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LongText Report for: 1XFD-pdb

Name Class
1XFD-pdb
HEADER    MEMBRANE PROTEIN                        14-SEP-04   1XFD              
TITLE     STRUCTURE OF A HUMAN A-TYPE POTASSIUM CHANNEL ACCELERATING            
TITLE    2 FACTOR DPPX, A MEMBER OF THE DIPEPTIDYL AMINOPEPTIDASE               
TITLE    3 FAMILY                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL AMINOPEPTIDASE-LIKE PROTEIN 6;                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND   5 SYNONYM: DIPEPTIDYLPEPTIDASE VI; DIPEPTIDYLPEPTIDASE 6;              
COMPND   6 DIPEPTIDYL PEPTIDASE IV LIKE PROTEIN;  DIPEPTIDYL                    
COMPND   7 AMINOPEPTIDASE-RELATED PROTEIN; DPPX; DIPEPTIDYLPEPTIDASE            
COMPND   8 VI;  DIPEPTIDYL AMINOPEPTIDASE IV-RELATED PROTEIN;                   
COMPND   9 DIPEPTIDYLPEPTIDASE VI ISOFORM 2;                                    
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: DPPX;                                                          
SOURCE   5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   7 OTHER_DETAILS: INSECT EXPRESSION SYSTEM                              
KEYWDS    DPPX; DPP6; KV4; KV; KAF                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.STROP,A.J.BANKOVICH,K.C.HANSEN,C.K.GARCIA,A.T.BRUNGER               
REVDAT   1   26-OCT-04 1XFD    0                                                
JRNL        AUTH   P.STROP,A.J.BANKOVICH,K.C.HANSEN,C.K.GARCIA,                 
JRNL        AUTH 2 A.T.BRUNGER                                                  
JRNL        TITL   STRUCTURE OF A HUMAN A-TYPE POTASSIUM CHANNEL                
JRNL        TITL 2 INTERACTING PROTEIN DPPX, A MEMBER OF THE                    
JRNL        TITL 3 DIPEPTIDYL AMINOPEPTIDASE FAMILY                             
JRNL        REF    J.MOL.BIOL.                                2004              
JRNL        REFN   ASTM JMOBAK  UK ESSN 1089-8638                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 3.00 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2096050.210                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 65968                          
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 SET) : 0.248                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3338                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.19                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 64.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7319                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3600                       
REMARK   3   BIN FREE R VALUE                    : 0.4040                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 413                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 23348                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 825                                     
REMARK   3   SOLVENT ATOMS            : 51                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 62.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 75.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.51000                                             
REMARK   3    B22 (A**2) : -27.24000                                            
REMARK   3    B33 (A**2) : 14.73000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.24000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.44                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.63                            
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) : 0.66                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.87                            
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) : 2.000 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.510 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.550 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.140 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 40.10                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1XFD COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PRAGUE ON 30-SEP-2004.              
REMARK 100 THE RCSB ID CODE IS RCSB030298.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JAN-2004                        
REMARK 200  TEMPERATURE           (KELVIN) : 113.0                              
REMARK 200  PH                             : 6.25                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0781                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76240                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.6                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   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: HOMOLOGY MODEL BASED ON PDB ENTRY 1N1M               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, NACL, PEG MME 2000, MAGNESIUM       
REMARK 280  CHLORIDE, PH 6.25, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  295K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,1/2+Y,-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       85.11500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 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 350 BIOMOLECULE: 2                                                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
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   OG   SER C   473     OD1  ASN D   362     2546     2.13            
REMARK 500   OG   SER A   473     OD1  ASN B   362     2655     2.17            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)                  
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLN A 161   CD    GLN A 161   OE1    0.096                        
REMARK 500    GLN A 161   CD    GLN A 161   NE2   -0.098                        
REMARK 500    ASN A 206   CG    ASN A 206   OD1    0.103                        
REMARK 500    ASN A 206   CG    ASN A 206   ND2   -0.096                        
REMARK 500    GLN A 212   CD    GLN A 212   OE1    0.102                        
REMARK 500    GLN A 212   CD    GLN A 212   NE2   -0.097                        
REMARK 500    ASN A 260   CG    ASN A 260   OD1    0.094                        
REMARK 500    ASN A 260   CG    ASN A 260   ND2   -0.099                        
REMARK 500    ASN A 351   CG    ASN A 351   OD1    0.095                        
REMARK 500    ASN A 351   CG    ASN A 351   ND2   -0.101                        
REMARK 500    ASN A 362   CG    ASN A 362   OD1    0.097                        
REMARK 500    ASN A 362   CG    ASN A 362   ND2   -0.097                        
REMARK 500    ASN A 400   CG    ASN A 400   OD1    0.101                        
REMARK 500    ASN A 400   CG    ASN A 400   ND2   -0.096                        
REMARK 500    ASN A 476   CG    ASN A 476   OD1    0.097                        
REMARK 500    ASN A 476   CG    ASN A 476   ND2   -0.098                        
REMARK 500    GLN A 513   CD    GLN A 513   OE1    0.100                        
REMARK 500    GLN A 513   CD    GLN A 513   NE2   -0.100                        
REMARK 500    ASN A 518   CG    ASN A 518   OD1    0.096                        
REMARK 500    ASN A 518   CG    ASN A 518   ND2   -0.096                        
REMARK 500    GLN A 526   CD    GLN A 526   OE1    0.100                        
REMARK 500    GLN A 526   CD    GLN A 526   NE2   -0.096                        
REMARK 500    ASN A 579   CG    ASN A 579   OD1    0.098                        
REMARK 500    ASN A 579   CG    ASN A 579   ND2   -0.098                        
REMARK 500    ASN A 587   CG    ASN A 587   OD1    0.099                        
REMARK 500    ASN A 587   CG    ASN A 587   ND2   -0.096                        
REMARK 500    GLN A 668   CD    GLN A 668   OE1    0.097                        
REMARK 500    GLN A 668   CD    GLN A 668   NE2   -0.095                        
REMARK 500    GLN A 688   CD    GLN A 688   OE1    0.100                        
REMARK 500    GLN A 688   CD    GLN A 688   NE2   -0.098                        
REMARK 500    GLN A 731   CD    GLN A 731   OE1    0.099                        
REMARK 500    GLN A 731   CD    GLN A 731   NE2   -0.095                        
REMARK 500    GLN A 783   CD    GLN A 783   OE1    0.098                        
REMARK 500    GLN A 783   CD    GLN A 783   NE2   -0.096                        
REMARK 500    GLN A 798   CD    GLN A 798   OE1    0.097                        
REMARK 500    GLN A 798   CD    GLN A 798   NE2   -0.100                        
REMARK 500    GLN A 817   CD    GLN A 817   OE1    0.100                        
REMARK 500    GLN A 817   CD    GLN A 817   NE2   -0.097                        
REMARK 500    ILE A 840   CB    ILE A 840   CG2   -0.075                        
REMARK 500    GLN B 161   CD    GLN B 161   OE1    0.097                        
REMARK 500    GLN B 161   CD    GLN B 161   NE2   -0.099                        
REMARK 500    ASN B 260   CG    ASN B 260   OD1    0.099                        
REMARK 500    ASN B 260   CG    ASN B 260   ND2   -0.094                        
REMARK 500    ASN B 351   CG    ASN B 351   OD1    0.095                        
REMARK 500    ASN B 351   CG    ASN B 351   ND2   -0.100                        
