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Database: PDB
Entry: 5HBT
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HEADER    TRANSPORT PROTEIN/TOXIN                 02-JAN-16   5HBT              
TITLE     COMPLEX STRUCTURE OF FAB35 AND HUMAN NACHR ALPHA1                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA 1;                    
COMPND   3 CHAIN: B;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 21-231;                                       
COMPND   5 SYNONYM: CHOLINERGIC RECEPTOR,NICOTINIC,ALPHA 1 (MUSCLE),ISOFORM     
COMPND   6 CRA_C;                                                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: FAB35, LIGHT CHAIN;                                        
COMPND  11 CHAIN: C;                                                            
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: FAB35, HEAVY CHAIN;                                        
COMPND  14 CHAIN: D;                                                            
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: ALPHA-BUNGAROTOXIN ISOFORM V31;                            
COMPND  17 CHAIN: A;                                                            
COMPND  18 FRAGMENT: UNP RESIDUES 22-95;                                        
COMPND  19 SYNONYM: BGTX V31,LONG NEUROTOXIN 1                                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CHRNA1, HCG_1811440;                                           
SOURCE   6 EXPRESSION_SYSTEM: PICHIA;                                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4919;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: KM71H;                                     
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  11 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  12 ORGANISM_TAXID: 10116;                                               
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  15 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  16 ORGANISM_TAXID: 10116;                                               
SOURCE  17 MOL_ID: 4;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: BUNGARUS MULTICINCTUS;                          
SOURCE  19 ORGANISM_COMMON: MANY-BANDED KRAIT;                                  
SOURCE  20 ORGANISM_TAXID: 8616                                                 
KEYWDS    NICOTINIC ACETYLCHOLINE RECEPTOR ALPHA1, FAB35, COMPLEX, MYASTHENIA   
KEYWDS   2 GRAVIS, TRANSPORT PROTEIN-TOXIN COMPLEX                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.NORIDOMI,G.WATANABE,M.N.HANSEN,G.W.HAN,L.CHEN                       
REVDAT   2   10-MAY-17 5HBT    1       JRNL                                     
REVDAT   1   03-MAY-17 5HBT    0                                                
JRNL        AUTH   K.NORIDOMI,G.WATANABE,M.N.HANSEN,G.W.HAN,L.CHEN              
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE MOLECULAR MECHANISMS OF         
JRNL        TITL 2 MYASTHENIA GRAVIS AND THEIR THERAPEUTIC IMPLICATIONS.        
JRNL        REF    ELIFE                         V.   6       2017              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   28440223                                                     
JRNL        DOI    10.7554/ELIFE.23043                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 23958                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1231                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.61                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.68                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1633                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 93                           
REMARK   3   BIN FREE R VALUE                    : 0.3500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5577                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 105                                     
REMARK   3   SOLVENT ATOMS            : 102                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.41000                                              
