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LongText Report for: 2HRR-pdb

Name Class
2HRR-pdb
HEADER    HYDROLASE                               20-JUL-06   2HRR              
TITLE     CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE 1 (HCE1)            
TITLE    2 IN COVALENT COMPLEX WITH THE NERVE AGENT TABUN (GA)                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIVER CARBOXYLESTERASE 1;                                  
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: ACYL COENZYME A:CHOLESTEROL ACYLTRANSFERASE, ACAT,          
COMPND   5 MONOCYTE/MACROPHAGE SERINE ESTERASE, HMSE, SERINE ESTERASE           
COMPND   6 1, BRAIN CARBOXYLESTERASE HBR1, TRIACYLGLYCEROL HYDROLASE,           
COMPND   7 TGH, EGASYN;                                                         
COMPND   8 EC: 3.1.1.1;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: CES1;                                                          
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM                              
KEYWDS    HYDROLASE, CARBOXYLESTERASE, TABUN                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.D.FLEMING,M.R.REDINBO                                               
REVDAT   1   01-MAY-07 2HRR    0                                                
JRNL        AUTH   C.D.FLEMING,C.C.EDWARDS,S.D.KIRBY,D.M.MAXWELL,               
JRNL        AUTH 2 P.M.POTTER,D.M.CERASOLI,M.R.REDINBO                          
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN CARBOXYLESTERASE 1 IN            
JRNL        TITL 2 COVALENT COMPLEXES WITH THE CHEMICAL WARFARE                 
JRNL        TITL 3 AGENTS SOMAN AND TABUN.                                      
JRNL        REF    BIOCHEMISTRY                               2007              
JRNL        REFN   ASTM BICHAW  US ISSN 0006-2960                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.70 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 72889.760                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 52209                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3705                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7979                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2060                       
REMARK   3   BIN FREE R VALUE                    : 0.2840                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 626                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12379                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 223                                     
REMARK   3   SOLVENT ATOMS            : 827                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.90000                                             
REMARK   3    B22 (A**2) : 1.30000                                              
REMARK   3    B33 (A**2) : -0.40000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.24                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.35                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.84                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.360 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.340 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.100 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.270 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 28.98                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : GAC.PAR                                        
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : GAC.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2HRR COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-2006.                
REMARK 100 THE RCSB ID CODE IS RCSB038685.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-2006                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53127                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11700                            
REMARK 200   FOR THE DATA SET  : 21.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.29200                            
REMARK 200   FOR SHELL         : 7.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY: 1MX1                                      
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRATE PH 5.5, 8-11% PEG          
REMARK 280  3350, 0.1-0.4M LITHIUM SULFATE, 0.1M LITHIUM CHLORIDE, 0.1M         
REMARK 280  SODIUM CHLORIDE, 5% GLYCEROL, VAPOR DIFFUSION, SITTING DROP,        
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   1/2-X,-Y,1/2+Z                                          
REMARK 290       3555   -X,1/2+Y,1/2-Z                                          
REMARK 290       4555   1/2+X,1/2-Y,-Z                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       27.78500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      101.46000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       90.52500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      101.46000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.78500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       90.52500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 3 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     SER B  2021                                                      
REMARK 465     SER C  3021                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI                             
REMARK 500   OG   SER B  2221     O1   NTJ       2              1.59            
REMARK 500   ND2  ASN A  1079     O5   NAG A   179              1.81            
REMARK 500   ND2  ASN C  3079     O5   NAG C   379              1.88            
REMARK 500   ND2  ASN C  3079     C2   NAG C   379              2.16            
REMARK 500   O    ASN B  2079     O2   SIA     282              2.17            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)                  