REMARK 500    ASN B 362   CG    ASN B 362   OD1    0.089                        
REMARK 500    ASN B 362   CG    ASN B 362   ND2   -0.095                        
REMARK 500    ASN B 400   CG    ASN B 400   OD1    0.096                        
REMARK 500    ASN B 400   CG    ASN B 400   ND2   -0.103                        
REMARK 500    ASN B 476   CG    ASN B 476   OD1    0.097                        
REMARK 500    ASN B 476   CG    ASN B 476   ND2   -0.097                        
REMARK 500    GLN B 513   CD    GLN B 513   OE1    0.094                        
REMARK 500    GLN B 513   CD    GLN B 513   NE2   -0.100                        
REMARK 500    ASN B 518   CG    ASN B 518   OD1    0.096                        
REMARK 500    ASN B 518   CG    ASN B 518   ND2   -0.095                        
REMARK 500    GLN B 526   CD    GLN B 526   OE1    0.098                        
REMARK 500    GLN B 526   CD    GLN B 526   NE2   -0.099                        
REMARK 500    ASN B 579   CG    ASN B 579   OD1    0.099                        
REMARK 500    ASN B 579   CG    ASN B 579   ND2   -0.096                        
REMARK 500    ASN B 587   CG    ASN B 587   OD1    0.100                        
REMARK 500    ASN B 587   CG    ASN B 587   ND2   -0.096                        
REMARK 500    GLN B 668   CD    GLN B 668   OE1    0.095                        
REMARK 500    GLN B 668   CD    GLN B 668   NE2   -0.099                        
REMARK 500    GLN B 688   CD    GLN B 688   OE1    0.094                        
REMARK 500    GLN B 688   CD    GLN B 688   NE2   -0.099                        
REMARK 500    GLN B 699   CD    GLN B 699   OE1    0.099                        
REMARK 500    GLN B 699   CD    GLN B 699   NE2   -0.097                        
REMARK 500    GLN B 731   CD    GLN B 731   OE1    0.098                        
REMARK 500    GLN B 731   CD    GLN B 731   NE2   -0.096                        
REMARK 500    GLN B 783   CD    GLN B 783   OE1    0.101                        
REMARK 500    GLN B 783   CD    GLN B 783   NE2   -0.095                        
REMARK 500    GLN B 798   CD    GLN B 798   OE1    0.098                        
REMARK 500    GLN B 798   CD    GLN B 798   NE2   -0.100                        
REMARK 500    GLN B 817   CD    GLN B 817   OE1    0.094                        
REMARK 500    GLN B 817   CD    GLN B 817   NE2   -0.098                        
REMARK 500    ILE B 840   CB    ILE B 840   CG2   -0.073                        
REMARK 500    GLN C 161   CD    GLN C 161   OE1    0.097                        
REMARK 500    GLN C 161   CD    GLN C 161   NE2   -0.096                        
REMARK 500    ARG C 191   CG    ARG C 191   CD    -0.136                        
REMARK 500    ARG C 191   CD    ARG C 191   NE    -0.136                        
REMARK 500    ARG C 191   NE    ARG C 191   CZ    -0.107                        
REMARK 500    ARG C 191   CZ    ARG C 191   NH2   -0.113                        
REMARK 500    GLN C 212   CD    GLN C 212   OE1    0.100                        
REMARK 500    GLN C 212   CD    GLN C 212   NE2   -0.096                        
REMARK 500    ASN C 260   CG    ASN C 260   OD1    0.097                        
REMARK 500    ASN C 260   CG    ASN C 260   ND2   -0.096                        
REMARK 500    ASN C 362   CG    ASN C 362   OD1    0.097                        
REMARK 500    ASN C 362   CG    ASN C 362   ND2   -0.095                        
REMARK 500    ASN C 400   CG    ASN C 400   OD1    0.097                        
REMARK 500    ASN C 400   CG    ASN C 400   ND2   -0.098                        
REMARK 500    ASN C 476   CG    ASN C 476   OD1    0.096                        
REMARK 500    ASN C 476   CG    ASN C 476   ND2   -0.097                        
REMARK 500    GLN C 513   CD    GLN C 513   OE1    0.099                        
REMARK 500    GLN C 513   CD    GLN C 513   NE2   -0.096                        
REMARK 500    ASN C 518   CG    ASN C 518   OD1    0.098                        
REMARK 500    ASN C 518   CG    ASN C 518   ND2   -0.096                        
REMARK 500    GLN C 526   CD    GLN C 526   OE1    0.100                        
REMARK 500    GLN C 526   CD    GLN C 526   NE2   -0.098                        
REMARK 500    ASN C 579   CG    ASN C 579   OD1    0.095                        
REMARK 500    ASN C 579   CG    ASN C 579   ND2   -0.099                        
REMARK 500    ASN C 587   CG    ASN C 587   OD1    0.098                        
REMARK 500    ASN C 587   CG    ASN C 587   ND2   -0.096                        
REMARK 500    GLN C 668   CD    GLN C 668   OE1    0.098                        
REMARK 500    GLN C 668   CD    GLN C 668   NE2   -0.095                        
REMARK 500    GLN C 688   CD    GLN C 688   OE1    0.098                        
REMARK 500    GLN C 688   CD    GLN C 688   NE2   -0.101                        
REMARK 500    GLN C 731   CD    GLN C 731   OE1    0.098                        
REMARK 500    GLN C 731   CD    GLN C 731   NE2   -0.094                        
REMARK 500    GLN C 783   CD    GLN C 783   OE1    0.101                        
REMARK 500    GLN C 783   CD    GLN C 783   NE2   -0.094                        
REMARK 500    GLN C 798   CD    GLN C 798   OE1    0.097                        
REMARK 500    GLN C 798   CD    GLN C 798   NE2   -0.100                        
REMARK 500    GLN C 817   CD    GLN C 817   OE1    0.101                        
REMARK 500    GLN C 817   CD    GLN C 817   NE2   -0.099                        
REMARK 500    ILE C 840   CB    ILE C 840   CG1   -0.110                        
REMARK 500    ILE C 840   CB    ILE C 840   CG2   -0.267                        
REMARK 500    GLN D 161   CD    GLN D 161   OE1    0.096                        
REMARK 500    GLN D 161   CD    GLN D 161   NE2   -0.097                        
REMARK 500    GLN D 212   CD    GLN D 212   OE1    0.097                        
REMARK 500    GLN D 212   CD    GLN D 212   NE2   -0.095                        
REMARK 500    ASN D 260   CG    ASN D 260   OD1    0.100                        
REMARK 500    ASN D 260   CG    ASN D 260   ND2   -0.098                        
REMARK 500    ASN D 362   CG    ASN D 362   OD1    0.090                        
REMARK 500    ASN D 362   CG    ASN D 362   ND2   -0.096                        
REMARK 500    ASN D 400   CG    ASN D 400   OD1    0.096                        
REMARK 500    ASN D 400   CG    ASN D 400   ND2   -0.100                        
REMARK 500    ASN D 476   CG    ASN D 476   OD1    0.097                        
REMARK 500    ASN D 476   CG    ASN D 476   ND2   -0.098                        
REMARK 500    GLN D 513   CD    GLN D 513   OE1    0.096                        
REMARK 500    GLN D 513   CD    GLN D 513   NE2   -0.100                        
REMARK 500    ASN D 518   CG    ASN D 518   OD1    0.098                        
REMARK 500    ASN D 518   CG    ASN D 518   ND2   -0.095                        
REMARK 500    GLN D 526   CD    GLN D 526   OE1    0.100                        
REMARK 500    GLN D 526   CD    GLN D 526   NE2   -0.099                        
REMARK 500    ASN D 579   CG    ASN D 579   OD1    0.095                        
REMARK 500    ASN D 579   CG    ASN D 579   ND2   -0.098                        
REMARK 500    ASN D 587   CG    ASN D 587   OD1    0.098                        
REMARK 500    ASN D 587   CG    ASN D 587   ND2   -0.095                        
REMARK 500    GLN D 668   CD    GLN D 668   OE1    0.099                        
REMARK 500    GLN D 668   CD    GLN D 668   NE2   -0.097                        
REMARK 500    GLN D 688   CD    GLN D 688   OE1    0.095                        
REMARK 500    GLN D 688   CD    GLN D 688   NE2   -0.101                        
REMARK 500    GLN D 731   CD    GLN D 731   OE1    0.097                        
REMARK 500    GLN D 731   CD    GLN D 731   NE2   -0.096                        
REMARK 500    GLN D 783   CD    GLN D 783   OE1    0.099                        
REMARK 500    GLN D 783   CD    GLN D 783   NE2   -0.096                        
REMARK 500    GLN D 798   CD    GLN D 798   OE1    0.099                        
REMARK 500    GLN D 798   CD    GLN D 798   NE2   -0.098                        
REMARK 500    GLN D 817   CD    GLN D 817   OE1    0.097                        
REMARK 500    GLN D 817   CD    GLN D 817   NE2   -0.099                        
REMARK 500    ILE D 840   CB    ILE D 840   CG2   -0.066                        
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: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ILE A 224   N   -  CA  -  C   ANGL. DEV. = 10.1 DEGREES           
REMARK 500    PRO A 225   C   -  N   -  CA  ANGL. DEV. =-11.7 DEGREES           
REMARK 500    ASP A 228   N   -  CA  -  C   ANGL. DEV. =  9.3 DEGREES           
REMARK 500    ASP A 290   N   -  CA  -  C   ANGL. DEV. =-12.1 DEGREES           
REMARK 500    GLU A 296   N   -  CA  -  C   ANGL. DEV. =  9.3 DEGREES           
REMARK 500    ILE A 383   N   -  CA  -  C   ANGL. DEV. = -9.9 DEGREES           
REMARK 500    SER A 472   N   -  CA  -  C   ANGL. DEV. = 11.7 DEGREES           
REMARK 500    VAL A 487   N   -  CA  -  C   ANGL. DEV. =-12.6 DEGREES           
