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Database: PDB
Entry: 1J88
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Original site: 1J88 
HEADER    IMMUNE SYSTEM                           20-MAY-01   1J88              
TITLE     HUMAN HIGH AFFINITY FC RECEPTOR FC(EPSILON)RI(ALPHA), TETRAGONAL      
TITLE    2 CRYSTAL FORM 1                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR ALPHA-       
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A, B, C, D, E;                                                
COMPND   5 FRAGMENT: EXTRACELLULAR FRAGMENT;                                    
COMPND   6 SYNONYM: FC(EPSILON)RI(ALPHA); IGE FC RECEPTOR, ALPHA-SUBUNIT; FC-   
COMPND   7 EPSILON RI-ALPHA;                                                    
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: GLYCOSYLATED PROTEIN, CHAIN A BY SUGARS F, B BY SUGARS
COMPND  10 G, C BY SUGARS H, D BY SUGARS I, E BY SUGARS J                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: LDLD.LEC1;                              
SOURCE   9 EXPRESSION_SYSTEM_ORGAN: OVARY                                       
KEYWDS    IMMUNE SYSTEM, FC RECEPTOR, IGE RECEPTOR, GLYCOPROTEIN                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.C.GARMAN,S.SECHI,J.P.KINET,T.S.JARDETZKY                            
REVDAT   5   29-JUL-20 1J88    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE   ATOM                              
REVDAT   4   13-JUL-11 1J88    1       VERSN                                    
REVDAT   3   24-FEB-09 1J88    1       VERSN                                    
REVDAT   2   01-APR-03 1J88    1       JRNL                                     
REVDAT   1   29-AUG-01 1J88    0                                                
JRNL        AUTH   S.C.GARMAN,S.SECHI,J.P.KINET,T.S.JARDETZKY                   
JRNL        TITL   THE ANALYSIS OF THE HUMAN HIGH AFFINITY IGE RECEPTOR FC      
JRNL        TITL 2 EPSILON RI ALPHA FROM MULTIPLE CRYSTAL FORMS.                
JRNL        REF    J.MOL.BIOL.                   V. 311  1049 2001              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   11531339                                                     
JRNL        DOI    10.1006/JMBI.2001.4929                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1760998.430                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 21343                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : SHELLS                          
REMARK   3   R VALUE            (WORKING SET) : 0.262                           
REMARK   3   FREE R VALUE                     : 0.310                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1065                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.40                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3107                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3560                       
REMARK   3   BIN FREE R VALUE                    : 0.3930                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 125                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.035                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6905                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 701                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 79.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 126.8                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.64000                                              
REMARK   3    B22 (A**2) : 2.64000                                              
REMARK   3    B33 (A**2) : -5.28000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.43                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.76                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.52                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.85                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.790                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 14.110; 2.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 19.910; 3.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 18.790; 3.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 28.590; 4.000                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.20                                                 
REMARK   3   BSOL        : 108.5                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : 0.04  ; 300.0                
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; 2.0                  
REMARK   3   GROUP  2  POSITIONAL            (A) : 0.04  ; 300.0                
REMARK   3   GROUP  2  B-FACTOR           (A**2) : NULL  ; 2.0                  
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  300 KCAL/MOL/A^2 NCS RESTRAINTS APPLIED TO ALL PROTEIN ATOMS        
REMARK   3  EXCEPT THOSE IN FLEXIBLE LOOPS, IN CRYSTAL CONTACTS, OR WITH        
REMARK   3  ATTACHED CARBOHYDRATE. NCS GROUP 1 REPRESENTS DOMAIN 1; GROUP2      
