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LongText Report for: 6scj-pdb

Name Class
6scj-pdb
HEADER    HORMONE                                 24-JUL-19   6SCJ              
TITLE     THE STRUCTURE OF HUMAN THYROGLOBULIN                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYROGLOBULIN;                                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: TG;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TG;                                                            
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: 293T;                                     
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK                                     
KEYWDS    THYROGLOBULIN, THYROID, THYROID HORMONES, TRI-IODO-THYRONINE,         
KEYWDS   2 THYROXINE, HORMONE                                                   
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    F.COSCIA,D.TURK,J.LOWE                                                
REVDAT   1   12-FEB-20 6SCJ    0                                                
JRNL        AUTH   F.COSCIA,D.TURK,J.LOWE                                       
JRNL        TITL   THE STRUCTURE OF HUMAN THYROGLOBULIN                         
JRNL        REF    NATURE                                     2020              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        DOI    10.1038/S41586-020-1995-4                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.600                          
REMARK   3   NUMBER OF PARTICLES               : 151601                         
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6SCJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUL-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292103446.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : HUMAN THYROGLOBULIN               
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.05                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 8.00                              
REMARK 245   SAMPLE DETAILS                 : DIMERIC                           
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 40.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 29540 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 238810 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 18.0 KCAL/MOL                         
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     ILE A     7                                                      
REMARK 465     PHE A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     ILE A    14                                                      
REMARK 465     CYS A    15                                                      
REMARK 465     TRP A    16                                                      
REMARK 465     VAL A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     ASN A    20                                                      
REMARK 465     ILE A    21                                                      
REMARK 465     PHE A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     LEU A   388                                                      
REMARK 465     PHE A   389                                                      
REMARK 465     SER A   390                                                      
REMARK 465     SER A   391                                                      
REMARK 465     PRO A   392                                                      
REMARK 465     GLU A   393                                                      
REMARK 465     LYS A   394                                                      
REMARK 465     ARG A   395                                                      
REMARK 465     TRP A   396                                                      
REMARK 465     ALA A   397                                                      
REMARK 465     SER A   398                                                      
REMARK 465     PRO A   399                                                      
REMARK 465     ARG A   400                                                      
REMARK 465     VAL A   401                                                      
REMARK 465     ALA A   402                                                      
REMARK 465     ARG A   403                                                      
REMARK 465     PHE A   404                                                      
REMARK 465     ALA A   405                                                      
REMARK 465     THR A   406                                                      
REMARK 465     SER A   407                                                      
REMARK 465     ASN A   511                                                      
REMARK 465     GLY A   512                                                      
REMARK 465     GLY A   513                                                      
REMARK 465     ARG A   514                                                      
REMARK 465     GLN A   515                                                      
REMARK 465     GLU A   516                                                      
REMARK 465     ASP A   517                                                      
REMARK 465     LEU A   518                                                      
REMARK 465     ALA A   519                                                      
REMARK 465     LYS A   520                                                      
REMARK 465     PRO A   521                                                      
REMARK 465     LEU A   522                                                      
REMARK 465     SER A   523                                                      
REMARK 465     VAL A   524                                                      
REMARK 465     GLY A   525                                                      
REMARK 465     LEU A   526                                                      
REMARK 465     ASP A   527                                                      
REMARK 465     SER A   528                                                      
REMARK 465     ASN A   529                                                      
REMARK 465     SER A   530                                                      
REMARK 465     SER A   531                                                      
REMARK 465     THR A   532                                                      
REMARK 465     GLY A   533                                                      
REMARK 465     THR A   534                                                      
REMARK 465     PRO A   535                                                      
REMARK 465     GLU A   536                                                      
REMARK 465     ALA A   537                                                      
REMARK 465     ALA A   538                                                      
REMARK 465     LYS A   539                                                      
REMARK 465     LYS A   540                                                      
REMARK 465     ASP A   541                                                      
REMARK 465     GLY A   542                                                      
REMARK 465     THR A   543                                                      
REMARK 465     MET A   544                                                      
REMARK 465     ASN A   545                                                      
REMARK 465     LYS A   546                                                      
REMARK 465     GLN A   837                                                      
REMARK 465     ASP A   838                                                      
REMARK 465     VAL A   839                                                      
REMARK 465     PHE A   840                                                      
REMARK 465     PRO A   841                                                      
REMARK 465     VAL A   842                                                      
REMARK 465     LEU A   843                                                      
REMARK 465     SER A   844                                                      
REMARK 465     GLN A   845                                                      
REMARK 465     TYR A   846                                                      
REMARK 465     PRO A   847                                                      
REMARK 465     SER A   848                                                      
REMARK 465     LEU A   849                                                      
REMARK 465     GLN A   850                                                      
REMARK 465     ASP A   851                                                      
REMARK 465     VAL A   852                                                      
REMARK 465     PRO A   853                                                      
REMARK 465     LEU A   854                                                      
REMARK 465     LEU A   869A                                                     
REMARK 465     GLU A   869B                                                     
REMARK 465     PRO A   869C                                                     
REMARK 465     TYR A   869D                                                     
REMARK 465     LEU A   869E                                                     
REMARK 465     PHE A   869F                                                     
REMARK 465     TRP A   869G                                                     
REMARK 465     GLN A   869H                                                     
REMARK 465     PHE A  1010                                                      
REMARK 465     SER A  1011                                                      
REMARK 465     PRO A  1012                                                      
REMARK 465     ASP A  1013                                                      
REMARK 465     ASP A  1014                                                      
REMARK 465     SER A  1015                                                      
REMARK 465     ALA A  1016                                                      
REMARK 465     GLY A  1017                                                      
REMARK 465     ALA A  1018                                                      
REMARK 465     SER A  1019                                                      
REMARK 465     ALA A  1020                                                      
REMARK 465     GLY A  1138                                                      
REMARK 465     SER A  1139                                                      
REMARK 465     SER A  1140                                                      
REMARK 465     SER A  1141                                                      
REMARK 465     SER A  1142                                                      
REMARK 465     ILE A  1234                                                      
REMARK 465     SER A  1235                                                      
REMARK 465     GLY A  1236                                                      
REMARK 465     PRO A  1237                                                      
REMARK 465     THR A  1238                                                      
REMARK 465     GLY A  1239                                                      
REMARK 465     SER A  1240                                                      
REMARK 465     ALA A  1241                                                      
REMARK 465     MET A  1242                                                      
REMARK 465     GLN A  1243                                                      
REMARK 465     PHE A  1424                                                      
REMARK 465     LEU A  1425                                                      
REMARK 465     GLN A  1426                                                      
REMARK 465     GLY A  1427                                                      
REMARK 465     ASP A  1428                                                      
REMARK 465     HIS A  1429                                                      
REMARK 465     PHE A  1430                                                      
REMARK 465     GLY A  1431                                                      
REMARK 465     THR A  1432                                                      
REMARK 465     THR A  1449                                                      
REMARK 465     SER A  1450                                                      
REMARK 465     GLU A  1451                                                      
REMARK 465     ALA A  1452                                                      
REMARK 465     SER A  1453                                                      
REMARK 465     GLN A  1454                                                      
REMARK 465     MET A  1640                                                      
REMARK 465     THR A  1641                                                      
REMARK 465     SER A  1642                                                      
REMARK 465     ASP A  1643                                                      
REMARK 465     GLN A  1644                                                      
REMARK 465     LYS A  1645                                                      
REMARK 465     ARG A  1646                                                      
REMARK 465     ASP A  1647                                                      
REMARK 465     ALA A  1648                                                      
REMARK 465     LEU A  1649                                                      
REMARK 465     GLY A  1650                                                      
REMARK 465     ASN A  1651                                                      
REMARK 465     SER A  1652                                                      
REMARK 465     LYS A  1653                                                      
REMARK 465     ALA A  1654                                                      
REMARK 465     THR A  1655                                                      
REMARK 465     SER A  1656                                                      
REMARK 465     PHE A  1657                                                      
REMARK 465     LEU A  1802                                                      
REMARK 465     THR A  1803                                                      
REMARK 465     PRO A  1804                                                      
REMARK 465     LEU A  1805                                                      
REMARK 465     GLU A  1806                                                      
REMARK 465     GLY A  1807                                                      
REMARK 465     THR A  1808                                                      
REMARK 465     GLN A  1809                                                      
REMARK 465     ASP A  1810                                                      
REMARK 465     THR A  1811                                                      
REMARK 465     PHE A  1812                                                      
REMARK 465     THR A  1813                                                      
REMARK 465     ASN A  1814                                                      
REMARK 465     ALA A  2729                                                      
REMARK 465     ASP A  2730                                                      
REMARK 465     GLY A  2731                                                      
REMARK 465     ALA A  2732                                                      
REMARK 465     LYS A  2733                                                      
REMARK 465     GLY A  2734                                                      
