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LongText Report for: 6i2t-pdb

Name Class
6i2t-pdb
HEADER    HYDROLASE                               01-NOV-18   6I2T              
TITLE     CRYOEM RECONSTRUCTION OF FULL-LENGTH, FULLY-GLYCOSYLATED HUMAN        
TITLE    2 BUTYRYLCHOLINESTERASE TETRAMER                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLINESTERASE;                                            
COMPND   3 CHAIN: B, A, C, D;                                                   
COMPND   4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE,BUTYRYLCHOLINE ESTERASE,CHOLINE   
COMPND   5 ESTERASE II,PSEUDOCHOLINESTERASE;                                    
COMPND   6 EC: 3.1.1.8;                                                         
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: LAMELLIPODIN-DERIVED POLYPROLINE PEPTIDE;                  
COMPND   9 CHAIN: J                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_TAXID: 9606                                                 
KEYWDS    CHOLINESTERASE, TETRAMER, HYDROLASE                                   
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    M.R.LEUNG,L.S.VAN BEZOUWEN,L.M.SCHOPFER,J.L.SUSSMAN,I.SILMAN,         
AUTHOR   2 O.LOCKRIDGE,T.ZEEV-BEN-MORDEHAI                                      
REVDAT   1   19-DEC-18 6I2T    0                                                
JRNL        AUTH   M.R.LEUNG,L.S.VAN BEZOUWEN,L.M.SCHOPFER,J.L.SUSSMAN,         
JRNL        AUTH 2 I.SILMAN,O.LOCKRIDGE,T.ZEEV-BEN-MORDEHAI                     
JRNL        TITL   CRYO-EM STRUCTURE OF THE NATIVE BUTYRYLCHOLINESTERASE        
JRNL        TITL 2 TETRAMER REVEALS A DIMER OF DIMERS STABILIZED BY A           
JRNL        TITL 3 SUPERHELICAL ASSEMBLY                                        
JRNL        REF    PROC.NATL.ACAD.SCI.USA                     2018              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        DOI    10.1073/PNAS.1817009115                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    5.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : RELION, EPU, GCTF, UCSF CHIMERA,          
REMARK   3                            RELION, RELION, RELION, PHENIX            
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 4AQD                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : RIGID BODY FIT                      
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)  : 5.700                          
REMARK   3   NUMBER OF PARTICLES               : 111986                         
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 6I2T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200012712.                                   
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                 : HETEROPENTAMERIC COMPLEX          
REMARK 245                                    CONSISTING OF FOUR COPIES OF      
REMARK 245                                    BUTYRYLCHOLINESTERASE AND ONE     
REMARK 245                                    COPY OF A LAMELLIPODIN-DERIVED    
REMARK 245                                    POLYPROLINE PEPTIDE               
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 3.30                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : BLOT FOR EITHER 2S OR 3S AT       
REMARK 245                                    BLOT FORCE -2 OR 0, RESPECTIVELY  
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 8.00                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : 4518                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TALOS ARCTICA              
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : 1200.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 2500.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 49.50                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 130000                         
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 200                            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10710 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 94730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, C, D, J                         
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     GLU B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     SER B   566                                                      
REMARK 465     LYS B   567                                                      
REMARK 465     LYS B   568                                                      
REMARK 465     GLU B   569                                                      
REMARK 465     SER B   570                                                      
REMARK 465     CYS B   571                                                      
REMARK 465     VAL B   572                                                      
REMARK 465     GLY B   573                                                      
REMARK 465     LEU B   574                                                      
REMARK 465     GLU A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     ASN A   562                                                      
REMARK 465     ASP A   563                                                      
REMARK 465     TYR A   564                                                      
REMARK 465     THR A   565                                                      
REMARK 465     SER A   566                                                      
REMARK 465     LYS A   567                                                      
REMARK 465     LYS A   568                                                      
REMARK 465     GLU A   569                                                      
REMARK 465     SER A   570                                                      
REMARK 465     CYS A   571                                                      
REMARK 465     VAL A   572                                                      
REMARK 465     GLY A   573                                                      
REMARK 465     LEU A   574                                                      
REMARK 465     GLU C     1                                                      
REMARK 465     ASP C     2                                                      
REMARK 465     ASP C     3                                                      
REMARK 465     ASN C   562                                                      
REMARK 465     ASP C   563                                                      
REMARK 465     TYR C   564                                                      