REMARK 500    GLY A 521   N   -  CA  -  C   ANGL. DEV. = 12.5 DEGREES           
REMARK 500    LEU A 532   N   -  CA  -  C   ANGL. DEV. =-13.3 DEGREES           
REMARK 500    TYR A 538   N   -  CA  -  C   ANGL. DEV. = -9.7 DEGREES           
REMARK 500    SER A 540   N   -  CA  -  C   ANGL. DEV. = -9.4 DEGREES           
REMARK 500    PRO A 613   N   -  CA  -  C   ANGL. DEV. = 10.0 DEGREES           
REMARK 500    ILE A 742   N   -  CA  -  C   ANGL. DEV. =-11.3 DEGREES           
REMARK 500    ALA A 766   N   -  CA  -  C   ANGL. DEV. =-12.2 DEGREES           
REMARK 500    THR A 790   N   -  CA  -  C   ANGL. DEV. =  9.8 DEGREES           
REMARK 500    GLN A 817   N   -  CA  -  C   ANGL. DEV. = -9.3 DEGREES           
REMARK 500    TYR A 825   N   -  CA  -  C   ANGL. DEV. = 15.9 DEGREES           
REMARK 500    VAL B 207   N   -  CA  -  C   ANGL. DEV. = -9.6 DEGREES           
REMARK 500    GLU B 208   N   -  CA  -  C   ANGL. DEV. = -9.4 DEGREES           
REMARK 500    ILE B 210   N   -  CA  -  C   ANGL. DEV. = -9.7 DEGREES           
REMARK 500    GLN B 212   N   -  CA  -  C   ANGL. DEV. =-18.3 DEGREES           
REMARK 500    HIS B 213   CB  -  CG  -  CD2 ANGL. DEV. = -9.4 DEGREES           
REMARK 500    HIS B 213   CB  -  CG  -  ND1 ANGL. DEV. =  9.3 DEGREES           
REMARK 500    ILE B 224   N   -  CA  -  C   ANGL. DEV. = 10.0 DEGREES           
REMARK 500    PRO B 225   C   -  N   -  CA  ANGL. DEV. =-11.5 DEGREES           
REMARK 500    ASP B 290   N   -  CA  -  C   ANGL. DEV. =-12.0 DEGREES           
REMARK 500    GLU B 296   N   -  CA  -  C   ANGL. DEV. =  9.4 DEGREES           
REMARK 500    ILE B 383   N   -  CA  -  C   ANGL. DEV. = -9.6 DEGREES           
REMARK 500    SER B 472   N   -  CA  -  C   ANGL. DEV. = 11.6 DEGREES           
REMARK 500    ASN B 476   N   -  CA  -  C   ANGL. DEV. = -9.2 DEGREES           
REMARK 500    VAL B 487   N   -  CA  -  C   ANGL. DEV. =-12.4 DEGREES           
REMARK 500    GLY B 521   N   -  CA  -  C   ANGL. DEV. = 12.6 DEGREES           
REMARK 500    LEU B 532   N   -  CA  -  C   ANGL. DEV. =-13.4 DEGREES           
REMARK 500    TYR B 538   N   -  CA  -  C   ANGL. DEV. = -9.6 DEGREES           
REMARK 500    SER B 540   N   -  CA  -  C   ANGL. DEV. = -9.3 DEGREES           
REMARK 500    PRO B 613   N   -  CA  -  C   ANGL. DEV. =  9.8 DEGREES           
REMARK 500    ILE B 742   N   -  CA  -  C   ANGL. DEV. =-10.8 DEGREES           
REMARK 500    ALA B 766   N   -  CA  -  C   ANGL. DEV. =-12.2 DEGREES           
REMARK 500    THR B 790   N   -  CA  -  C   ANGL. DEV. = 10.0 DEGREES           
REMARK 500    TYR B 825   N   -  CA  -  C   ANGL. DEV. = 15.9 DEGREES           
REMARK 500    ARG C 191   CG  -  CD  -  NE  ANGL. DEV. =-11.3 DEGREES           
REMARK 500    ARG C 191   CD  -  NE  -  CZ  ANGL. DEV. =-11.2 DEGREES           
REMARK 500    SER C 214   N   -  CA  -  C   ANGL. DEV. =  9.1 DEGREES           
REMARK 500    ILE C 224   N   -  CA  -  C   ANGL. DEV. = 10.3 DEGREES           
REMARK 500    PRO C 225   C   -  N   -  CA  ANGL. DEV. =-11.5 DEGREES           
REMARK 500    ASP C 228   N   -  CA  -  C   ANGL. DEV. =  9.3 DEGREES           
REMARK 500    GLY C 246   N   -  CA  -  C   ANGL. DEV. =  9.4 DEGREES           
REMARK 500    ASP C 290   N   -  CA  -  C   ANGL. DEV. =-12.1 DEGREES           
REMARK 500    GLU C 296   N   -  CA  -  C   ANGL. DEV. =  9.4 DEGREES           
REMARK 500    ILE C 383   N   -  CA  -  C   ANGL. DEV. = -9.8 DEGREES           
REMARK 500    SER C 472   N   -  CA  -  C   ANGL. DEV. = 11.9 DEGREES           
REMARK 500    ASN C 476   N   -  CA  -  C   ANGL. DEV. = -9.1 DEGREES           
REMARK 500    VAL C 487   N   -  CA  -  C   ANGL. DEV. =-12.5 DEGREES           
REMARK 500    GLY C 521   N   -  CA  -  C   ANGL. DEV. = 12.5 DEGREES           
REMARK 500    LEU C 532   N   -  CA  -  C   ANGL. DEV. =-13.2 DEGREES           
REMARK 500    TYR C 538   N   -  CA  -  C   ANGL. DEV. = -9.6 DEGREES           
REMARK 500    SER C 540   N   -  CA  -  C   ANGL. DEV. = -9.6 DEGREES           
REMARK 500    LEU C 552   CA  -  CB  -  CG  ANGL. DEV. =  9.3 DEGREES           
REMARK 500    PRO C 613   N   -  CA  -  C   ANGL. DEV. = 10.0 DEGREES           
REMARK 500    ILE C 742   N   -  CA  -  C   ANGL. DEV. =-11.0 DEGREES           
REMARK 500    ALA C 766   N   -  CA  -  C   ANGL. DEV. =-12.1 DEGREES           
REMARK 500    THR C 790   N   -  CA  -  C   ANGL. DEV. =  9.9 DEGREES           
REMARK 500    TYR C 825   N   -  CA  -  C   ANGL. DEV. = 15.9 DEGREES           
REMARK 500    ILE C 840   CG1 -  CB  -  CG2 ANGL. DEV. =-19.3 DEGREES           
REMARK 500    SER D 214   N   -  CA  -  C   ANGL. DEV. =  9.1 DEGREES           
REMARK 500    ILE D 224   N   -  CA  -  C   ANGL. DEV. = 10.1 DEGREES           
REMARK 500    PRO D 225   C   -  N   -  CA  ANGL. DEV. =-11.6 DEGREES           
REMARK 500    ASP D 228   N   -  CA  -  C   ANGL. DEV. =  9.2 DEGREES           
REMARK 500    ASP D 290   N   -  CA  -  C   ANGL. DEV. =-11.9 DEGREES           
REMARK 500    GLU D 296   N   -  CA  -  C   ANGL. DEV. =  9.3 DEGREES           
REMARK 500    ILE D 383   N   -  CA  -  C   ANGL. DEV. =-10.2 DEGREES           
REMARK 500    SER D 472   N   -  CA  -  C   ANGL. DEV. = 11.5 DEGREES           
REMARK 500    ASN D 476   N   -  CA  -  C   ANGL. DEV. = -9.1 DEGREES           
REMARK 500    VAL D 487   N   -  CA  -  C   ANGL. DEV. =-12.7 DEGREES           
REMARK 500    GLY D 521   N   -  CA  -  C   ANGL. DEV. = 12.4 DEGREES           
REMARK 500    LEU D 532   N   -  CA  -  C   ANGL. DEV. =-13.5 DEGREES           
REMARK 500    TYR D 538   N   -  CA  -  C   ANGL. DEV. = -9.7 DEGREES           
REMARK 500    SER D 540   N   -  CA  -  C   ANGL. DEV. = -9.3 DEGREES           
REMARK 500    PRO D 613   N   -  CA  -  C   ANGL. DEV. = 10.1 DEGREES           
REMARK 500    ILE D 742   N   -  CA  -  C   ANGL. DEV. =-11.3 DEGREES           
REMARK 500    ALA D 766   N   -  CA  -  C   ANGL. DEV. =-12.1 DEGREES           
REMARK 500    THR D 790   N   -  CA  -  C   ANGL. DEV. =  9.7 DEGREES           
REMARK 500    TYR D 825   N   -  CA  -  C   ANGL. DEV. = 16.0 DEGREES           
DBREF  1XFD A  127   849  GB     18765698 NP_570629      127    849             
DBREF  1XFD B  127   849  GB     18765698 NP_570629      127    849             
DBREF  1XFD C  127   849  GB     18765698 NP_570629      127    849             
DBREF  1XFD D  127   849  GB     18765698 NP_570629      127    849             
SEQRES   1 A  723  GLN LYS LYS LYS VAL THR VAL GLU ASP LEU PHE SER GLU          
SEQRES   2 A  723  ASP PHE LYS ILE HIS ASP PRO GLU ALA LYS TRP ILE SER          
SEQRES   3 A  723  ASP THR GLU PHE ILE TYR ARG GLU GLN LYS GLY THR VAL          
SEQRES   4 A  723  ARG LEU TRP ASN VAL GLU THR ASN THR SER THR VAL LEU          
SEQRES   5 A  723  ILE GLU GLY LYS LYS ILE GLU SER LEU ARG ALA ILE ARG          
SEQRES   6 A  723  TYR GLU ILE SER PRO ASP ARG GLU TYR ALA LEU PHE SER          
SEQRES   7 A  723  TYR ASN VAL GLU PRO ILE TYR GLN HIS SER TYR THR GLY          
SEQRES   8 A  723  TYR TYR VAL LEU SER LYS ILE PRO HIS GLY ASP PRO GLN          
SEQRES   9 A  723  SER LEU ASP PRO PRO GLU VAL SER ASN ALA LYS LEU GLN          
SEQRES  10 A  723  TYR ALA GLY TRP GLY PRO LYS GLY GLN GLN LEU ILE PHE          
SEQRES  11 A  723  ILE PHE GLU ASN ASN ILE TYR TYR CYS ALA HIS VAL GLY          
SEQRES  12 A  723  LYS GLN ALA ILE ARG VAL VAL SER THR GLY LYS GLU GLY          
SEQRES  13 A  723  VAL ILE TYR ASN GLY LEU SER ASP TRP LEU TYR GLU GLU          
SEQRES  14 A  723  GLU ILE LEU LYS THR HIS ILE ALA HIS TRP TRP SER PRO          
SEQRES  15 A  723  ASP GLY THR ARG LEU ALA TYR ALA ALA ILE ASN ASP SER          
SEQRES  16 A  723  ARG VAL PRO ILE MET GLU LEU PRO THR TYR THR GLY SER          
SEQRES  17 A  723  ILE TYR PRO THR VAL LYS PRO TYR HIS TYR PRO LYS ALA          
SEQRES  18 A  723  GLY SER GLU ASN PRO SER ILE SER LEU HIS VAL ILE GLY          
SEQRES  19 A  723  LEU ASN GLY PRO THR HIS ASP LEU GLU MET MET PRO PRO          
SEQRES  20 A  723  ASP ASP PRO ARG MET ARG GLU TYR TYR ILE THR MET VAL          
SEQRES  21 A  723  LYS TRP ALA THR SER THR LYS VAL ALA VAL THR TRP LEU          
SEQRES  22 A  723  ASN ARG ALA GLN ASN VAL SER ILE LEU THR LEU CYS ASP          
SEQRES  23 A  723  ALA THR THR GLY VAL CYS THR LYS LYS HIS GLU ASP GLU          
SEQRES  24 A  723  SER GLU ALA TRP LEU HIS ARG GLN ASN GLU GLU PRO VAL          
SEQRES  25 A  723  PHE SER LYS ASP GLY ARG LYS PHE PHE PHE ILE ARG ALA          
SEQRES  26 A  723  ILE PRO GLN GLY GLY ARG GLY LYS PHE TYR HIS ILE THR          
SEQRES  27 A  723  VAL SER SER SER GLN PRO ASN SER SER ASN ASP ASN ILE          
SEQRES  28 A  723  GLN SER ILE THR SER GLY ASP TRP ASP VAL THR LYS ILE          
SEQRES  29 A  723  LEU ALA TYR ASP GLU LYS GLY ASN LYS ILE TYR PHE LEU          
SEQRES  30 A  723  SER THR GLU ASP LEU PRO ARG ARG ARG GLN LEU TYR SER          
SEQRES  31 A  723  ALA ASN THR VAL GLY ASN PHE ASN ARG GLN CYS LEU SER          
SEQRES  32 A  723  CYS ASP LEU VAL GLU ASN CYS THR TYR PHE SER ALA SER          
SEQRES  33 A  723  PHE SER HIS SER MET ASP PHE PHE LEU LEU LYS CYS GLU          
SEQRES  34 A  723  GLY PRO GLY VAL PRO MET VAL THR VAL HIS ASN THR THR          
SEQRES  35 A  723  ASP LYS LYS LYS MET PHE ASP LEU GLU THR ASN GLU HIS          
SEQRES  36 A  723  VAL LYS LYS ALA ILE ASN ASP ARG GLN MET PRO LYS VAL          
