLN ASN          
SEQRES   9 B  346  LEU ASP LEU SER PHE ASN GLN LEU SER SER LEU HIS PRO          
SEQRES  10 B  346  GLU LEU PHE TYR GLY LEU ARG LYS LEU GLN THR LEU HIS          
SEQRES  11 B  346  LEU ARG SER ASN SER LEU ARG THR ILE PRO VAL ARG LEU          
SEQRES  12 B  346  PHE TRP ASP CYS ARG SER LEU GLU PHE LEU ASP LEU SER          
SEQRES  13 B  346  THR ASN ARG LEU ARG SER LEU ALA ARG ASN GLY PHE ALA          
SEQRES  14 B  346  GLY LEU ILE LYS LEU ARG GLU LEU HIS LEU GLU HIS ASN          
SEQRES  15 B  346  GLN LEU THR LYS ILE ASN PHE ALA HIS PHE LEU ARG LEU          
SEQRES  16 B  346  SER SER LEU HIS THR LEU PHE LEU GLN TRP ASN LYS ILE          
SEQRES  17 B  346  SER ASN LEU THR CYS GLY MET GLU TRP THR TRP GLY THR          
SEQRES  18 B  346  LEU GLU LYS LEU ASP LEU THR GLY ASN GLU ILE LYS ALA          
SEQRES  19 B  346  ILE ASP LEU THR VAL PHE GLU THR MET PRO ASN LEU LYS          
SEQRES  20 B  346  ILE LEU LEU MET ASP ASN ASN LYS LEU ASN SER LEU ASP          
SEQRES  21 B  346  SER LYS ILE LEU ASN SER LEU ARG SER LEU THR THR VAL          
SEQRES  22 B  346  GLY LEU SER GLY ASN LEU TRP GLU CYS SER ALA ARG ILE          
SEQRES  23 B  346  CYS ALA LEU ALA SER TRP LEU GLY SER PHE GLN GLY ARG          
SEQRES  24 B  346  TRP GLU HIS SER ILE LEU CYS HIS SER PRO ASP HIS THR          
SEQRES  25 B  346  GLN GLY GLU ASP ILE LEU ASP ALA VAL HIS GLY PHE GLN          
SEQRES  26 B  346  LEU CYS TRP ASN LEU SER THR THR VAL THR VAL MET ALA          
SEQRES  27 B  346  THR THR HIS HIS HIS HIS HIS HIS                              
SEQRES   1 C  346  CYS PRO PRO LYS CYS ARG CYS GLU LYS LEU LEU PHE TYR          
SEQRES   2 C  346  CYS ASP SER GLN GLY PHE HIS SER VAL PRO ASN ALA LEU          
SEQRES   3 C  346  ASP LYS GLY SER LEU GLY LEU SER LEU ARG HIS ASN HIS          
SEQRES   4 C  346  ILE THR GLU LEU GLU ARG ASP GLN PHE ALA SER PHE SER          
SEQRES   5 C  346  GLN LEU THR TRP LEU HIS LEU ASP HIS ASN GLN ILE SER          
SEQRES   6 C  346  THR VAL LYS GLU ASP ALA PHE GLN GLY LEU TYR LYS LEU          
SEQRES   7 C  346  LYS GLU LEU ILE LEU SER SER ASN LYS ILE PHE TYR LEU          
SEQRES   8 C  346  PRO ASN THR THR PHE THR GLN LEU ILE ASN LEU GLN ASN          
SEQRES   9 C  346  LEU ASP LEU SER PHE ASN GLN LEU SER SER LEU HIS PRO          
SEQRES  10 C  346  GLU LEU PHE TYR GLY LEU ARG LYS LEU GLN THR LEU HIS          
SEQRES  11 C  346  LEU ARG SER ASN SER LEU ARG THR ILE PRO VAL ARG LEU          
SEQRES  12 C  346  PHE TRP ASP CYS ARG SER LEU GLU PHE LEU ASP LEU SER          
SEQRES  13 C  346  THR ASN ARG LEU ARG SER LEU ALA ARG ASN GLY PHE ALA          
SEQRES  14 C  346  GLY LEU ILE LYS LEU ARG GLU LEU HIS LEU GLU HIS ASN          
SEQRES  15 C  346  GLN LEU THR LYS ILE ASN PHE ALA HIS PHE LEU ARG LEU          
SEQRES  16 C  346  SER SER LEU HIS THR LEU PHE LEU GLN TRP ASN LYS ILE          
SEQRES  17 C  346  SER ASN LEU THR CYS GLY MET GLU TRP THR TRP GLY THR          
SEQRES  18 C  346  LEU GLU LYS LEU ASP LEU THR GLY ASN GLU ILE LYS ALA          
SEQRES  19 C  346  ILE ASP LEU THR VAL PHE GLU THR MET PRO ASN LEU LYS          
SEQRES  20 C  346  ILE LEU LEU MET ASP ASN ASN LYS LEU ASN SER LEU ASP          
SEQRES  21 C  346  SER LYS ILE LEU ASN SER LEU ARG SER LEU THR THR VAL          
SEQRES  22 C  346  GLY LEU SER GLY ASN LEU TRP GLU CYS SER ALA ARG ILE          
SEQRES  23 C  346  CYS ALA LEU ALA SER TRP LEU GLY SER PHE GLN GLY ARG          