REMARK   3    B22 (A**2) : 0.13000                                              
REMARK   3    B33 (A**2) : -2.87000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.81000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.458         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.339         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.274         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.128        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5840 ; 0.008 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  5177 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7981 ; 1.341 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 12115 ; 0.909 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   713 ; 7.233 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   234 ;35.988 ;24.402       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   931 ;15.820 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;14.222 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   928 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6313 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1124 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2864 ; 1.287 ; 4.225       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2863 ; 1.287 ; 4.224       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3573 ; 2.349 ; 6.329       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3574 ; 2.349 ; 6.330       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2976 ; 1.020 ; 4.294       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2976 ; 1.020 ; 4.294       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4408 ; 1.859 ; 6.424       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5947 ; 3.732 ;47.419       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5941 ; 3.714 ;47.405       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    74                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.7161 -26.7122 -10.1000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0511 T22:   0.4068                                     
REMARK   3      T33:   0.1245 T12:   0.0367                                     
REMARK   3      T13:  -0.0539 T23:   0.0438                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.0290 L22:   0.0514                                     
REMARK   3      L33:   3.1063 L12:  -0.3266                                     
REMARK   3      L13:   0.5499 L23:   0.2474                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2480 S12:   0.5204 S13:   0.0275                       
REMARK   3      S21:   0.0018 S22:  -0.1406 S23:  -0.0485                       
REMARK   3      S31:  -0.0739 S32:  -0.7178 S33:  -0.1074                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     0        B   211                          
REMARK   3    RESIDUE RANGE :   B   301        B   309                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.8818 -12.2938   5.5857              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1906 T22:   0.0958                                     
REMARK   3      T33:   0.0993 T12:  -0.0139                                     
REMARK   3      T13:   0.0187 T23:  -0.0157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5004 L22:   0.0335                                     
REMARK   3      L33:   0.7397 L12:   0.0329                                     
REMARK   3      L13:   0.1060 L23:  -0.1168                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0234 S12:  -0.0125 S13:   0.0306                       
REMARK   3      S21:   0.0215 S22:  -0.0046 S23:   0.0357                       
REMARK   3      S31:   0.0032 S32:  -0.0097 S33:  -0.0188                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   212                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.2821 -20.1691  65.7725              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1944 T22:   0.1925                                     
REMARK   3      T33:   0.0245 T12:  -0.1294                                     