SEQRES  37 A  723  GLU TYR ARG ASP ILE GLU ILE ASP ASP TYR ASN LEU PRO          
SEQRES  38 A  723  MET GLN ILE LEU LYS PRO ALA THR PHE THR ASP THR THR          
SEQRES  39 A  723  HIS TYR PRO LEU LEU LEU VAL VAL ASP GLY THR PRO GLY          
SEQRES  40 A  723  SER GLN SER VAL ALA GLU LYS PHE GLU VAL SER TRP GLU          
SEQRES  41 A  723  THR VAL MET VAL SER SER HIS GLY ALA VAL VAL VAL LYS          
SEQRES  42 A  723  CYS ASP GLY ARG GLY SER GLY PHE GLN GLY THR LYS LEU          
SEQRES  43 A  723  LEU HIS GLU VAL ARG ARG ARG LEU GLY LEU LEU GLU GLU          
SEQRES  44 A  723  LYS ASP GLN MET GLU ALA VAL ARG THR MET LEU LYS GLU          
SEQRES  45 A  723  GLN TYR ILE ASP ARG THR ARG VAL ALA VAL PHE GLY LYS          
SEQRES  46 A  723  ASP TYR GLY GLY TYR LEU SER THR TYR ILE LEU PRO ALA          
SEQRES  47 A  723  LYS GLY GLU ASN GLN GLY GLN THR PHE THR CYS GLY SER          
SEQRES  48 A  723  ALA LEU SER PRO ILE THR ASP PHE LYS LEU TYR ALA SER          
SEQRES  49 A  723  ALA PHE SER GLU ARG TYR LEU GLY LEU HIS GLY LEU ASP          
SEQRES  50 A  723  ASN ARG ALA TYR GLU MET THR LYS VAL ALA HIS ARG VAL          
SEQRES  51 A  723  SER ALA LEU GLU GLU GLN GLN PHE LEU ILE ILE HIS PRO          
SEQRES  52 A  723  THR ALA ASP GLU LYS ILE HIS PHE GLN HIS THR ALA GLU          
SEQRES  53 A  723  LEU ILE THR GLN LEU ILE ARG GLY LYS ALA ASN TYR SER          
SEQRES  54 A  723  LEU GLN ILE TYR PRO ASP GLU SER HIS TYR PHE THR SER          
SEQRES  55 A  723  SER SER LEU LYS GLN HIS LEU TYR ARG SER ILE ILE ASN          
SEQRES  56 A  723  PHE PHE VAL GLU CYS PHE ARG ILE                              
SEQRES   1 B  723  GLN LYS LYS LYS VAL THR VAL GLU ASP LEU PHE SER GLU          
SEQRES   2 B  723  ASP PHE LYS ILE HIS ASP PRO GLU ALA LYS TRP ILE SER          
SEQRES   3 B  723  ASP THR GLU PHE ILE TYR ARG GLU GLN LYS GLY THR VAL          
SEQRES   4 B  723  ARG LEU TRP ASN VAL GLU THR ASN THR SER THR VAL LEU          
SEQRES   5 B  723  ILE GLU GLY LYS LYS ILE GLU SER LEU ARG ALA ILE ARG          
SEQRES   6 B  723  TYR GLU ILE SER PRO ASP ARG GLU TYR ALA LEU PHE SER          
SEQRES   7 B  723  TYR ASN VAL GLU PRO ILE TYR GLN HIS SER TYR THR GLY          
SEQRES   8 B  723  TYR TYR VAL LEU SER LYS ILE PRO HIS GLY ASP PRO GLN          
SEQRES   9 B  723  SER LEU ASP PRO PRO GLU VAL SER ASN ALA LYS LEU GLN          
SEQRES  10 B  723  TYR ALA GLY TRP GLY PRO LYS GLY GLN GLN LEU ILE PHE          
SEQRES  11 B  723  ILE PHE GLU ASN ASN ILE TYR TYR CYS ALA HIS VAL GLY          
SEQRES  12 B  723  LYS GLN ALA ILE ARG VAL VAL SER THR GLY LYS GLU GLY          
SEQRES  13 B  723  VAL ILE TYR ASN GLY LEU SER ASP TRP LEU TYR GLU GLU          
SEQRES  14 B  723  GLU ILE LEU LYS THR HIS ILE ALA HIS TRP TRP SER PRO          
SEQRES  15 B  723  ASP GLY THR ARG LEU ALA TYR ALA ALA ILE ASN ASP SER          
SEQRES  16 B  723  ARG VAL PRO ILE MET GLU LEU PRO THR TYR THR GLY SER          
SEQRES  17 B  723  ILE TYR PRO THR VAL LYS PRO TYR HIS TYR PRO LYS ALA          
SEQRES  18 B  723  GLY SER GLU ASN PRO SER ILE SER LEU HIS VAL ILE GLY          
SEQRES  19 B  723  LEU ASN GLY PRO THR HIS ASP LEU GLU MET MET PRO PRO          
SEQRES  20 B  723  ASP ASP PRO ARG MET ARG GLU TYR TYR ILE THR MET VAL          
SEQRES  21 B  723  LYS TRP ALA THR SER THR LYS VAL ALA VAL THR TRP LEU          
SEQRES  22 B  723  ASN ARG ALA GLN ASN VAL SER ILE LEU THR LEU CYS ASP          
SEQRES  23 B  723  ALA THR THR GLY VAL CYS THR LYS LYS HIS GLU ASP GLU          
SEQRES  24 B  723  SER GLU ALA TRP LEU HIS ARG GLN ASN GLU GLU PRO VAL          
SEQRES  25 B  723  PHE SER LYS ASP GLY ARG LYS PHE PHE PHE ILE ARG ALA          
SEQRES  26 B  723  ILE PRO GLN GLY GLY ARG GLY LYS PHE TYR HIS ILE THR          
SEQRES  27 B  723  VAL SER SER SER GLN PRO ASN SER SER ASN ASP ASN ILE          
SEQRES  28 B  723  GLN SER ILE THR SER GLY ASP TRP ASP VAL THR LYS ILE          
SEQRES  29 B  723  LEU ALA TYR ASP GLU LYS GLY ASN LYS ILE TYR PHE LEU          
SEQRES  30 B  723  SER THR GLU ASP LEU PRO ARG ARG ARG GLN LEU TYR SER          
SEQRES  31 B  723  ALA ASN THR VAL GLY ASN PHE ASN ARG GLN CYS LEU SER          
SEQRES  32 B  723  CYS ASP LEU VAL GLU ASN CYS THR TYR PHE SER ALA SER          
SEQRES  33 B  723  PHE SER HIS SER MET ASP PHE PHE LEU LEU LYS CYS GLU          
SEQRES  34 B  723  GLY PRO GLY VAL PRO MET VAL THR VAL HIS ASN THR THR          
SEQRES  35 B  723  ASP LYS LYS LYS MET PHE ASP LEU GLU THR ASN GLU HIS          
SEQRES  36 B  723  VAL LYS LYS ALA ILE ASN ASP ARG GLN MET PRO LYS VAL          
SEQRES  37 B  723  GLU TYR ARG ASP ILE GLU ILE ASP ASP TYR ASN LEU PRO          
SEQRES  38 B  723  MET GLN ILE LEU LYS PRO ALA THR PHE THR ASP THR THR          
SEQRES  39 B  723  HIS TYR PRO LEU LEU LEU VAL VAL ASP GLY THR PRO GLY          
SEQRES  40 B  723  SER GLN SER VAL ALA GLU LYS PHE GLU VAL SER TRP GLU          
SEQRES  41 B  723  THR VAL MET VAL SER SER HIS GLY ALA VAL VAL VAL LYS          
SEQRES  42 B  723  CYS ASP GLY ARG GLY SER GLY PHE GLN GLY THR LYS LEU          
SEQRES  43 B  723  LEU HIS GLU VAL ARG ARG ARG LEU GLY LEU LEU GLU GLU          
SEQRES  44 B  723  LYS ASP GLN MET GLU ALA VAL ARG THR MET LEU LYS GLU          
SEQRES  45 B  723  GLN TYR ILE ASP ARG THR ARG VAL ALA VAL PHE GLY LYS          
SEQRES  46 B  723  ASP TYR GLY GLY TYR LEU SER THR TYR ILE LEU PRO ALA          
SEQRES  47 B  723  LYS GLY GLU ASN GLN GLY GLN THR PHE THR CYS GLY SER          
SEQRES  48 B  723  ALA LEU SER PRO ILE THR ASP PHE LYS LEU TYR ALA SER          
SEQRES  49 B  723  ALA PHE SER GLU ARG TYR LEU GLY LEU HIS GLY LEU ASP          
SEQRES  50 B  723  ASN ARG ALA TYR GLU MET THR LYS VAL ALA HIS ARG VAL          
SEQRES  51 B  723  SER ALA LEU GLU GLU GLN GLN PHE LEU ILE ILE HIS PRO          
SEQRES  52 B  723  THR ALA ASP GLU LYS ILE HIS PHE GLN HIS THR ALA GLU          
SEQRES  53 B  723  LEU ILE THR GLN LEU ILE ARG GLY LYS ALA ASN TYR SER          
SEQRES  54 B  723  LEU GLN ILE TYR PRO ASP GLU SER HIS TYR PHE THR SER          
SEQRES  55 B  723  SER SER LEU LYS GLN HIS LEU TYR ARG SER ILE ILE ASN          
SEQRES  56 B  723  PHE PHE VAL GLU CYS PHE ARG ILE                              
SEQRES   1 C  723  GLN LYS LYS LYS VAL THR VAL GLU ASP LEU PHE SER GLU          
SEQRES   2 C  723  ASP PHE LYS ILE HIS ASP PRO GLU ALA LYS TRP ILE SER          
SEQRES   3 C  723  ASP THR GLU PHE ILE TYR ARG GLU GLN LYS GLY THR VAL          
SEQRES   4 C  723  ARG LEU TRP ASN VAL GLU THR ASN THR SER THR VAL LEU          
SEQRES   5 C  723  ILE GLU GLY LYS LYS ILE GLU SER LEU ARG ALA ILE ARG          
SEQRES   6 C  723  TYR GLU ILE SER PRO ASP ARG GLU TYR ALA LEU PHE SER          
SEQRES   7 C  723  TYR ASN VAL GLU PRO ILE TYR GLN HIS SER TYR THR GLY          
SEQRES   8 C  723  TYR TYR VAL LEU SER LYS ILE PRO HIS GLY ASP PRO GLN          
SEQRES   9 C  723  SER LEU ASP PRO PRO GLU VAL SER ASN ALA LYS LEU GLN          
SEQRES  10 C  723  TYR ALA GLY TRP GLY PRO LYS GLY GLN GLN LEU ILE PHE          
SEQRES  11 C  723  ILE PHE GLU ASN ASN ILE TYR TYR CYS ALA HIS VAL GLY          
SEQRES  12 C  723  LYS GLN ALA ILE ARG VAL VAL SER THR GLY LYS GLU GLY          
SEQRES  13 C  723  VAL ILE TYR ASN GLY LEU SER ASP TRP LEU TYR GLU GLU          
SEQRES  14 C  723  GLU ILE LEU LYS THR HIS ILE ALA HIS TRP TRP SER PRO          
SEQRES  15 C  723  ASP GLY THR ARG LEU ALA TYR ALA ALA ILE ASN ASP SER          
SEQRES  16 C  723  ARG VAL PRO ILE MET GLU LEU PRO THR TYR THR GLY SER          
SEQRES  17 C  723  ILE TYR PRO THR VAL LYS PRO TYR HIS TYR PRO LYS ALA          
SEQRES  18 C  723  GLY SER GLU ASN PRO SER ILE SER LEU HIS VAL ILE GLY          
SEQRES  19 C  723  LEU ASN GLY PRO THR HIS ASP LEU GLU MET MET PRO PRO          
SEQRES  20 C  723  ASP ASP PRO ARG MET ARG GLU TYR TYR ILE THR MET VAL          
SEQRES  21 C  723  LYS TRP ALA THR SER THR LYS VAL ALA VAL THR TRP LEU          
SEQRES  22 C  723  ASN ARG ALA GLN ASN VAL SER ILE LEU THR LEU CYS ASP          
SEQRES  23 C  723  ALA THR THR GLY VAL CYS THR LYS LYS HIS GLU ASP GLU          
SEQRES  24 C  723  SER GLU ALA TRP LEU HIS ARG GLN ASN GLU GLU PRO VAL          
SEQRES  25 C  723  PHE SER LYS ASP GLY ARG LYS PHE PHE PHE ILE ARG ALA          
SEQRES  26 C  723  ILE PRO GLN GLY GLY ARG GLY LYS PHE TYR HIS ILE THR          
SEQRES  27 C  723  VAL SER SER SER GLN PRO ASN SER SER ASN ASP ASN ILE          
SEQRES  28 C  723  GLN SER ILE THR SER GLY ASP TRP ASP VAL THR LYS ILE          
SEQRES  29 C  723  LEU ALA TYR ASP GLU LYS GLY ASN LYS ILE TYR PHE LEU          
SEQRES  30 C  723  SER THR GLU ASP LEU PRO ARG ARG ARG GLN LEU TYR SER          
SEQRES  31 C  723  ALA ASN THR VAL GLY ASN PHE ASN ARG GLN CYS LEU SER          
SEQRES  32 C  723  CYS ASP LEU VAL GLU ASN CYS THR TYR PHE SER ALA SER          
SEQRES  33 C  723  PHE SER HIS SER MET ASP PHE PHE LEU LEU LYS CYS GLU          
SEQRES  34 C  723  GLY PRO GLY VAL PRO MET VAL THR VAL HIS ASN THR THR          
SEQRES  35 C  723  ASP LYS LYS LYS MET PHE ASP LEU GLU THR ASN GLU HIS          
SEQRES  36 C  723  VAL LYS LYS ALA ILE ASN ASP ARG GLN MET PRO LYS VAL          
SEQRES  37 C  723  GLU TYR ARG ASP ILE GLU ILE ASP ASP TYR ASN LEU PRO          
SEQRES  38 C  723  MET GLN ILE LEU LYS PRO ALA THR PHE THR ASP THR THR          
SEQRES  39 C  723  HIS TYR PRO LEU LEU LEU VAL VAL ASP GLY THR PRO GLY          
SEQRES  40 C  723  SER GLN SER VAL ALA GLU LYS PHE GLU VAL SER TRP GLU          