REMARK 465     GLY A  2735                                                      
REMARK 465     GLN A  2736                                                      
REMARK 465     SER A  2737                                                      
REMARK 465     ALA A  2738                                                      
REMARK 465     GLU A  2739                                                      
REMARK 465     SER A  2740                                                      
REMARK 465     GLU A  2741                                                      
REMARK 465     GLU A  2742                                                      
REMARK 465     GLU A  2743                                                      
REMARK 465     GLU A  2744                                                      
REMARK 465     LEU A  2745                                                      
REMARK 465     THR A  2746                                                      
REMARK 465     ALA A  2747                                                      
REMARK 465     GLY A  2748                                                      
REMARK 465     SER A  2749                                                      
REMARK 465     GLY A  2750                                                      
REMARK 465     LEU A  2751                                                      
REMARK 465     ARG A  2752                                                      
REMARK 465     GLU A  2753                                                      
REMARK 465     ASP A  2754                                                      
REMARK 465     LEU A  2755                                                      
REMARK 465     LEU A  2756                                                      
REMARK 465     SER A  2757                                                      
REMARK 465     LEU A  2758                                                      
REMARK 465     GLN A  2759                                                      
REMARK 465     GLU A  2760                                                      
REMARK 465     PRO A  2761                                                      
REMARK 465     GLY A  2762                                                      
REMARK 465     SER A  2763                                                      
REMARK 465     LYS A  2764                                                      
REMARK 465     THR A  2765                                                      
REMARK 465     TYR A  2766                                                      
REMARK 465     SER A  2767                                                      
REMARK 465     LYS A  2768                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     LEU B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     ILE B     7                                                      
REMARK 465     PHE B     8                                                      
REMARK 465     THR B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     LEU B    11                                                      
REMARK 465     ALA B    12                                                      
REMARK 465     SER B    13                                                      
REMARK 465     ILE B    14                                                      
REMARK 465     CYS B    15                                                      
REMARK 465     TRP B    16                                                      
REMARK 465     VAL B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     ASN B    20                                                      
REMARK 465     ILE B    21                                                      
REMARK 465     PHE B    22                                                      
REMARK 465     GLU B    23                                                      
REMARK 465     LEU B   388                                                      
REMARK 465     PHE B   389                                                      
REMARK 465     SER B   390                                                      
REMARK 465     SER B   391                                                      
REMARK 465     PRO B   392                                                      
REMARK 465     GLU B   393                                                      
REMARK 465     LYS B   394                                                      
REMARK 465     ARG B   395                                                      
REMARK 465     TRP B   396                                                      
REMARK 465     ALA B   397                                                      
REMARK 465     SER B   398                                                      
REMARK 465     PRO B   399                                                      
REMARK 465     ARG B   400                                                      
REMARK 465     VAL B   401                                                      
REMARK 465     ALA B   402                                                      
REMARK 465     ARG B   403                                                      
REMARK 465     PHE B   404                                                      
REMARK 465     ALA B   405                                                      
REMARK 465     THR B   406                                                      
REMARK 465     SER B   407                                                      
REMARK 465     ASN B   511                                                      
REMARK 465     GLY B   512                                                      
REMARK 465     GLY B   513                                                      
REMARK 465     ARG B   514                                                      
REMARK 465     GLN B   515                                                      
REMARK 465     GLU B   516                                                      
REMARK 465     ASP B   517                                                      
REMARK 465     LEU B   518                                                      
REMARK 465     ALA B   519                                                      
REMARK 465     LYS B   520                                                      
REMARK 465     PRO B   521                                                      
REMARK 465     LEU B   522                                                      
REMARK 465     SER B   523                                                      
REMARK 465     VAL B   524                                                      
REMARK 465     GLY B   525                                                      
REMARK 465     LEU B   526                                                      
REMARK 465     ASP B   527                                                      
REMARK 465     SER B   528                                                      
REMARK 465     ASN B   529                                                      
REMARK 465     SER B   530                                                      
REMARK 465     SER B   531                                                      
REMARK 465     THR B   532                                                      
REMARK 465     GLY B   533                                                      
REMARK 465     THR B   534                                                      
REMARK 465     PRO B   535                                                      
REMARK 465     GLU B   536                                                      
REMARK 465     ALA B   537                                                      
REMARK 465     ALA B   538                                                      
REMARK 465     LYS B   539                                                      
REMARK 465     LYS B   540                                                      
REMARK 465     ASP B   541                                                      
REMARK 465     GLY B   542                                                      
REMARK 465     THR B   543                                                      
REMARK 465     MET B   544                                                      
REMARK 465     ASN B   545                                                      
REMARK 465     LYS B   546                                                      
REMARK 465     GLN B   837                                                      
REMARK 465     ASP B   838                                                      
REMARK 465     VAL B   839                                                      
REMARK 465     PHE B   840                                                      
REMARK 465     PRO B   841                                                      
REMARK 465     VAL B   842                                                      
REMARK 465     LEU B   843                                                      
REMARK 465     SER B   844                                                      
REMARK 465     GLN B   845                                                      
REMARK 465     TYR B   846                                                      
REMARK 465     PRO B   847                                                      
REMARK 465     SER B   848                                                      
REMARK 465     LEU B   849                                                      
REMARK 465     GLN B   850                                                      
REMARK 465     ASP B   851                                                      
REMARK 465     VAL B   852                                                      
REMARK 465     PRO B   853                                                      
REMARK 465     LEU B   854                                                      
REMARK 465     LEU B   869A                                                     
REMARK 465     GLU B   869B                                                     
REMARK 465     PRO B   869C                                                     
REMARK 465     TYR B   869D                                                     
REMARK 465     LEU B   869E                                                     
REMARK 465     PHE B   869F                                                     
REMARK 465     TRP B   869G                                                     
REMARK 465     GLN B   869H                                                     
REMARK 465     PHE B  1010                                                      
REMARK 465     SER B  1011                                                      
REMARK 465     PRO B  1012                                                      
REMARK 465     ASP B  1013                                                      
REMARK 465     ASP B  1014                                                      
REMARK 465     SER B  1015                                                      
REMARK 465     ALA B  1016                                                      
REMARK 465     GLY B  1017                                                      
REMARK 465     ALA B  1018                                                      
REMARK 465     SER B  1019                                                      
REMARK 465     ALA B  1020                                                      
REMARK 465     GLY B  1138                                                      
REMARK 465     SER B  1139                                                      
REMARK 465     SER B  1140                                                      
REMARK 465     SER B  1141                                                      
REMARK 465     SER B  1142                                                      
REMARK 465     ILE B  1234                                                      
REMARK 465     SER B  1235                                                      
REMARK 465     GLY B  1236                                                      
REMARK 465     PRO B  1237                                                      
REMARK 465     THR B  1238                                                      
REMARK 465     GLY B  1239                                                      
REMARK 465     SER B  1240                                                      
REMARK 465     ALA B  1241                                                      
REMARK 465     MET B  1242                                                      
REMARK 465     GLN B  1243                                                      
REMARK 465     PHE B  1424                                                      
REMARK 465     LEU B  1425                                                      
REMARK 465     GLN B  1426                                                      
REMARK 465     GLY B  1427                                                      
REMARK 465     ASP B  1428                                                      
REMARK 465     HIS B  1429                                                      
REMARK 465     PHE B  1430                                                      
REMARK 465     GLY B  1431                                                      
REMARK 465     THR B  1432                                                      
REMARK 465     THR B  1449                                                      
REMARK 465     SER B  1450                                                      
REMARK 465     GLU B  1451                                                      
REMARK 465     ALA B  1452                                                      
REMARK 465     SER B  1453                                                      
REMARK 465     GLN B  1454                                                      
REMARK 465     MET B  1640                                                      
REMARK 465     THR B  1641                                                      
REMARK 465     SER B  1642                                                      
REMARK 465     ASP B  1643                                                      
REMARK 465     GLN B  1644                                                      
REMARK 465     LYS B  1645                                                      
REMARK 465     ARG B  1646                                                      
REMARK 465     ASP B  1647                                                      
REMARK 465     ALA B  1648                                                      
REMARK 465     LEU B  1649                                                      
REMARK 465     GLY B  1650                                                      
REMARK 465     ASN B  1651                                                      
REMARK 465     SER B  1652                                                      
REMARK 465     LYS B  1653                                                      
REMARK 465     ALA B  1654                                                      
REMARK 465     THR B  1655                                                      
REMARK 465     SER B  1656                                                      
REMARK 465     PHE B  1657                                                      
REMARK 465     LEU B  1802                                                      
REMARK 465     THR B  1803                                                      
REMARK 465     PRO B  1804                                                      
REMARK 465     LEU B  1805                                                      
REMARK 465     GLU B  1806                                                      
REMARK 465     GLY B  1807                                                      
REMARK 465     THR B  1808                                                      
REMARK 465     GLN B  1809                                                      
REMARK 465     ASP B  1810                                                      