REMARK   3      T13:   0.0563 T23:  -0.0669                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2711 L22:   0.1154                                     
REMARK   3      L33:   2.0793 L12:  -0.3680                                     
REMARK   3      L13:  -1.0369 L23:   0.3886                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0317 S12:  -0.2046 S13:   0.0523                       
REMARK   3      S21:   0.0083 S22:   0.0494 S23:  -0.0171                       
REMARK   3      S31:   0.2952 S32:   0.1041 S33:  -0.0177                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   219                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7865 -19.9995  64.3352              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1229 T22:   0.2461                                     
REMARK   3      T33:   0.0311 T12:  -0.0080                                     
REMARK   3      T13:   0.0112 T23:  -0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0535 L22:   0.1269                                     
REMARK   3      L33:   1.2622 L12:  -0.1621                                     
REMARK   3      L13:  -0.3321 L23:  -0.2778                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0105 S12:  -0.3027 S13:  -0.1167                       
REMARK   3      S21:  -0.0126 S22:   0.0403 S23:   0.0343                       
REMARK   3      S31:  -0.0490 S32:   0.1827 S33:  -0.0298                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5HBT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000216517.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36729                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
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     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.11700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 57.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.97900                            
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: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CACODYLATE TRIHYDRATE, CALCIUM    
REMARK 280  ACETATE HYDRATE, PEG 8000, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       80.00300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.07150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       80.00300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       21.07150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, 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 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     CYS C   213                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PHE B 137    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG C 210    CZ   NH1  NH2                                       
REMARK 470     GLU C 212    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 216    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  72    CG   CD   NE   CZ   NH1  NH2                        
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    LEU B  56       79.06   -110.09                                   
REMARK 500    HIS B 134       99.39   -162.56                                   
REMARK 500    THR C  51      -50.17     66.99                                   
REMARK 500    ASN C  52       12.83   -142.65                                   
REMARK 500    LEU C  83      105.56    -46.44                                   
REMARK 500    ASN C 137       74.50     58.10                                   
REMARK 500    PRO C 140     -167.76    -76.23                                   
REMARK 500    LYS C 168      -71.30    -80.48                                   
REMARK 500    ASN C 189      -54.02   -124.62                                   
REMARK 500    ARG C 210     -100.75     54.60                                   
REMARK 500    SER D  15      -26.38     78.96                                   
REMARK 500    ARG D 102     -118.10     53.40                                   
REMARK 500    SER D 139       64.84   -106.69                                   
REMARK 500    SER D 163     -134.92     57.32                                   