REMARK   3  REPRESENTS DOMAIN2.                                                 
REMARK   4                                                                      
REMARK   4 1J88 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAY-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000013482.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAY-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.914                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21357                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.10500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
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: AMORE                                                 
REMARK 200 STARTING MODEL: 1F2Q                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 10000, AMMONIUM CITRATE, SODIUM      
REMARK 280  CHLORIDE, PH 5.6, VAPOR DIFFUSION, HANGING DROP AT 293K, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
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   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
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       31.37000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       47.05500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       15.68500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A PROTEIN MONOMER WITH ATTACHED   
REMARK 300 CARBOHYDRATE                                                         
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, F, G, H, I                         
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, J, K                               
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, L, M, N                            
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, O, P, Q                            
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: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, R                                  
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     VAL A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     ALA A   172                                                      
REMARK 465     VAL B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     ALA B   172                                                      
REMARK 465     VAL C     1                                                      
REMARK 465     PRO C     2                                                      
REMARK 465     GLN C     3                                                      
REMARK 465     ALA C   172                                                      
REMARK 465     VAL D     1                                                      
REMARK 465     PRO D     2                                                      
REMARK 465     GLN D     3                                                      
REMARK 465     ALA D   172                                                      
REMARK 465     VAL E     1                                                      
REMARK 465     PRO E     2                                                      
REMARK 465     GLN E     3                                                      
REMARK 465     ALA E   172                                                      
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   NE   ARG A   111     O    GLY C    28     1554     2.12            
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    PHE B  31   N   -  CA  -  C   ANGL. DEV. =  16.6 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    ASN A  27      159.28    175.97                                   
REMARK 500    SER A  36       61.37     62.01                                   
REMARK 500    ASN A  57       75.06     -9.28                                   
REMARK 500    GLU A  75      150.48    -49.93                                   
REMARK 500    GLU A  99      124.54    -38.58                                   
REMARK 500    ARG A 111       17.39     44.88                                   
REMARK 500    TRP A 113     -171.25    -62.53                                   
REMARK 500    LEU A 127      -51.25   -133.32                                   
REMARK 500    TYR A 131      -80.87    -75.03                                   
REMARK 500    THR A 139      -70.14    -80.17                                   
REMARK 500    TRP A 156      -94.63     63.52                                   
REMARK 500    GLN A 157       12.45   -143.55                                   
REMARK 500    CYS B  26       43.71    -95.66                                   
REMARK 500    ASN B  27      145.29   -170.29                                   
REMARK 500    THR B  49      -30.61   -135.85                                   
REMARK 500    ASN B  57       88.76     -8.60                                   
REMARK 500    PRO B  78      157.45    -36.99                                   
REMARK 500    ARG B 111       18.70     45.90                                   
REMARK 500    TRP B 113     -170.57    -59.99                                   