REMARK 465     THR B  1811                                                      
REMARK 465     PHE B  1812                                                      
REMARK 465     THR B  1813                                                      
REMARK 465     ASN B  1814                                                      
REMARK 465     ALA B  2729                                                      
REMARK 465     ASP B  2730                                                      
REMARK 465     GLY B  2731                                                      
REMARK 465     ALA B  2732                                                      
REMARK 465     LYS B  2733                                                      
REMARK 465     GLY B  2734                                                      
REMARK 465     GLY B  2735                                                      
REMARK 465     GLN B  2736                                                      
REMARK 465     SER B  2737                                                      
REMARK 465     ALA B  2738                                                      
REMARK 465     GLU B  2739                                                      
REMARK 465     SER B  2740                                                      
REMARK 465     GLU B  2741                                                      
REMARK 465     GLU B  2742                                                      
REMARK 465     GLU B  2743                                                      
REMARK 465     GLU B  2744                                                      
REMARK 465     LEU B  2745                                                      
REMARK 465     THR B  2746                                                      
REMARK 465     ALA B  2747                                                      
REMARK 465     GLY B  2748                                                      
REMARK 465     SER B  2749                                                      
REMARK 465     GLY B  2750                                                      
REMARK 465     LEU B  2751                                                      
REMARK 465     ARG B  2752                                                      
REMARK 465     GLU B  2753                                                      
REMARK 465     ASP B  2754                                                      
REMARK 465     LEU B  2755                                                      
REMARK 465     LEU B  2756                                                      
REMARK 465     SER B  2757                                                      
REMARK 465     LEU B  2758                                                      
REMARK 465     GLN B  2759                                                      
REMARK 465     GLU B  2760                                                      
REMARK 465     PRO B  2761                                                      
REMARK 465     GLY B  2762                                                      
REMARK 465     SER B  2763                                                      
REMARK 465     LYS B  2764                                                      
REMARK 465     THR B  2765                                                      
REMARK 465     TYR B  2766                                                      
REMARK 465     SER B  2767                                                      
REMARK 465     LYS B  2768                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A  25    CG   CD   OE1  NE2                                  
REMARK 470     VAL A  26    CG1  CG2                                            
REMARK 470     ASP A  27    CG   OD1  OD2                                       
REMARK 470     GLN A  29    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 857    CG   CD1  CD2                                       
REMARK 470     GLU A 858    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 860    CG   CD   CE   NZ                                   
REMARK 470     ARG A 861    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO A 862    CG   CD                                             
REMARK 470     GLN A 863    CG   CD   OE1  NE2                                  
REMARK 470     PRO A 864    CG   CD                                             
REMARK 470     ARG A 865    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 866    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 867    CG   OD1  ND2                                       
REMARK 470     ILE A 868    CG1  CG2  CD1                                       
REMARK 470     LEU A 869    CG   CD1  CD2                                       
REMARK 470     TRP A1772    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A1772    CZ3  CH2                                            
REMARK 470     GLU A2349    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  25    CG   CD   OE1  NE2                                  
REMARK 470     VAL B  26    CG1  CG2                                            
REMARK 470     ASP B  27    CG   OD1  OD2                                       
REMARK 470     GLN B  29    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 857    CG   CD1  CD2                                       
REMARK 470     GLU B 858    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 860    CG   CD   CE   NZ                                   
REMARK 470     ARG B 861    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO B 862    CG   CD                                             
REMARK 470     GLN B 863    CG   CD   OE1  NE2                                  
REMARK 470     PRO B 864    CG   CD                                             
REMARK 470     ARG B 865    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 866    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 867    CG   OD1  ND2                                       
REMARK 470     ILE B 868    CG1  CG2  CD1                                       
REMARK 470     LEU B 869    CG   CD1  CD2                                       
REMARK 470     TRP B1772    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B1772    CZ3  CH2                                            
REMARK 470     GLU B2349    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A2035   CA  -  CB  -  SG  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    CYS B2035   CA  -  CB  -  SG  ANGL. DEV. =   9.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  32       79.69     58.69                                   
REMARK 500    PRO A  33       53.42    -64.61                                   
REMARK 500    ASN A  76       56.43    -96.74                                   
REMARK 500    SER A  83       14.76   -144.59                                   
REMARK 500    SER A 115       57.65    -91.11                                   
REMARK 500    CYS A 131     -167.39   -163.48                                   
REMARK 500    ASP A 132     -168.81   -103.24                                   
REMARK 500    THR A 151       49.74    -93.19                                   
REMARK 500    LEU A 154       56.83    -99.51                                   
REMARK 500    ALA A 185      -10.36     71.75                                   
REMARK 500    PHE A 295       53.49    -93.50                                   
REMARK 500    PRO A 314     -177.76    -68.78                                   
REMARK 500    ARG A 320       48.95    -93.28                                   
REMARK 500    ARG A 321       -6.71     70.81                                   
REMARK 500    ASP A 340     -166.36    -78.30                                   
REMARK 500    TYR A 376       34.99    -98.75                                   
REMARK 500    SER A 380       -5.27     68.18                                   
REMARK 500    THR A 411       26.52     48.76                                   
REMARK 500    SER A 419       49.97    -94.15                                   
REMARK 500    SER A 430     -164.77   -160.46                                   
REMARK 500    PHE A 460       31.49    -97.81                                   
REMARK 500    ASN A 484       61.34   -100.10                                   
REMARK 500    ASN A 496       71.90     58.66                                   
REMARK 500    GLU A 573       53.08    -92.70                                   
REMARK 500    SER A 625       17.63   -142.88                                   
REMARK 500    TYR A 626       70.07     60.26                                   
REMARK 500    LEU A 752       74.11     52.26                                   
REMARK 500    THR A 754       28.18     46.23                                   
REMARK 500    SER A 756       30.68   -140.82                                   
REMARK 500    SER A 764      -73.36    -84.07                                   
REMARK 500    THR A 765      -56.65   -122.26                                   
REMARK 500    ALA A 790     -163.10    -78.20                                   
REMARK 500    LEU A 797      -63.93    -95.00                                   
REMARK 500    GLU A 826       -3.03     67.84                                   
REMARK 500    ALA A 827       -5.72     67.49                                   
REMARK 500    ALA A 891      149.37   -171.13                                   
REMARK 500    ASP A 894       48.86    -96.55                                   
REMARK 500    LEU A 895       12.10   -143.28                                   
REMARK 500    SER A 924      -11.56     69.83                                   
REMARK 500    GLU A1054       72.68     59.88                                   
REMARK 500    SER A1094      -11.08     71.11                                   
REMARK 500    GLN A1095       -0.60     62.33                                   
REMARK 500    ASN A1097       76.47   -161.32                                   
REMARK 500    ALA A1115       75.64     59.07                                   
REMARK 500    ARG A1116      138.10    -37.91                                   
REMARK 500    PRO A1178       46.04    -77.50                                   
REMARK 500    GLU A1211     -168.98   -122.63                                   
REMARK 500    ARG A1214       -4.11     68.36                                   
REMARK 500    GLN A1244      112.33   -164.55                                   
REMARK 500    GLU A1267       51.40    -94.60                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     245 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG A   32     PRO A   33                 -149.90                    
REMARK 500 PRO A   33     CYS A   34                  148.68                    
REMARK 500 PRO A  799     ALA A  800                  144.73                    
REMARK 500 SER A 1902     PHE A 1903                  148.19                    
REMARK 500 ARG B   32     PRO B   33                 -149.97                    
REMARK 500 PRO B   33     CYS B   34                  148.74                    
REMARK 500 PRO B  799     ALA B  800                  144.72                    
REMARK 500 SER B 1902     PHE B 1903                  148.25                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 2816        
REMARK 800  bound to ASN A 76                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 2818        
REMARK 800  bound to ASN A 110                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 2815        
REMARK 800  bound to ASN A 198                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 2817        
REMARK 800  bound to ASN A 484                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 2801        
REMARK 800  bound to ASN A 947                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 2802        
REMARK 800  bound to ASN A 1220                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 2803        
REMARK 800  bound to ASN A 1349                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 2804        
REMARK 800  bound to ASN A 1365                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 2805        
REMARK 800  bound to ASN A 1716                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 2814        
REMARK 800  bound to ASN A 1774                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 2813        
REMARK 800  bound to ASN A 1869                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  2806 through BMA A 2808 bound to ASN A 2013                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 2812        
REMARK 800  bound to ASN A 2122                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 2809        
REMARK 800  bound to ASN A 2250                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 2810        
REMARK 800  bound to ASN A 2295                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 2811        
REMARK 800  bound to ASN A 2582                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2816        
REMARK 800  bound to ASN B 76                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2818        
REMARK 800  bound to ASN B 110                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2815        
REMARK 800  bound to ASN B 198                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2817        
REMARK 800  bound to ASN B 484                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2801        
REMARK 800  bound to ASN B 947                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2802        
REMARK 800  bound to ASN B 1220                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2803        
REMARK 800  bound to ASN B 1349                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2804        
REMARK 800  bound to ASN B 1365                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2805        
REMARK 800  bound to ASN B 1716                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2814        
REMARK 800  bound to ASN B 1774                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2813        
REMARK 800  bound to ASN B 1869                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  2806 through BMA B 2808 bound to ASN B 2013                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2812        
REMARK 800  bound to ASN B 2122                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2809        
REMARK 800  bound to ASN B 2250                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2810        
REMARK 800  bound to ASN B 2295                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 2811        
REMARK 800  bound to ASN B 2582                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-10141   RELATED DB: EMDB                             
REMARK 900 THE STRUCTURE OF HUMAN THYROGLOBULIN                                 
DBREF  6SCJ A    1  2768  UNP    P01266   THYG_HUMAN       1   2768             
DBREF  6SCJ B    1  2768  UNP    P01266   THYG_HUMAN       1   2768             
SEQRES   1 A 2768  MET ALA LEU VAL LEU GLU ILE PHE THR LEU LEU ALA SER          
SEQRES   2 A 2768  ILE CYS TRP VAL SER ALA ASN ILE PHE GLU TYR GLN VAL          
SEQRES   3 A 2768  ASP ALA GLN PRO LEU ARG PRO CYS GLU LEU GLN ARG GLU          
SEQRES   4 A 2768  THR ALA PHE LEU LYS GLN ALA ASP TYR VAL PRO GLN CYS          
SEQRES   5 A 2768  ALA GLU ASP GLY SER PHE GLN THR VAL GLN CYS GLN ASN          
SEQRES   6 A 2768  ASP GLY ARG SER CYS TRP CYS VAL GLY ALA ASN GLY SER          
SEQRES   7 A 2768  GLU VAL LEU GLY SER ARG GLN PRO GLY ARG PRO VAL ALA          
SEQRES   8 A 2768  CYS LEU SER PHE CYS GLN LEU GLN LYS GLN GLN ILE LEU          
SEQRES   9 A 2768  LEU SER GLY TYR ILE ASN SER THR ASP THR SER TYR LEU          