SEQRES  41 C  723  THR VAL MET VAL SER SER HIS GLY ALA VAL VAL VAL LYS          
SEQRES  42 C  723  CYS ASP GLY ARG GLY SER GLY PHE GLN GLY THR LYS LEU          
SEQRES  43 C  723  LEU HIS GLU VAL ARG ARG ARG LEU GLY LEU LEU GLU GLU          
SEQRES  44 C  723  LYS ASP GLN MET GLU ALA VAL ARG THR MET LEU LYS GLU          
SEQRES  45 C  723  GLN TYR ILE ASP ARG THR ARG VAL ALA VAL PHE GLY LYS          
SEQRES  46 C  723  ASP TYR GLY GLY TYR LEU SER THR TYR ILE LEU PRO ALA          
SEQRES  47 C  723  LYS GLY GLU ASN GLN GLY GLN THR PHE THR CYS GLY SER          
SEQRES  48 C  723  ALA LEU SER PRO ILE THR ASP PHE LYS LEU TYR ALA SER          
SEQRES  49 C  723  ALA PHE SER GLU ARG TYR LEU GLY LEU HIS GLY LEU ASP          
SEQRES  50 C  723  ASN ARG ALA TYR GLU MET THR LYS VAL ALA HIS ARG VAL          
SEQRES  51 C  723  SER ALA LEU GLU GLU GLN GLN PHE LEU ILE ILE HIS PRO          
SEQRES  52 C  723  THR ALA ASP GLU LYS ILE HIS PHE GLN HIS THR ALA GLU          
SEQRES  53 C  723  LEU ILE THR GLN LEU ILE ARG GLY LYS ALA ASN TYR SER          
SEQRES  54 C  723  LEU GLN ILE TYR PRO ASP GLU SER HIS TYR PHE THR SER          
SEQRES  55 C  723  SER SER LEU LYS GLN HIS LEU TYR ARG SER ILE ILE ASN          
SEQRES  56 C  723  PHE PHE VAL GLU CYS PHE ARG ILE                              
SEQRES   1 D  723  GLN LYS LYS LYS VAL THR VAL GLU ASP LEU PHE SER GLU          
SEQRES   2 D  723  ASP PHE LYS ILE HIS ASP PRO GLU ALA LYS TRP ILE SER          
SEQRES   3 D  723  ASP THR GLU PHE ILE TYR ARG GLU GLN LYS GLY THR VAL          
SEQRES   4 D  723  ARG LEU TRP ASN VAL GLU THR ASN THR SER THR VAL LEU          
SEQRES   5 D  723  ILE GLU GLY LYS LYS ILE GLU SER LEU ARG ALA ILE ARG          
SEQRES   6 D  723  TYR GLU ILE SER PRO ASP ARG GLU TYR ALA LEU PHE SER          
SEQRES   7 D  723  TYR ASN VAL GLU PRO ILE TYR GLN HIS SER TYR THR GLY          
SEQRES   8 D  723  TYR TYR VAL LEU SER LYS ILE PRO HIS GLY ASP PRO GLN          
SEQRES   9 D  723  SER LEU ASP PRO PRO GLU VAL SER ASN ALA LYS LEU GLN          
SEQRES  10 D  723  TYR ALA GLY TRP GLY PRO LYS GLY GLN GLN LEU ILE PHE          
SEQRES  11 D  723  ILE PHE GLU ASN ASN ILE TYR TYR CYS ALA HIS VAL GLY          
SEQRES  12 D  723  LYS GLN ALA ILE ARG VAL VAL SER THR GLY LYS GLU GLY          
SEQRES  13 D  723  VAL ILE TYR ASN GLY LEU SER ASP TRP LEU TYR GLU GLU          
SEQRES  14 D  723  GLU ILE LEU LYS THR HIS ILE ALA HIS TRP TRP SER PRO          
SEQRES  15 D  723  ASP GLY THR ARG LEU ALA TYR ALA ALA ILE ASN ASP SER          
SEQRES  16 D  723  ARG VAL PRO ILE MET GLU LEU PRO THR TYR THR GLY SER          
SEQRES  17 D  723  ILE TYR PRO THR VAL LYS PRO TYR HIS TYR PRO LYS ALA          
SEQRES  18 D  723  GLY SER GLU ASN PRO SER ILE SER LEU HIS VAL ILE GLY          
SEQRES  19 D  723  LEU ASN GLY PRO THR HIS ASP LEU GLU MET MET PRO PRO          
SEQRES  20 D  723  ASP ASP PRO ARG MET ARG GLU TYR TYR ILE THR MET VAL          
SEQRES  21 D  723  LYS TRP ALA THR SER THR LYS VAL ALA VAL THR TRP LEU          
SEQRES  22 D  723  ASN ARG ALA GLN ASN VAL SER ILE LEU THR LEU CYS ASP          
SEQRES  23 D  723  ALA THR THR GLY VAL CYS THR LYS LYS HIS GLU ASP GLU          
SEQRES  24 D  723  SER GLU ALA TRP LEU HIS ARG GLN ASN GLU GLU PRO VAL          
SEQRES  25 D  723  PHE SER LYS ASP GLY ARG LYS PHE PHE PHE ILE ARG ALA          
SEQRES  26 D  723  ILE PRO GLN GLY GLY ARG GLY LYS PHE TYR HIS ILE THR          
SEQRES  27 D  723  VAL SER SER SER GLN PRO ASN SER SER ASN ASP ASN ILE          
SEQRES  28 D  723  GLN SER ILE THR SER GLY ASP TRP ASP VAL THR LYS ILE          
SEQRES  29 D  723  LEU ALA TYR ASP GLU LYS GLY ASN LYS ILE TYR PHE LEU          
SEQRES  30 D  723  SER THR GLU ASP LEU PRO ARG ARG ARG GLN LEU TYR SER          
SEQRES  31 D  723  ALA ASN THR VAL GLY ASN PHE ASN ARG GLN CYS LEU SER          
SEQRES  32 D  723  CYS ASP LEU VAL GLU ASN CYS THR TYR PHE SER ALA SER          
SEQRES  33 D  723  PHE SER HIS SER MET ASP PHE PHE LEU LEU LYS CYS GLU          
SEQRES  34 D  723  GLY PRO GLY VAL PRO MET VAL THR VAL HIS ASN THR THR          
SEQRES  35 D  723  ASP LYS LYS LYS MET PHE ASP LEU GLU THR ASN GLU HIS          
SEQRES  36 D  723  VAL LYS LYS ALA ILE ASN ASP ARG GLN MET PRO LYS VAL          
SEQRES  37 D  723  GLU TYR ARG ASP ILE GLU ILE ASP ASP TYR ASN LEU PRO          
SEQRES  38 D  723  MET GLN ILE LEU LYS PRO ALA THR PHE THR ASP THR THR          
SEQRES  39 D  723  HIS TYR PRO LEU LEU LEU VAL VAL ASP GLY THR PRO GLY          
SEQRES  40 D  723  SER GLN SER VAL ALA GLU LYS PHE GLU VAL SER TRP GLU          
SEQRES  41 D  723  THR VAL MET VAL SER SER HIS GLY ALA VAL VAL VAL LYS          
SEQRES  42 D  723  CYS ASP GLY ARG GLY SER GLY PHE GLN GLY THR LYS LEU          
SEQRES  43 D  723  LEU HIS GLU VAL ARG ARG ARG LEU GLY LEU LEU GLU GLU          
SEQRES  44 D  723  LYS ASP GLN MET GLU ALA VAL ARG THR MET LEU LYS GLU          
SEQRES  45 D  723  GLN TYR ILE ASP ARG THR ARG VAL ALA VAL PHE GLY LYS          
SEQRES  46 D  723  ASP TYR GLY GLY TYR LEU SER THR TYR ILE LEU PRO ALA          
SEQRES  47 D  723  LYS GLY GLU ASN GLN GLY GLN THR PHE THR CYS GLY SER          
SEQRES  48 D  723  ALA LEU SER PRO ILE THR ASP PHE LYS LEU TYR ALA SER          
SEQRES  49 D  723  ALA PHE SER GLU ARG TYR LEU GLY LEU HIS GLY LEU ASP          
SEQRES  50 D  723  ASN ARG ALA TYR GLU MET THR LYS VAL ALA HIS ARG VAL          
SEQRES  51 D  723  SER ALA LEU GLU GLU GLN GLN PHE LEU ILE ILE HIS PRO          
SEQRES  52 D  723  THR ALA ASP GLU LYS ILE HIS PHE GLN HIS THR ALA GLU          
SEQRES  53 D  723  LEU ILE THR GLN LEU ILE ARG GLY LYS ALA ASN TYR SER          
SEQRES  54 D  723  LEU GLN ILE TYR PRO ASP GLU SER HIS TYR PHE THR SER          
SEQRES  55 D  723  SER SER LEU LYS GLN HIS LEU TYR ARG SER ILE ILE ASN          
SEQRES  56 D  723  PHE PHE VAL GLU CYS PHE ARG ILE                              
MODRES 1XFD ASN A  173  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN A  319  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN A  404  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN A  535  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN A  566  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN A  813  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN B  173  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN B  319  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN B  404  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN B  535  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN B  566  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN B  813  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN C  173  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN C  319  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN C  404  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN C  535  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN C  813  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN D  173  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN D  319  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN D  404  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN D  535  ASN  GLYCOSYLATION SITE                                 
MODRES 1XFD ASN D  813  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A1319      14                                                       
HET    NAG  A2319      14                                                       
HET    MAN  A3319      11                                                       
HET    NAG  A1173      14                                                       
HET    NAG  A2173      14                                                       
HET    MAN  A3173      11                                                       
HET    MAN  A4173      11                                                       
HET    NAG  A1404      14                                                       
HET    NAG  A2404      14                                                       
HET    MAN  A3404      11                                                       
HET    NAG  A1813      14                                                       
HET    NAG  A2813      14                                                       
HET    MAN  A3813      11                                                       
HET    MAN  A4813      11                                                       
HET    NAG  A1535      14                                                       
HET    NAG  A2535      14                                                       
HET    MAN  A3535      11                                                       
HET    NAG  A1566      14                                                       
HET    NAG  A2566      14                                                       
HET    NAG  B1319      14                                                       
HET    NAG  B2319      14                                                       
HET    MAN  B3319      11                                                       
HET    NAG  B1173      14                                                       
HET    NAG  B2173      14                                                       
HET    MAN  B3173      11                                                       
HET    NAG  B1404      14                                                       