REMARK 465     THR C   565                                                      
REMARK 465     SER C   566                                                      
REMARK 465     LYS C   567                                                      
REMARK 465     LYS C   568                                                      
REMARK 465     GLU C   569                                                      
REMARK 465     SER C   570                                                      
REMARK 465     CYS C   571                                                      
REMARK 465     VAL C   572                                                      
REMARK 465     GLY C   573                                                      
REMARK 465     LEU C   574                                                      
REMARK 465     GLU D     1                                                      
REMARK 465     ASP D     2                                                      
REMARK 465     ASP D     3                                                      
REMARK 465     SER D   566                                                      
REMARK 465     LYS D   567                                                      
REMARK 465     LYS D   568                                                      
REMARK 465     GLU D   569                                                      
REMARK 465     SER D   570                                                      
REMARK 465     CYS D   571                                                      
REMARK 465     VAL D   572                                                      
REMARK 465     GLY D   573                                                      
REMARK 465     LEU D   574                                                      
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 B 263   CA  -  CB  -  SG  ANGL. DEV. =  13.2 DEGREES          
REMARK 500    PHE B 298   CB  -  CG  -  CD2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    LEU B 428   CB  -  CG  -  CD2 ANGL. DEV. = -10.7 DEGREES          
REMARK 500    LEU A 318   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    LEU A 330   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    LEU C 318   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    LEU C 330   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    CYS D 263   CA  -  CB  -  SG  ANGL. DEV. =  13.2 DEGREES          
REMARK 500    PHE D 298   CB  -  CG  -  CD2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    LEU D 428   CB  -  CG  -  CD2 ANGL. DEV. = -10.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE B  43      -12.07     75.83                                   
REMARK 500    THR B  50      -82.54    -74.99                                   
REMARK 500    ASP B  54     -150.09     12.05                                   
REMARK 500    ASN B 106       52.97   -158.25                                   
REMARK 500    ALA B 162       68.08   -160.55                                   
REMARK 500    SER B 198      -31.03     60.55                                   
REMARK 500    ALA B 199      -26.00   -140.77                                   
REMARK 500    SER B 215       16.89   -142.05                                   
REMARK 500    GLU B 255      -73.99    -47.48                                   
REMARK 500    ASP B 297      -71.67   -105.55                                   
REMARK 500    ARG B 381       90.29     25.84                                   
REMARK 500    PHE B 398      -60.83   -126.14                                   
REMARK 500    GLU B 482      -72.43   -109.92                                   
REMARK 500    ASN B 485      128.55     79.31                                   
REMARK 500    THR B 533       13.25     49.18                                   
REMARK 500    GLU B 538       -6.65     72.90                                   
REMARK 500    PHE A  43      -11.71     76.71                                   
REMARK 500    THR A  50      -81.80    -75.52                                   
REMARK 500    ASP A  54     -150.48     13.30                                   
REMARK 500    ASN A 106       54.05   -158.05                                   
REMARK 500    ALA A 162       68.96   -160.09                                   
REMARK 500    SER A 198      -29.72     61.09                                   
REMARK 500    ALA A 199      -25.75   -144.21                                   
REMARK 500    GLU A 255      -73.91    -46.83                                   
REMARK 500    ASP A 297      -71.41   -105.27                                   
REMARK 500    ARG A 381       89.93     24.98                                   
REMARK 500    PHE A 398      -61.30   -126.12                                   
REMARK 500    GLU A 482      -72.08   -109.36                                   
REMARK 500    ASN A 485      128.82     80.01                                   
REMARK 500    ASP A 537        2.18    -64.39                                   
REMARK 500    LYS A 558       40.99    -98.28                                   
REMARK 500    PHE C  43      -11.77     76.71                                   
REMARK 500    THR C  50      -81.88    -75.52                                   
REMARK 500    ASP C  54     -150.54     13.26                                   
REMARK 500    ASN C 106       54.14   -158.09                                   
REMARK 500    ALA C 162       69.07   -159.94                                   
REMARK 500    SER C 198      -29.63     61.09                                   
REMARK 500    ALA C 199      -25.73   -144.31                                   
REMARK 500    GLU C 255      -73.95    -46.77                                   
REMARK 500    ASP C 297      -71.39   -105.41                                   
REMARK 500    ARG C 381       89.95     24.92                                   
REMARK 500    PHE C 398      -61.32   -126.02                                   
REMARK 500    GLU C 482      -72.05   -109.45                                   
REMARK 500    ASN C 485      128.87     80.00                                   
REMARK 500    ASP C 537        2.31    -64.39                                   
REMARK 500    LYS C 558       41.11    -98.32                                   
REMARK 500    PHE D  43      -12.02     75.81                                   
REMARK 500    THR D  50      -82.40    -75.11                                   
REMARK 500    ASP D  54     -150.08     11.82                                   
REMARK 500    ASN D 106       52.93   -158.19                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.                        