SEQRES  10 A 2768  PRO GLN CYS GLN ASP SER GLY ASP TYR ALA PRO VAL GLN          
SEQRES  11 A 2768  CYS ASP VAL GLN GLN VAL GLN CYS TRP CYS VAL ASP ALA          
SEQRES  12 A 2768  GLU GLY MET GLU VAL TYR GLY THR ARG GLN LEU GLY ARG          
SEQRES  13 A 2768  PRO LYS ARG CYS PRO ARG SER CYS GLU ILE ARG ASN ARG          
SEQRES  14 A 2768  ARG LEU LEU HIS GLY VAL GLY ASP LYS SER PRO PRO GLN          
SEQRES  15 A 2768  CYS SER ALA GLU GLY GLU PHE MET PRO VAL GLN CYS LYS          
SEQRES  16 A 2768  PHE VAL ASN THR THR ASP MET MET ILE PHE ASP LEU VAL          
SEQRES  17 A 2768  HIS SER TYR ASN ARG PHE PRO ASP ALA PHE VAL THR PHE          
SEQRES  18 A 2768  SER SER PHE GLN ARG ARG PHE PRO GLU VAL SER GLY TYR          
SEQRES  19 A 2768  CYS HIS CYS ALA ASP SER GLN GLY ARG GLU LEU ALA GLU          
SEQRES  20 A 2768  THR GLY LEU GLU LEU LEU LEU ASP GLU ILE TYR ASP THR          
SEQRES  21 A 2768  ILE PHE ALA GLY LEU ASP LEU PRO SER THR PHE THR GLU          
SEQRES  22 A 2768  THR THR LEU TYR ARG ILE LEU GLN ARG ARG PHE LEU ALA          
SEQRES  23 A 2768  VAL GLN SER VAL ILE SER GLY ARG PHE ARG CYS PRO THR          
SEQRES  24 A 2768  LYS CYS GLU VAL GLU ARG PHE THR ALA THR SER PHE GLY          
SEQRES  25 A 2768  HIS PRO TYR VAL PRO SER CYS ARG ARG ASN GLY ASP TYR          
SEQRES  26 A 2768  GLN ALA VAL GLN CYS GLN THR GLU GLY PRO CYS TRP CYS          
SEQRES  27 A 2768  VAL ASP ALA GLN GLY LYS GLU MET HIS GLY THR ARG GLN          
SEQRES  28 A 2768  GLN GLY GLU PRO PRO SER CYS ALA GLU GLY GLN SER CYS          
SEQRES  29 A 2768  ALA SER GLU ARG GLN GLN ALA LEU SER ARG LEU TYR PHE          
SEQRES  30 A 2768  GLY THR SER GLY TYR PHE SER GLN HIS ASP LEU PHE SER          
SEQRES  31 A 2768  SER PRO GLU LYS ARG TRP ALA SER PRO ARG VAL ALA ARG          
SEQRES  32 A 2768  PHE ALA THR SER CYS PRO PRO THR ILE LYS GLU LEU PHE          
SEQRES  33 A 2768  VAL ASP SER GLY LEU LEU ARG PRO MET VAL GLU GLY GLN          
SEQRES  34 A 2768  SER GLN GLN PHE SER VAL SER GLU ASN LEU LEU LYS GLU          
SEQRES  35 A 2768  ALA ILE ARG ALA ILE PHE PRO SER ARG GLY LEU ALA ARG          
SEQRES  36 A 2768  LEU ALA LEU GLN PHE THR THR ASN PRO LYS ARG LEU GLN          
SEQRES  37 A 2768  GLN ASN LEU PHE GLY GLY LYS PHE LEU VAL ASN VAL GLY          
SEQRES  38 A 2768  GLN PHE ASN LEU SER GLY ALA LEU GLY THR ARG GLY THR          
SEQRES  39 A 2768  PHE ASN PHE SER GLN PHE PHE GLN GLN LEU GLY LEU ALA          
SEQRES  40 A 2768  SER PHE LEU ASN GLY GLY ARG GLN GLU ASP LEU ALA LYS          
SEQRES  41 A 2768  PRO LEU SER VAL GLY LEU ASP SER ASN SER SER THR GLY          
SEQRES  42 A 2768  THR PRO GLU ALA ALA LYS LYS ASP GLY THR MET ASN LYS          
SEQRES  43 A 2768  PRO THR VAL GLY SER PHE GLY PHE GLU ILE ASN LEU GLN          
SEQRES  44 A 2768  GLU ASN GLN ASN ALA LEU LYS PHE LEU ALA SER LEU LEU          
SEQRES  45 A 2768  GLU LEU PRO GLU PHE LEU LEU PHE LEU GLN HIS ALA ILE          
SEQRES  46 A 2768  SER VAL PRO GLU ASP VAL ALA ARG ASP LEU GLY ASP VAL          
SEQRES  47 A 2768  MET GLU THR VAL LEU SER SER GLN THR CYS GLU GLN THR          
SEQRES  48 A 2768  PRO GLU ARG LEU PHE VAL PRO SER CYS THR THR GLU GLY          
SEQRES  49 A 2768  SER TYR GLU ASP VAL GLN CYS PHE SER GLY GLU CYS TRP          
SEQRES  50 A 2768  CYS VAL ASN SER TRP GLY LYS GLU LEU PRO GLY SER ARG          
SEQRES  51 A 2768  VAL ARG GLY GLY GLN PRO ARG CYS PRO THR ASP CYS GLU          
SEQRES  52 A 2768  LYS GLN ARG ALA ARG MET GLN SER LEU MET GLY SER GLN          
SEQRES  53 A 2768  PRO ALA GLY SER THR LEU PHE VAL PRO ALA CYS THR SER          
SEQRES  54 A 2768  GLU GLY HIS PHE LEU PRO VAL GLN CYS PHE ASN SER GLU          
SEQRES  55 A 2768  CYS TYR CYS VAL ASP ALA GLU GLY GLN ALA ILE PRO GLY          
SEQRES  56 A 2768  THR ARG SER ALA ILE GLY LYS PRO LYS LYS CYS PRO THR          
SEQRES  57 A 2768  PRO CYS GLN LEU GLN SER GLU GLN ALA PHE LEU ARG THR          
SEQRES  58 A 2768  VAL GLN ALA LEU LEU SER ASN SER SER MET LEU PRO THR          
SEQRES  59 A 2768  LEU SER ASP THR TYR ILE PRO GLN CYS SER THR ASP GLY          
SEQRES  60 A 2768  GLN TRP ARG GLN VAL GLN CYS ASN GLY PRO PRO GLU GLN          
SEQRES  61 A 2768  VAL PHE GLU LEU TYR GLN ARG TRP GLU ALA GLN ASN LYS          
SEQRES  62 A 2768  GLY GLN ASP LEU THR PRO ALA LYS LEU LEU VAL LYS ILE          
SEQRES  63 A 2768  MET SER TYR ARG GLU ALA ALA SER GLY ASN PHE SER LEU          
SEQRES  64 A 2768  PHE ILE GLN SER LEU TYR GLU ALA GLY GLN GLN ASP VAL          
SEQRES  65 A 2768  PHE PRO VAL LEU SER GLN TYR PRO SER LEU GLN ASP VAL          
SEQRES  66 A 2768  PRO LEU ALA ALA LEU GLU GLY LYS ARG PRO GLN PRO ARG          
SEQRES  67 A 2768  GLU ASN ILE LEU LEU GLU PRO TYR LEU PHE TRP GLN ILE          
SEQRES  68 A 2768  LEU ASN GLY GLN LEU SER GLN TYR PRO GLY SER TYR SER          
SEQRES  69 A 2768  ASP PHE SER THR PRO LEU ALA HIS PHE ASP LEU ARG ASN          
SEQRES  70 A 2768  CYS TRP CYS VAL ASP GLU ALA GLY GLN GLU LEU GLU GLY          
SEQRES  71 A 2768  MET ARG SER GLU PRO SER LYS LEU PRO THR CYS PRO GLY          
SEQRES  72 A 2768  SER CYS GLU GLU ALA LYS LEU ARG VAL LEU GLN PHE ILE          
SEQRES  73 A 2768  ARG GLU THR GLU GLU ILE VAL SER ALA SER ASN SER SER          
SEQRES  74 A 2768  ARG PHE PRO LEU GLY GLU SER PHE LEU VAL ALA LYS GLY          
SEQRES  75 A 2768  ILE ARG LEU ARG ASN GLU ASP LEU GLY LEU PRO PRO LEU          
SEQRES  76 A 2768  PHE PRO PRO ARG GLU ALA PHE ALA GLU GLN PHE LEU ARG          
SEQRES  77 A 2768  GLY SER ASP TYR ALA ILE ARG LEU ALA ALA GLN SER THR          
SEQRES  78 A 2768  LEU SER PHE TYR GLN ARG ARG ARG PHE SER PRO ASP ASP          
SEQRES  79 A 2768  SER ALA GLY ALA SER ALA LEU LEU ARG SER GLY PRO TYR          
SEQRES  80 A 2768  MET PRO GLN CYS ASP ALA PHE GLY SER TRP GLU PRO VAL          
SEQRES  81 A 2768  GLN CYS HIS ALA GLY THR GLY HIS CYS TRP CYS VAL ASP          
SEQRES  82 A 2768  GLU LYS GLY GLY PHE ILE PRO GLY SER LEU THR ALA ARG          
SEQRES  83 A 2768  SER LEU GLN ILE PRO GLN CYS PRO THR THR CYS GLU LYS          
SEQRES  84 A 2768  SER ARG THR SER GLY LEU LEU SER SER TRP LYS GLN ALA          
SEQRES  85 A 2768  ARG SER GLN GLU ASN PRO SER PRO LYS ASP LEU PHE VAL          
SEQRES  86 A 2768  PRO ALA CYS LEU GLU THR GLY GLU TYR ALA ARG LEU GLN          
SEQRES  87 A 2768  ALA SER GLY ALA GLY THR TRP CYS VAL ASP PRO ALA SER          
SEQRES  88 A 2768  GLY GLU GLU LEU ARG PRO GLY SER SER SER SER ALA GLN          
SEQRES  89 A 2768  CYS PRO SER LEU CYS ASN VAL LEU LYS SER GLY VAL LEU          
SEQRES  90 A 2768  SER ARG ARG VAL SER PRO GLY TYR VAL PRO ALA CYS ARG          
SEQRES  91 A 2768  ALA GLU ASP GLY GLY PHE SER PRO VAL GLN CYS ASP GLN          
SEQRES  92 A 2768  ALA GLN GLY SER CYS TRP CYS VAL MET ASP SER GLY GLU          
SEQRES  93 A 2768  GLU VAL PRO GLY THR ARG VAL THR GLY GLY GLN PRO ALA          
SEQRES  94 A 2768  CYS GLU SER PRO ARG CYS PRO LEU PRO PHE ASN ALA SER          
SEQRES  95 A 2768  GLU VAL VAL GLY GLY THR ILE LEU CYS GLU THR ILE SER          
SEQRES  96 A 2768  GLY PRO THR GLY SER ALA MET GLN GLN CYS GLN LEU LEU          
SEQRES  97 A 2768  CYS ARG GLN GLY SER TRP SER VAL PHE PRO PRO GLY PRO          
SEQRES  98 A 2768  LEU ILE CYS SER LEU GLU SER GLY ARG TRP GLU SER GLN          
SEQRES  99 A 2768  LEU PRO GLN PRO ARG ALA CYS GLN ARG PRO GLN LEU TRP          
SEQRES 100 A 2768  GLN THR ILE GLN THR GLN GLY HIS PHE GLN LEU GLN LEU          
SEQRES 101 A 2768  PRO PRO GLY LYS MET CYS SER ALA ASP TYR ALA ASP LEU          
SEQRES 102 A 2768  LEU GLN THR PHE GLN VAL PHE ILE LEU ASP GLU LEU THR          
SEQRES 103 A 2768  ALA ARG GLY PHE CYS GLN ILE GLN VAL LYS THR PHE GLY          
SEQRES 104 A 2768  THR LEU VAL SER ILE PRO VAL CYS ASN ASN SER SER VAL          
SEQRES 105 A 2768  GLN VAL GLY CYS LEU THR ARG GLU ARG LEU GLY VAL ASN          
SEQRES 106 A 2768  VAL THR TRP LYS SER ARG LEU GLU ASP ILE PRO VAL ALA          
SEQRES 107 A 2768  SER LEU PRO ASP LEU HIS ASP ILE GLU ARG ALA LEU VAL          
SEQRES 108 A 2768  GLY LYS ASP LEU LEU GLY ARG PHE THR ASP LEU ILE GLN          
SEQRES 109 A 2768  SER GLY SER PHE GLN LEU HIS LEU ASP SER LYS THR PHE          
SEQRES 110 A 2768  PRO ALA GLU THR ILE ARG PHE LEU GLN GLY ASP HIS PHE          
SEQRES 111 A 2768  GLY THR SER PRO ARG THR TRP PHE GLY CYS SER GLU GLY          
SEQRES 112 A 2768  PHE TYR GLN VAL LEU THR SER GLU ALA SER GLN ASP GLY          
SEQRES 113 A 2768  LEU GLY CYS VAL LYS CYS PRO GLU GLY SER TYR SER GLN          
SEQRES 114 A 2768  ASP GLU GLU CYS ILE PRO CYS PRO VAL GLY PHE TYR GLN          
SEQRES 115 A 2768  GLU GLN ALA GLY SER LEU ALA CYS VAL PRO CYS PRO VAL          
SEQRES 116 A 2768  GLY ARG THR THR ILE SER ALA GLY ALA PHE SER GLN THR          
SEQRES 117 A 2768  HIS CYS VAL THR ASP CYS GLN ARG ASN GLU ALA GLY LEU          
SEQRES 118 A 2768  GLN CYS ASP GLN ASN GLY GLN TYR ARG ALA SER GLN LYS          
SEQRES 119 A 2768  ASP ARG GLY SER GLY LYS ALA PHE CYS VAL ASP GLY GLU          
SEQRES 120 A 2768  GLY ARG ARG LEU PRO TRP TRP GLU THR GLU ALA PRO LEU          
SEQRES 121 A 2768  GLU ASP SER GLN CYS LEU MET MET GLN LYS PHE GLU LYS          
SEQRES 122 A 2768  VAL PRO GLU SER LYS VAL ILE PHE ASP ALA ASN ALA PRO          
SEQRES 123 A 2768  VAL ALA VAL ARG SER LYS VAL PRO ASP SER GLU PHE PRO          
SEQRES 124 A 2768  VAL MET GLN CYS LEU THR ASP CYS THR GLU ASP GLU ALA          
SEQRES 125 A 2768  CYS SER PHE PHE THR VAL SER THR THR GLU PRO GLU ILE          
SEQRES 126 A 2768  SER CYS ASP PHE TYR ALA TRP THR SER ASP ASN VAL ALA          
SEQRES 127 A 2768  CYS MET THR SER ASP GLN LYS ARG ASP ALA LEU GLY ASN          
SEQRES 128 A 2768  SER LYS ALA THR SER PHE GLY SER LEU ARG CYS GLN VAL          
SEQRES 129 A 2768  LYS VAL ARG SER HIS GLY GLN ASP SER PRO ALA VAL TYR          
SEQRES 130 A 2768  LEU LYS LYS GLY GLN GLY SER THR THR THR LEU GLN LYS          
SEQRES 131 A 2768  ARG PHE GLU PRO THR GLY PHE GLN ASN MET LEU SER GLY          
SEQRES 132 A 2768  LEU TYR ASN PRO ILE VAL PHE SER ALA SER GLY ALA ASN          
SEQRES 133 A 2768  LEU THR ASP ALA HIS LEU PHE CYS LEU LEU ALA CYS ASP          
SEQRES 134 A 2768  ARG ASP LEU CYS CYS ASP GLY PHE VAL LEU THR GLN VAL          
SEQRES 135 A 2768  GLN GLY GLY ALA ILE ILE CYS GLY LEU LEU SER SER PRO          
SEQRES 136 A 2768  SER VAL LEU LEU CYS ASN VAL LYS ASP TRP MET ASP PRO          
SEQRES 137 A 2768  SER GLU ALA TRP ALA ASN ALA THR CYS PRO GLY VAL THR          
SEQRES 138 A 2768  TYR ASP GLN GLU SER HIS GLN VAL ILE LEU ARG LEU GLY          
SEQRES 139 A 2768  ASP GLN GLU PHE ILE LYS SER LEU THR PRO LEU GLU GLY          
SEQRES 140 A 2768  THR GLN ASP THR PHE THR ASN PHE GLN GLN VAL TYR LEU          
SEQRES 141 A 2768  TRP LYS ASP SER ASP MET GLY SER ARG PRO GLU SER MET          
SEQRES 142 A 2768  GLY CYS ARG LYS ASP THR VAL PRO ARG PRO ALA SER PRO          
SEQRES 143 A 2768  THR GLU ALA GLY LEU THR THR GLU LEU PHE SER PRO VAL          
SEQRES 144 A 2768  ASP LEU ASN GLN VAL ILE VAL ASN GLY ASN GLN SER LEU          
SEQRES 145 A 2768  SER SER GLN LYS HIS TRP LEU PHE LYS HIS LEU PHE SER          
SEQRES 146 A 2768  ALA GLN GLN ALA ASN LEU TRP CYS LEU SER ARG CYS VAL          
SEQRES 147 A 2768  GLN GLU HIS SER PHE CYS GLN LEU ALA GLU ILE THR GLU          
SEQRES 148 A 2768  SER ALA SER LEU TYR PHE THR CYS THR LEU TYR PRO GLU          
SEQRES 149 A 2768  ALA GLN VAL CYS ASP ASP ILE MET GLU SER ASN ALA GLN          
SEQRES 150 A 2768  GLY CYS ARG LEU ILE LEU PRO GLN MET PRO LYS ALA LEU          
SEQRES 151 A 2768  PHE ARG LYS LYS VAL ILE LEU GLU ASP LYS VAL LYS ASN          
SEQRES 152 A 2768  PHE TYR THR ARG LEU PRO PHE GLN LYS LEU MET GLY ILE          
SEQRES 153 A 2768  SER ILE ARG ASN LYS VAL PRO MET SER GLU LYS SER ILE          
SEQRES 154 A 2768  SER ASN GLY PHE PHE GLU CYS GLU ARG ARG CYS ASP ALA          
SEQRES 155 A 2768  ASP PRO CYS CYS THR GLY PHE GLY PHE LEU ASN VAL SER          
SEQRES 156 A 2768  GLN LEU LYS GLY GLY GLU VAL THR CYS LEU THR LEU ASN          
SEQRES 157 A 2768  SER LEU GLY ILE GLN MET CYS SER GLU GLU ASN GLY GLY          
SEQRES 158 A 2768  ALA TRP ARG ILE LEU ASP CYS GLY SER PRO ASP ILE GLU          
SEQRES 159 A 2768  VAL HIS THR TYR PRO PHE GLY TRP TYR GLN LYS PRO ILE          
SEQRES 160 A 2768  ALA GLN ASN ASN ALA PRO SER PHE CYS PRO LEU VAL VAL          
SEQRES 161 A 2768  LEU PRO SER LEU THR GLU LYS VAL SER LEU ASP SER TRP          
SEQRES 162 A 2768  GLN SER LEU ALA LEU SER SER VAL VAL VAL ASP PRO SER          
SEQRES 163 A 2768  ILE ARG HIS PHE ASP VAL ALA HIS VAL SER THR ALA ALA          
SEQRES 164 A 2768  THR SER ASN PHE SER ALA VAL ARG ASP LEU CYS LEU SER          
SEQRES 165 A 2768  GLU CYS SER GLN HIS GLU ALA CYS LEU ILE THR THR LEU          
SEQRES 166 A 2768  GLN THR GLN PRO GLY ALA VAL ARG CYS MET PHE TYR ALA          
SEQRES 167 A 2768  ASP THR GLN SER CYS THR HIS SER LEU GLN GLY GLN ASN          
SEQRES 168 A 2768  CYS ARG LEU LEU LEU ARG GLU GLU ALA THR HIS ILE TYR          
SEQRES 169 A 2768  ARG LYS PRO GLY ILE SER LEU LEU SER TYR GLU ALA SER          
SEQRES 170 A 2768  VAL PRO SER VAL PRO ILE SER THR HIS GLY ARG LEU LEU          
SEQRES 171 A 2768  GLY ARG SER GLN ALA ILE GLN VAL GLY THR SER TRP LYS          
SEQRES 172 A 2768  GLN VAL ASP GLN PHE LEU GLY VAL PRO TYR ALA ALA PRO          
SEQRES 173 A 2768  PRO LEU ALA GLU ARG ARG PHE GLN ALA PRO GLU PRO LEU          
SEQRES 174 A 2768  ASN TRP THR GLY SER TRP ASP ALA SER LYS PRO ARG ALA          
SEQRES 175 A 2768  SER CYS TRP GLN PRO GLY THR ARG THR SER THR SER PRO          
SEQRES 176 A 2768  GLY VAL SER GLU ASP CYS LEU TYR LEU ASN VAL PHE ILE          
SEQRES 177 A 2768  PRO GLN ASN VAL ALA PRO ASN ALA SER VAL LEU VAL PHE          
SEQRES 178 A 2768  PHE HIS ASN THR MET ASP ARG GLU GLU SER GLU GLY TRP          
SEQRES 179 A 2768  PRO ALA ILE ASP GLY SER PHE LEU ALA ALA VAL GLY ASN          
SEQRES 180 A 2768  LEU ILE VAL VAL THR ALA SER TYR ARG VAL GLY VAL PHE          
SEQRES 181 A 2768  GLY PHE LEU SER SER GLY SER GLY GLU VAL SER GLY ASN          
SEQRES 182 A 2768  TRP GLY LEU LEU ASP GLN VAL ALA ALA LEU THR TRP VAL          
SEQRES 183 A 2768  GLN THR HIS ILE ARG GLY PHE GLY GLY ASP PRO ARG ARG          
SEQRES 184 A 2768  VAL SER LEU ALA ALA ASP ARG GLY GLY ALA ASP VAL ALA          
SEQRES 185 A 2768  SER ILE HIS LEU LEU THR ALA ARG ALA THR ASN SER GLN          
SEQRES 186 A 2768  LEU PHE ARG ARG ALA VAL LEU MET GLY GLY SER ALA LEU          
SEQRES 187 A 2768  SER PRO ALA ALA VAL ILE SER HIS GLU ARG ALA GLN GLN          
SEQRES 188 A 2768  GLN ALA ILE ALA LEU ALA LYS GLU VAL SER CYS PRO MET          
SEQRES 189 A 2768  SER SER SER GLN GLU VAL VAL SER CYS LEU ARG GLN LYS          
SEQRES 190 A 2768  PRO ALA ASN VAL LEU ASN ASP ALA GLN THR LYS LEU LEU          
SEQRES 191 A 2768  ALA VAL SER GLY PRO PHE HIS TYR TRP GLY PRO VAL ILE          
SEQRES 192 A 2768  ASP GLY HIS PHE LEU ARG GLU PRO PRO ALA ARG ALA LEU          
SEQRES 193 A 2768  LYS ARG SER LEU TRP VAL GLU VAL ASP LEU LEU ILE GLY          
SEQRES 194 A 2768  SER SER GLN ASP ASP GLY LEU ILE ASN ARG ALA LYS ALA          
SEQRES 195 A 2768  VAL LYS GLN PHE GLU GLU SER ARG GLY ARG THR SER SER          
SEQRES 196 A 2768  LYS THR ALA PHE TYR GLN ALA LEU GLN ASN SER LEU GLY          
SEQRES 197 A 2768  GLY GLU ASP SER ASP ALA ARG VAL GLU ALA ALA ALA THR          
SEQRES 198 A 2768  TRP TYR TYR SER LEU GLU HIS SER THR ASP ASP TYR ALA          
SEQRES 199 A 2768  SER PHE SER ARG ALA LEU GLU ASN ALA THR ARG ASP TYR          
SEQRES 200 A 2768  PHE ILE ILE CYS PRO ILE ILE ASP MET ALA SER ALA TRP          
SEQRES 201 A 2768  ALA LYS ARG ALA ARG GLY ASN VAL PHE MET TYR HIS ALA          
SEQRES 202 A 2768  PRO GLU ASN TYR GLY HIS GLY SER LEU GLU LEU LEU ALA          
SEQRES 203 A 2768  ASP VAL GLN PHE ALA LEU GLY LEU PRO PHE TYR PRO ALA          
SEQRES 204 A 2768  TYR GLU GLY GLN PHE SER LEU GLU GLU LYS SER LEU SER          
SEQRES 205 A 2768  LEU LYS ILE MET GLN TYR PHE SER HIS PHE ILE ARG SER          
SEQRES 206 A 2768  GLY ASN PRO ASN TYR PRO TYR GLU PHE SER ARG LYS VAL          
SEQRES 207 A 2768  PRO THR PHE ALA THR PRO TRP PRO ASP PHE VAL PRO ARG          