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS A1092   CD    LYS A1092   CE    -0.056                        
REMARK 500    LYS A1092   CE    LYS A1092   NZ    -0.154                        
REMARK 500    PRO A1317   CB    PRO A1317   CG     0.097                        
REMARK 500    PRO A1317   CG    PRO A1317   CD     0.054                        
REMARK 500    MET A1459   SD    MET A1459   CE     0.040                        
REMARK 500    LYS B2092   CD    LYS B2092   CE    -0.058                        
REMARK 500    LYS B2092   CE    LYS B2092   NZ    -0.158                        
REMARK 500    LYS C3092   CD    LYS C3092   CE    -0.058                        
REMARK 500    LYS C3092   CE    LYS C3092   NZ    -0.156                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER A1075   N   -  CA  -  C   ANGL. DEV. = 10.3 DEGREES           
REMARK 500    ASP A1090   N   -  CA  -  C   ANGL. DEV. = -8.4 DEGREES           
REMARK 500    LYS A1092   CD  -  CE  -  NZ  ANGL. DEV. = 12.4 DEGREES           
REMARK 500    ASP A1126   N   -  CA  -  C   ANGL. DEV. =-10.7 DEGREES           
REMARK 500    ARG A1242   N   -  CA  -  C   ANGL. DEV. = -8.1 DEGREES           
REMARK 500    THR A1252   N   -  CA  -  C   ANGL. DEV. = -9.0 DEGREES           
REMARK 500    SER A1253   N   -  CA  -  C   ANGL. DEV. =  8.7 DEGREES           
REMARK 500    GLN A1316   N   -  CA  -  C   ANGL. DEV. = 14.0 DEGREES           
REMARK 500    PRO A1317   N   -  CA  -  C   ANGL. DEV. =-15.4 DEGREES           
REMARK 500    PRO A1317   C   -  N   -  CA  ANGL. DEV. =-12.3 DEGREES           
REMARK 500    PRO A1317   C   -  N   -  CD  ANGL. DEV. =  7.7 DEGREES           
REMARK 500    ILE A1323   N   -  CA  -  C   ANGL. DEV. = -9.5 DEGREES           
REMARK 500    GLU A1448   N   -  CA  -  C   ANGL. DEV. = -8.7 DEGREES           
REMARK 500    TRP A1517   N   -  CA  -  C   ANGL. DEV. = -8.1 DEGREES           
REMARK 500    GLN A1528   N   -  CA  -  C   ANGL. DEV. = -8.2 DEGREES           
REMARK 500    SER B2075   N   -  CA  -  C   ANGL. DEV. = 11.5 DEGREES           
REMARK 500    LYS B2092   CD  -  CE  -  NZ  ANGL. DEV. = 12.0 DEGREES           
REMARK 500    ASP B2115   N   -  CA  -  C   ANGL. DEV. = -7.6 DEGREES           
REMARK 500    PHE B2177   N   -  CA  -  C   ANGL. DEV. =  8.9 DEGREES           
REMARK 500    THR B2252   N   -  CA  -  C   ANGL. DEV. = -7.8 DEGREES           
REMARK 500    SER B2253   N   -  CA  -  C   ANGL. DEV. =  9.5 DEGREES           
REMARK 500    LEU B2319   N   -  CA  -  C   ANGL. DEV. = -8.3 DEGREES           
REMARK 500    LEU C3034   CA  -  CB  -  CG  ANGL. DEV. =  9.7 DEGREES           
REMARK 500    SER C3075   N   -  CA  -  C   ANGL. DEV. =  8.8 DEGREES           
REMARK 500    MET C3086   N   -  CA  -  C   ANGL. DEV. = -7.8 DEGREES           
REMARK 500    PRO C3091   C   -  N   -  CD  ANGL. DEV. =  8.1 DEGREES           
REMARK 500    LYS C3092   CD  -  CE  -  NZ  ANGL. DEV. = 12.3 DEGREES           
REMARK 500    ASP C3115   N   -  CA  -  C   ANGL. DEV. = -7.8 DEGREES           
REMARK 500    TYR C3122   N   -  CA  -  C   ANGL. DEV. = -8.2 DEGREES           
REMARK 500    PHE C3177   N   -  CA  -  C   ANGL. DEV. =  8.8 DEGREES           
REMARK 500    ASN C3204   N   -  CA  -  C   ANGL. DEV. =  7.9 DEGREES           
REMARK 500    SER C3253   N   -  CA  -  C   ANGL. DEV. =  8.6 DEGREES           
REMARK 500    LEU C3319   N   -  CA  -  C   ANGL. DEV. = -7.6 DEGREES           
REMARK 500    ILE C3323   N   -  CA  -  C   ANGL. DEV. = -8.5 DEGREES           
REMARK 500    ALA C3536   N   -  CA  -  C   ANGL. DEV. = -8.0 DEGREES           
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A1221     -119.59     63.81                                   
REMARK 500    SER C3221     -115.03     64.19                                   
DBREF  2HRR A 1021  1553  UNP    Q9UK77   EST1_HUMAN      21    553             
DBREF  2HRR B 2021  2553  UNP    Q9UK77   EST1_HUMAN      21    553             
DBREF  2HRR C 3021  3553  UNP    Q9UK77   EST1_HUMAN      21    553             
SEQADV 2HRR     A       UNP  Q9UK77    GLN   362 DELETION                       
SEQADV 2HRR     B       UNP  Q9UK77    GLN   362 DELETION                       
SEQADV 2HRR     C       UNP  Q9UK77    GLN   362 DELETION                       
SEQRES   1 A  532  SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL          
SEQRES   2 A  532  LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO          
SEQRES   3 A  532  VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO          
SEQRES   4 A  532  LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU          
SEQRES   5 A  532  PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO          
SEQRES   6 A  532  MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER          
SEQRES   7 A  532  GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS          
SEQRES   8 A  532  LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO          
SEQRES   9 A  532  ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL          
SEQRES  10 A  532  TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER          
SEQRES  11 A  532  THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL          
SEQRES  12 A  532  VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY          
SEQRES  13 A  532  PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP          
SEQRES  14 A  532  GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN          
SEQRES  15 A  532  ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL          
SEQRES  16 A  532  THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER          
SEQRES  17 A  532  VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS          
SEQRES  18 A  532  ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL          
SEQRES  19 A  532  LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN          