SEQRES  24 C  346  TRP GLU HIS SER ILE LEU CYS HIS SER PRO ASP HIS THR          
SEQRES  25 C  346  GLN GLY GLU ASP ILE LEU ASP ALA VAL HIS GLY PHE GLN          
SEQRES  26 C  346  LEU CYS TRP ASN LEU SER THR THR VAL THR VAL MET ALA          
SEQRES  27 C  346  THR THR HIS HIS HIS HIS HIS HIS                              
SEQRES   1 D  346  CYS PRO PRO LYS CYS ARG CYS GLU LYS LEU LEU PHE TYR          
SEQRES   2 D  346  CYS ASP SER GLN GLY PHE HIS SER VAL PRO ASN ALA LEU          
SEQRES   3 D  346  ASP LYS GLY SER LEU GLY LEU SER LEU ARG HIS ASN HIS          
SEQRES   4 D  346  ILE THR GLU LEU GLU ARG ASP GLN PHE ALA SER PHE SER          
SEQRES   5 D  346  GLN LEU THR TRP LEU HIS LEU ASP HIS ASN GLN ILE SER          
SEQRES   6 D  346  THR VAL LYS GLU ASP ALA PHE GLN GLY LEU TYR LYS LEU          
SEQRES   7 D  346  LYS GLU LEU ILE LEU SER SER ASN LYS ILE PHE TYR LEU          
SEQRES   8 D  346  PRO ASN THR THR PHE THR GLN LEU ILE ASN LEU GLN ASN          
SEQRES   9 D  346  LEU ASP LEU SER PHE ASN GLN LEU SER SER LEU HIS PRO          
SEQRES  10 D  346  GLU LEU PHE TYR GLY LEU ARG LYS LEU GLN THR LEU HIS          
SEQRES  11 D  346  LEU ARG SER ASN SER LEU ARG THR ILE PRO VAL ARG LEU          
SEQRES  12 D  346  PHE TRP ASP CYS ARG SER LEU GLU PHE LEU ASP LEU SER          
SEQRES  13 D  346  THR ASN ARG LEU ARG SER LEU ALA ARG ASN GLY PHE ALA          
SEQRES  14 D  346  GLY LEU ILE LYS LEU ARG GLU LEU HIS LEU GLU HIS ASN          
SEQRES  15 D  346  GLN LEU THR LYS ILE ASN PHE ALA HIS PHE LEU ARG LEU          
SEQRES  16 D  346  SER SER LEU HIS THR LEU PHE LEU GLN TRP ASN LYS ILE          
SEQRES  17 D  346  SER ASN LEU THR CYS GLY MET GLU TRP THR TRP GLY THR          
SEQRES  18 D  346  LEU GLU LYS LEU ASP LEU THR GLY ASN GLU ILE LYS ALA          
SEQRES  19 D  346  ILE ASP LEU THR VAL PHE GLU THR MET PRO ASN LEU LYS          
SEQRES  20 D  346  ILE LEU LEU MET ASP ASN ASN LYS LEU ASN SER LEU ASP          
SEQRES  21 D  346  SER LYS ILE LEU ASN SER LEU ARG SER LEU THR THR VAL          
SEQRES  22 D  346  GLY LEU SER GLY ASN LEU TRP GLU CYS SER ALA ARG ILE          
SEQRES  23 D  346  CYS ALA LEU ALA SER TRP LEU GLY SER PHE GLN GLY ARG          
SEQRES  24 D  346  TRP GLU HIS SER ILE LEU CYS HIS SER PRO ASP HIS THR          
SEQRES  25 D  346  GLN GLY GLU ASP ILE LEU ASP ALA VAL HIS GLY PHE GLN          
SEQRES  26 D  346  LEU CYS TRP ASN LEU SER THR THR VAL THR VAL MET ALA          
SEQRES  27 D  346  THR THR HIS HIS HIS HIS HIS HIS                              
HET    NAG  A1000      14                                                       
HET    NAG  A1001      14                                                       
HET    NAG  B1000      14                                                       
HET    NAG  B1001      14                                                       
HET    NAG  C1000      14                                                       
HET    NAG  C1001      14                                                       
HET    NAG  D1000      14                                                       
HET    NAG  D1001      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   5  NAG    8(C8 H15 N O6)                                               
HELIX    1 AA1 ALA A  223  LEU A  226  5                                   4    
HELIX    2 AA2 ASP A  293  ASN A  298  1                                   6    