REMARK 500    LEU B 127      -52.89   -130.79                                   
REMARK 500    TYR B 131      -76.68    -87.74                                   
REMARK 500    ASN B 133      165.85    -42.31                                   
REMARK 500    ILE B 136      109.65    -46.64                                   
REMARK 500    THR B 139      -83.23    -75.77                                   
REMARK 500    TRP B 156      -94.81     64.11                                   
REMARK 500    GLN B 157       12.25   -143.41                                   
REMARK 500    ASN C  29       42.60     17.68                                   
REMARK 500    ASN C  50      151.69    -49.60                                   
REMARK 500    ASN C  57       86.62     -6.75                                   
REMARK 500    PRO C  78      154.51    -44.63                                   
REMARK 500    ARG C 111       18.96     44.87                                   
REMARK 500    TRP C 113     -171.18    -62.06                                   
REMARK 500    LEU C 127      -54.69   -130.26                                   
REMARK 500    TYR C 131      -81.46    -80.33                                   
REMARK 500    ILE C 136      118.98    -37.99                                   
REMARK 500    THR C 139      -73.35    -82.18                                   
REMARK 500    TRP C 156      -93.93     64.69                                   
REMARK 500    GLN C 157       12.67   -144.46                                   
REMARK 500    ASN D  27      -29.70   -140.11                                   
REMARK 500    SER D  35      -63.36   -109.79                                   
REMARK 500    VAL D  56     -168.53   -101.54                                   
REMARK 500    ASN D  57       89.02    -10.54                                   
REMARK 500    GLU D  75      150.13    -44.01                                   
REMARK 500    ARG D 111       18.82     45.91                                   
REMARK 500    TRP D 113     -172.26    -62.16                                   
REMARK 500    LEU D 127      -51.67   -131.37                                   
REMARK 500    HIS D 134     -144.63   -119.53                                   
REMARK 500    THR D 139      -73.10    -72.76                                   
REMARK 500    TRP D 156      -94.12     64.10                                   
REMARK 500    GLN D 157       12.48   -143.98                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR C 129         0.07    SIDE CHAIN                              
REMARK 500    TYR D 131         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1F2Q   RELATED DB: PDB                                   
REMARK 900 MONOCLINIC CRYSTAL FORM 1                                            
REMARK 900 RELATED ID: 1F6A   RELATED DB: PDB                                   
REMARK 900 COMPLEX WITH IGE-FC C(EPSILON)3-4                                    
REMARK 900 RELATED ID: 1J86   RELATED DB: PDB                                   
REMARK 900 MONOCLINIC CRYSTAL FORM 2                                            
REMARK 900 RELATED ID: 1J87   RELATED DB: PDB                                   
REMARK 900 HEXAGONAL CRYSTAL FORM 1                                             
REMARK 900 RELATED ID: 1J89   RELATED DB: PDB                                   
REMARK 900 TETRAGONAL CRYSTAL FORM 2                                            
DBREF  1J88 A    1   172  UNP    P12319   FCEA_HUMAN      26    197             
DBREF  1J88 B    1   172  UNP    P12319   FCEA_HUMAN      26    197             
DBREF  1J88 C    1   172  UNP    P12319   FCEA_HUMAN      26    197             
DBREF  1J88 D    1   172  UNP    P12319   FCEA_HUMAN      26    197             
DBREF  1J88 E    1   172  UNP    P12319   FCEA_HUMAN      26    197             
SEQRES   1 A  172  VAL PRO GLN LYS PRO LYS VAL SER LEU ASN PRO PRO TRP          
SEQRES   2 A  172  ASN ARG ILE PHE LYS GLY GLU ASN VAL THR LEU THR CYS          
SEQRES   3 A  172  ASN GLY ASN ASN PHE PHE GLU VAL SER SER THR LYS TRP          
SEQRES   4 A  172  PHE HIS ASN GLY SER LEU SER GLU GLU THR ASN SER SER          
SEQRES   5 A  172  LEU ASN ILE VAL ASN ALA LYS PHE GLU ASP SER GLY GLU          
SEQRES   6 A  172  TYR LYS CYS GLN HIS GLN GLN VAL ASN GLU SER GLU PRO          
SEQRES   7 A  172  VAL TYR LEU GLU VAL PHE SER ASP TRP LEU LEU LEU GLN          
SEQRES   8 A  172  ALA SER ALA GLU VAL VAL MET GLU GLY GLN PRO LEU PHE          
SEQRES   9 A  172  LEU ARG CYS HIS GLY TRP ARG ASN TRP ASP VAL TYR LYS          
SEQRES  10 A  172  VAL ILE TYR TYR LYS ASP GLY GLU ALA LEU LYS TYR TRP          
SEQRES  11 A  172  TYR GLU ASN HIS ASN ILE SER ILE THR ASN ALA THR VAL          
SEQRES  12 A  172  GLU ASP SER GLY THR TYR TYR CYS THR GLY LYS VAL TRP          
SEQRES  13 A  172  GLN LEU ASP TYR GLU SER GLU PRO LEU ASN ILE THR VAL          
SEQRES  14 A  172  ILE LYS ALA                                                  
SEQRES   1 B  172  VAL PRO GLN LYS PRO LYS VAL SER LEU ASN PRO PRO TRP          