SEQRES  20 A  532  ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA          
SEQRES  21 A  532  VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU          
SEQRES  22 A  532  LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU          
SEQRES  23 A  532  ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU          
SEQRES  24 A  532  GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO          
SEQRES  25 A  532  GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO          
SEQRES  26 A  532  TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU          
SEQRES  27 A  532  ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN          
SEQRES  28 A  532  LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER          
SEQRES  29 A  532  TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU          
SEQRES  30 A  532  ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL          
SEQRES  31 A  532  LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL          
SEQRES  32 A  532  MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS          
SEQRES  33 A  532  ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN          
SEQRES  34 A  532  TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR          
SEQRES  35 A  532  VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE          
SEQRES  36 A  532  GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU          
SEQRES  37 A  532  ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN          
SEQRES  38 A  532  PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO          
SEQRES  39 A  532  HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN          
SEQRES  40 A  532  ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP          
SEQRES  41 A  532  LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS              
SEQRES   1 B  532  SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL          
SEQRES   2 B  532  LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO          
SEQRES   3 B  532  VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO          
SEQRES   4 B  532  LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU          
SEQRES   5 B  532  PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO          
SEQRES   6 B  532  MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER          
SEQRES   7 B  532  GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS          
SEQRES   8 B  532  LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO          
SEQRES   9 B  532  ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL          
SEQRES  10 B  532  TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER          
SEQRES  11 B  532  THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL          
SEQRES  12 B  532  VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY          
SEQRES  13 B  532  PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP          
SEQRES  14 B  532  GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN          
SEQRES  15 B  532  ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL          
SEQRES  16 B  532  THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER          
SEQRES  17 B  532  VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS          
SEQRES  18 B  532  ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL          
SEQRES  19 B  532  LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN          
SEQRES  20 B  532  ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA          
SEQRES  21 B  532  VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU          
SEQRES  22 B  532  LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU          
SEQRES  23 B  532  ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU          
SEQRES  24 B  532  GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO          
SEQRES  25 B  532  GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO          
SEQRES  26 B  532  TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU          
SEQRES  27 B  532  ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN          
SEQRES  28 B  532  LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER          
SEQRES  29 B  532  TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU          
SEQRES  30 B  532  ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL          
SEQRES  31 B  532  LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL          
SEQRES  32 B  532  MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS          
SEQRES  33 B  532  ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN          
SEQRES  34 B  532  TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR          
SEQRES  35 B  532  VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE          
SEQRES  36 B  532  GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU          
SEQRES  37 B  532  ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN          
SEQRES  38 B  532  PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO          
SEQRES  39 B  532  HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN          
SEQRES  40 B  532  ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP          
SEQRES  41 B  532  LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS              
SEQRES   1 C  532  SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL          
SEQRES   2 C  532  LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO          
SEQRES   3 C  532  VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO          
SEQRES   4 C  532  LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU          
SEQRES   5 C  532  PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO          
SEQRES   6 C  532  MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER          
SEQRES   7 C  532  GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS          