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 601 bound   
REMARK 800  to ASN A 17                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound   
REMARK 800  to ASN A 341                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 603 bound   
REMARK 800  to ASN A 481                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound   
REMARK 800  to ASN B 341                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 601 bound   
REMARK 800  to ASN C 17                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 602 bound   
REMARK 800  to ASN C 341                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 603 bound   
REMARK 800  to ASN C 481                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 601 bound   
REMARK 800  to ASN D 341                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-4400   RELATED DB: EMDB                              
REMARK 900 MODEL OF FULL-LENGTH, FULLY-GLYCOSYLATED HUMAN                       
REMARK 900 BUTYRYLCHOLINESTERASE TETRAMER                                       
DBREF  6I2T B    1   574  UNP    P06276   CHLE_HUMAN      29    602             
DBREF  6I2T A    1   574  UNP    P06276   CHLE_HUMAN      29    602             
DBREF  6I2T C    1   574  UNP    P06276   CHLE_HUMAN      29    602             
DBREF  6I2T D    1   574  UNP    P06276   CHLE_HUMAN      29    602             
DBREF  6I2T J    4    15  PDB    6I2T     6I2T             4     15             
SEQRES   1 B  574  GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL          
SEQRES   2 B  574  ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR          
SEQRES   3 B  574  ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY          
SEQRES   4 B  574  ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP          
SEQRES   5 B  574  SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS          
SEQRES   6 B  574  CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY          
SEQRES   7 B  574  SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP          
SEQRES   8 B  574  CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO          
SEQRES   9 B  574  LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY          
SEQRES  10 B  574  PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY          
SEQRES  11 B  574  LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER          
SEQRES  12 B  574  MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU          
SEQRES  13 B  574  PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE          
SEQRES  14 B  574  ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE          
SEQRES  15 B  574  ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE          
SEQRES  16 B  574  GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU          
SEQRES  17 B  574  LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE          
SEQRES  18 B  574  LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR          
SEQRES  19 B  574  SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA          
SEQRES  20 B  574  LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE          
SEQRES  21 B  574  ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU          
SEQRES  22 B  574  LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU          
SEQRES  23 B  574  SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU          
SEQRES  24 B  574  THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE          
SEQRES  25 B  574  LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU          
SEQRES  26 B  574  GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER          
SEQRES  27 B  574  LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN          
SEQRES  28 B  574  GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE          
SEQRES  29 B  574  GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL          
SEQRES  30 B  574  ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY          
SEQRES  31 B  574  ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU          
SEQRES  32 B  574  GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA          
SEQRES  33 B  574  PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO          
SEQRES  34 B  574  TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE          
SEQRES  35 B  574  GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN          
SEQRES  36 B  574  TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL          
SEQRES  37 B  574  LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN          
SEQRES  38 B  574  GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS          
SEQRES  39 B  574  SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER          
SEQRES  40 B  574  THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG          
SEQRES  41 B  574  PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR          
SEQRES  42 B  574  GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY          
SEQRES  43 B  574  PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN          
SEQRES  44 B  574  GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL          
SEQRES  45 B  574  GLY LEU                                                      
SEQRES   1 A  574  GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL          
SEQRES   2 A  574  ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR          
SEQRES   3 A  574  ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY          
SEQRES   4 A  574  ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP          
SEQRES   5 A  574  SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS          
SEQRES   6 A  574  CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY          
SEQRES   7 A  574  SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP          