SEQRES   2 B  172  ASN ARG ILE PHE LYS GLY GLU ASN VAL THR LEU THR CYS          
SEQRES   3 B  172  ASN GLY ASN ASN PHE PHE GLU VAL SER SER THR LYS TRP          
SEQRES   4 B  172  PHE HIS ASN GLY SER LEU SER GLU GLU THR ASN SER SER          
SEQRES   5 B  172  LEU ASN ILE VAL ASN ALA LYS PHE GLU ASP SER GLY GLU          
SEQRES   6 B  172  TYR LYS CYS GLN HIS GLN GLN VAL ASN GLU SER GLU PRO          
SEQRES   7 B  172  VAL TYR LEU GLU VAL PHE SER ASP TRP LEU LEU LEU GLN          
SEQRES   8 B  172  ALA SER ALA GLU VAL VAL MET GLU GLY GLN PRO LEU PHE          
SEQRES   9 B  172  LEU ARG CYS HIS GLY TRP ARG ASN TRP ASP VAL TYR LYS          
SEQRES  10 B  172  VAL ILE TYR TYR LYS ASP GLY GLU ALA LEU LYS TYR TRP          
SEQRES  11 B  172  TYR GLU ASN HIS ASN ILE SER ILE THR ASN ALA THR VAL          
SEQRES  12 B  172  GLU ASP SER GLY THR TYR TYR CYS THR GLY LYS VAL TRP          
SEQRES  13 B  172  GLN LEU ASP TYR GLU SER GLU PRO LEU ASN ILE THR VAL          
SEQRES  14 B  172  ILE LYS ALA                                                  
SEQRES   1 C  172  VAL PRO GLN LYS PRO LYS VAL SER LEU ASN PRO PRO TRP          
SEQRES   2 C  172  ASN ARG ILE PHE LYS GLY GLU ASN VAL THR LEU THR CYS          
SEQRES   3 C  172  ASN GLY ASN ASN PHE PHE GLU VAL SER SER THR LYS TRP          
SEQRES   4 C  172  PHE HIS ASN GLY SER LEU SER GLU GLU THR ASN SER SER          
SEQRES   5 C  172  LEU ASN ILE VAL ASN ALA LYS PHE GLU ASP SER GLY GLU          
SEQRES   6 C  172  TYR LYS CYS GLN HIS GLN GLN VAL ASN GLU SER GLU PRO          
SEQRES   7 C  172  VAL TYR LEU GLU VAL PHE SER ASP TRP LEU LEU LEU GLN          
SEQRES   8 C  172  ALA SER ALA GLU VAL VAL MET GLU GLY GLN PRO LEU PHE          
SEQRES   9 C  172  LEU ARG CYS HIS GLY TRP ARG ASN TRP ASP VAL TYR LYS          
SEQRES  10 C  172  VAL ILE TYR TYR LYS ASP GLY GLU ALA LEU LYS TYR TRP          
SEQRES  11 C  172  TYR GLU ASN HIS ASN ILE SER ILE THR ASN ALA THR VAL          
SEQRES  12 C  172  GLU ASP SER GLY THR TYR TYR CYS THR GLY LYS VAL TRP          
SEQRES  13 C  172  GLN LEU ASP TYR GLU SER GLU PRO LEU ASN ILE THR VAL          
SEQRES  14 C  172  ILE LYS ALA                                                  
SEQRES   1 D  172  VAL PRO GLN LYS PRO LYS VAL SER LEU ASN PRO PRO TRP          
SEQRES   2 D  172  ASN ARG ILE PHE LYS GLY GLU ASN VAL THR LEU THR CYS          
SEQRES   3 D  172  ASN GLY ASN ASN PHE PHE GLU VAL SER SER THR LYS TRP          
SEQRES   4 D  172  PHE HIS ASN GLY SER LEU SER GLU GLU THR ASN SER SER          
SEQRES   5 D  172  LEU ASN ILE VAL ASN ALA LYS PHE GLU ASP SER GLY GLU          
SEQRES   6 D  172  TYR LYS CYS GLN HIS GLN GLN VAL ASN GLU SER GLU PRO          
SEQRES   7 D  172  VAL TYR LEU GLU VAL PHE SER ASP TRP LEU LEU LEU GLN          
SEQRES   8 D  172  ALA SER ALA GLU VAL VAL MET GLU GLY GLN PRO LEU PHE          
SEQRES   9 D  172  LEU ARG CYS HIS GLY TRP ARG ASN TRP ASP VAL TYR LYS          
SEQRES  10 D  172  VAL ILE TYR TYR LYS ASP GLY GLU ALA LEU LYS TYR TRP          
SEQRES  11 D  172  TYR GLU ASN HIS ASN ILE SER ILE THR ASN ALA THR VAL          
SEQRES  12 D  172  GLU ASP SER GLY THR TYR TYR CYS THR GLY LYS VAL TRP          
SEQRES  13 D  172  GLN LEU ASP TYR GLU SER GLU PRO LEU ASN ILE THR VAL          
SEQRES  14 D  172  ILE LYS ALA                                                  
SEQRES   1 E  172  VAL PRO GLN LYS PRO LYS VAL SER LEU ASN PRO PRO TRP          
SEQRES   2 E  172  ASN ARG ILE PHE LYS GLY GLU ASN VAL THR LEU THR CYS          
SEQRES   3 E  172  ASN GLY ASN ASN PHE PHE GLU VAL SER SER THR LYS TRP          
SEQRES   4 E  172  PHE HIS ASN GLY SER LEU SER GLU GLU THR ASN SER SER          
SEQRES   5 E  172  LEU ASN ILE VAL ASN ALA LYS PHE GLU ASP SER GLY GLU          
SEQRES   6 E  172  TYR LYS CYS GLN HIS GLN GLN VAL ASN GLU SER GLU PRO          
SEQRES   7 E  172  VAL TYR LEU GLU VAL PHE SER ASP TRP LEU LEU LEU GLN          
SEQRES   8 E  172  ALA SER ALA GLU VAL VAL MET GLU GLY GLN PRO LEU PHE          
SEQRES   9 E  172  LEU ARG CYS HIS GLY TRP ARG ASN TRP ASP VAL TYR LYS          
SEQRES  10 E  172  VAL ILE TYR TYR LYS ASP GLY GLU ALA LEU LYS TYR TRP          
SEQRES  11 E  172  TYR GLU ASN HIS ASN ILE SER ILE THR ASN ALA THR VAL          
SEQRES  12 E  172  GLU ASP SER GLY THR TYR TYR CYS THR GLY LYS VAL TRP          
SEQRES  13 E  172  GLN LEU ASP TYR GLU SER GLU PRO LEU ASN ILE THR VAL          
SEQRES  14 E  172  ILE LYS ALA                                                  