SEQRES 208 A 2768  ALA GLY GLY GLU ASN TYR LYS GLU PHE SER GLU LEU LEU          
SEQRES 209 A 2768  PRO ASN ARG GLN GLY LEU LYS LYS ALA ASP CYS SER PHE          
SEQRES 210 A 2768  TRP SER LYS TYR ILE SER SER LEU LYS THR SER ALA ASP          
SEQRES 211 A 2768  GLY ALA LYS GLY GLY GLN SER ALA GLU SER GLU GLU GLU          
SEQRES 212 A 2768  GLU LEU THR ALA GLY SER GLY LEU ARG GLU ASP LEU LEU          
SEQRES 213 A 2768  SER LEU GLN GLU PRO GLY SER LYS THR TYR SER LYS              
SEQRES   1 B 2768  MET ALA LEU VAL LEU GLU ILE PHE THR LEU LEU ALA SER          
SEQRES   2 B 2768  ILE CYS TRP VAL SER ALA ASN ILE PHE GLU TYR GLN VAL          
SEQRES   3 B 2768  ASP ALA GLN PRO LEU ARG PRO CYS GLU LEU GLN ARG GLU          
SEQRES   4 B 2768  THR ALA PHE LEU LYS GLN ALA ASP TYR VAL PRO GLN CYS          
SEQRES   5 B 2768  ALA GLU ASP GLY SER PHE GLN THR VAL GLN CYS GLN ASN          
SEQRES   6 B 2768  ASP GLY ARG SER CYS TRP CYS VAL GLY ALA ASN GLY SER          
SEQRES   7 B 2768  GLU VAL LEU GLY SER ARG GLN PRO GLY ARG PRO VAL ALA          
SEQRES   8 B 2768  CYS LEU SER PHE CYS GLN LEU GLN LYS GLN GLN ILE LEU          
SEQRES   9 B 2768  LEU SER GLY TYR ILE ASN SER THR ASP THR SER TYR LEU          
SEQRES  10 B 2768  PRO GLN CYS GLN ASP SER GLY ASP TYR ALA PRO VAL GLN          
SEQRES  11 B 2768  CYS ASP VAL GLN GLN VAL GLN CYS TRP CYS VAL ASP ALA          
SEQRES  12 B 2768  GLU GLY MET GLU VAL TYR GLY THR ARG GLN LEU GLY ARG          
SEQRES  13 B 2768  PRO LYS ARG CYS PRO ARG SER CYS GLU ILE ARG ASN ARG          
SEQRES  14 B 2768  ARG LEU LEU HIS GLY VAL GLY ASP LYS SER PRO PRO GLN          
SEQRES  15 B 2768  CYS SER ALA GLU GLY GLU PHE MET PRO VAL GLN CYS LYS          
SEQRES  16 B 2768  PHE VAL ASN THR THR ASP MET MET ILE PHE ASP LEU VAL          
SEQRES  17 B 2768  HIS SER TYR ASN ARG PHE PRO ASP ALA PHE VAL THR PHE          
SEQRES  18 B 2768  SER SER PHE GLN ARG ARG PHE PRO GLU VAL SER GLY TYR          
SEQRES  19 B 2768  CYS HIS CYS ALA ASP SER GLN GLY ARG GLU LEU ALA GLU          
SEQRES  20 B 2768  THR GLY LEU GLU LEU LEU LEU ASP GLU ILE TYR ASP THR          
SEQRES  21 B 2768  ILE PHE ALA GLY LEU ASP LEU PRO SER THR PHE THR GLU          
SEQRES  22 B 2768  THR THR LEU TYR ARG ILE LEU GLN ARG ARG PHE LEU ALA          
SEQRES  23 B 2768  VAL GLN SER VAL ILE SER GLY ARG PHE ARG CYS PRO THR          
SEQRES  24 B 2768  LYS CYS GLU VAL GLU ARG PHE THR ALA THR SER PHE GLY          
SEQRES  25 B 2768  HIS PRO TYR VAL PRO SER CYS ARG ARG ASN GLY ASP TYR          
SEQRES  26 B 2768  GLN ALA VAL GLN CYS GLN THR GLU GLY PRO CYS TRP CYS          
SEQRES  27 B 2768  VAL ASP ALA GLN GLY LYS GLU MET HIS GLY THR ARG GLN          
SEQRES  28 B 2768  GLN GLY GLU PRO PRO SER CYS ALA GLU GLY GLN SER CYS          
SEQRES  29 B 2768  ALA SER GLU ARG GLN GLN ALA LEU SER ARG LEU TYR PHE          
SEQRES  30 B 2768  GLY THR SER GLY TYR PHE SER GLN HIS ASP LEU PHE SER          
SEQRES  31 B 2768  SER PRO GLU LYS ARG TRP ALA SER PRO ARG VAL ALA ARG          
SEQRES  32 B 2768  PHE ALA THR SER CYS PRO PRO THR ILE LYS GLU LEU PHE          
SEQRES  33 B 2768  VAL ASP SER GLY LEU LEU ARG PRO MET VAL GLU GLY GLN          
SEQRES  34 B 2768  SER GLN GLN PHE SER VAL SER GLU ASN LEU LEU LYS GLU          
SEQRES  35 B 2768  ALA ILE ARG ALA ILE PHE PRO SER ARG GLY LEU ALA ARG          
SEQRES  36 B 2768  LEU ALA LEU GLN PHE THR THR ASN PRO LYS ARG LEU GLN          
SEQRES  37 B 2768  GLN ASN LEU PHE GLY GLY LYS PHE LEU VAL ASN VAL GLY          
SEQRES  38 B 2768  GLN PHE ASN LEU SER GLY ALA LEU GLY THR ARG GLY THR          
SEQRES  39 B 2768  PHE ASN PHE SER GLN PHE PHE GLN GLN LEU GLY LEU ALA          
SEQRES  40 B 2768  SER PHE LEU ASN GLY GLY ARG GLN GLU ASP LEU ALA LYS          
SEQRES  41 B 2768  PRO LEU SER VAL GLY LEU ASP SER ASN SER SER THR GLY          
SEQRES  42 B 2768  THR PRO GLU ALA ALA LYS LYS ASP GLY THR MET ASN LYS          
SEQRES  43 B 2768  PRO THR VAL GLY SER PHE GLY PHE GLU ILE ASN LEU GLN          
SEQRES  44 B 2768  GLU ASN GLN ASN ALA LEU LYS PHE LEU ALA SER LEU LEU          
SEQRES  45 B 2768  GLU LEU PRO GLU PHE LEU LEU PHE LEU GLN HIS ALA ILE          
SEQRES  46 B 2768  SER VAL PRO GLU ASP VAL ALA ARG ASP LEU GLY ASP VAL          
SEQRES  47 B 2768  MET GLU THR VAL LEU SER SER GLN THR CYS GLU GLN THR          
SEQRES  48 B 2768  PRO GLU ARG LEU PHE VAL PRO SER CYS THR THR GLU GLY          
SEQRES  49 B 2768  SER TYR GLU ASP VAL GLN CYS PHE SER GLY GLU CYS TRP          
SEQRES  50 B 2768  CYS VAL ASN SER TRP GLY LYS GLU LEU PRO GLY SER ARG          
SEQRES  51 B 2768  VAL ARG GLY GLY GLN PRO ARG CYS PRO THR ASP CYS GLU          
SEQRES  52 B 2768  LYS GLN ARG ALA ARG MET GLN SER LEU MET GLY SER GLN          
SEQRES  53 B 2768  PRO ALA GLY SER THR LEU PHE VAL PRO ALA CYS THR SER          
SEQRES  54 B 2768  GLU GLY HIS PHE LEU PRO VAL GLN CYS PHE ASN SER GLU          
SEQRES  55 B 2768  CYS TYR CYS VAL ASP ALA GLU GLY GLN ALA ILE PRO GLY          
SEQRES  56 B 2768  THR ARG SER ALA ILE GLY LYS PRO LYS LYS CYS PRO THR          
SEQRES  57 B 2768  PRO CYS GLN LEU GLN SER GLU GLN ALA PHE LEU ARG THR          
SEQRES  58 B 2768  VAL GLN ALA LEU LEU SER ASN SER SER MET LEU PRO THR          
SEQRES  59 B 2768  LEU SER ASP THR TYR ILE PRO GLN CYS SER THR ASP GLY          
SEQRES  60 B 2768  GLN TRP ARG GLN VAL GLN CYS ASN GLY PRO PRO GLU GLN          
SEQRES  61 B 2768  VAL PHE GLU LEU TYR GLN ARG TRP GLU ALA GLN ASN LYS          
SEQRES  62 B 2768  GLY GLN ASP LEU THR PRO ALA LYS LEU LEU VAL LYS ILE          
SEQRES  63 B 2768  MET SER TYR ARG GLU ALA ALA SER GLY ASN PHE SER LEU          
SEQRES  64 B 2768  PHE ILE GLN SER LEU TYR GLU ALA GLY GLN GLN ASP VAL          
SEQRES  65 B 2768  PHE PRO VAL LEU SER GLN TYR PRO SER LEU GLN ASP VAL          
SEQRES  66 B 2768  PRO LEU ALA ALA LEU GLU GLY LYS ARG PRO GLN PRO ARG          
SEQRES  67 B 2768  GLU ASN ILE LEU LEU GLU PRO TYR LEU PHE TRP GLN ILE          
SEQRES  68 B 2768  LEU ASN GLY GLN LEU SER GLN TYR PRO GLY SER TYR SER          
SEQRES  69 B 2768  ASP PHE SER THR PRO LEU ALA HIS PHE ASP LEU ARG ASN          
SEQRES  70 B 2768  CYS TRP CYS VAL ASP GLU ALA GLY GLN GLU LEU GLU GLY          
SEQRES  71 B 2768  MET ARG SER GLU PRO SER LYS LEU PRO THR CYS PRO GLY          
SEQRES  72 B 2768  SER CYS GLU GLU ALA LYS LEU ARG VAL LEU GLN PHE ILE          
SEQRES  73 B 2768  ARG GLU THR GLU GLU ILE VAL SER ALA SER ASN SER SER          
SEQRES  74 B 2768  ARG PHE PRO LEU GLY GLU SER PHE LEU VAL ALA LYS GLY          
SEQRES  75 B 2768  ILE ARG LEU ARG ASN GLU ASP LEU GLY LEU PRO PRO LEU          
SEQRES  76 B 2768  PHE PRO PRO ARG GLU ALA PHE ALA GLU GLN PHE LEU ARG          
SEQRES  77 B 2768  GLY SER ASP TYR ALA ILE ARG LEU ALA ALA GLN SER THR          
SEQRES  78 B 2768  LEU SER PHE TYR GLN ARG ARG ARG PHE SER PRO ASP ASP          
SEQRES  79 B 2768  SER ALA GLY ALA SER ALA LEU LEU ARG SER GLY PRO TYR          
SEQRES  80 B 2768  MET PRO GLN CYS ASP ALA PHE GLY SER TRP GLU PRO VAL          
SEQRES  81 B 2768  GLN CYS HIS ALA GLY THR GLY HIS CYS TRP CYS VAL ASP          
SEQRES  82 B 2768  GLU LYS GLY GLY PHE ILE PRO GLY SER LEU THR ALA ARG          
SEQRES  83 B 2768  SER LEU GLN ILE PRO GLN CYS PRO THR THR CYS GLU LYS          
SEQRES  84 B 2768  SER ARG THR SER GLY LEU LEU SER SER TRP LYS GLN ALA          
SEQRES  85 B 2768  ARG SER GLN GLU ASN PRO SER PRO LYS ASP LEU PHE VAL          
SEQRES  86 B 2768  PRO ALA CYS LEU GLU THR GLY GLU TYR ALA ARG LEU GLN          
SEQRES  87 B 2768  ALA SER GLY ALA GLY THR TRP CYS VAL ASP PRO ALA SER          
SEQRES  88 B 2768  GLY GLU GLU LEU ARG PRO GLY SER SER SER SER ALA GLN          
SEQRES  89 B 2768  CYS PRO SER LEU CYS ASN VAL LEU LYS SER GLY VAL LEU          
SEQRES  90 B 2768  SER ARG ARG VAL SER PRO GLY TYR VAL PRO ALA CYS ARG          
SEQRES  91 B 2768  ALA GLU ASP GLY GLY PHE SER PRO VAL GLN CYS ASP GLN          
SEQRES  92 B 2768  ALA GLN GLY SER CYS TRP CYS VAL MET ASP SER GLY GLU          
SEQRES  93 B 2768  GLU VAL PRO GLY THR ARG VAL THR GLY GLY GLN PRO ALA          
SEQRES  94 B 2768  CYS GLU SER PRO ARG CYS PRO LEU PRO PHE ASN ALA SER          
SEQRES  95 B 2768  GLU VAL VAL GLY GLY THR ILE LEU CYS GLU THR ILE SER          
SEQRES  96 B 2768  GLY PRO THR GLY SER ALA MET GLN GLN CYS GLN LEU LEU          
SEQRES  97 B 2768  CYS ARG GLN GLY SER TRP SER VAL PHE PRO PRO GLY PRO          
SEQRES  98 B 2768  LEU ILE CYS SER LEU GLU SER GLY ARG TRP GLU SER GLN          
SEQRES  99 B 2768  LEU PRO GLN PRO ARG ALA CYS GLN ARG PRO GLN LEU TRP          
SEQRES 100 B 2768  GLN THR ILE GLN THR GLN GLY HIS PHE GLN LEU GLN LEU          
SEQRES 101 B 2768  PRO PRO GLY LYS MET CYS SER ALA ASP TYR ALA ASP LEU          
SEQRES 102 B 2768  LEU GLN THR PHE GLN VAL PHE ILE LEU ASP GLU LEU THR          
SEQRES 103 B 2768  ALA ARG GLY PHE CYS GLN ILE GLN VAL LYS THR PHE GLY          
SEQRES 104 B 2768  THR LEU VAL SER ILE PRO VAL CYS ASN ASN SER SER VAL          
SEQRES 105 B 2768  GLN VAL GLY CYS LEU THR ARG GLU ARG LEU GLY VAL ASN          
SEQRES 106 B 2768  VAL THR TRP LYS SER ARG LEU GLU ASP ILE PRO VAL ALA          
SEQRES 107 B 2768  SER LEU PRO ASP LEU HIS ASP ILE GLU ARG ALA LEU VAL          
SEQRES 108 B 2768  GLY LYS ASP LEU LEU GLY ARG PHE THR ASP LEU ILE GLN          
SEQRES 109 B 2768  SER GLY SER PHE GLN LEU HIS LEU ASP SER LYS THR PHE          
SEQRES 110 B 2768  PRO ALA GLU THR ILE ARG PHE LEU GLN GLY ASP HIS PHE          
SEQRES 111 B 2768  GLY THR SER PRO ARG THR TRP PHE GLY CYS SER GLU GLY          
SEQRES 112 B 2768  PHE TYR GLN VAL LEU THR SER GLU ALA SER GLN ASP GLY          
SEQRES 113 B 2768  LEU GLY CYS VAL LYS CYS PRO GLU GLY SER TYR SER GLN          
SEQRES 114 B 2768  ASP GLU GLU CYS ILE PRO CYS PRO VAL GLY PHE TYR GLN          
SEQRES 115 B 2768  GLU GLN ALA GLY SER LEU ALA CYS VAL PRO CYS PRO VAL          
SEQRES 116 B 2768  GLY ARG THR THR ILE SER ALA GLY ALA PHE SER GLN THR          
SEQRES 117 B 2768  HIS CYS VAL THR ASP CYS GLN ARG ASN GLU ALA GLY LEU          
SEQRES 118 B 2768  GLN CYS ASP GLN ASN GLY GLN TYR ARG ALA SER GLN LYS          
SEQRES 119 B 2768  ASP ARG GLY SER GLY LYS ALA PHE CYS VAL ASP GLY GLU          
SEQRES 120 B 2768  GLY ARG ARG LEU PRO TRP TRP GLU THR GLU ALA PRO LEU          
SEQRES 121 B 2768  GLU ASP SER GLN CYS LEU MET MET GLN LYS PHE GLU LYS          
SEQRES 122 B 2768  VAL PRO GLU SER LYS VAL ILE PHE ASP ALA ASN ALA PRO          
SEQRES 123 B 2768  VAL ALA VAL ARG SER LYS VAL PRO ASP SER GLU PHE PRO          
SEQRES 124 B 2768  VAL MET GLN CYS LEU THR ASP CYS THR GLU ASP GLU ALA          
SEQRES 125 B 2768  CYS SER PHE PHE THR VAL SER THR THR GLU PRO GLU ILE          
SEQRES 126 B 2768  SER CYS ASP PHE TYR ALA TRP THR SER ASP ASN VAL ALA          
SEQRES 127 B 2768  CYS MET THR SER ASP GLN LYS ARG ASP ALA LEU GLY ASN          
SEQRES 128 B 2768  SER LYS ALA THR SER PHE GLY SER LEU ARG CYS GLN VAL          
SEQRES 129 B 2768  LYS VAL ARG SER HIS GLY GLN ASP SER PRO ALA VAL TYR          
SEQRES 130 B 2768  LEU LYS LYS GLY GLN GLY SER THR THR THR LEU GLN LYS          
SEQRES 131 B 2768  ARG PHE GLU PRO THR GLY PHE GLN ASN MET LEU SER GLY          
SEQRES 132 B 2768  LEU TYR ASN PRO ILE VAL PHE SER ALA SER GLY ALA ASN          
SEQRES 133 B 2768  LEU THR ASP ALA HIS LEU PHE CYS LEU LEU ALA CYS ASP          
SEQRES 134 B 2768  ARG ASP LEU CYS CYS ASP GLY PHE VAL LEU THR GLN VAL          
SEQRES 135 B 2768  GLN GLY GLY ALA ILE ILE CYS GLY LEU LEU SER SER PRO          
SEQRES 136 B 2768  SER VAL LEU LEU CYS ASN VAL LYS ASP TRP MET ASP PRO          
SEQRES 137 B 2768  SER GLU ALA TRP ALA ASN ALA THR CYS PRO GLY VAL THR          
SEQRES 138 B 2768  TYR ASP GLN GLU SER HIS GLN VAL ILE LEU ARG LEU GLY          
SEQRES 139 B 2768  ASP GLN GLU PHE ILE LYS SER LEU THR PRO LEU GLU GLY          
SEQRES 140 B 2768  THR GLN ASP THR PHE THR ASN PHE GLN GLN VAL TYR LEU          
SEQRES 141 B 2768  TRP LYS ASP SER ASP MET GLY SER ARG PRO GLU SER MET          
SEQRES 142 B 2768  GLY CYS ARG LYS ASP THR VAL PRO ARG PRO ALA SER PRO          
SEQRES 143 B 2768  THR GLU ALA GLY LEU THR THR GLU LEU PHE SER PRO VAL          
SEQRES 144 B 2768  ASP LEU ASN GLN VAL ILE VAL ASN GLY ASN GLN SER LEU          
SEQRES 145 B 2768  SER SER GLN LYS HIS TRP LEU PHE LYS HIS LEU PHE SER          
SEQRES 146 B 2768  ALA GLN GLN ALA ASN LEU TRP CYS LEU SER ARG CYS VAL          
SEQRES 147 B 2768  GLN GLU HIS SER PHE CYS GLN LEU ALA GLU ILE THR GLU          
SEQRES 148 B 2768  SER ALA SER LEU TYR PHE THR CYS THR LEU TYR PRO GLU          
SEQRES 149 B 2768  ALA GLN VAL CYS ASP ASP ILE MET GLU SER ASN ALA GLN          
SEQRES 150 B 2768  GLY CYS ARG LEU ILE LEU PRO GLN MET PRO LYS ALA LEU          
SEQRES 151 B 2768  PHE ARG LYS LYS VAL ILE LEU GLU ASP LYS VAL LYS ASN          
SEQRES 152 B 2768  PHE TYR THR ARG LEU PRO PHE GLN LYS LEU MET GLY ILE          
SEQRES 153 B 2768  SER ILE ARG ASN LYS VAL PRO MET SER GLU LYS SER ILE          
SEQRES 154 B 2768  SER ASN GLY PHE PHE GLU CYS GLU ARG ARG CYS ASP ALA          
SEQRES 155 B 2768  ASP PRO CYS CYS THR GLY PHE GLY PHE LEU ASN VAL SER          
SEQRES 156 B 2768  GLN LEU LYS GLY GLY GLU VAL THR CYS LEU THR LEU ASN          
SEQRES 157 B 2768  SER LEU GLY ILE GLN MET CYS SER GLU GLU ASN GLY GLY          
SEQRES 158 B 2768  ALA TRP ARG ILE LEU ASP CYS GLY SER PRO ASP ILE GLU          
SEQRES 159 B 2768  VAL HIS THR TYR PRO PHE GLY TRP TYR GLN LYS PRO ILE          
SEQRES 160 B 2768  ALA GLN ASN ASN ALA PRO SER PHE CYS PRO LEU VAL VAL          
SEQRES 161 B 2768  LEU PRO SER LEU THR GLU LYS VAL SER LEU ASP SER TRP          
SEQRES 162 B 2768  GLN SER LEU ALA LEU SER SER VAL VAL VAL ASP PRO SER          
SEQRES 163 B 2768  ILE ARG HIS PHE ASP VAL ALA HIS VAL SER THR ALA ALA          
SEQRES 164 B 2768  THR SER ASN PHE SER ALA VAL ARG ASP LEU CYS LEU SER          
SEQRES 165 B 2768  GLU CYS SER GLN HIS GLU ALA CYS LEU ILE THR THR LEU          
SEQRES 166 B 2768  GLN THR GLN PRO GLY ALA VAL ARG CYS MET PHE TYR ALA          
SEQRES 167 B 2768  ASP THR GLN SER CYS THR HIS SER LEU GLN GLY GLN ASN          
SEQRES 168 B 2768  CYS ARG LEU LEU LEU ARG GLU GLU ALA THR HIS ILE TYR          
SEQRES 169 B 2768  ARG LYS PRO GLY ILE SER LEU LEU SER TYR GLU ALA SER          
SEQRES 170 B 2768  VAL PRO SER VAL PRO ILE SER THR HIS GLY ARG LEU LEU          
SEQRES 171 B 2768  GLY ARG SER GLN ALA ILE GLN VAL GLY THR SER TRP LYS          
SEQRES 172 B 2768  GLN VAL ASP GLN PHE LEU GLY VAL PRO TYR ALA ALA PRO          
SEQRES 173 B 2768  PRO LEU ALA GLU ARG ARG PHE GLN ALA PRO GLU PRO LEU          
SEQRES 174 B 2768  ASN TRP THR GLY SER TRP ASP ALA SER LYS PRO ARG ALA          
SEQRES 175 B 2768  SER CYS TRP GLN PRO GLY THR ARG THR SER THR SER PRO          
SEQRES 176 B 2768  GLY VAL SER GLU ASP CYS LEU TYR LEU ASN VAL PHE ILE          
SEQRES 177 B 2768  PRO GLN ASN VAL ALA PRO ASN ALA SER VAL LEU VAL PHE          
SEQRES 178 B 2768  PHE HIS ASN THR MET ASP ARG GLU GLU SER GLU GLY TRP          
SEQRES 179 B 2768  PRO ALA ILE ASP GLY SER PHE LEU ALA ALA VAL GLY ASN          
SEQRES 180 B 2768  LEU ILE VAL VAL THR ALA SER TYR ARG VAL GLY VAL PHE          
SEQRES 181 B 2768  GLY PHE LEU SER SER GLY SER GLY GLU VAL SER GLY ASN          
SEQRES 182 B 2768  TRP GLY LEU LEU ASP GLN VAL ALA ALA LEU THR TRP VAL          
SEQRES 183 B 2768  GLN THR HIS ILE ARG GLY PHE GLY GLY ASP PRO ARG ARG          
SEQRES 184 B 2768  VAL SER LEU ALA ALA ASP ARG GLY GLY ALA ASP VAL ALA          
SEQRES 185 B 2768  SER ILE HIS LEU LEU THR ALA ARG ALA THR ASN SER GLN          
SEQRES 186 B 2768  LEU PHE ARG ARG ALA VAL LEU MET GLY GLY SER ALA LEU          
SEQRES 187 B 2768  SER PRO ALA ALA VAL ILE SER HIS GLU ARG ALA GLN GLN          
SEQRES 188 B 2768  GLN ALA ILE ALA LEU ALA LYS GLU VAL SER CYS PRO MET          
SEQRES 189 B 2768  SER SER SER GLN GLU VAL VAL SER CYS LEU ARG GLN LYS          
SEQRES 190 B 2768  PRO ALA ASN VAL LEU ASN ASP ALA GLN THR LYS LEU LEU          
SEQRES 191 B 2768  ALA VAL SER GLY PRO PHE HIS TYR TRP GLY PRO VAL ILE          
SEQRES 192 B 2768  ASP GLY HIS PHE LEU ARG GLU PRO PRO ALA ARG ALA LEU          