SEQRES   8 A  574  CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO          
SEQRES   9 A  574  LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY          
SEQRES  10 A  574  PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY          
SEQRES  11 A  574  LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER          
SEQRES  12 A  574  MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU          
SEQRES  13 A  574  PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE          
SEQRES  14 A  574  ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE          
SEQRES  15 A  574  ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE          
SEQRES  16 A  574  GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU          
SEQRES  17 A  574  LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE          
SEQRES  18 A  574  LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR          
SEQRES  19 A  574  SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA          
SEQRES  20 A  574  LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE          
SEQRES  21 A  574  ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU          
SEQRES  22 A  574  LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU          
SEQRES  23 A  574  SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU          
SEQRES  24 A  574  THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE          
SEQRES  25 A  574  LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU          
SEQRES  26 A  574  GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER          
SEQRES  27 A  574  LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN          
SEQRES  28 A  574  GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE          
SEQRES  29 A  574  GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL          
SEQRES  30 A  574  ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY          
SEQRES  31 A  574  ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU          
SEQRES  32 A  574  GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA          
SEQRES  33 A  574  PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO          
SEQRES  34 A  574  TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE          
SEQRES  35 A  574  GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN          
SEQRES  36 A  574  TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL          
SEQRES  37 A  574  LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN          
SEQRES  38 A  574  GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS          
SEQRES  39 A  574  SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER          
SEQRES  40 A  574  THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG          
SEQRES  41 A  574  PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR          
SEQRES  42 A  574  GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY          
SEQRES  43 A  574  PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN          
SEQRES  44 A  574  GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL          
SEQRES  45 A  574  GLY LEU                                                      
SEQRES   1 C  574  GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL          
SEQRES   2 C  574  ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR          
SEQRES   3 C  574  ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY          
SEQRES   4 C  574  ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP          
SEQRES   5 C  574  SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS          
SEQRES   6 C  574  CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY          
SEQRES   7 C  574  SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP          
SEQRES   8 C  574  CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO          
SEQRES   9 C  574  LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY          
SEQRES  10 C  574  PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY          
SEQRES  11 C  574  LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER          
SEQRES  12 C  574  MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU          
SEQRES  13 C  574  PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE          
SEQRES  14 C  574  ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE          
SEQRES  15 C  574  ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE          
SEQRES  16 C  574  GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU          
SEQRES  17 C  574  LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE          
SEQRES  18 C  574  LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR          
SEQRES  19 C  574  SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA          
SEQRES  20 C  574  LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE          
SEQRES  21 C  574  ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU          
SEQRES  22 C  574  LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU          
SEQRES  23 C  574  SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU          
SEQRES  24 C  574  THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE          
SEQRES  25 C  574  LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU          
SEQRES  26 C  574  GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER          
SEQRES  27 C  574  LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN          
SEQRES  28 C  574  GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE          
SEQRES  29 C  574  GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL          
SEQRES  30 C  574  ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY          
SEQRES  31 C  574  ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU          