MODRES 1J88 ASN E  140  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN A   42  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN C   74  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN B  166  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN A  166  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN D  166  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN E  166  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN C   42  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN C  166  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN C   21  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN E   21  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN A   21  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN D  140  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN B  140  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN E   74  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN D   74  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN B   74  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN A  135  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN D   21  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN C  140  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN E   42  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN A   74  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN B   21  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN C   50  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN D   42  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN A  140  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN A   50  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN D  135  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN B   42  ASN  GLYCOSYLATION SITE                                 
MODRES 1J88 ASN B  135  ASN  GLYCOSYLATION SITE                                 
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    BMA  F   3      11                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    MAN  G   3      11                                                       
HET    MAN  G   4      11                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    NAG  I   1      14                                                       
HET    NAG  I   2      14                                                       
HET    NAG  J   1      14                                                       
HET    NAG  J   2      14                                                       
HET    BMA  J   3      11                                                       
HET    NAG  K   1      14                                                       
HET    NAG  K   2      14                                                       
HET    NAG  L   1      14                                                       
HET    NAG  L   2      14                                                       
HET    NAG  M   1      14                                                       
HET    NAG  M   2      14                                                       
HET    BMA  M   3      11                                                       
HET    NAG  N   1      14                                                       
HET    NAG  N   2      14                                                       
HET    NAG  O   1      14                                                       
HET    NAG  O   2      14                                                       
HET    BMA  O   3      11                                                       
HET    NAG  P   1      14                                                       
HET    NAG  P   2      14                                                       
HET    BMA  P   3      11                                                       
HET    NAG  Q   1      14                                                       
HET    NAG  Q   2      14                                                       
HET    NAG  R   1      14                                                       
HET    NAG  R   2      14                                                       
HET    BMA  R   3      11                                                       
HET    MAN  R   4      11                                                       
HET    NAG  A 274      14                                                       
HET    NAG  A 335      14                                                       
HET    NAG  A 340      14                                                       
HET    NAG  B 221      14                                                       
HET    NAG  B 274      14                                                       
HET    NAG  B 335      14                                                       
HET    NAG  B 340      14                                                       
HET    NAG  C 250      14                                                       
HET    NAG  C 274      14                                                       
HET    NAG  C 340      14                                                       
HET    NAG  D 274      14                                                       
HET    NAG  D 335      14                                                       
HET    NAG  D 340      14                                                       
HET    NAG  E 221      14                                                       
HET    NAG  E 274      14                                                       
HET    NAG  E 340      14                                                       
HET    NAG  E 366      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
