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Database: PDB
Entry: 1SYT
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Original site: 1SYT 
HEADER    SIGNALING PROTEIN                       02-APR-04   1SYT              
TITLE     CRYSTAL STRUCTURE OF SIGNALLING PROTEIN FROM GOAT SPG-40 IN THE       
TITLE    2 PRESENSE OF N,N',N''-TRIACETYL-CHITOTRIOSE AT 2.6A RESOLUTION        
CAVEAT     1SYT    NAG B 1 HAS WRONG CHIRALITY AT ATOM C1                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BP40;                                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SPG-40                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAPRA HIRCUS;                                   
SOURCE   3 ORGANISM_COMMON: GOAT;                                               
SOURCE   4 ORGANISM_TAXID: 9925                                                 
KEYWDS    SIGNALLING PROTEIN, GOAT SPG-40, 2.6A RESOLUTION, SIGNALING PROTEIN   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.KUMAR,R.PREM KUMAR,D.B.SRIVASTAVA,S.SHARMA,T.P.SINGH                
REVDAT   5   25-OCT-23 1SYT    1       HETSYN                                   
REVDAT   4   29-JUL-20 1SYT    1       CAVEAT COMPND REMARK HETNAM              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   13-JUL-11 1SYT    1       VERSN                                    
REVDAT   2   24-FEB-09 1SYT    1       VERSN                                    
REVDAT   1   20-APR-04 1SYT    0                                                
JRNL        AUTH   J.KUMAR,R.PREM KUMAR,D.B.SRIVASTAVA,S.SHARMA,T.P.SINGH       
JRNL        TITL   CRYSTAL STRUCTURE OF SIGNALLING PROTEIN FROM GOAT SPG-40 IN  
JRNL        TITL 2 THE PRESENSE OF N,N',N''-TRIACETYL-CHITOTRIOSE AT 2.6A       
JRNL        TITL 3 RESOLUTION                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 12892                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 671                             
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.72                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 926                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 52                           
REMARK   3   BIN FREE R VALUE                    : 0.3360                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2874                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 204                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.27000                                             
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.30000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.313         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.288         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.304         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.361        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2992 ; 0.019 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2649 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4056 ; 1.725 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6126 ; 1.256 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   359 ; 2.605 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   496 ;19.652 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   437 ; 0.129 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3318 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   671 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   697 ; 0.252 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2635 ; 0.243 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):     1 ; 0.157 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   202 ; 0.143 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     3 ; 0.177 ; 0.500       
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):     3 ; 0.121 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    26 ; 0.260 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.115 ; 0.500       
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):  1791 ; 1.353 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2869 ; 2.538 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1201 ; 2.971 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1187 ; 4.850 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 1SYT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-APR-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000022101.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JAN-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 298.0                              
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5414                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13563                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 8.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.37600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