SEQRES  32 C  574  GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA          
SEQRES  33 C  574  PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO          
SEQRES  34 C  574  TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE          
SEQRES  35 C  574  GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN          
SEQRES  36 C  574  TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL          
SEQRES  37 C  574  LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN          
SEQRES  38 C  574  GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS          
SEQRES  39 C  574  SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER          
SEQRES  40 C  574  THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG          
SEQRES  41 C  574  PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR          
SEQRES  42 C  574  GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY          
SEQRES  43 C  574  PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN          
SEQRES  44 C  574  GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL          
SEQRES  45 C  574  GLY LEU                                                      
SEQRES   1 D  574  GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL          
SEQRES   2 D  574  ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR          
SEQRES   3 D  574  ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY          
SEQRES   4 D  574  ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP          
SEQRES   5 D  574  SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS          
SEQRES   6 D  574  CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY          
SEQRES   7 D  574  SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP          
SEQRES   8 D  574  CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO          
SEQRES   9 D  574  LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY          
SEQRES  10 D  574  PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY          
SEQRES  11 D  574  LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER          
SEQRES  12 D  574  MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU          
SEQRES  13 D  574  PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE          
SEQRES  14 D  574  ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE          
SEQRES  15 D  574  ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE          
SEQRES  16 D  574  GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU          
SEQRES  17 D  574  LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE          
SEQRES  18 D  574  LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR          
SEQRES  19 D  574  SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA          
SEQRES  20 D  574  LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE          
SEQRES  21 D  574  ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU          
SEQRES  22 D  574  LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU          
SEQRES  23 D  574  SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU          
SEQRES  24 D  574  THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE          
SEQRES  25 D  574  LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU          
SEQRES  26 D  574  GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER          
SEQRES  27 D  574  LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN          
SEQRES  28 D  574  GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE          
SEQRES  29 D  574  GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL          
SEQRES  30 D  574  ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY          
SEQRES  31 D  574  ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU          
SEQRES  32 D  574  GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA          
SEQRES  33 D  574  PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO          
SEQRES  34 D  574  TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE          
SEQRES  35 D  574  GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN          
SEQRES  36 D  574  TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL          
SEQRES  37 D  574  LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN          
SEQRES  38 D  574  GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS          
SEQRES  39 D  574  SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER          
SEQRES  40 D  574  THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG          
SEQRES  41 D  574  PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR          
SEQRES  42 D  574  GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY          
SEQRES  43 D  574  PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN          
SEQRES  44 D  574  GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL          
SEQRES  45 D  574  GLY LEU                                                      
SEQRES   1 J   12  PRO PRO PRO PRO PRO PRO PRO PRO PRO PRO PRO PRO              
HET    NAG  B 601      14                                                       
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HET    NAG  C 601      14                                                       
HET    NAG  C 602      14                                                       
HET    NAG  C 603      14                                                       
HET    NAG  D 601      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   6  NAG    8(C8 H15 N O6)                                               
HELIX    1 AA1 LEU B   38  ARG B   42  5                                   5    
HELIX    2 AA2 PHE B   76  MET B   81  1                                   6    
HELIX    3 AA3 LEU B  125  ASP B  129  5                                   5    
HELIX    4 AA4 GLY B  130  ARG B  138  1                                   9    