FORMUL   6  NAG    43(C8 H15 N O6)                                              
FORMUL   6  BMA    6(C6 H12 O6)                                                 
FORMUL   7  MAN    3(C6 H12 O6)                                                 
HELIX    1   1 LYS A   59  SER A   63  5                                   5    
HELIX    2   2 ARG A  111  TRP A  113  5                                   3    
HELIX    3   3 LYS B   59  SER B   63  5                                   5    
HELIX    4   4 ARG B  111  TRP B  113  5                                   3    
HELIX    5   5 LYS C   59  SER C   63  5                                   5    
HELIX    6   6 ARG C  111  TRP C  113  5                                   3    
HELIX    7   7 LYS D   59  SER D   63  5                                   5    
HELIX    8   8 ARG D  111  TRP D  113  5                                   3    
HELIX    9   9 LYS E   59  SER E   63  5                                   5    
HELIX   10  10 ARG E  111  TRP E  113  5                                   3    
SHEET    1   A 3 SER A   8  ASN A  10  0                                        
SHEET    2   A 3 VAL A  22  THR A  25 -1  N  THR A  23   O  ASN A  10           
SHEET    3   A 3 SER A  52  ILE A  55 -1  O  LEU A  53   N  LEU A  24           
SHEET    1   B 3 ARG A  15  PHE A  17  0                                        
SHEET    2   B 3 VAL A  79  PHE A  84  1  O  GLU A  82   N  ILE A  16           
SHEET    3   B 3 GLY A  64  TYR A  66 -1  O  GLY A  64   N  LEU A  81           
SHEET    1   C 3 SER A  44  LEU A  45  0                                        
SHEET    2   C 3 LYS A  38  HIS A  41 -1  N  HIS A  41   O  SER A  44           
SHEET    3   C 3 CYS A  68  GLN A  69 -1  O  GLN A  69   N  LYS A  38           
SHEET    1   D 3 LEU A  88  ALA A  92  0                                        
SHEET    2   D 3 LEU A 103  GLY A 109 -1  O  ARG A 106   N  GLN A  91           
SHEET    3   D 3 SER A 137  ILE A 138 -1  O  ILE A 138   N  LEU A 103           
SHEET    1   E 4 GLU A 125  GLU A 132  0                                        
SHEET    2   E 4 VAL A 115  LYS A 122 -1  N  LYS A 117   O  TYR A 131           
SHEET    3   E 4 GLY A 147  VAL A 155 -1  O  TYR A 150   N  TYR A 121           
SHEET    4   E 4 LEU A 158  GLU A 161 -1  N  LEU A 158   O  VAL A 155           
SHEET    1   F 5 GLU A 125  GLU A 132  0                                        
SHEET    2   F 5 VAL A 115  LYS A 122 -1  N  LYS A 117   O  TYR A 131           
SHEET    3   F 5 GLY A 147  VAL A 155 -1  O  TYR A 150   N  TYR A 121           
SHEET    4   F 5 LEU A 165  ILE A 170 -1  N  LEU A 165   O  TYR A 149           
SHEET    5   F 5 VAL A  96  MET A  98  1  N  VAL A  97   O  THR A 168           
SHEET    1   G 3 SER B   8  ASN B  10  0                                        
SHEET    2   G 3 VAL B  22  THR B  25 -1  N  THR B  23   O  ASN B  10           
SHEET    3   G 3 SER B  52  ILE B  55 -1  O  LEU B  53   N  LEU B  24           
SHEET    1   H 3 ARG B  15  PHE B  17  0                                        
SHEET    2   H 3 VAL B  79  PHE B  84  1  O  GLU B  82   N  ILE B  16           
SHEET    3   H 3 GLY B  64  TYR B  66 -1  N  GLY B  64   O  LEU B  81           
SHEET    1   I 3 SER B  44  LEU B  45  0                                        
SHEET    2   I 3 LYS B  38  HIS B  41 -1  N  HIS B  41   O  SER B  44           
SHEET    3   I 3 CYS B  68  GLN B  69 -1  O  GLN B  69   N  LYS B  38           
SHEET    1   J 3 LEU B  88  ALA B  92  0                                        
SHEET    2   J 3 LEU B 103  GLY B 109 -1  O  ARG B 106   N  GLN B  91           
SHEET    3   J 3 SER B 137  ILE B 138 -1  O  ILE B 138   N  LEU B 103           
SHEET    1   K 4 GLU B 125  GLU B 132  0                                        
SHEET    2   K 4 VAL B 115  LYS B 122 -1  N  LYS B 117   O  TYR B 131           
SHEET    3   K 4 GLY B 147  VAL B 155 -1  O  TYR B 150   N  TYR B 121           
SHEET    4   K 4 LEU B 158  GLU B 161 -1  O  LEU B 158   N  VAL B 155           
SHEET    1   L 5 GLU B 125  GLU B 132  0                                        
SHEET    2   L 5 VAL B 115  LYS B 122 -1  N  LYS B 117   O  TYR B 131           
SHEET    3   L 5 GLY B 147  VAL B 155 -1  O  TYR B 150   N  TYR B 121           
SHEET    4   L 5 LEU B 165  ILE B 170 -1  N  LEU B 165   O  TYR B 149           
SHEET    5   L 5 VAL B  96  MET B  98  1  N  VAL B  97   O  THR B 168           
SHEET    1   M 3 SER C   8  ASN C  10  0                                        
SHEET    2   M 3 VAL C  22  THR C  25 -1  N  THR C  23   O  ASN C  10           
SHEET    3   M 3 SER C  52  ILE C  55 -1  N  LEU C  53   O  LEU C  24           
SHEET    1   N 3 ARG C  15  PHE C  17  0                                        
SHEET    2   N 3 VAL C  79  PHE C  84  1  O  GLU C  82   N  ILE C  16           
SHEET    3   N 3 GLY C  64  TYR C  66 -1  O  GLY C  64   N  LEU C  81           
SHEET    1   O 3 SER C  44  LEU C  45  0                                        
SHEET    2   O 3 LYS C  38  HIS C  41 -1  N  HIS C  41   O  SER C  44           