HELIX    3 AA3 SER A  316  ARG A  318  5                                   3    
HELIX    4 AA4 ILE A  319  PHE A  329  1                                  11    
HELIX    5 AA5 ASP A  349  PHE A  357  1                                   9    
HELIX    6 AA6 ALA B  223  LEU B  226  5                                   4    
HELIX    7 AA7 ASP B  293  ASN B  298  1                                   6    
HELIX    8 AA8 SER B  316  ARG B  318  5                                   3    
HELIX    9 AA9 ILE B  319  PHE B  329  1                                  11    
HELIX   10 AB1 ASP B  349  PHE B  357  1                                   9    
HELIX   11 AB2 ALA C  223  LEU C  226  5                                   4    
HELIX   12 AB3 ASP C  293  ASN C  298  1                                   6    
HELIX   13 AB4 SER C  316  ARG C  318  5                                   3    
HELIX   14 AB5 ILE C  319  PHE C  329  1                                  11    
HELIX   15 AB6 PRO C  342  GLN C  346  5                                   5    
HELIX   16 AB7 ASP C  349  PHE C  357  1                                   9    
HELIX   17 AB8 ALA D  223  LEU D  226  5                                   4    
HELIX   18 AB9 ASP D  293  ASN D  298  1                                   6    
HELIX   19 AC1 SER D  316  ARG D  318  5                                   3    
HELIX   20 AC2 ILE D  319  PHE D  329  1                                  11    
HELIX   21 AC3 ASP D  349  PHE D  357  1                                   9    
SHEET    1 AA112 LEU A  44  TYR A  46  0                                        
SHEET    2 AA112 GLY A  65  SER A  67  1  O  SER A  67   N  PHE A  45           
SHEET    3 AA112 TRP A  89  HIS A  91  1  O  HIS A  91   N  LEU A  66           
SHEET    4 AA112 GLU A 113  ILE A 115  1  O  GLU A 113   N  LEU A  90           
SHEET    5 AA112 ASN A 137  ASP A 139  1  O  ASN A 137   N  LEU A 114           
SHEET    6 AA112 THR A 161  HIS A 163  1  O  HIS A 163   N  LEU A 138           
SHEET    7 AA112 PHE A 185  ASP A 187  1  O  ASP A 187   N  LEU A 162           
SHEET    8 AA112 GLU A 209  HIS A 211  1  O  HIS A 211   N  LEU A 186           
SHEET    9 AA112 THR A 233  PHE A 235  1  O  PHE A 235   N  LEU A 210           
SHEET   10 AA112 LYS A 257  ASP A 259  1  O  LYS A 257   N  LEU A 234           
SHEET   11 AA112 ILE A 281  LEU A 283  1  O  ILE A 281   N  LEU A 258           
SHEET   12 AA112 THR A 305  GLY A 307  1  O  THR A 305   N  LEU A 282           
SHEET    1 AA2 2 GLU A  75  LEU A  76  0                                        
SHEET    2 AA2 2 THR A  99  VAL A 100  1  O  THR A  99   N  LEU A  76           
SHEET    1 AA3 3 LYS A 219  ASN A 221  0                                        
SHEET    2 AA3 3 ASN A 243  THR A 245  1  O  THR A 245   N  ILE A 220           
SHEET    3 AA3 3 ALA A 267  ILE A 268  1  O  ALA A 267   N  LEU A 244           
SHEET    1 AA414 ARG B  39  CYS B  40  0                                        
SHEET    2 AA414 LEU B  44  TYR B  46 -1  O  TYR B  46   N  ARG B  39           
SHEET    3 AA414 GLY B  65  SER B  67  1  O  SER B  67   N  PHE B  45           
SHEET    4 AA414 TRP B  89  HIS B  91  1  O  HIS B  91   N  LEU B  66           
SHEET    5 AA414 GLU B 113  ILE B 115  1  O  ILE B 115   N  LEU B  90           
SHEET    6 AA414 ASN B 137  ASP B 139  1  O  ASN B 137   N  LEU B 114           