HELIX    5 AA5 VAL B  148  LEU B  154  1                                   7    
HELIX    6 AA6 ASN B  165  ILE B  182  1                                  18    
HELIX    7 AA7 ALA B  183  PHE B  185  5                                   3    
HELIX    8 AA8 ALA B  199  SER B  210  1                                  12    
HELIX    9 AA9 PRO B  211  HIS B  214  5                                   4    
HELIX   10 AB1 SER B  235  THR B  250  1                                  16    
HELIX   11 AB2 ASN B  256  ARG B  265  1                                  10    
HELIX   12 AB3 ASP B  268  GLU B  276  1                                   9    
HELIX   13 AB4 ALA B  277  VAL B  279  5                                   3    
HELIX   14 AB5 MET B  302  LEU B  309  1                                   8    
HELIX   15 AB6 GLY B  326  GLY B  333  5                                   8    
HELIX   16 AB7 THR B  346  PHE B  358  1                                  13    
HELIX   17 AB8 SER B  362  TYR B  373  1                                  12    
HELIX   18 AB9 GLU B  383  PHE B  398  1                                  16    
HELIX   19 AC1 PHE B  398  GLU B  411  1                                  14    
HELIX   20 AC2 PRO B  431  GLY B  435  5                                   5    
HELIX   21 AC3 GLU B  441  PHE B  446  1                                   6    
HELIX   22 AC4 GLY B  447  ASN B  455  5                                   9    
HELIX   23 AC5 THR B  457  GLY B  478  1                                  22    
HELIX   24 AC6 ARG B  515  PHE B  525  1                                  11    
HELIX   25 AC7 PHE B  526  LEU B  530  5                                   5    
HELIX   26 AC8 GLU B  538  ASP B  556  1                                  19    
HELIX   27 AC9 TRP B  557  ASN B  562  1                                   6    
HELIX   28 AD1 LEU A   38  ARG A   42  5                                   5    
HELIX   29 AD2 PHE A   76  MET A   81  1                                   6    
HELIX   30 AD3 LEU A  125  ASP A  129  5                                   5    
HELIX   31 AD4 GLY A  130  ARG A  138  1                                   9    
HELIX   32 AD5 GLY A  149  LEU A  154  1                                   6    
HELIX   33 AD6 ASN A  165  ILE A  182  1                                  18    
HELIX   34 AD7 ALA A  183  PHE A  185  5                                   3    
HELIX   35 AD8 ALA A  199  SER A  210  1                                  12    
HELIX   36 AD9 PRO A  211  HIS A  214  5                                   4    
HELIX   37 AE1 SER A  235  THR A  250  1                                  16    
HELIX   38 AE2 ASN A  256  ARG A  265  1                                  10    
HELIX   39 AE3 ASP A  268  GLU A  276  1                                   9    
HELIX   40 AE4 ALA A  277  VAL A  279  5                                   3    
HELIX   41 AE5 MET A  302  LEU A  309  1                                   8    
HELIX   42 AE6 GLY A  326  GLY A  333  5                                   8    
HELIX   43 AE7 THR A  346  PHE A  358  1                                  13    
HELIX   44 AE8 SER A  362  THR A  374  1                                  13    
HELIX   45 AE9 GLU A  383  PHE A  398  1                                  16    
HELIX   46 AF1 PHE A  398  GLU A  411  1                                  14    
HELIX   47 AF2 PRO A  431  GLY A  435  5                                   5    
HELIX   48 AF3 GLU A  441  PHE A  446  1                                   6    
HELIX   49 AF4 GLY A  447  ASN A  455  5                                   9    
HELIX   50 AF5 THR A  457  GLY A  478  1                                  22    
HELIX   51 AF6 ARG A  515  PHE A  525  1                                  11    
HELIX   52 AF7 PHE A  526  GLU A  531  1                                   6    
HELIX   53 AF8 ASP A  537  ASN A  551  1                                  15    
HELIX   54 AF9 ASN A  552  LYS A  558  1                                   7    
HELIX   55 AG1 LEU C   38  ARG C   42  5                                   5    
HELIX   56 AG2 PHE C   76  MET C   81  1                                   6    
HELIX   57 AG3 LEU C  125  ASP C  129  5                                   5    
HELIX   58 AG4 GLY C  130  ARG C  138  1                                   9    
HELIX   59 AG5 GLY C  149  LEU C  154  1                                   6    
HELIX   60 AG6 ASN C  165  ILE C  182  1                                  18    
HELIX   61 AG7 ALA C  183  PHE C  185  5                                   3    
HELIX   62 AG8 ALA C  199  SER C  210  1                                  12    
HELIX   63 AG9 PRO C  211  HIS C  214  5                                   4    
HELIX   64 AH1 SER C  235  THR C  250  1                                  16    
HELIX   65 AH2 ASN C  256  ARG C  265  1                                  10    
HELIX   66 AH3 ASP C  268  GLU C  276  1                                   9    
HELIX   67 AH4 ALA C  277  VAL C  279  5                                   3    
HELIX   68 AH5 MET C  302  LEU C  309  1                                   8    
HELIX   69 AH6 GLY C  326  GLY C  333  5                                   8    
HELIX   70 AH7 THR C  346  PHE C  358  1                                  13    
HELIX   71 AH8 SER C  362  THR C  374  1                                  13    
HELIX   72 AH9 GLU C  383  PHE C  398  1                                  16    
HELIX   73 AI1 PHE C  398  GLU C  411  1                                  14    
HELIX   74 AI2 PRO C  431  GLY C  435  5                                   5    
HELIX   75 AI3 GLU C  441  PHE C  446  1                                   6    
HELIX   76 AI4 GLY C  447  ASN C  455  5                                   9    