SHEET    3   O 3 CYS C  68  GLN C  69 -1  O  GLN C  69   N  LYS C  38           
SHEET    1   P 3 LEU C  88  ALA C  92  0                                        
SHEET    2   P 3 LEU C 103  GLY C 109 -1  O  ARG C 106   N  GLN C  91           
SHEET    3   P 3 SER C 137  ILE C 138 -1  O  ILE C 138   N  LEU C 103           
SHEET    1   Q 4 GLU C 125  GLU C 132  0                                        
SHEET    2   Q 4 VAL C 115  LYS C 122 -1  N  LYS C 117   O  TYR C 131           
SHEET    3   Q 4 GLY C 147  VAL C 155 -1  O  TYR C 150   N  TYR C 121           
SHEET    4   Q 4 LEU C 158  GLU C 161 -1  N  LEU C 158   O  VAL C 155           
SHEET    1   R 5 GLU C 125  GLU C 132  0                                        
SHEET    2   R 5 VAL C 115  LYS C 122 -1  N  LYS C 117   O  TYR C 131           
SHEET    3   R 5 GLY C 147  VAL C 155 -1  O  TYR C 150   N  TYR C 121           
SHEET    4   R 5 LEU C 165  ILE C 170 -1  N  LEU C 165   O  TYR C 149           
SHEET    5   R 5 VAL C  96  MET C  98  1  N  VAL C  97   O  THR C 168           
SHEET    1   S 3 SER D   8  ASN D  10  0                                        
SHEET    2   S 3 VAL D  22  THR D  25 -1  N  THR D  23   O  ASN D  10           
SHEET    3   S 3 SER D  52  ILE D  55 -1  O  LEU D  53   N  LEU D  24           
SHEET    1   T 3 ARG D  15  PHE D  17  0                                        
SHEET    2   T 3 VAL D  79  PHE D  84  1  O  GLU D  82   N  ILE D  16           
SHEET    3   T 3 GLY D  64  TYR D  66 -1  O  GLY D  64   N  LEU D  81           
SHEET    1   U 3 SER D  44  LEU D  45  0                                        
SHEET    2   U 3 LYS D  38  HIS D  41 -1  N  HIS D  41   O  SER D  44           
SHEET    3   U 3 CYS D  68  GLN D  69 -1  O  GLN D  69   N  LYS D  38           
SHEET    1   V 3 LEU D  88  ALA D  92  0                                        
SHEET    2   V 3 LEU D 103  GLY D 109 -1  O  ARG D 106   N  GLN D  91           
SHEET    3   V 3 SER D 137  ILE D 138 -1  O  ILE D 138   N  LEU D 103           
SHEET    1   W 4 GLU D 125  GLU D 132  0                                        
SHEET    2   W 4 VAL D 115  LYS D 122 -1  N  LYS D 117   O  TYR D 131           
SHEET    3   W 4 GLY D 147  VAL D 155 -1  O  TYR D 150   N  TYR D 121           
SHEET    4   W 4 LEU D 158  GLU D 161 -1  N  LEU D 158   O  VAL D 155           
SHEET    1   X 5 GLU D 125  GLU D 132  0                                        
SHEET    2   X 5 VAL D 115  LYS D 122 -1  N  LYS D 117   O  TYR D 131           
SHEET    3   X 5 GLY D 147  VAL D 155 -1  O  TYR D 150   N  TYR D 121           
SHEET    4   X 5 LEU D 165  ILE D 170 -1  N  LEU D 165   O  TYR D 149           
SHEET    5   X 5 VAL D  96  MET D  98  1  N  VAL D  97   O  THR D 168           
SHEET    1   Y 3 SER E   8  ASN E  10  0                                        
SHEET    2   Y 3 VAL E  22  THR E  25 -1  N  THR E  23   O  ASN E  10           
SHEET    3   Y 3 SER E  52  ILE E  55 -1  O  LEU E  53   N  LEU E  24           
SHEET    1   Z 3 ARG E  15  PHE E  17  0                                        
SHEET    2   Z 3 VAL E  79  PHE E  84  1  O  GLU E  82   N  ILE E  16           
SHEET    3   Z 3 GLY E  64  TYR E  66 -1  N  GLY E  64   O  LEU E  81           
SHEET    1  AA 3 SER E  44  LEU E  45  0                                        
SHEET    2  AA 3 LYS E  38  HIS E  41 -1  N  HIS E  41   O  SER E  44           
SHEET    3  AA 3 CYS E  68  GLN E  69 -1  O  GLN E  69   N  LYS E  38           
SHEET    1  AB 3 LEU E  88  ALA E  92  0                                        
SHEET    2  AB 3 LEU E 103  GLY E 109 -1  O  ARG E 106   N  GLN E  91           
SHEET    3  AB 3 SER E 137  ILE E 138 -1  O  ILE E 138   N  LEU E 103           
SHEET    1  AC 4 GLU E 125  GLU E 132  0                                        
SHEET    2  AC 4 VAL E 115  LYS E 122 -1  N  LYS E 117   O  TYR E 131           
SHEET    3  AC 4 GLY E 147  VAL E 155 -1  O  TYR E 150   N  TYR E 121           
SHEET    4  AC 4 LEU E 158  GLU E 161 -1  O  LEU E 158   N  VAL E 155           
SHEET    1  AD 5 GLU E 125  GLU E 132  0                                        
SHEET    2  AD 5 VAL E 115  LYS E 122 -1  N  LYS E 117   O  TYR E 131           
SHEET    3  AD 5 GLY E 147  VAL E 155 -1  O  TYR E 150   N  TYR E 121           
SHEET    4  AD 5 LEU E 165  ILE E 170 -1  N  LEU E 165   O  TYR E 149           
SHEET    5  AD 5 VAL E  96  MET E  98  1  N  VAL E  97   O  THR E 168           
SSBOND   1 CYS A   26    CYS A   68                          1555   1555  2.04  
SSBOND   2 CYS A  107    CYS A  151                          1555   1555  2.05  
SSBOND   3 CYS B   26    CYS B   68                          1555   1555  2.04  
SSBOND   4 CYS B  107    CYS B  151                          1555   1555  2.06  
SSBOND   5 CYS C   26    CYS C   68                          1555   1555  2.03  
SSBOND   6 CYS C  107    CYS C  151                          1555   1555  2.04  
SSBOND   7 CYS D   26    CYS D   68                          1555   1555  2.04  
SSBOND   8 CYS D  107    CYS D  151                          1555   1555  2.05  