SHEET    7 AA414 THR B 161  HIS B 163  1  O  HIS B 163   N  LEU B 138           
SHEET    8 AA414 PHE B 185  ASP B 187  1  O  PHE B 185   N  LEU B 162           
SHEET    9 AA414 GLU B 209  HIS B 211  1  O  HIS B 211   N  LEU B 186           
SHEET   10 AA414 THR B 233  PHE B 235  1  O  PHE B 235   N  LEU B 210           
SHEET   11 AA414 LYS B 257  ASP B 259  1  O  ASP B 259   N  LEU B 234           
SHEET   12 AA414 ILE B 281  LEU B 283  1  O  ILE B 281   N  LEU B 258           
SHEET   13 AA414 THR B 305  GLY B 307  1  O  THR B 305   N  LEU B 282           
SHEET   14 AA414 ARG B 332  TRP B 333  1  O  ARG B 332   N  VAL B 306           
SHEET    1 AA5 2 GLU B  75  LEU B  76  0                                        
SHEET    2 AA5 2 THR B  99  VAL B 100  1  O  THR B  99   N  LEU B  76           
SHEET    1 AA6 3 LYS B 219  ASN B 221  0                                        
SHEET    2 AA6 3 ASN B 243  THR B 245  1  O  THR B 245   N  ILE B 220           
SHEET    3 AA6 3 ALA B 267  ILE B 268  1  O  ALA B 267   N  LEU B 244           
SHEET    1 AA713 ARG C  39  CYS C  40  0                                        
SHEET    2 AA713 LEU C  44  TYR C  46 -1  O  TYR C  46   N  ARG C  39           
SHEET    3 AA713 GLY C  65  SER C  67  1  O  SER C  67   N  PHE C  45           
SHEET    4 AA713 TRP C  89  HIS C  91  1  O  HIS C  91   N  LEU C  66           
SHEET    5 AA713 GLU C 113  ILE C 115  1  O  ILE C 115   N  LEU C  90           
SHEET    6 AA713 ASN C 137  ASP C 139  1  O  ASN C 137   N  LEU C 114           
SHEET    7 AA713 THR C 161  HIS C 163  1  O  THR C 161   N  LEU C 138           
SHEET    8 AA713 PHE C 185  ASP C 187  1  O  PHE C 185   N  LEU C 162           
SHEET    9 AA713 GLU C 209  HIS C 211  1  O  HIS C 211   N  LEU C 186           
SHEET   10 AA713 THR C 233  PHE C 235  1  O  PHE C 235   N  LEU C 210           
SHEET   11 AA713 LYS C 257  ASP C 259  1  O  ASP C 259   N  LEU C 234           
SHEET   12 AA713 ILE C 281  LEU C 283  1  O  ILE C 281   N  LEU C 258           
SHEET   13 AA713 THR C 305  GLY C 307  1  O  THR C 305   N  LEU C 282           
SHEET    1 AA8 2 GLU C  75  LEU C  76  0                                        
SHEET    2 AA8 2 THR C  99  VAL C 100  1  O  THR C  99   N  LEU C  76           
SHEET    1 AA9 3 LYS C 219  ASN C 221  0                                        
SHEET    2 AA9 3 ASN C 243  THR C 245  1  O  THR C 245   N  ILE C 220           
SHEET    3 AA9 3 ALA C 267  ILE C 268  1  O  ALA C 267   N  LEU C 244           
SHEET    1 AB1 2 TRP C 313  GLU C 314  0                                        
SHEET    2 AB1 2 CYS C 339  SER C 341  1  O  HIS C 340   N  TRP C 313           
SHEET    1 AB213 ARG D  39  CYS D  40  0                                        
SHEET    2 AB213 LEU D  44  TYR D  46 -1  O  TYR D  46   N  ARG D  39           
SHEET    3 AB213 GLY D  65  SER D  67  1  O  SER D  67   N  PHE D  45           
SHEET    4 AB213 TRP D  89  HIS D  91  1  O  HIS D  91   N  LEU D  66           
SHEET    5 AB213 GLU D 113  ILE D 115  1  O  GLU D 113   N  LEU D  90           
SHEET    6 AB213 ASN D 137  ASP D 139  1  O  ASN D 137   N  LEU D 114           
SHEET    7 AB213 THR D 161  HIS D 163  1  O  HIS D 163   N  LEU D 138           
SHEET    8 AB213 PHE D 185  ASP D 187  1  O  PHE D 185   N  LEU D 162           
SHEET    9 AB213 GLU D 209  HIS D 211  1  O  HIS D 211   N  LEU D 186           