SEQRES 193 B 2768  LYS ARG SER LEU TRP VAL GLU VAL ASP LEU LEU ILE GLY          
SEQRES 194 B 2768  SER SER GLN ASP ASP GLY LEU ILE ASN ARG ALA LYS ALA          
SEQRES 195 B 2768  VAL LYS GLN PHE GLU GLU SER ARG GLY ARG THR SER SER          
SEQRES 196 B 2768  LYS THR ALA PHE TYR GLN ALA LEU GLN ASN SER LEU GLY          
SEQRES 197 B 2768  GLY GLU ASP SER ASP ALA ARG VAL GLU ALA ALA ALA THR          
SEQRES 198 B 2768  TRP TYR TYR SER LEU GLU HIS SER THR ASP ASP TYR ALA          
SEQRES 199 B 2768  SER PHE SER ARG ALA LEU GLU ASN ALA THR ARG ASP TYR          
SEQRES 200 B 2768  PHE ILE ILE CYS PRO ILE ILE ASP MET ALA SER ALA TRP          
SEQRES 201 B 2768  ALA LYS ARG ALA ARG GLY ASN VAL PHE MET TYR HIS ALA          
SEQRES 202 B 2768  PRO GLU ASN TYR GLY HIS GLY SER LEU GLU LEU LEU ALA          
SEQRES 203 B 2768  ASP VAL GLN PHE ALA LEU GLY LEU PRO PHE TYR PRO ALA          
SEQRES 204 B 2768  TYR GLU GLY GLN PHE SER LEU GLU GLU LYS SER LEU SER          
SEQRES 205 B 2768  LEU LYS ILE MET GLN TYR PHE SER HIS PHE ILE ARG SER          
SEQRES 206 B 2768  GLY ASN PRO ASN TYR PRO TYR GLU PHE SER ARG LYS VAL          
SEQRES 207 B 2768  PRO THR PHE ALA THR PRO TRP PRO ASP PHE VAL PRO ARG          
SEQRES 208 B 2768  ALA GLY GLY GLU ASN TYR LYS GLU PHE SER GLU LEU LEU          
SEQRES 209 B 2768  PRO ASN ARG GLN GLY LEU LYS LYS ALA ASP CYS SER PHE          
SEQRES 210 B 2768  TRP SER LYS TYR ILE SER SER LEU LYS THR SER ALA ASP          
SEQRES 211 B 2768  GLY ALA LYS GLY GLY GLN SER ALA GLU SER GLU GLU GLU          
SEQRES 212 B 2768  GLU LEU THR ALA GLY SER GLY LEU ARG GLU ASP LEU LEU          
SEQRES 213 B 2768  SER LEU GLN GLU PRO GLY SER LYS THR TYR SER LYS              
HET    NAG  A2801      14                                                       
HET    NAG  A2802      14                                                       
HET    NAG  A2803      14                                                       
HET    NAG  A2804      14                                                       
HET    NAG  A2805      14                                                       
HET    NAG  A2806      14                                                       
HET    NAG  A2807      14                                                       
HET    BMA  A2808      11                                                       
HET    NAG  A2809      14                                                       
HET    NAG  A2810      14                                                       
HET    NAG  A2811      14                                                       
HET    NAG  A2812      14                                                       
HET    NAG  A2813      14                                                       
HET    NAG  A2814      14                                                       
HET    NAG  A2815      14                                                       
HET    NAG  A2816      14                                                       
HET    NAG  A2817      14                                                       
HET    NAG  A2818      14                                                       
HET    NAG  B2801      14                                                       
HET    NAG  B2802      14                                                       
HET    NAG  B2803      14                                                       
HET    NAG  B2804      14                                                       
HET    NAG  B2805      14                                                       
HET    NAG  B2806      14                                                       
HET    NAG  B2807      14                                                       
HET    BMA  B2808      11                                                       
HET    NAG  B2809      14                                                       
HET    NAG  B2810      14                                                       
HET    NAG  B2811      14                                                       
HET    NAG  B2812      14                                                       
HET    NAG  B2813      14                                                       
HET    NAG  B2814      14                                                       
HET    NAG  B2815      14                                                       
HET    NAG  B2816      14                                                       
HET    NAG  B2817      14                                                       
HET    NAG  B2818      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
FORMUL   3  NAG    34(C8 H15 N O6)                                              
FORMUL   8  BMA    2(C6 H12 O6)                                                 
HELIX    1 AA1 CYS A   34  LEU A   43  1                                  10    
HELIX    2 AA2 SER A   94  ASN A  110  1                                  17    
HELIX    3 AA3 ARG A  162  GLY A  174  1                                  13    
HELIX    4 AA4 HIS A  209  PHE A  214  1                                   6    
HELIX    5 AA5 PRO A  215  VAL A  219  5                                   5    
HELIX    6 AA6 THR A  220  ARG A  226  1                                   7    
HELIX    7 AA7 THR A  274  GLY A  293  1                                  20    
HELIX    8 AA8 THR A  299  GLY A  312  1                                  14    
HELIX    9 AA9 SER A  363  TYR A  376  1                                  14    
HELIX   10 AB1 LEU A  439  PHE A  448  1                                  10    
HELIX   11 AB2 SER A  450  PHE A  460  1                                  11    
HELIX   12 AB3 ASN A  463  LEU A  467  5                                   5    
HELIX   13 AB4 GLN A  468  GLY A  473  1                                   6    
HELIX   14 AB5 LYS A  475  GLN A  482  1                                   8    
HELIX   15 AB6 PHE A  497  GLN A  502  1                                   6    
HELIX   16 AB7 ASN A  557  GLU A  573  1                                  17    
HELIX   17 AB8 LEU A  574  SER A  586  1                                  13    
HELIX   18 AB9 ASP A  594  GLN A  606  1                                  13    
HELIX   19 AC1 CYS A  662  LEU A  672  1                                  11    
HELIX   20 AC2 MET A  673  GLN A  676  5                                   4    
HELIX   21 AC3 CYS A  730  GLN A  743  1                                  14    
HELIX   22 AC4 ALA A  744  LEU A  746  5                                   3    
HELIX   23 AC5 GLN A  780  TRP A  788  1                                   9    
HELIX   24 AC6 ALA A  800  ILE A  806  1                                   7    
HELIX   25 AC7 MET A  807  GLY A  815  1                                   9    
HELIX   26 AC8 GLN A  863  ASN A  867  5                                   5    
HELIX   27 AC9 LEU A  872  SER A  877  1                                   6    
HELIX   28 AD1 GLU A  926  SER A  949  1                                  24    
HELIX   29 AD2 GLY A  954  LYS A  961  1                                   8    
HELIX   30 AD3 ARG A  979  PHE A  986  1                                   8    
HELIX   31 AD4 GLY A  989  ARG A 1009  1                                  21    
HELIX   32 AD5 CYS A 1077  SER A 1087  1                                  11    
HELIX   33 AD6 SER A 1099  LYS A 1101  5                                   3    
HELIX   34 AD7 SER A 1147  LEU A 1157  1                                  11    
HELIX   35 AD8 VAL A 1319  ARG A 1328  1                                  10    
HELIX   36 AD9 ASN A 1348  VAL A 1352  5                                   5    
HELIX   37 AE1 GLU A 1373  ILE A 1375  5                                   3    
HELIX   38 AE2 ASP A 1382  GLY A 1392  1                                  11    
HELIX   39 AE3 LEU A 1395  SER A 1405  1                                  11    
HELIX   40 AE4 SER A 1506  CYS A 1510  5                                   5    
HELIX   41 AE5 GLU A 1561  MET A 1567  1                                   7    
HELIX   42 AE6 MET A 1601  GLU A 1609  1                                   9    
HELIX   43 AE7 ASN A 1716  LEU A 1726  1                                  11    
HELIX   44 AE8 ALA A 1727  ASP A 1729  5                                   3    
HELIX   45 AE9 GLU A 1848  THR A 1853  1                                   6    
HELIX   46 AF1 SER A 1885  GLU A 1900  1                                  16    
HELIX   47 AF2 ASN A 1935  CYS A 1939  5                                   5    
HELIX   48 AF3 SER A 1988  ALA A 2002  1                                  15    
HELIX   49 AF4 SER A 2015  GLY A 2019  5                                   5    
HELIX   50 AF5 SER A 2089  TRP A 2093  5                                   5    
HELIX   51 AF6 ALA A 2097  SER A 2099  5                                   3    
HELIX   52 AF7 ASN A 2122  SER A 2135  1                                  14    
HELIX   53 AF8 GLY A 2319  ASN A 2327  1                                   9    
HELIX   54 AF9 LEU A 2357  GLY A 2374  1                                  18    
HELIX   55 AG1 GLY A 2387  ALA A 2392  1                                   6    
HELIX   56 AG2 SER A 2393  LEU A 2397  5                                   5    
HELIX   57 AG3 ALA A 2401  GLN A 2405  5                                   5    
HELIX   58 AG4 SER A 2425  LYS A 2438  1                                  14    
HELIX   59 AG5 CYS A 2453  LYS A 2457  5                                   5    
HELIX   60 AG6 ASN A 2460  ALA A 2471  1                                  12    
HELIX   61 AG7 PRO A 2491  LEU A 2496  1                                   6    
HELIX   62 AG8 ILE A 2517  ARG A 2519  5                                   3    
HELIX   63 AG9 ALA A 2520  GLY A 2531  1                                  12    
HELIX   64 AH1 THR A 2533  SER A 2546  1                                  14    
HELIX   65 AH2 ASP A 2553  TYR A 2564  1                                  12    
HELIX   66 AH3 ALA A 2574  ILE A 2589  1                                  16    
HELIX   67 AH4 ILE A 2589  LYS A 2602  1                                  14    
HELIX   68 AH5 GLY A 2633  TYR A 2637  5                                   5    
HELIX   69 AH6 GLU A 2647  ILE A 2655  1                                   9    
HELIX   70 AH7 ILE A 2655  GLY A 2666  1                                  12    
HELIX   71 AH8 ALA A 2713  TYR A 2721  1                                   9    
HELIX   72 AH9 TYR A 2721  LYS A 2726  1                                   6    
HELIX   73 AI1 CYS B   34  LEU B   43  1                                  10    
HELIX   74 AI2 SER B   94  ASN B  110  1                                  17    
HELIX   75 AI3 ARG B  162  GLY B  174  1                                  13    
HELIX   76 AI4 HIS B  209  PHE B  214  1                                   6    
HELIX   77 AI5 PRO B  215  VAL B  219  5                                   5    
HELIX   78 AI6 THR B  220  ARG B  226  1                                   7    
HELIX   79 AI7 THR B  274  GLY B  293  1                                  20    
HELIX   80 AI8 THR B  299  GLY B  312  1                                  14    
HELIX   81 AI9 SER B  363  TYR B  376  1                                  14    
HELIX   82 AJ1 LEU B  439  PHE B  448  1                                  10    
HELIX   83 AJ2 SER B  450  PHE B  460  1                                  11    
HELIX   84 AJ3 ASN B  463  LEU B  467  5                                   5    
HELIX   85 AJ4 GLN B  468  GLY B  473  1                                   6    
HELIX   86 AJ5 LYS B  475  GLN B  482  1                                   8    
HELIX   87 AJ6 PHE B  497  GLN B  502  1                                   6    
HELIX   88 AJ7 ASN B  557  GLU B  573  1                                  17    
HELIX   89 AJ8 LEU B  574  SER B  586  1                                  13    
HELIX   90 AJ9 ASP B  594  GLN B  606  1                                  13    
HELIX   91 AK1 CYS B  662  LEU B  672  1                                  11    
HELIX   92 AK2 MET B  673  GLN B  676  5                                   4    
HELIX   93 AK3 CYS B  730  GLN B  743  1                                  14    
HELIX   94 AK4 ALA B  744  LEU B  746  5                                   3    
HELIX   95 AK5 GLN B  780  TRP B  788  1                                   9    
HELIX   96 AK6 ALA B  800  ILE B  806  1                                   7    
HELIX   97 AK7 MET B  807  GLY B  815  1                                   9    
HELIX   98 AK8 GLN B  863  ASN B  867  5                                   5    
HELIX   99 AK9 LEU B  872  SER B  877  1                                   6    
HELIX  100 AL1 GLU B  926  SER B  949  1                                  24    
HELIX  101 AL2 GLY B  954  LYS B  961  1                                   8    
HELIX  102 AL3 ARG B  979  PHE B  986  1                                   8    
HELIX  103 AL4 GLY B  989  ARG B 1009  1                                  21    
HELIX  104 AL5 CYS B 1077  SER B 1087  1                                  11    
HELIX  105 AL6 SER B 1099  LYS B 1101  5                                   3    
HELIX  106 AL7 SER B 1147  LEU B 1157  1                                  11    
HELIX  107 AL8 VAL B 1319  ARG B 1328  1                                  10    
HELIX  108 AL9 ASN B 1348  VAL B 1352  5                                   5    
HELIX  109 AM1 GLU B 1373  ILE B 1375  5                                   3    
HELIX  110 AM2 ASP B 1382  GLY B 1392  1                                  11    
HELIX  111 AM3 LEU B 1395  SER B 1405  1                                  11    
HELIX  112 AM4 SER B 1506  CYS B 1510  5                                   5    
HELIX  113 AM5 GLU B 1561  MET B 1567  1                                   7    
HELIX  114 AM6 MET B 1601  GLU B 1609  1                                   9    
HELIX  115 AM7 ASN B 1716  LEU B 1726  1                                  11    
HELIX  116 AM8 ALA B 1727  ASP B 1729  5                                   3    
HELIX  117 AM9 GLU B 1848  THR B 1853  1                                   6    
HELIX  118 AN1 SER B 1885  GLU B 1900  1                                  16    
HELIX  119 AN2 ASN B 1935  CYS B 1939  5                                   5    
HELIX  120 AN3 SER B 1988  ALA B 2002  1                                  15    
HELIX  121 AN4 SER B 2015  GLY B 2019  5                                   5    
HELIX  122 AN5 SER B 2089  TRP B 2093  5                                   5    
HELIX  123 AN6 ALA B 2097  SER B 2099  5                                   3    
HELIX  124 AN7 ASN B 2122  SER B 2135  1                                  14    
HELIX  125 AN8 GLY B 2319  ASN B 2327  1                                   9    
HELIX  126 AN9 LEU B 2357  GLY B 2374  1                                  18    
HELIX  127 AO1 GLY B 2387  ALA B 2392  1                                   6    
HELIX  128 AO2 SER B 2393  LEU B 2397  5                                   5    
HELIX  129 AO3 ALA B 2401  GLN B 2405  5                                   5    
HELIX  130 AO4 SER B 2425  LYS B 2438  1                                  14    
HELIX  131 AO5 CYS B 2453  LYS B 2457  5                                   5    
HELIX  132 AO6 ASN B 2460  ALA B 2471  1                                  12    
HELIX  133 AO7 PRO B 2491  LEU B 2496  1                                   6    
HELIX  134 AO8 ILE B 2517  ARG B 2519  5                                   3    
HELIX  135 AO9 ALA B 2520  GLY B 2531  1                                  12    
HELIX  136 AP1 THR B 2533  SER B 2546  1                                  14    
HELIX  137 AP2 ASP B 2553  TYR B 2564  1                                  12    
HELIX  138 AP3 ALA B 2574  ILE B 2589  1                                  16    
HELIX  139 AP4 ILE B 2589  LYS B 2602  1                                  14    