SSBOND   9 CYS E   26    CYS E   68                          1555   1555  2.04  
SSBOND  10 CYS E  107    CYS E  151                          1555   1555  2.05  
LINK         ND2 ASN A  21                 C1  NAG F   1     1555   1555  1.45  
LINK         ND2 ASN A  42                 C1  NAG G   1     1555   1555  1.44  
LINK         ND2 ASN A  50                 C1  NAG H   1     1555   1555  1.46  
LINK         ND2 ASN A  74                 C1  NAG A 274     1555   1555  1.46  
LINK         ND2 ASN A 135                 C1  NAG A 335     1555   1555  1.45  
LINK         ND2 ASN A 140                 C1  NAG A 340     1555   1555  1.46  
LINK         ND2 ASN A 166                 C1  NAG I   1     1555   1555  1.44  
LINK         ND2 ASN B  21                 C1  NAG B 221     1555   1555  1.46  
LINK         ND2 ASN B  42                 C1  NAG J   1     1555   1555  1.46  
LINK         ND2 ASN B  74                 C1  NAG B 274     1555   1555  1.45  
LINK         ND2 ASN B 135                 C1  NAG B 335     1555   1555  1.46  
LINK         ND2 ASN B 140                 C1  NAG B 340     1555   1555  1.45  
LINK         ND2 ASN B 166                 C1  NAG K   1     1555   1555  1.44  
LINK         ND2 ASN C  21                 C1  NAG L   1     1555   1555  1.45  
LINK         ND2 ASN C  42                 C1  NAG M   1     1555   1555  1.44  
LINK         ND2 ASN C  50                 C1  NAG C 250     1555   1555  1.46  
LINK         ND2 ASN C  74                 C1  NAG C 274     1555   1555  1.44  
LINK         ND2 ASN C 140                 C1  NAG C 340     1555   1555  1.45  
LINK         ND2 ASN C 166                 C1  NAG N   1     1555   1555  1.44  
LINK         ND2 ASN D  21                 C1  NAG O   1     1555   1555  1.45  
LINK         ND2 ASN D  42                 C1  NAG P   1     1555   1555  1.46  
LINK         ND2 ASN D  74                 C1  NAG D 274     1555   1555  1.45  
LINK         ND2 ASN D 135                 C1  NAG D 335     1555   1555  1.46  
LINK         ND2 ASN D 140                 C1  NAG D 340     1555   1555  1.45  
LINK         ND2 ASN D 166                 C1  NAG Q   1     1555   1555  1.44  
LINK         ND2 ASN E  21                 C1  NAG E 221     1555   1555  1.45  
LINK         ND2 ASN E  42                 C1  NAG R   1     1555   1555  1.46  
LINK         ND2 ASN E  74                 C1  NAG E 274     1555   1555  1.45  
LINK         ND2 ASN E 140                 C1  NAG E 340     1555   1555  1.43  
LINK         ND2 ASN E 166                 C1  NAG E 366     1555   1555  1.44  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.38  
LINK         O4  NAG F   2                 C1  BMA F   3     1555   1555  1.40  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.38  
LINK         O4  NAG G   2                 C1  MAN G   3     1555   1555  1.38  
LINK         O3  MAN G   3                 C1  MAN G   4     1555   1555  1.41  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.39  
LINK         O4  NAG I   1                 C1  NAG I   2     1555   1555  1.39  
LINK         O4  NAG J   1                 C1  NAG J   2     1555   1555  1.39  
LINK         O4  NAG J   2                 C1  BMA J   3     1555   1555  1.39  
LINK         O4  NAG K   1                 C1  NAG K   2     1555   1555  1.37  
LINK         O4  NAG L   1                 C1  NAG L   2     1555   1555  1.37  
LINK         O4  NAG M   1                 C1  NAG M   2     1555   1555  1.37  
LINK         O4  NAG M   2                 C1  BMA M   3     1555   1555  1.37  
LINK         O4  NAG N   1                 C1  NAG N   2     1555   1555  1.38  
LINK         O4  NAG O   1                 C1  NAG O   2     1555   1555  1.40  
LINK         O4  NAG O   2                 C1  BMA O   3     1555   1555  1.41  
LINK         O4  NAG P   1                 C1  NAG P   2     1555   1555  1.40  
LINK         O4  NAG P   2                 C1  BMA P   3     1555   1555  1.39  
LINK         O4  NAG Q   1                 C1  NAG Q   2     1555   1555  1.38  
LINK         O4  NAG R   1                 C1  NAG R   2     1555   1555  1.40  
LINK         O4  NAG R   2                 C1  BMA R   3     1555   1555  1.38  
LINK         O6  BMA R   3                 C1  MAN R   4     1555   1555  1.41  
CISPEP   1 ASN A   10    PRO A   11          0        -0.66                     
CISPEP   2 ASN B   10    PRO B   11          0         0.11                     
CISPEP   3 ASN C   10    PRO C   11          0         0.43                     
CISPEP   4 ASN D   10    PRO D   11          0        -0.11                     
CISPEP   5 ASN E   10    PRO E   11          0        -0.04                     
CRYST1  145.080  145.080   62.740  90.00  90.00  90.00 P 43         20          
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      0.006893  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006893  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015939        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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