REMARK 500    LEU D 166      -50.35   -141.21                                   
REMARK 500    SER D 167     -163.52     62.62                                   
REMARK 500    SER D 168       34.09    -80.79                                   
REMARK 500    GLN D 178      -91.21   -106.94                                   
REMARK 500    SER D 179       68.15   -101.73                                   
REMARK 500    ALA A  13       66.47   -101.93                                   
REMARK 500    PRO A  73     -168.58    -66.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TYR B   93     ASN B   94                 -143.61                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  301 through MAN B 309 bound to ASN B 141                            
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5HBV   RELATED DB: PDB                                   
DBREF  5HBT B    1   211  UNP    G5E9G9   G5E9G9_HUMAN    21    231             
DBREF  5HBT C    1   213  PDB    5HBT     5HBT             1    213             
DBREF  5HBT D    1   219  PDB    5HBT     5HBT             1    219             
DBREF  5HBT A    1    74  UNP    P60616   3L21V_BUNMU     22     95             
SEQADV 5HBT LYS B    0  UNP  G5E9G9              EXPRESSION TAG                 
SEQADV 5HBT GLU B    8  UNP  G5E9G9    VAL    28 ENGINEERED MUTATION            
SEQADV 5HBT ARG B  149  UNP  G5E9G9    TRP   169 ENGINEERED MUTATION            
SEQADV 5HBT ALA B  155  UNP  G5E9G9    VAL   175 ENGINEERED MUTATION            
SEQRES   1 B  212  LYS SER GLU HIS GLU THR ARG LEU GLU ALA LYS LEU PHE          
SEQRES   2 B  212  LYS ASP TYR SER SER VAL VAL ARG PRO VAL GLU ASP HIS          
SEQRES   3 B  212  ARG GLN VAL VAL GLU VAL THR VAL GLY LEU GLN LEU ILE          
SEQRES   4 B  212  GLN LEU ILE ASN VAL ASP GLU VAL ASN GLN ILE VAL THR          
SEQRES   5 B  212  THR ASN VAL ARG LEU LYS GLN GLN TRP VAL ASP TYR ASN          
SEQRES   6 B  212  LEU LYS TRP ASN PRO ASP ASP TYR GLY GLY VAL LYS LYS          
SEQRES   7 B  212  ILE HIS ILE PRO SER GLU LYS ILE TRP ARG PRO ASP LEU          
SEQRES   8 B  212  VAL LEU TYR ASN ASN ALA ASP GLY ASP PHE ALA ILE VAL          
SEQRES   9 B  212  LYS PHE THR LYS VAL LEU LEU GLN TYR THR GLY HIS ILE          
SEQRES  10 B  212  THR TRP THR PRO PRO ALA ILE PHE LYS SER TYR CYS GLU          
SEQRES  11 B  212  ILE ILE VAL THR HIS PHE PRO PHE ASP GLU GLN ASN CYS          
SEQRES  12 B  212  SER MET LYS LEU GLY THR ARG THR TYR ASP GLY SER ALA          
SEQRES  13 B  212  VAL ALA ILE ASN PRO GLU SER ASP GLN PRO ASP LEU SER          
SEQRES  14 B  212  ASN PHE MET GLU SER GLY GLU TRP VAL ILE LYS GLU SER          
SEQRES  15 B  212  ARG GLY TRP LYS HIS SER VAL THR TYR SER CYS CYS PRO          
SEQRES  16 B  212  ASP THR PRO TYR LEU ASP ILE THR TYR HIS PHE VAL MET          
SEQRES  17 B  212  GLN ARG LEU PRO                                              
SEQRES   1 C  213  ASP ILE VAL ILE THR GLN SER PRO SER LEU LEU SER ALA          
SEQRES   2 C  213  SER VAL GLY ASP ARG VAL THR LEU THR CYS LYS GLY SER          
SEQRES   3 C  213  GLN ASN ILE ASP ASN TYR LEU ALA TRP TYR GLN GLN LYS          
SEQRES   4 C  213  LEU GLY GLU ALA PRO LYS LEU LEU ILE TYR LYS THR ASN          
SEQRES   5 C  213  SER LEU GLN THR GLY ILE PRO SER ARG PHE SER GLY SER          
SEQRES   6 C  213  GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU          
SEQRES   7 C  213  HIS SER GLU ASP LEU ALA THR TYR TYR CYS TYR GLN TYR          
SEQRES   8 C  213  ILE ASN GLY TYR THR PHE GLY THR GLY THR LYS LEU GLU          
SEQRES   9 C  213  LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE          
SEQRES  10 C  213  PRO PRO SER THR GLU GLN LEU ALA THR GLY GLY ALA SER          
SEQRES  11 C  213  VAL VAL CYS LEU MET ASN ASN PHE TYR PRO ARG ASP ILE          
SEQRES  12 C  213  SER VAL LYS TRP LYS ILE ASP GLY THR GLU ARG ARG ASP          
SEQRES  13 C  213  GLY VAL LEU ASP SER VAL THR ASP GLN ASP SER LYS ASP          
SEQRES  14 C  213  SER THR TYR SER MET SER SER THR LEU SER LEU THR LYS          
SEQRES  15 C  213  ALA ASP TYR GLU SER HIS ASN LEU TYR THR CYS GLU VAL          