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: 1QZO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM TRIS-HCL, 50MM NACL, 19% ETHANOL,   
REMARK 280  PH 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       31.55550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.81300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.01800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.81300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.55550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.01800            
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 300 REMARK: THE BIOLOGICAL UNIT IS MONOMER                               
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, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    ASP A 112   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 178   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 280   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    LEU A 320   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    ARG A 361   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG A 361   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 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    PHE A  37      103.93     78.44                                   
REMARK 500    TRP A  48      -63.89   -126.48                                   
REMARK 500    ALA A 117       50.50   -111.58                                   
REMARK 500    TRP A 118       95.50    -66.04                                   
REMARK 500    TYR A 120       99.16     77.32                                   
REMARK 500    ASP A 169       71.13   -104.60                                   
REMARK 500    TYR A 185       23.20   -157.85                                   
REMARK 500    ALA A 190       -4.62    -53.47                                   
REMARK 500    GLN A 193       56.90    -53.29                                   
REMARK 500    ASN A 205       73.01    -61.36                                   
REMARK 500    SER A 206       10.29   -167.73                                   
REMARK 500    ASP A 207      104.08   -178.22                                   
REMARK 500    SER A 210       45.96     76.56                                   
REMARK 500    SER A 214       51.19    -94.77                                   
REMARK 500    ALA A 332      107.37     72.23                                   
REMARK 500    GLN A 345      122.50    -21.26                                   
REMARK 500    ASN A 346       13.73    -65.27                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QZO   RELATED DB: PDB                                   
DBREF  1SYT A    1   362  GB     19526603 AAL87007        22    383             
SEQADV 1SYT VAL A   33  GB   19526603  ILE    54 SEE REMARK 999                 
SEQADV 1SYT ALA A  131  GB   19526603  GLY   152 SEE REMARK 999                 
SEQADV 1SYT ASN A  205  GB   19526603  GLN   226 SEE REMARK 999                 
SEQADV 1SYT SER A  206  GB   19526603  GLU   227 SEE REMARK 999                 
SEQADV 1SYT     A       GB   19526603  ASP   232 SEE REMARK 999                 
SEQADV 1SYT GLY A  253  GB   19526603  VAL   274 SEE REMARK 999                 
SEQADV 1SYT ARG A  361  GB   19526603  GLU   382 SEE REMARK 999                 
SEQRES   1 A  361  TYR LYS LEU ILE CYS TYR TYR THR SER TRP SER GLN TYR          
SEQRES   2 A  361  ARG GLU GLY ASP GLY SER CYS PHE PRO ASP ALA ILE ASP          
SEQRES   3 A  361  PRO PHE LEU CYS THR HIS VAL ILE TYR SER PHE ALA ASN          
SEQRES   4 A  361  ILE SER ASN ASN GLU ILE ASP THR TRP GLU TRP ASN ASP          
SEQRES   5 A  361  VAL THR LEU TYR ASP THR LEU ASN THR LEU LYS ASN ARG          
SEQRES   6 A  361  ASN PRO LYS LEU LYS THR LEU LEU SER VAL GLY GLY TRP          
SEQRES   7 A  361  ASN PHE GLY PRO GLU ARG PHE SER LYS ILE ALA SER LYS          
SEQRES   8 A  361  THR GLN SER ARG ARG THR PHE ILE LYS SER VAL PRO PRO          
SEQRES   9 A  361  PHE LEU ARG THR HIS GLY PHE ASP GLY LEU ASP LEU ALA          
SEQRES  10 A  361  TRP LEU TYR PRO GLY ARG ARG ASP LYS ARG HIS LEU THR          
SEQRES  11 A  361  ALA LEU VAL LYS GLU MET LYS ALA GLU PHE ALA ARG GLU          
SEQRES  12 A  361  ALA GLN ALA GLY THR GLU ARG LEU LEU LEU SER ALA ALA          
SEQRES  13 A  361  VAL SER ALA GLY LYS ILE ALA ILE ASP ARG GLY TYR ASP          
SEQRES  14 A  361  ILE ALA GLN ILE SER ARG HIS LEU ASP PHE ILE SER LEU          
SEQRES  15 A  361  LEU THR TYR ASP PHE HIS GLY ALA TRP ARG GLN THR VAL          
SEQRES  16 A  361  GLY HIS HIS SER PRO LEU PHE ARG GLY ASN SER ASP ALA          
SEQRES  17 A  361  SER SER ARG PHE SER ASN ALA ASP TYR ALA VAL SER TYR          