HET    NAG  B2404      14                                                       
HET    NAG  B1813      14                                                       
HET    NAG  B2813      14                                                       
HET    MAN  B3813      11                                                       
HET    NAG  B1535      14                                                       
HET    NAG  B2535      14                                                       
HET    NAG  B1566      14                                                       
HET    NAG  B2566      14                                                       
HET    NAG  C1319      14                                                       
HET    NAG  C2319      14                                                       
HET    MAN  C3319      11                                                       
HET    NAG  C1173      14                                                       
HET    NAG  C2173      14                                                       
HET    MAN  C3173      11                                                       
HET    NAG  C1404      14                                                       
HET    NAG  C2404      14                                                       
HET    NAG  C1813      14                                                       
HET    NAG  C2813      14                                                       
HET    MAN  C3813      11                                                       
HET    NAG  C1535      14                                                       
HET    NAG  C2535      14                                                       
HET    NAG  D1319      14                                                       
HET    NAG  D2319      14                                                       
HET    MAN  D3319      11                                                       
HET    NAG  D1173      14                                                       
HET    NAG  D2173      14                                                       
HET    MAN  D3173      11                                                       
HET    NAG  D1404      14                                                       
HET    NAG  D2404      14                                                       
HET    MAN  D3404      11                                                       
HET    MAN  D4404      11                                                       
HET    NAG  D1813      14                                                       
HET    NAG  D2813      14                                                       
HET    MAN  D3813      11                                                       
HET    NAG  D1535      14                                                       
HET    NAG  D2535      14                                                       
HET    MAN  D3535      11                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETSYN     NAG NAG                                                              
FORMUL   5  NAG    44(C8 H15 N1 O6)                                             
FORMUL   5  MAN    19(C6 H12 O6)                                                
FORMUL  27  HOH   *51(H2 O1)                                                    
HELIX    1   1 THR A  132  PHE A  137  1                                   6    
HELIX    2   2 ASN A  169  ASN A  173  5                                   5    
HELIX    3   3 ASP A  290  GLU A  296  1                                   7    
HELIX    4   4 ASP A  375  ARG A  379  5                                   5    
HELIX    5   5 ASN A  579  ASP A  588  1                                  10    
HELIX    6   6 SER A  644  SER A  652  1                                   9    
HELIX    7   7 GLN A  668  GLU A  675  1                                   8    
HELIX    8   8 LEU A  682  LYS A  697  1                                  16    
HELIX    9   9 ASP A  712  ILE A  721  1                                  10    
HELIX   10  10 ALA A  749  GLY A  758  1                                  10    
HELIX   11  11 VAL A  772  SER A  777  1                                   6    
HELIX   12  12 HIS A  796  GLY A  810  1                                  15    
HELIX   13  13 SER A  828  VAL A  844  1                                  17    
HELIX   14  14 THR B  132  PHE B  137  1                                   6    
HELIX   15  15 ASN B  169  ASN B  173  5                                   5    
HELIX   16  16 ASP B  290  GLU B  296  1                                   7    
HELIX   17  17 ASP B  375  ARG B  379  5                                   5    
HELIX   18  18 ASN B  579  ASP B  588  1                                  10    
HELIX   19  19 SER B  644  SER B  652  1                                   9    
HELIX   20  20 GLN B  668  GLU B  675  1                                   8    
HELIX   21  21 LEU B  682  LYS B  697  1                                  16    
HELIX   22  22 ASP B  712  ILE B  721  1                                  10    
HELIX   23  23 ALA B  749  GLY B  758  1                                  10    
HELIX   24  24 VAL B  772  SER B  777  1                                   6    
HELIX   25  25 HIS B  796  GLY B  810  1                                  15    
HELIX   26  26 SER B  828  VAL B  844  1                                  17    
HELIX   27  27 THR C  132  PHE C  137  1                                   6    
HELIX   28  28 ASN C  169  ASN C  173  5                                   5    
HELIX   29  29 ASP C  290  GLU C  296  1                                   7    
HELIX   30  30 ASP C  375  ARG C  379  5                                   5    
HELIX   31  31 ASN C  579  ASP C  588  1                                  10    
HELIX   32  32 SER C  644  SER C  652  1                                   9    
HELIX   33  33 GLN C  668  GLU C  675  1                                   8    
HELIX   34  34 LEU C  682  LYS C  697  1                                  16    
HELIX   35  35 ASP C  712  ILE C  721  1                                  10    
HELIX   36  36 ALA C  749  GLY C  758  1                                  10    
HELIX   37  37 VAL C  772  SER C  777  1                                   6    
HELIX   38  38 HIS C  796  GLY C  810  1                                  15    
HELIX   39  39 SER C  828  VAL C  844  1                                  17    
HELIX   40  40 THR D  132  PHE D  137  1                                   6    
HELIX   41  41 ASN D  169  ASN D  173  5                                   5    
HELIX   42  42 ASP D  290  GLU D  296  1                                   7    
HELIX   43  43 ASP D  375  ARG D  379  5                                   5    
HELIX   44  44 ASN D  579  ASP D  588  1                                  10    
HELIX   45  45 SER D  644  SER D  652  1                                   9    
HELIX   46  46 GLN D  668  GLU D  675  1                                   8    
HELIX   47  47 LEU D  682  LYS D  697  1                                  16    
HELIX   48  48 ASP D  712  ILE D  721  1                                  10    
HELIX   49  49 ALA D  749  GLY D  758  1                                  10    
HELIX   50  50 VAL D  772  SER D  777  1                                   6    
HELIX   51  51 HIS D  796  GLY D  810  1                                  15    
HELIX   52  52 SER D  828  VAL D  844  1                                  17    
SHEET    1   A 2 VAL A 165  LEU A 167  0                                        
SHEET    2   A 2 THR A 176  ILE A 179 -1  O  ILE A 179   N  VAL A 165           
SHEET    1   B 4 ARG A 191  ILE A 194  0                                        
SHEET    2   B 4 TYR A 200  TYR A 205 -1  O  LEU A 202   N  GLU A 193           
SHEET    3   B 4 TYR A 218  LYS A 223 -1  O  VAL A 220   N  PHE A 203           
SHEET    4   B 4 GLN A 230  SER A 231 -1  O  GLN A 230   N  LEU A 221           
SHEET    1   C 3 LEU A 254  PHE A 258  0                                        
SHEET    2   C 3 ASN A 261  CYS A 265 -1  O  CYS A 265   N  LEU A 254           
SHEET    3   C 3 ILE A 273  VAL A 276 -1  O  ILE A 273   N  TYR A 264           
SHEET    1   D 6 LEU A 368  GLU A 369  0                                        
SHEET    2   D 6 SER A 353  GLY A 360 -1  N  VAL A 358   O  LEU A 368           
SHEET    3   D 6 ARG A 312  ASN A 319 -1  N  ASN A 319   O  SER A 353           
SHEET    4   D 6 ILE A 302  TRP A 306 -1  N  TRP A 305   O  ALA A 314           
SHEET    5   D 6 ILE A 284  LEU A 288 -1  N  GLY A 287   O  ALA A 303           
SHEET    6   D 6 ARG A 312  ASN A 319 -1  O  ILE A 318   N  TYR A 285           
SHEET    1   E 2 ILE A 325  LEU A 328  0                                        
SHEET    2   E 2 LYS A 340  HIS A 343 -1  O  LYS A 340   N  LEU A 328           
SHEET    1   F 4 TYR A 381  TRP A 388  0                                        
SHEET    2   F 4 LYS A 393  ASN A 400 -1  O  LEU A 399   N  TYR A 382           
SHEET    3   F 4 VAL A 405  ASP A 412 -1  O  THR A 409   N  VAL A 396           
SHEET    4   F 4 CYS A 418  GLU A 425 -1  O  ASP A 424   N  SER A 406           
SHEET    1   G 3 VAL A 438  PHE A 439  0                                        