SEQRES  16 C  213  VAL HIS LYS THR SER SER SER PRO VAL VAL LYS SER PHE          
SEQRES  17 C  213  ASN ARG ASN GLU CYS                                          
SEQRES   1 D  219  GLU VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL GLN          
SEQRES   2 D  219  PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY          
SEQRES   3 D  219  PHE SER LEU THR SER TYR SER VAL SER TRP LEU ARG GLN          
SEQRES   4 D  219  PRO SER GLY LYS GLY PRO GLU TRP MET GLY ARG MET TRP          
SEQRES   5 D  219  ASP ASP GLY GLY THR VAL TYR ASN SER GLY LEU LYS SER          
SEQRES   6 D  219  ARG LEU SER ILE SER ARG ASP THR SER LYS ASN GLN VAL          
SEQRES   7 D  219  PHE LEU LYS MET ASN SER LEU GLN THR ASP ASP THR GLY          
SEQRES   8 D  219  THR TYR TYR CYS THR ARG ASP GLU ARG ILE ARG ALA ILE          
SEQRES   9 D  219  ASN TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR          
SEQRES  10 D  219  VAL SER SER ALA GLU THR THR ALA PRO SER VAL TYR PRO          
SEQRES  11 D  219  LEU ALA PRO GLY THR ALA LEU LYS SER ASN SER MET VAL          
SEQRES  12 D  219  THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO          
SEQRES  13 D  219  VAL THR VAL THR TRP ASN SER GLY ALA LEU SER SER GLY          
SEQRES  14 D  219  VAL HIS THR PHE PRO ALA VAL LEU GLN SER GLY LEU TYR          
SEQRES  15 D  219  THR LEU THR SER SER VAL THR VAL PRO SER SER THR TRP          
SEQRES  16 D  219  PRO SER GLN THR VAL THR CYS ASN VAL ALA HIS PRO GLY          
SEQRES  17 D  219  GLN GLN HIS GLN ARG TRP THR ARG LYS LEU CYS                  
SEQRES   1 A   74  ILE VAL CYS HIS THR THR ALA THR SER PRO ILE SER ALA          
SEQRES   2 A   74  VAL THR CYS PRO PRO GLY GLU ASN LEU CYS TYR ARG LYS          
SEQRES   3 A   74  MET TRP CYS ASP VAL PHE CYS SER SER ARG GLY LYS VAL          
SEQRES   4 A   74  VAL GLU LEU GLY CYS ALA ALA THR CYS PRO SER LYS LYS          
SEQRES   5 A   74  PRO TYR GLU GLU VAL THR CYS CYS SER THR ASP LYS CYS          
SEQRES   6 A   74  ASN PRO HIS PRO LYS GLN ARG PRO GLY                          
HET    NAG  B 301      14                                                       
HET    NAG  B 302      14                                                       
HET    BMA  B 303      11                                                       
HET    MAN  B 304      11                                                       
HET    MAN  B 305      11                                                       
HET    MAN  B 306      11                                                       
HET    MAN  B 307      11                                                       
HET    MAN  B 308      11                                                       
HET    MAN  B 309      11                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
FORMUL   5  NAG    2(C8 H15 N O6)                                               
FORMUL   5  BMA    C6 H12 O6                                                    
FORMUL   5  MAN    6(C6 H12 O6)                                                 
FORMUL   6  HOH   *102(H2 O)                                                    
HELIX    1 AA1 LYS B    0  LYS B   13  1                                  14    
HELIX    2 AA2 TYR B   63  LYS B   66  5                                   4    
HELIX    3 AA3 ASN B   68  GLY B   73  5                                   6    
HELIX    4 AA4 GLU B   83  ILE B   85  5                                   3    
HELIX    5 AA5 SER C  120  ALA C  125  1                                   6    
HELIX    6 AA6 LYS C  182  SER C  187  1                                   6    
HELIX    7 AA7 SER D   61  SER D   65  5                                   5    
HELIX    8 AA8 THR D   73  LYS D   75  5                                   3    
HELIX    9 AA9 GLN D   86  ASP D   89  5                                   4    
HELIX   10 AB1 LEU D  166  SER D  168  5                                   3    
HELIX   11 AB2 SER D  193  GLN D  198  1                                   6    
HELIX   12 AB3 PRO D  207  GLN D  210  5                                   4    
HELIX   13 AB4 PHE A   32  GLY A   37  1                                   6    