HELIX   77 AI5 THR C  457  GLY C  478  1                                  22    
HELIX   78 AI6 ARG C  515  PHE C  525  1                                  11    
HELIX   79 AI7 PHE C  526  GLU C  531  1                                   6    
HELIX   80 AI8 ASP C  537  ASN C  551  1                                  15    
HELIX   81 AI9 ASN C  552  LYS C  558  1                                   7    
HELIX   82 AJ1 LEU D   38  ARG D   42  5                                   5    
HELIX   83 AJ2 PHE D   76  MET D   81  1                                   6    
HELIX   84 AJ3 LEU D  125  ASP D  129  5                                   5    
HELIX   85 AJ4 GLY D  130  ARG D  138  1                                   9    
HELIX   86 AJ5 VAL D  148  LEU D  154  1                                   7    
HELIX   87 AJ6 ASN D  165  ILE D  182  1                                  18    
HELIX   88 AJ7 ALA D  183  PHE D  185  5                                   3    
HELIX   89 AJ8 ALA D  199  SER D  210  1                                  12    
HELIX   90 AJ9 PRO D  211  HIS D  214  5                                   4    
HELIX   91 AK1 SER D  235  THR D  250  1                                  16    
HELIX   92 AK2 ASN D  256  ARG D  265  1                                  10    
HELIX   93 AK3 ASP D  268  GLU D  276  1                                   9    
HELIX   94 AK4 ALA D  277  VAL D  279  5                                   3    
HELIX   95 AK5 MET D  302  LEU D  309  1                                   8    
HELIX   96 AK6 GLY D  326  GLY D  333  5                                   8    
HELIX   97 AK7 THR D  346  PHE D  358  1                                  13    
HELIX   98 AK8 SER D  362  TYR D  373  1                                  12    
HELIX   99 AK9 GLU D  383  PHE D  398  1                                  16    
HELIX  100 AL1 PHE D  398  GLU D  411  1                                  14    
HELIX  101 AL2 PRO D  431  GLY D  435  5                                   5    
HELIX  102 AL3 GLU D  441  PHE D  446  1                                   6    
HELIX  103 AL4 GLY D  447  ASN D  455  5                                   9    
HELIX  104 AL5 THR D  457  GLY D  478  1                                  22    
HELIX  105 AL6 ARG D  515  PHE D  525  1                                  11    
HELIX  106 AL7 PHE D  526  LEU D  530  5                                   5    
HELIX  107 AL8 GLU D  538  ASP D  556  1                                  19    
HELIX  108 AL9 TRP D  557  ASN D  562  1                                   6    
SHEET    1 AA1 3 ILE B   5  THR B   8  0                                        
SHEET    2 AA1 3 GLY B  11  ARG B  14 -1  O  VAL B  13   N  ILE B   6           
SHEET    3 AA1 3 TRP B  56  ASN B  57  1  O  TRP B  56   N  ARG B  14           
SHEET    1 AA211 MET B  16  VAL B  20  0                                        
SHEET    2 AA211 GLY B  23  PRO B  32 -1  O  ALA B  27   N  MET B  16           
SHEET    3 AA211 TYR B  94  ALA B 101 -1  O  LEU B  95   N  ILE B  31           
SHEET    4 AA211 ILE B 140  MET B 144 -1  O  SER B 143   N  ASN B  96           
SHEET    5 AA211 ALA B 107  ILE B 113  1  N  LEU B 110   O  ILE B 140           
SHEET    6 AA211 GLY B 187  GLU B 197  1  O  PHE B 195   N  ILE B 111           
SHEET    7 AA211 ARG B 219  GLN B 223  1  O  ILE B 221   N  LEU B 194           
SHEET    8 AA211 ILE B 317  ASN B 322  1  O  LEU B 318   N  LEU B 222           
SHEET    9 AA211 ALA B 416  PHE B 421  1  O  PHE B 417   N  VAL B 319           
SHEET   10 AA211 LYS B 499  LEU B 503  1  O  LEU B 503   N  TYR B 420           
SHEET   11 AA211 ILE B 510  THR B 512 -1  O  MET B 511   N  TYR B 500           
SHEET    1 AA3 2 SER B  64  CYS B  65  0                                        
SHEET    2 AA3 2 LEU B  88  SER B  89  1  O  SER B  89   N  SER B  64           
SHEET    1 AA4 3 ILE A   5  THR A   8  0                                        
SHEET    2 AA4 3 GLY A  11  ARG A  14 -1  O  GLY A  11   N  THR A   8           
SHEET    3 AA4 3 TRP A  56  ASN A  57  1  O  TRP A  56   N  ARG A  14           
SHEET    1 AA511 MET A  16  VAL A  20  0                                        
SHEET    2 AA511 GLY A  23  PRO A  32 -1  O  ALA A  27   N  MET A  16           
SHEET    3 AA511 TYR A  94  PRO A 100 -1  O  LEU A  95   N  ILE A  31           
SHEET    4 AA511 ILE A 140  MET A 144 -1  O  SER A 143   N  ASN A  96           
SHEET    5 AA511 ALA A 107  ILE A 113  1  N  LEU A 110   O  ILE A 140           
SHEET    6 AA511 GLY A 187  GLU A 197  1  O  THR A 193   N  ILE A 111           
SHEET    7 AA511 ARG A 219  GLN A 223  1  O  ILE A 221   N  LEU A 194           
SHEET    8 AA511 ILE A 317  ASN A 322  1  O  LEU A 318   N  LEU A 222           
SHEET    9 AA511 ALA A 416  PHE A 421  1  O  PHE A 417   N  VAL A 319           
SHEET   10 AA511 LYS A 499  LEU A 503  1  O  LEU A 501   N  TYR A 420           
SHEET   11 AA511 ILE A 510  THR A 512 -1  O  MET A 511   N  TYR A 500           
SHEET    1 AA6 2 SER A  64  CYS A  65  0                                        
SHEET    2 AA6 2 LEU A  88  SER A  89  1  O  SER A  89   N  SER A  64           
SHEET    1 AA7 3 ILE C   5  THR C   8  0                                        
SHEET    2 AA7 3 GLY C  11  ARG C  14 -1  O  GLY C  11   N  THR C   8           
SHEET    3 AA7 3 TRP C  56  ASN C  57  1  O  TRP C  56   N  ARG C  14           
SHEET    1 AA811 MET C  16  VAL C  20  0                                        
SHEET    2 AA811 GLY C  23  PRO C  32 -1  O  ALA C  27   N  MET C  16           
SHEET    3 AA811 TYR C  94  PRO C 100 -1  O  LEU C  95   N  ILE C  31           
SHEET    4 AA811 ILE C 140  MET C 144 -1  O  SER C 143   N  ASN C  96           
SHEET    5 AA811 ALA C 107  ILE C 113  1  N  LEU C 110   O  ILE C 140           
SHEET    6 AA811 GLY C 187  GLU C 197  1  O  THR C 193   N  ILE C 111           