HELIX  140 AP5 GLY B 2633  TYR B 2637  5                                   5    
HELIX  141 AP6 GLU B 2647  ILE B 2655  1                                   9    
HELIX  142 AP7 ILE B 2655  GLY B 2666  1                                  12    
HELIX  143 AP8 ALA B 2713  TYR B 2721  1                                   9    
HELIX  144 AP9 TYR B 2721  LYS B 2726  1                                   6    
SHEET    1 AA1 2 VAL A  61  CYS A  63  0                                        
SHEET    2 AA1 2 CYS A  70  CYS A  72 -1  O  TRP A  71   N  GLN A  62           
SHEET    1 AA2 3 VAL A 129  GLN A 130  0                                        
SHEET    2 AA2 3 TRP A 139  VAL A 141 -1  O  TRP A 139   N  GLN A 130           
SHEET    3 AA2 3 GLU A 147  ARG A 152 -1  O  VAL A 148   N  CYS A 140           
SHEET    1 AA3 3 VAL A 192  ASN A 198  0                                        
SHEET    2 AA3 3 VAL A 231  CYS A 237 -1  O  HIS A 236   N  GLN A 193           
SHEET    3 AA3 3 LEU A 250  LEU A 252 -1  O  LEU A 250   N  CYS A 235           
SHEET    1 AA4 2 VAL A 328  CYS A 330  0                                        
SHEET    2 AA4 2 CYS A 336  CYS A 338 -1  O  TRP A 337   N  GLN A 329           
SHEET    1 AA5 3 VAL A 629  CYS A 631  0                                        
SHEET    2 AA5 3 GLU A 635  CYS A 638 -1  O  TRP A 637   N  GLN A 630           
SHEET    3 AA5 3 VAL A 651  ARG A 652 -1  O  VAL A 651   N  CYS A 636           
SHEET    1 AA6 3 VAL A 696  PHE A 699  0                                        
SHEET    2 AA6 3 GLU A 702  VAL A 706 -1  O  GLU A 702   N  PHE A 699           
SHEET    3 AA6 3 ALA A 712  ALA A 719 -1  O  SER A 718   N  CYS A 703           
SHEET    1 AA7 2 VAL A1040  CYS A1042  0                                        
SHEET    2 AA7 2 CYS A1049  CYS A1051 -1  O  TRP A1050   N  GLN A1041           
SHEET    1 AA8 2 GLN A1091  ALA A1092  0                                        
SHEET    2 AA8 2 LEU A1103  PHE A1104 -1  O  PHE A1104   N  GLN A1091           
SHEET    1 AA9 2 GLN A1118  SER A1120  0                                        
SHEET    2 AA9 2 GLY A1123  TRP A1125 -1  O  TRP A1125   N  GLN A1118           
SHEET    1 AB1 2 TRP A1189  VAL A1191  0                                        
SHEET    2 AB1 2 GLU A1197  THR A1201 -1  O  VAL A1198   N  CYS A1190           
SHEET    1 AB2 2 GLY A1227  CYS A1231  0                                        
SHEET    2 AB2 2 CYS A1245  CYS A1249 -1  O  LEU A1248   N  THR A1228           
SHEET    1 AB3 2 TRP A1254  SER A1255  0                                        
SHEET    2 AB3 2 CYS A1281  GLN A1282 -1  O  GLN A1282   N  TRP A1254           
SHEET    1 AB4 3 LYS A1369  ARG A1371  0                                        
SHEET    2 AB4 3 THR A1289  GLN A1291 -1  N  ILE A1290   O  SER A1370           
SHEET    3 AB4 3 TRP A1437  GLY A1439 -1  O  TRP A1437   N  GLN A1291           
SHEET    1 AB5 3 PHE A1296  GLN A1297  0                                        
SHEET    2 AB5 3 LEU A1362  VAL A1364 -1  O  VAL A1364   N  PHE A1296           
SHEET    3 AB5 3 VAL A1354  CYS A1356 -1  N  GLY A1355   O  GLY A1363           
SHEET    1 AB6 2 ILE A1333  THR A1337  0                                        
SHEET    2 AB6 2 THR A1340  ILE A1344 -1  O  ILE A1344   N  ILE A1333           
SHEET    1 AB7 2 GLN A1409  LEU A1412  0                                        
SHEET    2 AB7 2 LYS A1415  PRO A1418 -1  O  LYS A1415   N  LEU A1412           
SHEET    1 AB8 2 SER A1466  SER A1468  0                                        
SHEET    2 AB8 2 CYS A1473  PRO A1475 -1  O  ILE A1474   N  TYR A1467           
SHEET    1 AB9 2 PHE A1480  TYR A1481  0                                        
SHEET    2 AB9 2 VAL A1491  PRO A1492 -1  O  VAL A1491   N  TYR A1481           
SHEET    1 AC1 2 GLN A1533  ASP A1535  0                                        
SHEET    2 AC1 2 LYS A1540  PHE A1542 -1  O  LYS A1540   N  ASP A1535           
SHEET    1 AC2 3 SER A1626  TYR A1630  0                                        
SHEET    2 AC2 3 PHE A1615  SER A1619 -1  N  SER A1619   O  SER A1626           
SHEET    3 AC2 3 TYR A1677  LEU A1678 -1  O  TYR A1677   N  PHE A1616           
SHEET    1 AC3 4 TYR A1705  PHE A1710  0                                        
SHEET    2 AC3 4 ILE A1747  LEU A1752 -1  O  LEU A1751   N  TYR A1705           
SHEET    3 AC3 4 GLY A1736  LEU A1739 -1  N  GLY A1736   O  LEU A1752           
SHEET    4 AC3 4 TYR A1819  LEU A1820 -1  O  TYR A1819   N  LEU A1739           
SHEET    1 AC4 2 VAL A1757  LEU A1759  0                                        
SHEET    2 AC4 2 HIS A1877  LEU A1879 -1  O  TRP A1878   N  LEU A1758           
SHEET    1 AC5 4 PHE A1856  PRO A1858  0                                        
SHEET    2 AC5 4 ALA A1949  LYS A1953 -1  O  ARG A1952   N  SER A1857           
SHEET    3 AC5 4 LEU A1906  ILE A1909 -1  N  ALA A1907   O  PHE A1951           
SHEET    4 AC5 4 CYS A1919  TYR A1922 -1  O  TYR A1922   N  LEU A1906           
SHEET    1 AC6 3 VAL A1864  VAL A1866  0                                        
SHEET    2 AC6 3 ARG A1940  LEU A1943  1  O  LEU A1943   N  ILE A1865           
SHEET    3 AC6 3 GLN A1926  VAL A1927 -1  N  VAL A1927   O  ARG A1940           
SHEET    1 AC7 2 THR A1966  ARG A1967  0                                        
SHEET    2 AC7 2 TYR A2063  GLN A2064 -1  O  GLN A2064   N  THR A1966           
SHEET    1 AC8 7 LYS A1972  MET A1974  0                                        
SHEET    2 AC8 7 ILE A2032  MET A2034 -1  O  ILE A2032   N  MET A1974           
SHEET    3 AC8 7 PHE A2110  SER A2116 -1  O  HIS A2114   N  GLN A2033           
SHEET    4 AC8 7 ALA A2151  TYR A2157 -1  O  VAL A2152   N  VAL A2115           
SHEET    5 AC8 7 ILE A2142  GLN A2148 -1  N  THR A2144   O  MET A2155           
SHEET    6 AC8 7 HIS A2182  ARG A2185 -1  O  TYR A2184   N  THR A2143           
SHEET    7 AC8 7 GLN A2094  LEU A2096 -1  N  GLN A2094   O  ARG A2185           
SHEET    1 AC9 3 SER A1977  ASN A1980  0                                        
SHEET    2 AC9 3 THR A2026  SER A2029 -1  O  ASN A2028   N  SER A1977           
SHEET    3 AC9 3 GLY A2008  PHE A2009 -1  N  GLY A2008   O  LEU A2027           
SHEET    1 AD1 2 LEU A2012  ASN A2013  0                                        
SHEET    2 AD1 2 VAL A2022  THR A2023 -1  O  THR A2023   N  LEU A2012           
SHEET    1 AD2 2 VAL A2101  VAL A2103  0                                        
SHEET    2 AD2 2 LEU A2174  LEU A2176  1  O  LEU A2176   N  VAL A2102           
SHEET    1 AD3 2 THR A2164  HIS A2165  0                                        
SHEET    2 AD3 2 GLN A2170  ASN A2171 -1  O  ASN A2171   N  THR A2164           
SHEET    1 AD4 2 SER A2193  GLU A2195  0                                        
SHEET    2 AD4 2 VAL A2198  SER A2200 -1  O  SER A2200   N  SER A2193           
SHEET    1 AD5 2 GLY A2207  LEU A2210  0                                        
SHEET    2 AD5 2 GLY A2253  ASP A2256  1  O  GLY A2253   N  ARG A2208           
SHEET    1 AD611 GLN A2214  VAL A2218  0                                        
SHEET    2 AD611 SER A2221  PRO A2232 -1  O  VAL A2225   N  GLN A2214           
SHEET    3 AD611 TYR A2283  PRO A2289 -1  O  LEU A2284   N  VAL A2231           
SHEET    4 AD611 ILE A2329  ALA A2333 -1  O  VAL A2330   N  PHE A2287           
SHEET    5 AD611 VAL A2298  PHE A2302  1  N  PHE A2301   O  ALA A2333           
SHEET    6 AD611 SER A2381  ALA A2384  1  O  SER A2381   N  VAL A2298           
SHEET    7 AD611 ARG A2409  MET A2413  1  O  VAL A2411   N  LEU A2382           
SHEET    8 AD611 ASP A2505  SER A2510  1  O  LEU A2507   N  ALA A2410           
SHEET    9 AD611 VAL A2608  HIS A2612  1  O  PHE A2609   N  LEU A2506           
SHEET   10 AD611 ASN A2696  GLU A2699  1  O  LYS A2698   N  HIS A2612           
SHEET   11 AD611 ASN A2706  GLN A2708 -1  O  ARG A2707   N  TYR A2697           
SHEET    1 AD7 2 SER A2263  CYS A2264  0                                        
SHEET    2 AD7 2 VAL A2277  SER A2278  1  O  SER A2278   N  SER A2263           
SHEET    1 AD8 2 VAL B  61  CYS B  63  0                                        
SHEET    2 AD8 2 CYS B  70  CYS B  72 -1  O  TRP B  71   N  GLN B  62           
SHEET    1 AD9 3 VAL B 129  GLN B 130  0                                        
SHEET    2 AD9 3 TRP B 139  VAL B 141 -1  O  TRP B 139   N  GLN B 130           
SHEET    3 AD9 3 GLU B 147  ARG B 152 -1  O  VAL B 148   N  CYS B 140           
SHEET    1 AE1 3 VAL B 192  ASN B 198  0                                        
SHEET    2 AE1 3 VAL B 231  CYS B 237 -1  O  HIS B 236   N  GLN B 193           
SHEET    3 AE1 3 LEU B 250  LEU B 252 -1  O  LEU B 250   N  CYS B 235           
SHEET    1 AE2 2 VAL B 328  CYS B 330  0                                        
SHEET    2 AE2 2 CYS B 336  CYS B 338 -1  O  TRP B 337   N  GLN B 329           
SHEET    1 AE3 3 VAL B 629  CYS B 631  0                                        
SHEET    2 AE3 3 GLU B 635  CYS B 638 -1  O  TRP B 637   N  GLN B 630           
SHEET    3 AE3 3 VAL B 651  ARG B 652 -1  O  VAL B 651   N  CYS B 636           
SHEET    1 AE4 3 VAL B 696  PHE B 699  0                                        
SHEET    2 AE4 3 GLU B 702  VAL B 706 -1  O  GLU B 702   N  PHE B 699           
SHEET    3 AE4 3 ALA B 712  ALA B 719 -1  O  SER B 718   N  CYS B 703           
SHEET    1 AE5 2 VAL B1040  CYS B1042  0                                        
SHEET    2 AE5 2 CYS B1049  CYS B1051 -1  O  TRP B1050   N  GLN B1041           
SHEET    1 AE6 2 GLN B1091  ALA B1092  0                                        
SHEET    2 AE6 2 LEU B1103  PHE B1104 -1  O  PHE B1104   N  GLN B1091           
SHEET    1 AE7 2 GLN B1118  SER B1120  0                                        
SHEET    2 AE7 2 GLY B1123  TRP B1125 -1  O  TRP B1125   N  GLN B1118           
SHEET    1 AE8 2 TRP B1189  VAL B1191  0                                        
SHEET    2 AE8 2 GLU B1197  THR B1201 -1  O  VAL B1198   N  CYS B1190           
SHEET    1 AE9 2 GLY B1227  CYS B1231  0                                        
SHEET    2 AE9 2 CYS B1245  CYS B1249 -1  O  LEU B1248   N  THR B1228           
SHEET    1 AF1 2 TRP B1254  SER B1255  0                                        
SHEET    2 AF1 2 CYS B1281  GLN B1282 -1  O  GLN B1282   N  TRP B1254           
SHEET    1 AF2 3 LYS B1369  ARG B1371  0                                        
SHEET    2 AF2 3 THR B1289  GLN B1291 -1  N  ILE B1290   O  SER B1370           
SHEET    3 AF2 3 TRP B1437  GLY B1439 -1  O  TRP B1437   N  GLN B1291           
SHEET    1 AF3 3 PHE B1296  GLN B1297  0                                        
SHEET    2 AF3 3 LEU B1362  VAL B1364 -1  O  VAL B1364   N  PHE B1296           
SHEET    3 AF3 3 VAL B1354  CYS B1356 -1  N  GLY B1355   O  GLY B1363           
SHEET    1 AF4 2 ILE B1333  THR B1337  0                                        
SHEET    2 AF4 2 THR B1340  ILE B1344 -1  O  ILE B1344   N  ILE B1333           
SHEET    1 AF5 2 GLN B1409  LEU B1412  0                                        
SHEET    2 AF5 2 LYS B1415  PRO B1418 -1  O  LYS B1415   N  LEU B1412           
SHEET    1 AF6 2 SER B1466  SER B1468  0                                        
SHEET    2 AF6 2 CYS B1473  PRO B1475 -1  O  ILE B1474   N  TYR B1467           
SHEET    1 AF7 2 PHE B1480  TYR B1481  0                                        
SHEET    2 AF7 2 VAL B1491  PRO B1492 -1  O  VAL B1491   N  TYR B1481           
SHEET    1 AF8 2 GLN B1533  ASP B1535  0                                        
SHEET    2 AF8 2 LYS B1540  PHE B1542 -1  O  LYS B1540   N  ASP B1535           
SHEET    1 AF9 3 SER B1626  TYR B1630  0                                        
SHEET    2 AF9 3 PHE B1615  SER B1619 -1  N  SER B1619   O  SER B1626           
SHEET    3 AF9 3 TYR B1677  LEU B1678 -1  O  TYR B1677   N  PHE B1616           
SHEET    1 AG1 4 TYR B1705  PHE B1710  0                                        
SHEET    2 AG1 4 ILE B1747  LEU B1752 -1  O  LEU B1751   N  TYR B1705           
SHEET    3 AG1 4 GLY B1736  LEU B1739 -1  N  GLY B1736   O  LEU B1752           
SHEET    4 AG1 4 TYR B1819  LEU B1820 -1  O  TYR B1819   N  LEU B1739           
SHEET    1 AG2 2 VAL B1757  LEU B1759  0                                        
SHEET    2 AG2 2 HIS B1877  LEU B1879 -1  O  TRP B1878   N  LEU B1758           
SHEET    1 AG3 4 PHE B1856  PRO B1858  0                                        
SHEET    2 AG3 4 ALA B1949  LYS B1953 -1  O  ARG B1952   N  SER B1857           
SHEET    3 AG3 4 LEU B1906  ILE B1909 -1  N  ALA B1907   O  PHE B1951           
SHEET    4 AG3 4 CYS B1919  TYR B1922 -1  O  TYR B1922   N  LEU B1906           
SHEET    1 AG4 3 VAL B1864  VAL B1866  0                                        
SHEET    2 AG4 3 ARG B1940  LEU B1943  1  O  LEU B1943   N  ILE B1865           
SHEET    3 AG4 3 GLN B1926  VAL B1927 -1  N  VAL B1927   O  ARG B1940           
SHEET    1 AG5 2 THR B1966  ARG B1967  0                                        
SHEET    2 AG5 2 TYR B2063  GLN B2064 -1  O  GLN B2064   N  THR B1966           
SHEET    1 AG6 7 LYS B1972  MET B1974  0                                        
SHEET    2 AG6 7 ILE B2032  MET B2034 -1  O  ILE B2032   N  MET B1974           
SHEET    3 AG6 7 PHE B2110  SER B2116 -1  O  HIS B2114   N  GLN B2033           
SHEET    4 AG6 7 ALA B2151  TYR B2157 -1  O  VAL B2152   N  VAL B2115           
SHEET    5 AG6 7 ILE B2142  GLN B2148 -1  N  THR B2144   O  MET B2155           
SHEET    6 AG6 7 HIS B2182  ARG B2185 -1  O  TYR B2184   N  THR B2143           
SHEET    7 AG6 7 GLN B2094  LEU B2096 -1  N  GLN B2094   O  ARG B2185           
SHEET    1 AG7 3 SER B1977  ASN B1980  0                                        
SHEET    2 AG7 3 THR B2026  SER B2029 -1  O  ASN B2028   N  SER B1977           
SHEET    3 AG7 3 GLY B2008  PHE B2009 -1  N  GLY B2008   O  LEU B2027           
SHEET    1 AG8 2 LEU B2012  ASN B2013  0                                        
SHEET    2 AG8 2 VAL B2022  THR B2023 -1  O  THR B2023   N  LEU B2012           
SHEET    1 AG9 2 VAL B2101  VAL B2103  0                                        
SHEET    2 AG9 2 LEU B2174  LEU B2176  1  O  LEU B2176   N  VAL B2102           
SHEET    1 AH1 2 THR B2164  HIS B2165  0                                        
SHEET    2 AH1 2 GLN B2170  ASN B2171 -1  O  ASN B2171   N  THR B2164           
SHEET    1 AH2 2 SER B2193  GLU B2195  0                                        
SHEET    2 AH2 2 VAL B2198  SER B2200 -1  O  SER B2200   N  SER B2193           
SHEET    1 AH3 2 GLY B2207  LEU B2210  0                                        
SHEET    2 AH3 2 GLY B2253  ASP B2256  1  O  GLY B2253   N  ARG B2208           
SHEET    1 AH411 GLN B2214  VAL B2218  0                                        
SHEET    2 AH411 SER B2221  PRO B2232 -1  O  VAL B2225   N  GLN B2214           
SHEET    3 AH411 TYR B2283  PRO B2289 -1  O  LEU B2284   N  VAL B2231           
SHEET    4 AH411 ILE B2329  ALA B2333 -1  O  VAL B2330   N  PHE B2287           
SHEET    5 AH411 VAL B2298  PHE B2302  1  N  PHE B2301   O  ALA B2333           
SHEET    6 AH411 SER B2381  ALA B2384  1  O  SER B2381   N  VAL B2298           
SHEET    7 AH411 ARG B2409  MET B2413  1  O  VAL B2411   N  LEU B2382           
SHEET    8 AH411 ASP B2505  SER B2510  1  O  LEU B2507   N  ALA B2410           
SHEET    9 AH411 VAL B2608  HIS B2612  1  O  PHE B2609   N  LEU B2506           
SHEET   10 AH411 ASN B2696  GLU B2699  1  O  LYS B2698   N  HIS B2612           
SHEET   11 AH411 ASN B2706  GLN B2708 -1  O  ARG B2707   N  TYR B2697           
SHEET    1 AH5 2 SER B2263  CYS B2264  0                                        
SHEET    2 AH5 2 VAL B2277  SER B2278  1  O  SER B2278   N  SER B2263           
SSBOND   1 CYS A   34    CYS A   52                          1555   1555  2.03  
SSBOND   2 CYS A   63    CYS A   70                          1555   1555  2.03  
SSBOND   3 CYS A   72    CYS A   92                          1555   1555  2.03  