SHEET    1 AA1 5 LYS B  77  PRO B  81  0                                        
SHEET    2 AA1 5 LYS B 107  GLN B 111 -1  O  LEU B 110   N  ILE B  78           
SHEET    3 AA1 5 HIS B 115  TRP B 118 -1  O  THR B 117   N  LEU B 109           
SHEET    4 AA1 5 ILE B  49  VAL B  61 -1  N  TRP B  60   O  ILE B 116           
SHEET    5 AA1 5 PRO B 121  TYR B 127 -1  O  ALA B 122   N  VAL B  54           
SHEET    1 AA2 6 LYS B  77  PRO B  81  0                                        
SHEET    2 AA2 6 LYS B 107  GLN B 111 -1  O  LEU B 110   N  ILE B  78           
SHEET    3 AA2 6 HIS B 115  TRP B 118 -1  O  THR B 117   N  LEU B 109           
SHEET    4 AA2 6 ILE B  49  VAL B  61 -1  N  TRP B  60   O  ILE B 116           
SHEET    5 AA2 6 VAL B  29  ASP B  44 -1  N  GLN B  36   O  ARG B  55           
SHEET    6 AA2 6 VAL B 156  PRO B 160  1  O  ASN B 159   N  VAL B  33           
SHEET    1 AA3 3 LEU B  90  TYR B  93  0                                        
SHEET    2 AA3 3 GLU B 139  THR B 148 -1  O  GLY B 147   N  VAL B  91           
SHEET    3 AA3 3 GLU B 129  ILE B 130 -1  N  GLU B 129   O  ASN B 141           
SHEET    1 AA4 7 LEU B  90  TYR B  93  0                                        
SHEET    2 AA4 7 GLU B 139  THR B 148 -1  O  GLY B 147   N  VAL B  91           
SHEET    3 AA4 7 TYR B 198  ARG B 209 -1  O  ILE B 201   N  LEU B 146           
SHEET    4 AA4 7 TRP B 176  TYR B 190 -1  N  HIS B 186   O  ASP B 200           
SHEET    5 AA4 7 VAL A  39  ALA A  45 -1  O  VAL A  40   N  THR B 189           
SHEET    6 AA4 7 LEU A  22  TRP A  28 -1  N  TRP A  28   O  VAL A  39           
SHEET    7 AA4 7 GLU A  56  CYS A  60 -1  O  GLU A  56   N  MET A  27           
SHEET    1 AA5 4 ILE C   4  SER C   7  0                                        
SHEET    2 AA5 4 VAL C  19  GLY C  25 -1  O  THR C  22   N  SER C   7           
SHEET    3 AA5 4 ASP C  70  ILE C  75 -1  O  LEU C  73   N  LEU C  21           
SHEET    4 AA5 4 PHE C  62  SER C  67 -1  N  SER C  63   O  THR C  74           
SHEET    1 AA6 6 LEU C  10  ALA C  13  0                                        
SHEET    2 AA6 6 THR C 101  LEU C 105  1  O  GLU C 104   N  LEU C  11           
SHEET    3 AA6 6 THR C  85  GLN C  90 -1  N  TYR C  86   O  THR C 101           
SHEET    4 AA6 6 LEU C  33  GLN C  38 -1  N  ALA C  34   O  TYR C  89           
SHEET    5 AA6 6 LYS C  45  TYR C  49 -1  O  LEU C  47   N  TRP C  35           
SHEET    6 AA6 6 SER C  53  LEU C  54 -1  O  SER C  53   N  TYR C  49           
SHEET    1 AA7 4 LEU C  10  ALA C  13  0                                        
SHEET    2 AA7 4 THR C 101  LEU C 105  1  O  GLU C 104   N  LEU C  11           
SHEET    3 AA7 4 THR C  85  GLN C  90 -1  N  TYR C  86   O  THR C 101           
SHEET    4 AA7 4 THR C  96  PHE C  97 -1  O  THR C  96   N  GLN C  90           
SHEET    1 AA8 4 THR C 113  PHE C 117  0                                        
SHEET    2 AA8 4 GLY C 128  PHE C 138 -1  O  LEU C 134   N  SER C 115           
SHEET    3 AA8 4 TYR C 172  THR C 181 -1  O  LEU C 178   N  VAL C 131           
SHEET    4 AA8 4 VAL C 158  VAL C 162 -1  N  LEU C 159   O  THR C 177           
SHEET    1 AA9 4 THR C 152  ARG C 154  0                                        
SHEET    2 AA9 4 ILE C 143  ILE C 149 -1  N  ILE C 149   O  THR C 152           
SHEET    3 AA9 4 LEU C 190  HIS C 197 -1  O  VAL C 196   N  SER C 144           
SHEET    4 AA9 4 VAL C 204  ASN C 209 -1  O  LYS C 206   N  CYS C 193           
SHEET    1 AB1 4 GLN D   3  SER D   7  0                                        
SHEET    2 AB1 4 LEU D  18  SER D  25 -1  O  THR D  23   N  GLN D   5           
SHEET    3 AB1 4 GLN D  77  MET D  82 -1  O  VAL D  78   N  CYS D  22           
SHEET    4 AB1 4 LEU D  67  ASP D  72 -1  N  SER D  70   O  PHE D  79           
SHEET    1 AB2 6 LEU D  11  VAL D  12  0                                        
SHEET    2 AB2 6 THR D 114  VAL D 118  1  O  THR D 117   N  VAL D  12           
SHEET    3 AB2 6 GLY D  91  ILE D 101 -1  N  GLY D  91   O  VAL D 116           
SHEET    4 AB2 6 SER D  33  PRO D  40 -1  N  GLN D  39   O  THR D  92           
SHEET    5 AB2 6 GLU D  46  MET D  51 -1  O  MET D  51   N  VAL D  34           