SHEET   10 AB213 THR D 233  PHE D 235  1  O  PHE D 235   N  LEU D 210           
SHEET   11 AB213 LYS D 257  ASP D 259  1  O  ASP D 259   N  LEU D 234           
SHEET   12 AB213 ILE D 281  LEU D 283  1  O  ILE D 281   N  LEU D 258           
SHEET   13 AB213 THR D 305  GLY D 307  1  O  THR D 305   N  LEU D 282           
SHEET    1 AB3 2 GLU D  75  LEU D  76  0                                        
SHEET    2 AB3 2 THR D  99  VAL D 100  1  O  THR D  99   N  LEU D  76           
SHEET    1 AB4 3 LYS D 219  ASN D 221  0                                        
SHEET    2 AB4 3 ASN D 243  THR D 245  1  O  THR D 245   N  ILE D 220           
SHEET    3 AB4 3 ALA D 267  ILE D 268  1  O  ALA D 267   N  LEU D 244           
SSBOND   1 CYS A   34    CYS A   40                          1555   1555  2.04  
SSBOND   2 CYS A   38    CYS A   47                          1555   1555  2.03  
SSBOND   3 CYS A  315    CYS A  339                          1555   1555  2.02  
SSBOND   4 CYS A  320    CYS A  360                          1555   1555  2.03  
SSBOND   5 CYS B   34    CYS B   40                          1555   1555  2.04  
SSBOND   6 CYS B   38    CYS B   47                          1555   1555  2.03  
SSBOND   7 CYS B  315    CYS B  339                          1555   1555  2.01  
SSBOND   8 CYS B  320    CYS B  360                          1555   1555  2.03  
SSBOND   9 CYS C   34    CYS C   40                          1555   1555  2.03  
SSBOND  10 CYS C   38    CYS C   47                          1555   1555  2.03  
SSBOND  11 CYS C  315    CYS C  339                          1555   1555  2.02  
SSBOND  12 CYS C  320    CYS C  360                          1555   1555  2.04  
SSBOND  13 CYS D   34    CYS D   40                          1555   1555  2.03  
SSBOND  14 CYS D   38    CYS D   47                          1555   1555  2.03  
SSBOND  15 CYS D  315    CYS D  339                          1555   1555  2.02  
SSBOND  16 CYS D  320    CYS D  360                          1555   1555  2.03  
LINK         ND2 ASN A 126                 C1  NAG A1001     1555   1555  1.45  
LINK         ND2 ASN A 243                 C1  NAG A1000     1555   1555  1.44  
LINK         ND2 ASN B 126                 C1  NAG B1001     1555   1555  1.44  
LINK         ND2 ASN B 243                 C1  NAG B1000     1555   1555  1.44  
LINK         ND2 ASN C 126                 C1  NAG C1001     1555   1555  1.45  
LINK         ND2 ASN C 243                 C1  NAG C1000     1555   1555  1.43  
LINK         ND2 ASN D 126                 C1  NAG D1001     1555   1555  1.45  
LINK         ND2 ASN D 243                 C1  NAG D1000     1555   1555  1.44  
CISPEP   1 SER A  341    PRO A  342          0        -1.05                     
CISPEP   2 SER B  341    PRO B  342          0        -5.17                     
CISPEP   3 SER C  341    PRO C  342          0        -1.41                     
CISPEP   4 SER D  341    PRO D  342          0        -1.15                     
CRYST1   90.691  240.959  259.434  90.00  90.00  90.00 C 2 2 21     32          
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      0.011026  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004150  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003855        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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