SSBOND   4 CYS A   96    CYS A  120                          1555   1555  2.02  
SSBOND   5 CYS A  131    CYS A  138                          1555   1555  2.04  
SSBOND   6 CYS A  140    CYS A  160                          1555   1555  2.03  
SSBOND   7 CYS A  164    CYS A  183                          1555   1555  2.03  
SSBOND   8 CYS A  194    CYS A  235                          1555   1555  2.03  
SSBOND   9 CYS A  237    CYS A  297                          1555   1555  2.03  
SSBOND  10 CYS A  301    CYS A  319                          1555   1555  2.03  
SSBOND  11 CYS A  330    CYS A  336                          1555   1555  2.03  
SSBOND  12 CYS A  338    CYS A  358                          1555   1555  2.03  
SSBOND  13 CYS A  364    CYS A  620                          1555   1555  2.03  
SSBOND  14 CYS A  408    CYS A  608                          1555   1555  2.03  
SSBOND  15 CYS A  631    CYS A  636                          1555   1555  2.03  
SSBOND  16 CYS A  638    CYS A  658                          1555   1555  2.03  
SSBOND  17 CYS A  662    CYS A  687                          1555   1555  2.02  
SSBOND  18 CYS A  698    CYS A  703                          1555   1555  2.03  
SSBOND  19 CYS A  705    CYS A  726                          1555   1555  2.04  
SSBOND  20 CYS A  730    CYS A  763                          1555   1555  2.02  
SSBOND  21 CYS A  774    CYS A  898                          1555   1555  2.03  
SSBOND  22 CYS A  900    CYS A  921                          1555   1555  2.03  
SSBOND  23 CYS A  925    CYS A 1031                          1555   1555  2.05  
SSBOND  24 CYS A 1042    CYS A 1049                          1555   1555  2.03  
SSBOND  25 CYS A 1051    CYS A 1073                          1555   1555  2.03  
SSBOND  26 CYS A 1077    CYS A 1108                          1555   1555  2.02  
SSBOND  27 CYS A 1126    CYS A 1145                          1555   1555  2.04  
SSBOND  28 CYS A 1149    CYS A 1169                          1555   1555  2.03  
SSBOND  29 CYS A 1181    CYS A 1188                          1555   1555  2.04  
SSBOND  30 CYS A 1190    CYS A 1210                          1555   1555  2.02  
SSBOND  31 CYS A 1215    CYS A 1264                          1555   1555  2.03  
SSBOND  32 CYS A 1231    CYS A 1245                          1555   1555  2.03  
SSBOND  33 CYS A 1306    CYS A 1356                          1555   1555  2.04  
SSBOND  34 CYS A 1331    CYS A 1347                          1555   1555  2.03  
SSBOND  35 CYS A 1440    CYS A 1459                          1555   1555  2.04  
SSBOND  36 CYS A 1462    CYS A 1473                          1555   1555  2.03  
SSBOND  37 CYS A 1476    CYS A 1490                          1555   1555  2.03  
SSBOND  38 CYS A 1493    CYS A 1510                          1555   1555  2.03  
SSBOND  39 CYS A 1514    CYS A 1523                          1555   1555  2.03  
SSBOND  40 CYS A 1543    CYS A 1565                          1555   1555  2.02  
SSBOND  41 CYS A 1603    CYS A 1627                          1555   1555  2.03  
SSBOND  42 CYS A 1607    CYS A 1613                          1555   1555  2.03  
SSBOND  43 CYS A 1639    CYS A 1662                          1555   1555  2.03  
SSBOND  44 CYS A 1724    CYS A 1749                          1555   1555  2.04  
SSBOND  45 CYS A 1728    CYS A 1734                          1555   1555  2.03  
SSBOND  46 CYS A 1733    CYS A 1835                          1555   1555  2.03  
SSBOND  47 CYS A 1760    CYS A 1777                          1555   1555  2.03  
SSBOND  48 CYS A 1893    CYS A 1919                          1555   1555  2.03  
SSBOND  49 CYS A 1897    CYS A 1904                          1555   1555  2.03  
SSBOND  50 CYS A 1928    CYS A 1939                          1555   1555  2.04  
SSBOND  51 CYS A 1996    CYS A 2024                          1555   1555  2.03  
SSBOND  52 CYS A 2000    CYS A 2006                          1555   1555  2.04  
SSBOND  53 CYS A 2005    CYS A 2076                          1555   1555  2.03  
SSBOND  54 CYS A 2035    CYS A 2048                          1555   1555  2.03  
SSBOND  55 CYS A 2130    CYS A 2154                          1555   1555  2.03  
SSBOND  56 CYS A 2134    CYS A 2140                          1555   1555  2.03  
SSBOND  57 CYS A 2163    CYS A 2172                          1555   1555  2.03  
SSBOND  58 CYS A 2264    CYS A 2281                          1555   1555  2.03  
SSBOND  59 CYS A 2442    CYS A 2453                          1555   1555  2.03  
SSBOND  60 CYS A 2591    CYS A 2715                          1555   1555  2.04  
SSBOND  61 CYS B   34    CYS B   52                          1555   1555  2.03  
SSBOND  62 CYS B   63    CYS B   70                          1555   1555  2.03  
SSBOND  63 CYS B   72    CYS B   92                          1555   1555  2.03  
SSBOND  64 CYS B   96    CYS B  120                          1555   1555  2.02  
SSBOND  65 CYS B  131    CYS B  138                          1555   1555  2.04  
SSBOND  66 CYS B  140    CYS B  160                          1555   1555  2.03  
SSBOND  67 CYS B  164    CYS B  183                          1555   1555  2.03  
SSBOND  68 CYS B  194    CYS B  235                          1555   1555  2.03  
SSBOND  69 CYS B  237    CYS B  297                          1555   1555  2.03  
SSBOND  70 CYS B  301    CYS B  319                          1555   1555  2.03  
SSBOND  71 CYS B  330    CYS B  336                          1555   1555  2.03  
SSBOND  72 CYS B  338    CYS B  358                          1555   1555  2.03  
SSBOND  73 CYS B  364    CYS B  620                          1555   1555  2.03  
SSBOND  74 CYS B  408    CYS B  608                          1555   1555  2.03  
SSBOND  75 CYS B  631    CYS B  636                          1555   1555  2.03  
SSBOND  76 CYS B  638    CYS B  658                          1555   1555  2.03  
SSBOND  77 CYS B  662    CYS B  687                          1555   1555  2.02  
SSBOND  78 CYS B  698    CYS B  703                          1555   1555  2.03  
SSBOND  79 CYS B  705    CYS B  726                          1555   1555  2.04  
SSBOND  80 CYS B  730    CYS B  763                          1555   1555  2.02  
SSBOND  81 CYS B  774    CYS B  898                          1555   1555  2.03  
SSBOND  82 CYS B  900    CYS B  921                          1555   1555  2.03  
SSBOND  83 CYS B  925    CYS B 1031                          1555   1555  2.04  
SSBOND  84 CYS B 1042    CYS B 1049                          1555   1555  2.03  
SSBOND  85 CYS B 1051    CYS B 1073                          1555   1555  2.03  
SSBOND  86 CYS B 1077    CYS B 1108                          1555   1555  2.02  
SSBOND  87 CYS B 1126    CYS B 1145                          1555   1555  2.04  
SSBOND  88 CYS B 1149    CYS B 1169                          1555   1555  2.03  
SSBOND  89 CYS B 1181    CYS B 1188                          1555   1555  2.04  
SSBOND  90 CYS B 1190    CYS B 1210                          1555   1555  2.03  
SSBOND  91 CYS B 1215    CYS B 1264                          1555   1555  2.03  
SSBOND  92 CYS B 1231    CYS B 1245                          1555   1555  2.03  
SSBOND  93 CYS B 1306    CYS B 1356                          1555   1555  2.04  
SSBOND  94 CYS B 1331    CYS B 1347                          1555   1555  2.03  
SSBOND  95 CYS B 1440    CYS B 1459                          1555   1555  2.04  
SSBOND  96 CYS B 1462    CYS B 1473                          1555   1555  2.03  
SSBOND  97 CYS B 1476    CYS B 1490                          1555   1555  2.03  
SSBOND  98 CYS B 1493    CYS B 1510                          1555   1555  2.03  
SSBOND  99 CYS B 1514    CYS B 1523                          1555   1555  2.03  
SSBOND 100 CYS B 1543    CYS B 1565                          1555   1555  2.02  
SSBOND 101 CYS B 1603    CYS B 1627                          1555   1555  2.03  
SSBOND 102 CYS B 1607    CYS B 1613                          1555   1555  2.03  
SSBOND 103 CYS B 1639    CYS B 1662                          1555   1555  2.03  
SSBOND 104 CYS B 1724    CYS B 1749                          1555   1555  2.04  
SSBOND 105 CYS B 1728    CYS B 1734                          1555   1555  2.03  
SSBOND 106 CYS B 1733    CYS B 1835                          1555   1555  2.03  
SSBOND 107 CYS B 1760    CYS B 1777                          1555   1555  2.03  
SSBOND 108 CYS B 1893    CYS B 1919                          1555   1555  2.03  
SSBOND 109 CYS B 1897    CYS B 1904                          1555   1555  2.03  
SSBOND 110 CYS B 1928    CYS B 1939                          1555   1555  2.04  
SSBOND 111 CYS B 1996    CYS B 2024                          1555   1555  2.03  
SSBOND 112 CYS B 2000    CYS B 2006                          1555   1555  2.04  
SSBOND 113 CYS B 2005    CYS B 2076                          1555   1555  2.03  
SSBOND 114 CYS B 2035    CYS B 2048                          1555   1555  2.03  
SSBOND 115 CYS B 2130    CYS B 2154                          1555   1555  2.03  
SSBOND 116 CYS B 2134    CYS B 2140                          1555   1555  2.03  
SSBOND 117 CYS B 2163    CYS B 2172                          1555   1555  2.03  
SSBOND 118 CYS B 2264    CYS B 2281                          1555   1555  2.03  
SSBOND 119 CYS B 2442    CYS B 2453                          1555   1555  2.03  
SSBOND 120 CYS B 2591    CYS B 2715                          1555   1555  2.03  
LINK         ND2 ASN A  76                 C1  NAG A2816     1555   1555  1.44  
LINK         ND2 ASN A 110                 C1  NAG A2818     1555   1555  1.44  
LINK         ND2 ASN A 198                 C1  NAG A2815     1555   1555  1.44  
LINK         ND2 ASN A 484                 C1  NAG A2817     1555   1555  1.45  
LINK         ND2 ASN A 947                 C1  NAG A2801     1555   1555  1.44  
LINK         ND2 ASN A1220                 C1  NAG A2802     1555   1555  1.44  
LINK         ND2 ASN A1349                 C1  NAG A2803     1555   1555  1.44  
LINK         ND2 ASN A1365                 C1  NAG A2804     1555   1555  1.44  
LINK         ND2 ASN A1716                 C1  NAG A2805     1555   1555  1.44  
LINK         ND2 ASN A1774                 C1  NAG A2814     1555   1555  1.44  
LINK         ND2 ASN A1869                 C1  NAG A2813     1555   1555  1.44  
LINK         ND2 ASN A2013                 C1  NAG A2806     1555   1555  1.44  
LINK         ND2 ASN A2122                 C1  NAG A2812     1555   1555  1.44  
LINK         ND2 ASN A2250                 C1  NAG A2809     1555   1555  1.44  
LINK         ND2 ASN A2295                 C1  NAG A2810     1555   1555  1.44  
LINK         ND2 ASN A2582                 C1  NAG A2811     1555   1555  1.44  
LINK         ND2 ASN B  76                 C1  NAG B2816     1555   1555  1.44  
LINK         ND2 ASN B 110                 C1  NAG B2818     1555   1555  1.44  
LINK         ND2 ASN B 198                 C1  NAG B2815     1555   1555  1.44  
LINK         ND2 ASN B 484                 C1  NAG B2817     1555   1555  1.45  
LINK         ND2 ASN B 947                 C1  NAG B2801     1555   1555  1.44  
LINK         ND2 ASN B1220                 C1  NAG B2802     1555   1555  1.44  
LINK         ND2 ASN B1349                 C1  NAG B2803     1555   1555  1.44  
LINK         ND2 ASN B1365                 C1  NAG B2804     1555   1555  1.44  
LINK         ND2 ASN B1716                 C1  NAG B2805     1555   1555  1.44  
LINK         ND2 ASN B1774                 C1  NAG B2814     1555   1555  1.44  
LINK         ND2 ASN B1869                 C1  NAG B2813     1555   1555  1.44  
LINK         ND2 ASN B2013                 C1  NAG B2806     1555   1555  1.44  
LINK         ND2 ASN B2122                 C1  NAG B2812     1555   1555  1.44  
LINK         ND2 ASN B2250                 C1  NAG B2809     1555   1555  1.44  
LINK         ND2 ASN B2295                 C1  NAG B2810     1555   1555  1.44  
LINK         ND2 ASN B2582                 C1  NAG B2811     1555   1555  1.44  
LINK         O4  NAG A2806                 C1  NAG A2807     1555   1555  1.38  
LINK         O4  NAG A2807                 C1  BMA A2808     1555   1555  1.38  
LINK         O4  NAG B2806                 C1  NAG B2807     1555   1555  1.38  
LINK         O4  NAG B2807                 C1  BMA B2808     1555   1555  1.38  
CISPEP   1 VAL A 1198    PRO A 1199          0        -6.85                     
CISPEP   2 VAL B 1198    PRO B 1199          0        -6.87                     
SITE     1 AC1  1 ASN A  76                                                     
SITE     1 AC2  2 ILE A 109  ASN A 110                                          
SITE     1 AC3  5 ASN A 198  THR A 200  ASP A 201  PHE A 205                    
SITE     2 AC3  5 GLU A 230                                                     
SITE     1 AC4  3 GLU A 256  ASN A 479  ASN A 484                               
SITE     1 AC5  2 ASN A 947  ARG A1007                                          
SITE     1 AC6  1 ASN A1220                                                     
SITE     1 AC7  2 ASN A1349  VAL B 133                                          
SITE     1 AC8  3 HIS A1295  GLN A1353  ASN A1365                               
SITE     1 AC9  3 GLU A1572  GLY A1714  ASN A1716                               
SITE     1 AD1  2 ALA A1773  ASN A1774                                          
SITE     1 AD2  1 ASN A1869                                                     
SITE     1 AD3 10 ASN A2013  GLN A2016  GLY A2019  GLY A2020                    
SITE     2 AD3 10 GLU A2054  THR A2057  ASN B 212  ARG B 213                    
SITE     3 AD3 10 PHE B 214  PRO B 215                                          
SITE     1 AD4  1 ASN A2122                                                     
SITE     1 AD5  2 PRO A2248  ASN A2250                                          
SITE     1 AD6  3 GLU A2138  PRO A2294  ASN A2295                               
SITE     1 AD7  2 ALA A2579  ASN A2582                                          
SITE     1 AD8  1 ASN B  76                                                     
SITE     1 AD9  2 ILE B 109  ASN B 110                                          
SITE     1 AE1  5 ASN B 198  THR B 200  ASP B 201  PHE B 205                    
SITE     2 AE1  5 GLU B 230                                                     
SITE     1 AE2  3 GLU B 256  ASN B 479  ASN B 484                               
SITE     1 AE3  2 ASN B 947  ARG B1007                                          
SITE     1 AE4  1 ASN B1220                                                     
SITE     1 AE5  2 VAL A 133  ASN B1349                                          
SITE     1 AE6  3 HIS B1295  GLN B1353  ASN B1365                               
SITE     1 AE7  3 GLU B1572  GLY B1714  ASN B1716                               
SITE     1 AE8  2 ALA B1773  ASN B1774                                          
SITE     1 AE9  1 ASN B1869                                                     
SITE     1 AF1 10 ASN A 212  ARG A 213  PHE A 214  PRO A 215                    
SITE     2 AF1 10 ASN B2013  GLN B2016  GLY B2019  GLY B2020                    
SITE     3 AF1 10 GLU B2054  THR B2057                                          
SITE     1 AF2  1 ASN B2122                                                     
SITE     1 AF3  2 PRO B2248  ASN B2250                                          
SITE     1 AF4  3 GLU B2138  PRO B2294  ASN B2295                               
SITE     1 AF5  2 ALA B2579  ASN B2582                                          
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
TER   19694      SER A2728                                                      
TER   39388      SER B2728                                                      
MASTER      855    0   36  144  190    0   38    639884    2  770  426          
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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