SHEET    6 AB2 6 THR D  57  TYR D  59 -1  O  VAL D  58   N  ARG D  50           
SHEET    1 AB3 4 LEU D  11  VAL D  12  0                                        
SHEET    2 AB3 4 THR D 114  VAL D 118  1  O  THR D 117   N  VAL D  12           
SHEET    3 AB3 4 GLY D  91  ILE D 101 -1  N  GLY D  91   O  VAL D 116           
SHEET    4 AB3 4 ILE D 104  TRP D 110 -1  O  TRP D 106   N  GLU D  99           
SHEET    1 AB4 4 SER D 127  LEU D 131  0                                        
SHEET    2 AB4 4 VAL D 143  TYR D 152 -1  O  LYS D 150   N  SER D 127           
SHEET    3 AB4 4 TYR D 182  VAL D 190 -1  O  LEU D 184   N  VAL D 149           
SHEET    4 AB4 4 VAL D 170  THR D 172 -1  N  HIS D 171   O  SER D 187           
SHEET    1 AB5 4 SER D 127  LEU D 131  0                                        
SHEET    2 AB5 4 VAL D 143  TYR D 152 -1  O  LYS D 150   N  SER D 127           
SHEET    3 AB5 4 TYR D 182  VAL D 190 -1  O  LEU D 184   N  VAL D 149           
SHEET    4 AB5 4 VAL D 176  LEU D 177 -1  N  VAL D 176   O  THR D 183           
SHEET    1 AB6 3 THR D 158  TRP D 161  0                                        
SHEET    2 AB6 3 THR D 201  HIS D 206 -1  O  ASN D 203   N  THR D 160           
SHEET    3 AB6 3 HIS D 211  ARG D 216 -1  O  ARG D 213   N  VAL D 204           
SSBOND   1 CYS B  128    CYS B  142                          1555   1555  2.05  
SSBOND   2 CYS B  192    CYS B  193                          1555   1555  2.06  
SSBOND   3 CYS C   23    CYS C   88                          1555   1555  2.08  
SSBOND   4 CYS C  133    CYS C  193                          1555   1555  2.05  
SSBOND   5 CYS D   22    CYS D   95                          1555   1555  2.06  
SSBOND   6 CYS D  147    CYS D  202                          1555   1555  2.03  
SSBOND   7 CYS A    3    CYS A   23                          1555   1555  2.04  
SSBOND   8 CYS A    3    CYS A   16                          1555   1555  2.07  
SSBOND   9 CYS A   16    CYS A   44                          1555   1555  2.04  
SSBOND  10 CYS A   29    CYS A   33                          1555   1555  2.07  
SSBOND  11 CYS A   48    CYS A   59                          1555   1555  2.04  
SSBOND  12 CYS A   60    CYS A   65                          1555   1555  2.03  
LINK         ND2 ASN B 141                 C1  NAG B 301     1555   1555  1.43  
LINK         O4  NAG B 301                 C1  NAG B 302     1555   1555  1.44  
LINK         O4  NAG B 302                 C1  BMA B 303     1555   1555  1.43  
LINK         O3  BMA B 303                 C1  MAN B 304     1555   1555  1.45  
LINK         O6  BMA B 303                 C1  MAN B 307     1555   1555  1.44  
LINK         O2  MAN B 304                 C1  MAN B 305     1555   1555  1.45  
LINK         O2  MAN B 305                 C1  MAN B 306     1555   1555  1.45  
LINK         O3  MAN B 307                 C1  MAN B 309     1555   1555  1.45  
LINK         O6  MAN B 307                 C1  MAN B 308     1555   1555  1.45  
CISPEP   1 SER C    7    PRO C    8          0       -10.70                     
CISPEP   2 TYR C  139    PRO C  140          0         4.73                     
CISPEP   3 PHE D  153    PRO D  154          0        -8.67                     
CISPEP   4 GLU D  155    PRO D  156          0         6.54                     
CISPEP   5 SER A    9    PRO A   10          0        -0.04                     
SITE     1 AC1 13 THR A   6  ALA A   7  THR A   8  GLU A  41                    
SITE     2 AC1 13 LEU A  42  ASN B 141  TRP B 184  LYS B 185                    
SITE     3 AC1 13 HIS B 186  THR B 202  HOH B 419  HOH B 426                    
SITE     4 AC1 13 HOH B 430                                                     
CRYST1  160.006   42.143  136.488  90.00 117.05  90.00 C 1 2 1       4          
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      0.006250  0.000000  0.003191        0.00000                         
SCALE2      0.000000  0.023729  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008226        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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