SEQRES  18 A  361  MET LEU ARG LEU GLY ALA PRO ALA ASN LYS LEU VAL MET          
SEQRES  19 A  361  GLY ILE PRO THR PHE GLY ARG SER PHE THR LEU ALA SER          
SEQRES  20 A  361  SER LYS THR ASP GLY GLY ALA PRO ILE SER GLY PRO GLY          
SEQRES  21 A  361  ILE PRO GLY ARG PHE THR LYS GLU LYS GLY ILE LEU ALA          
SEQRES  22 A  361  TYR TYR GLU ILE CYS ASP PHE LEU HIS GLY ALA THR THR          
SEQRES  23 A  361  HIS ARG PHE ARG ASP GLN GLN VAL PRO TYR ALA THR LYS          
SEQRES  24 A  361  GLY ASN GLN TRP VAL ALA TYR ASP ASP GLN GLU SER VAL          
SEQRES  25 A  361  LYS ASN LYS ALA ARG TYR LEU LYS ASN ARG GLN LEU ALA          
SEQRES  26 A  361  GLY ALA MET VAL TRP ALA LEU ASP LEU ASP ASP PHE ARG          
SEQRES  27 A  361  GLY THR PHE CYS GLY GLN ASN LEU THR PHE PRO LEU THR          
SEQRES  28 A  361  SER ALA VAL LYS ASP VAL LEU ALA ARG VAL                      
MODRES 1SYT ASN A   39  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET    MAN  B   3      11                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE                              
FORMUL   2  NAG    2(C8 H15 N O6)                                               
FORMUL   2  MAN    C6 H12 O6                                                    
FORMUL   3  HOH   *204(H2 O)                                                    
HELIX    1   1 TRP A   10  ARG A   14  5                                   5    
HELIX    2   2 GLU A   15  SER A   19  5                                   5    
HELIX    3   3 PHE A   21  ILE A   25  5                                   5    
HELIX    4   4 ASN A   51  THR A   61  1                                  11    
HELIX    5   5 THR A   61  ASN A   66  1                                   6    
HELIX    6   6 GLY A   81  LYS A   91  1                                  11    
HELIX    7   7 LYS A   91  GLY A  110  1                                  20    
HELIX    8   8 ASP A  125  ALA A  144  1                                  20    
HELIX    9   9 GLN A  145  GLY A  147  5                                   3    
HELIX   10  10 GLY A  160  TYR A  168  1                                   9    
HELIX   11  11 ASP A  169  ARG A  175  1                                   7    
HELIX   12  12 ASN A  215  LEU A  226  1                                  12    
HELIX   13  13 PRO A  229  ASN A  231  5                                   3    
HELIX   14  14 TYR A  275  LEU A  282  1                                   8    
HELIX   15  15 ASP A  309  ARG A  323  1                                  15    
HELIX   16  16 PHE A  349  ARG A  361  1                                  13    
SHEET    1   A10 GLU A  44  ASP A  46  0                                        
SHEET    2   A10 HIS A  32  SER A  41 -1  N  SER A  41   O  GLU A  44           
SHEET    3   A10 LYS A  70  GLY A  76  1  O  LEU A  72   N  TYR A  35           
SHEET    4   A10 GLY A 113  ALA A 117  1  O  ASP A 115   N  LEU A  73           
SHEET    5   A10 LEU A 152  VAL A 157  1  O  LEU A 152   N  LEU A 114           
SHEET    6   A10 PHE A 179  LEU A 182  1  O  SER A 181   N  VAL A 157           
SHEET    7   A10 LEU A 233  PRO A 238  1  O  VAL A 234   N  LEU A 182           
SHEET    8   A10 GLY A 327  TRP A 331  1  O  MET A 329   N  ILE A 237           
SHEET    9   A10 LYS A   2  THR A   8  1  N  ILE A   4   O  VAL A 330           
SHEET   10   A10 HIS A  32  SER A  41  1  O  SER A  36   N  TYR A   7           
SHEET    1   B 3 ILE A 257  PRO A 260  0                                        
SHEET    2   B 3 PHE A 240  LEU A 246 -1  N  THR A 245   O  GLY A 259           
SHEET    3   B 3 ILE A 272  ALA A 274 -1  O  LEU A 273   N  GLY A 241           
SHEET    1   C 5 ILE A 257  PRO A 260  0                                        
SHEET    2   C 5 PHE A 240  LEU A 246 -1  N  THR A 245   O  GLY A 259           
SHEET    3   C 5 GLN A 303  ALA A 306 -1  O  ALA A 306   N  ARG A 242           
SHEET    4   C 5 VAL A 295  LYS A 300 -1  N  ALA A 298   O  VAL A 305           
SHEET    5   C 5 THR A 286  PHE A 290 -1  N  HIS A 288   O  TYR A 297           
SSBOND   1 CYS A    5    CYS A   30                          1555   1555  2.01  
SSBOND   2 CYS A  279    CYS A  343                          1555   1555  2.04  
LINK         ND2 ASN A  39                 C1  NAG B   1     1555   1555  1.45  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  2.00  
LINK         O4  NAG B   2                 C1  MAN B   3     1555   1555  1.47  
CRYST1   63.111   66.036  107.626  90.00  90.00  90.00 P 21 21 21    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      0.015845  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015143  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009291        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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