SHEET    2   G 3 PHE A 446  ILE A 452 -1  O  PHE A 447   N  VAL A 438           
SHEET    3   G 3 PHE A 460  SER A 466 -1  O  SER A 466   N  PHE A 446           
SHEET    1   H 3 VAL A 487  ASP A 494  0                                        
SHEET    2   H 3 LYS A 499  SER A 504 -1  O  TYR A 501   N  LEU A 491           
SHEET    3   H 3 GLN A 513  ALA A 517 -1  O  TYR A 515   N  PHE A 502           
SHEET    1   I 4 SER A 540  PHE A 543  0                                        
SHEET    2   I 4 PHE A 549  LYS A 553 -1  O  LYS A 553   N  SER A 540           
SHEET    3   I 4 VAL A 562  ASN A 566 -1  O  THR A 563   N  LEU A 552           
SHEET    4   I 4 LYS A 572  GLU A 577 -1  O  GLU A 577   N  VAL A 562           
SHEET    1   J 2 ILE A 599  ILE A 601  0                                        
SHEET    2   J 2 TYR A 604  LEU A 606 -1  O  LEU A 606   N  ILE A 599           
SHEET    1   K 7 ILE A 610  LEU A 611  0                                        
SHEET    2   K 7 VAL A 656  VAL A 658 -1  O  VAL A 657   N  LEU A 611           
SHEET    3   K 7 TYR A 622  VAL A 627  1  N  LEU A 625   O  VAL A 656           
SHEET    4   K 7 ILE A 701  LYS A 711  1  O  ALA A 707   N  LEU A 626           
SHEET    5   K 7 CYS A 735  LEU A 739  1  O  LEU A 739   N  GLY A 710           
SHEET    6   K 7 GLN A 783  PRO A 789  1  O  ILE A 787   N  ALA A 738           
SHEET    7   K 7 SER A 815  TYR A 819  1  O  SER A 815   N  ILE A 786           
SHEET    1   L 2 VAL B 165  LEU B 167  0                                        
SHEET    2   L 2 THR B 176  ILE B 179 -1  O  ILE B 179   N  VAL B 165           
SHEET    1   M 4 ARG B 191  ILE B 194  0                                        
SHEET    2   M 4 TYR B 200  TYR B 205 -1  O  LEU B 202   N  GLU B 193           
SHEET    3   M 4 TYR B 218  LYS B 223 -1  O  VAL B 220   N  PHE B 203           
SHEET    4   M 4 GLN B 230  SER B 231 -1  O  GLN B 230   N  LEU B 221           
SHEET    1   N 3 LEU B 254  PHE B 258  0                                        
SHEET    2   N 3 ASN B 261  CYS B 265 -1  O  CYS B 265   N  LEU B 254           
SHEET    3   N 3 ILE B 273  VAL B 276 -1  O  ILE B 273   N  TYR B 264           
SHEET    1   O 6 LEU B 368  GLU B 369  0                                        
SHEET    2   O 6 SER B 353  GLY B 360 -1  N  VAL B 358   O  LEU B 368           
SHEET    3   O 6 ARG B 312  ASN B 319 -1  N  ASN B 319   O  SER B 353           
SHEET    4   O 6 ILE B 302  TRP B 306 -1  N  TRP B 305   O  ALA B 314           
SHEET    5   O 6 ILE B 284  LEU B 288 -1  N  GLY B 287   O  ALA B 303           
SHEET    6   O 6 ARG B 312  ASN B 319 -1  O  ILE B 318   N  TYR B 285           
SHEET    1   P 2 ILE B 325  LEU B 328  0                                        
SHEET    2   P 2 LYS B 340  HIS B 343 -1  O  LYS B 340   N  LEU B 328           
SHEET    1   Q 4 TYR B 381  TRP B 388  0                                        
SHEET    2   Q 4 LYS B 393  ASN B 400 -1  O  LEU B 399   N  TYR B 382           
SHEET    3   Q 4 VAL B 405  ASP B 412 -1  O  THR B 409   N  VAL B 396           
SHEET    4   Q 4 CYS B 418  GLU B 425 -1  O  ASP B 424   N  SER B 406           
SHEET    1   R 3 VAL B 438  PHE B 439  0                                        
SHEET    2   R 3 PHE B 446  ILE B 452 -1  O  PHE B 447   N  VAL B 438           
SHEET    3   R 3 PHE B 460  SER B 466 -1  O  SER B 466   N  PHE B 446           
SHEET    1   S 3 VAL B 487  ASP B 494  0                                        
SHEET    2   S 3 LYS B 499  SER B 504 -1  O  TYR B 501   N  LEU B 491           
SHEET    3   S 3 GLN B 513  ALA B 517 -1  O  TYR B 515   N  PHE B 502           
SHEET    1   T 4 SER B 540  PHE B 543  0                                        
SHEET    2   T 4 PHE B 549  LYS B 553 -1  O  LYS B 553   N  SER B 540           
SHEET    3   T 4 VAL B 562  ASN B 566 -1  O  THR B 563   N  LEU B 552           
SHEET    4   T 4 LYS B 572  GLU B 577 -1  O  GLU B 577   N  VAL B 562           
SHEET    1   U 2 ILE B 599  ILE B 601  0                                        
SHEET    2   U 2 TYR B 604  LEU B 606 -1  O  LEU B 606   N  ILE B 599           
SHEET    1   V 7 ILE B 610  LEU B 611  0                                        
SHEET    2   V 7 VAL B 656  VAL B 658 -1  O  VAL B 657   N  LEU B 611           
SHEET    3   V 7 TYR B 622  VAL B 627  1  N  LEU B 625   O  VAL B 656           
SHEET    4   V 7 ILE B 701  LYS B 711  1  O  ALA B 707   N  LEU B 624           
SHEET    5   V 7 CYS B 735  LEU B 739  1  O  LEU B 739   N  GLY B 710           
SHEET    6   V 7 GLN B 783  PRO B 789  1  O  ILE B 787   N  ALA B 738           
SHEET    7   V 7 SER B 815  TYR B 819  1  O  SER B 815   N  ILE B 786           
SHEET    1   W 2 VAL C 165  LEU C 167  0                                        
SHEET    2   W 2 THR C 176  ILE C 179 -1  O  ILE C 179   N  VAL C 165           
SHEET    1   X 4 ARG C 191  ILE C 194  0                                        
SHEET    2   X 4 TYR C 200  TYR C 205 -1  O  LEU C 202   N  GLU C 193           
SHEET    3   X 4 TYR C 218  LYS C 223 -1  O  TYR C 218   N  TYR C 205           
SHEET    4   X 4 GLN C 230  SER C 231 -1  O  GLN C 230   N  LEU C 221           
SHEET    1   Y 3 LEU C 254  PHE C 258  0                                        
SHEET    2   Y 3 ASN C 261  CYS C 265 -1  O  CYS C 265   N  LEU C 254           
SHEET    3   Y 3 ILE C 273  VAL C 276 -1  O  ILE C 273   N  TYR C 264           
SHEET    1   Z 6 LEU C 368  GLU C 369  0                                        
SHEET    2   Z 6 SER C 353  GLY C 360 -1  N  VAL C 358   O  LEU C 368           
SHEET    3   Z 6 ARG C 312  ASN C 319 -1  N  ASN C 319   O  SER C 353           
SHEET    4   Z 6 ILE C 302  TRP C 306 -1  N  TRP C 305   O  ALA C 314           
SHEET    5   Z 6 ILE C 284  LEU C 288 -1  N  GLY C 287   O  ALA C 303           
SHEET    6   Z 6 ARG C 312  ASN C 319 -1  O  ILE C 318   N  TYR C 285           
SHEET    1  AA 2 ILE C 325  LEU C 328  0                                        
SHEET    2  AA 2 LYS C 340  HIS C 343 -1  O  LYS C 340   N  LEU C 328           
SHEET    1  AB 4 TYR C 381  TRP C 388  0                                        
SHEET    2  AB 4 LYS C 393  ASN C 400 -1  O  LEU C 399   N  TYR C 382           
SHEET    3  AB 4 VAL C 405  ASP C 412 -1  O  THR C 409   N  VAL C 396           
SHEET    4  AB 4 CYS C 418  GLU C 425 -1  O  ASP C 424   N  SER C 406           
SHEET    1  AC 3 VAL C 438  PHE C 439  0                                        
SHEET    2  AC 3 PHE C 446  ILE C 452 -1  O  PHE C 447   N  VAL C 438           
SHEET    3  AC 3 PHE C 460  SER C 466 -1  O  SER C 466   N  PHE C 446           
SHEET    1  AD 3 VAL C 487  ASP C 494  0                                        
SHEET    2  AD 3 LYS C 499  SER C 504 -1  O  TYR C 501   N  LEU C 491           
SHEET    3  AD 3 GLN C 513  ALA C 517 -1  O  TYR C 515   N  PHE C 502           
SHEET    1  AE 4 SER C 540  PHE C 543  0                                        
SHEET    2  AE 4 PHE C 549  LYS C 553 -1  O  LYS C 553   N  SER C 540           
SHEET    3  AE 4 VAL C 562  ASN C 566 -1  O  THR C 563   N  LEU C 552           
SHEET    4  AE 4 LYS C 572  GLU C 577 -1  O  GLU C 577   N  VAL C 562           
SHEET    1  AF 2 ILE C 599  ILE C 601  0                                        
SHEET    2  AF 2 TYR C 604  LEU C 606 -1  O  LEU C 606   N  ILE C 599           
SHEET    1  AG 7 ILE C 610  LEU C 611  0                                        
SHEET    2  AG 7 VAL C 656  VAL C 658 -1  O  VAL C 657   N  LEU C 611           
SHEET    3  AG 7 TYR C 622  VAL C 627  1  N  LEU C 625   O  VAL C 656           
SHEET    4  AG 7 ILE C 701  LYS C 711  1  O  ALA C 707   N  LEU C 626           
SHEET    5  AG 7 CYS C 735  LEU C 739  1  O  LEU C 739   N  GLY C 710           
SHEET    6  AG 7 GLN C 783  PRO C 789  1  O  GLN C 783   N  GLY C 736           
SHEET    7  AG 7 SER C 815  TYR C 819  1  O  SER C 815   N  ILE C 786           
SHEET    1  AH 2 VAL D 165  LEU D 167  0                                        
SHEET    2  AH 2 THR D 176  ILE D 179 -1  O  ILE D 179   N  VAL D 165           
SHEET    1  AI 4 ARG D 191  ILE D 194  0                                        
SHEET    2  AI 4 TYR D 200  TYR D 205 -1  O  LEU D 202   N  GLU D 193           
SHEET    3  AI 4 TYR D 218  LYS D 223 -1  O  VAL D 220   N  PHE D 203           
SHEET    4  AI 4 GLN D 230  SER D 231 -1  O  GLN D 230   N  LEU D 221           
SHEET    1  AJ 3 LEU D 254  PHE D 258  0                                        
SHEET    2  AJ 3 ASN D 261  CYS D 265 -1  O  CYS D 265   N  LEU D 254           
SHEET    3  AJ 3 ILE D 273  VAL D 276 -1  O  ILE D 273   N  TYR D 264           
SHEET    1  AK 6 LEU D 368  GLU D 369  0                                        
SHEET    2  AK 6 SER D 353  GLY D 360 -1  N  VAL D 358   O  LEU D 368           
SHEET    3  AK 6 ARG D 312  ASN D 319 -1  N  ASN D 319   O  SER D 353           
SHEET    4  AK 6 ILE D 302  TRP D 306 -1  N  TRP D 305   O  ALA D 314           
SHEET    5  AK 6 ILE D 284  LEU D 288 -1  N  GLY D 287   O  ALA D 303           
SHEET    6  AK 6 ARG D 312  ASN D 319 -1  O  ILE D 318   N  TYR D 285           
SHEET    1  AL 2 ILE D 325  LEU D 328  0                                        
SHEET    2  AL 2 LYS D 340  HIS D 343 -1  O  LYS D 340   N  LEU D 328           
SHEET    1  AM 4 TYR D 381  TRP D 388  0                                        