SHEET    7 AA811 ARG C 219  GLN C 223  1  O  ILE C 221   N  LEU C 194           
SHEET    8 AA811 ILE C 317  ASN C 322  1  O  LEU C 318   N  LEU C 222           
SHEET    9 AA811 ALA C 416  PHE C 421  1  O  PHE C 417   N  VAL C 319           
SHEET   10 AA811 LYS C 499  LEU C 503  1  O  LEU C 501   N  TYR C 420           
SHEET   11 AA811 ILE C 510  THR C 512 -1  O  MET C 511   N  TYR C 500           
SHEET    1 AA9 2 SER C  64  CYS C  65  0                                        
SHEET    2 AA9 2 LEU C  88  SER C  89  1  O  SER C  89   N  SER C  64           
SHEET    1 AB1 3 ILE D   5  THR D   8  0                                        
SHEET    2 AB1 3 GLY D  11  ARG D  14 -1  O  VAL D  13   N  ILE D   6           
SHEET    3 AB1 3 TRP D  56  ASN D  57  1  O  TRP D  56   N  ARG D  14           
SHEET    1 AB211 MET D  16  VAL D  20  0                                        
SHEET    2 AB211 GLY D  23  PRO D  32 -1  O  ALA D  27   N  MET D  16           
SHEET    3 AB211 TYR D  94  ALA D 101 -1  O  LEU D  95   N  ILE D  31           
SHEET    4 AB211 ILE D 140  MET D 144 -1  O  SER D 143   N  ASN D  96           
SHEET    5 AB211 ALA D 107  ILE D 113  1  N  LEU D 110   O  ILE D 140           
SHEET    6 AB211 GLY D 187  GLU D 197  1  O  PHE D 195   N  ILE D 111           
SHEET    7 AB211 ARG D 219  GLN D 223  1  O  ILE D 221   N  LEU D 194           
SHEET    8 AB211 ILE D 317  ASN D 322  1  O  LEU D 318   N  LEU D 222           
SHEET    9 AB211 ALA D 416  PHE D 421  1  O  PHE D 417   N  VAL D 319           
SHEET   10 AB211 LYS D 499  LEU D 503  1  O  LEU D 503   N  TYR D 420           
SHEET   11 AB211 ILE D 510  THR D 512 -1  O  MET D 511   N  TYR D 500           
SHEET    1 AB3 2 SER D  64  CYS D  65  0                                        
SHEET    2 AB3 2 LEU D  88  SER D  89  1  O  SER D  89   N  SER D  64           
SSBOND   1 CYS B   65    CYS B   92                          1555   1555  2.05  
SSBOND   2 CYS B  252    CYS B  263                          1555   1555  2.03  
SSBOND   3 CYS B  400    CYS B  519                          1555   1555  2.04  
SSBOND   4 CYS A   65    CYS A   92                          1555   1555  2.04  
SSBOND   5 CYS A  252    CYS A  263                          1555   1555  2.04  
SSBOND   6 CYS A  400    CYS A  519                          1555   1555  2.04  
SSBOND   7 CYS C   65    CYS C   92                          1555   1555  2.04  
SSBOND   8 CYS C  252    CYS C  263                          1555   1555  2.04  
SSBOND   9 CYS C  400    CYS C  519                          1555   1555  2.03  
SSBOND  10 CYS D   65    CYS D   92                          1555   1555  2.05  
SSBOND  11 CYS D  252    CYS D  263                          1555   1555  2.03  
SSBOND  12 CYS D  400    CYS D  519                          1555   1555  2.04  
LINK         ND2 ASN B 341                 C1  NAG B 601     1555   1555  1.43  
LINK         ND2 ASN A  17                 C1  NAG A 601     1555   1555  1.43  
LINK         ND2 ASN A 341                 C1  NAG A 602     1555   1555  1.44  
LINK         ND2 ASN A 481                 C1  NAG A 603     1555   1555  1.44  
LINK         ND2 ASN C  17                 C1  NAG C 601     1555   1555  1.43  
LINK         ND2 ASN C 341                 C1  NAG C 602     1555   1555  1.44  
LINK         ND2 ASN C 481                 C1  NAG C 603     1555   1555  1.44  
LINK         ND2 ASN D 341                 C1  NAG D 601     1555   1555  1.43  
CISPEP   1 ALA B  101    PRO B  102          0         0.13                     
CISPEP   2 ASP B  379    GLN B  380          0        -4.63                     
CISPEP   3 ALA A  101    PRO A  102          0        -0.20                     
CISPEP   4 ASP A  379    GLN A  380          0        -3.57                     
CISPEP   5 ALA C  101    PRO C  102          0        -0.22                     
CISPEP   6 ASP C  379    GLN C  380          0        -3.48                     
CISPEP   7 ALA D  101    PRO D  102          0         0.11                     
CISPEP   8 ASP D  379    GLN D  380          0        -4.69                     
SITE     1 AC1  2 ILE A   4  ASN A  17                                          
SITE     1 AC2  3 GLY A 336  ASN A 341  ASN A 342                               
SITE     1 AC3  5 TYR A 477  ASN A 479  ASN A 481  THR A 483                    
SITE     2 AC3  5 GLN A 484                                                     
SITE     1 AC4  2 ASN B 341  ASN B 342                                          
SITE     1 AC5  2 ILE C   4  ASN C  17                                          
SITE     1 AC6  3 GLY C 336  ASN C 341  ASN C 342                               
SITE     1 AC7  5 TYR C 477  ASN C 479  ASN C 481  THR C 483                    
SITE     2 AC7  5 GLN C 484                                                     
SITE     1 AC8  2 ASN D 341  ASN D 342                                          
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      0.003241  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.003241  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003241        0.00000                         
TER    4513      THR B 565                                                      
TER    8991      PHE A 561                                                      
TER   13469      PHE C 561                                                      
TER   17982      THR D 565                                                      
TER   18067      PRO J  15                                                      
MASTER      310    0    8  108   64    0   10    618174    5  144  181          
END                                                                             

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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:
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