SHEET    2  AM 4 LYS D 393  ASN D 400 -1  O  LEU D 399   N  TYR D 382           
SHEET    3  AM 4 VAL D 405  ASP D 412 -1  O  THR D 409   N  VAL D 396           
SHEET    4  AM 4 CYS D 418  GLU D 425 -1  O  ASP D 424   N  SER D 406           
SHEET    1  AN 3 VAL D 438  PHE D 439  0                                        
SHEET    2  AN 3 PHE D 446  ILE D 452 -1  O  PHE D 447   N  VAL D 438           
SHEET    3  AN 3 PHE D 460  SER D 466 -1  O  SER D 466   N  PHE D 446           
SHEET    1  AO 3 VAL D 487  ASP D 494  0                                        
SHEET    2  AO 3 LYS D 499  SER D 504 -1  O  TYR D 501   N  LEU D 491           
SHEET    3  AO 3 GLN D 513  ALA D 517 -1  O  TYR D 515   N  PHE D 502           
SHEET    1  AP 4 SER D 540  PHE D 543  0                                        
SHEET    2  AP 4 PHE D 549  LYS D 553 -1  O  LYS D 553   N  SER D 540           
SHEET    3  AP 4 VAL D 562  ASN D 566 -1  O  THR D 563   N  LEU D 552           
SHEET    4  AP 4 LYS D 572  GLU D 577 -1  O  GLU D 577   N  VAL D 562           
SHEET    1  AQ 2 ILE D 599  ILE D 601  0                                        
SHEET    2  AQ 2 TYR D 604  LEU D 606 -1  O  LEU D 606   N  ILE D 599           
SHEET    1  AR 7 ILE D 610  LEU D 611  0                                        
SHEET    2  AR 7 VAL D 656  VAL D 658 -1  O  VAL D 657   N  LEU D 611           
SHEET    3  AR 7 TYR D 622  VAL D 627  1  N  LEU D 625   O  VAL D 656           
SHEET    4  AR 7 ILE D 701  LYS D 711  1  O  ALA D 707   N  LEU D 626           
SHEET    5  AR 7 CYS D 735  LEU D 739  1  O  LEU D 739   N  GLY D 710           
SHEET    6  AR 7 GLN D 783  PRO D 789  1  O  ILE D 787   N  ALA D 738           
SHEET    7  AR 7 SER D 815  TYR D 819  1  O  SER D 815   N  ILE D 786           
SSBOND   1 CYS A  411    CYS A  418                                             
SSBOND   2 CYS A  527    CYS A  530                                             
SSBOND   3 CYS A  536    CYS A  554                                             
SSBOND   4 CYS A  735    CYS A  846                                             
SSBOND   5 CYS B  411    CYS B  418                                             
SSBOND   6 CYS B  527    CYS B  530                                             
SSBOND   7 CYS B  536    CYS B  554                                             
SSBOND   8 CYS B  735    CYS B  846                                             
SSBOND   9 CYS C  411    CYS C  418                                             
SSBOND  10 CYS C  527    CYS C  530                                             
SSBOND  11 CYS C  536    CYS C  554                                             
SSBOND  12 CYS C  735    CYS C  846                                             
SSBOND  13 CYS D  411    CYS D  418                                             
SSBOND  14 CYS D  527    CYS D  530                                             
SSBOND  15 CYS D  536    CYS D  554                                             
SSBOND  16 CYS D  735    CYS D  846                                             
LINK         ND2 ASN A 173                 C1  NAG A1173                        
LINK         ND2 ASN A 319                 C1  NAG A1319                        
LINK         ND2 ASN A 404                 C1  NAG A1404                        
LINK         ND2 ASN A 535                 C1  NAG A1535                        
LINK         ND2 ASN A 566                 C1  NAG A1566                        
LINK         ND2 ASN A 813                 C1  NAG A1813                        
LINK         ND2 ASN B 173                 C1  NAG B1173                        
LINK         ND2 ASN B 319                 C1  NAG B1319                        
LINK         ND2 ASN B 404                 C1  NAG B1404                        
LINK         ND2 ASN B 535                 C1  NAG B1535                        
LINK         ND2 ASN B 566                 C1  NAG B1566                        
LINK         ND2 ASN B 813                 C1  NAG B1813                        
LINK         ND2 ASN C 173                 C1  NAG C1173                        
LINK         ND2 ASN C 319                 C1  NAG C1319                        
LINK         ND2 ASN C 404                 C1  NAG C1404                        
LINK         ND2 ASN C 535                 C1  NAG C1535                        
LINK         ND2 ASN C 813                 C1  NAG C1813                        
LINK         ND2 ASN D 173                 C1  NAG D1173                        
LINK         ND2 ASN D 319                 C1  NAG D1319                        
LINK         ND2 ASN D 404                 C1  NAG D1404                        
LINK         ND2 ASN D 535                 C1  NAG D1535                        
LINK         ND2 ASN D 813                 C1  NAG D1813                        
LINK         O4  NAG A1319                 C1  NAG A2319                        
LINK         O4  NAG A2319                 C1  MAN A3319                        
LINK         O4  NAG A1173                 C1  NAG A2173                        
LINK         O4  NAG A2173                 C1  MAN A3173                        
LINK         O4  MAN A3173                 C1  MAN A4173                        
LINK         O4  NAG A1404                 C1  NAG A2404                        
LINK         O4  NAG A2404                 C1  MAN A3404                        
LINK         O4  NAG A1813                 C1  NAG A2813                        
LINK         O4  NAG A2813                 C1  MAN A3813                        
LINK         O4  MAN A3813                 C1  MAN A4813                        
LINK         O4  NAG A1535                 C1  NAG A2535                        
LINK         O4  NAG A2535                 C1  MAN A3535                        
LINK         O4  NAG A1566                 C1  NAG A2566                        
LINK         O4  NAG B1319                 C1  NAG B2319                        
LINK         O4  NAG B2319                 C1  MAN B3319                        
LINK         O4  NAG B1173                 C1  NAG B2173                        
LINK         O4  NAG B2173                 C1  MAN B3173                        
LINK         O4  NAG B1404                 C1  NAG B2404                        
LINK         O4  NAG B1813                 C1  NAG B2813                        
LINK         O4  NAG B2813                 C1  MAN B3813                        
LINK         O4  NAG B1535                 C1  NAG B2535                        
LINK         O4  NAG B1566                 C1  NAG B2566                        
LINK         O4  NAG C1319                 C1  NAG C2319                        
LINK         O4  NAG C2319                 C1  MAN C3319                        
LINK         O4  NAG C1173                 C1  NAG C2173                        
LINK         O4  NAG C2173                 C1  MAN C3173                        
LINK         O4  NAG C1404                 C1  NAG C2404                        
LINK         O4  NAG C1813                 C1  NAG C2813                        
LINK         O4  NAG C2813                 C1  MAN C3813                        
LINK         O4  NAG C1535                 C1  NAG C2535                        
LINK         O4  NAG D1319                 C1  NAG D2319                        
LINK         O4  NAG D2319                 C1  MAN D3319                        
LINK         O4  NAG D1173                 C1  NAG D2173                        
LINK         O4  NAG D2173                 C1  MAN D3173                        
LINK         O4  NAG D1404                 C1  NAG D2404                        
LINK         O4  NAG D2404                 C1  MAN D3404                        
LINK         O4  MAN D3404                 C1  MAN D4404                        
LINK         O4  NAG D1813                 C1  NAG D2813                        
LINK         O4  NAG D2813                 C1  MAN D3813                        
LINK         O4  NAG D1535                 C1  NAG D2535                        
LINK         O4  NAG D2535                 C1  MAN D3535                        
CISPEP   1 GLY A  556    PRO A  557          0        -0.26                     
CISPEP   2 GLY B  556    PRO B  557          0        -0.15                     
CISPEP   3 GLY C  556    PRO C  557          0        -0.21                     
CISPEP   4 GLY D  556    PRO D  557          0        -0.06                     
CRYST1   68.980  170.230  159.316  90.00  92.11  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014497  0.000000  0.000534        0.00000                         
SCALE2      0.000000  0.005874  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006281        0.00000                         
TER    5838      ILE A 849                                                      
TER   11676      ILE B 849                                                      
TER   17514      ILE C 849                                                      
TER   23352      ILE D 849                                                      
MASTER      494    0   63   52  160    0    0    624224    4  879  224          
END                                                                             

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