SEQRES   8 C  532  LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO          
SEQRES   9 C  532  ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL          
SEQRES  10 C  532  TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER          
SEQRES  11 C  532  THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL          
SEQRES  12 C  532  VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY          
SEQRES  13 C  532  PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP          
SEQRES  14 C  532  GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN          
SEQRES  15 C  532  ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL          
SEQRES  16 C  532  THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER          
SEQRES  17 C  532  VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS          
SEQRES  18 C  532  ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL          
SEQRES  19 C  532  LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN          
SEQRES  20 C  532  ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA          
SEQRES  21 C  532  VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU          
SEQRES  22 C  532  LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU          
SEQRES  23 C  532  ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU          
SEQRES  24 C  532  GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO          
SEQRES  25 C  532  GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO          
SEQRES  26 C  532  TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU          
SEQRES  27 C  532  ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN          
SEQRES  28 C  532  LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER          
SEQRES  29 C  532  TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU          
SEQRES  30 C  532  ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL          
SEQRES  31 C  532  LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL          
SEQRES  32 C  532  MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS          
SEQRES  33 C  532  ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN          
SEQRES  34 C  532  TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR          
SEQRES  35 C  532  VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE          
SEQRES  36 C  532  GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU          
SEQRES  37 C  532  ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN          
SEQRES  38 C  532  PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO          
SEQRES  39 C  532  HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN          
SEQRES  40 C  532  ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP          
SEQRES  41 C  532  LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS              
MODRES 2HRR ASN A 1079  ASN  GLYCOSYLATION SITE                                 
MODRES 2HRR ASN B 2079  ASN  GLYCOSYLATION SITE                                 
MODRES 2HRR ASN C 3079  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 179      14                                                       
HET    SIA    182      21                                                       
HET    NAG  B 279      14                                                       
HET    SIA    282      21                                                       
HET    NAG  C 379      14                                                       
HET    SIA    382      21                                                       
HET    SUC     11      23                                                       
HET    SUC     22      23                                                       
HET    SUC     33      23                                                       
HET    SO4    184       5                                                       
HET    SO4    185       5                                                       
HET    SO4    284       5                                                       
HET    SO4    285       5                                                       
HET    SO4    384       5                                                       
HET    NTJ      1       8                                                       
HET    NTJ      2       8                                                       
HET    NTJ      3       8                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     SIA O-SIALIC ACID                                                    
HETNAM     SUC SUCROSE                                                          
HETNAM     SO4 SULFATE ION                                                      
HETNAM     NTJ R-ETHYL N,N-DIMETHYLPHOSPHONAMIDOATE                             
HETSYN     NAG NAG                                                              
FORMUL   4  NAG    3(C8 H15 N1 O6)                                              
FORMUL   5  SIA    3(C11 H19 N1 O9)                                             
FORMUL  10  SUC    3(C12 H22 O11)                                               
FORMUL  13  SO4    5(O4 S1 2-)                                                  
FORMUL  18  NTJ    3(C4 H11 N1 O2 P1)                                           
FORMUL  21  HOH   *827(H2 O1)                                                   
HELIX    1   1 LEU A 1060  ARG A 1064  5                                   5    
HELIX    2   2 ASP A 1090  THR A 1102  1                                  13    
HELIX    3   3 ALA A 1148  TYR A 1152  5                                   5    
HELIX    4   4 GLY A 1154  ASN A 1162  1                                   9    
HELIX    5   5 LEU A 1172  PHE A 1178  1                                   7    
HELIX    6   6 ASN A 1188  ILE A 1205  1                                  18    
HELIX    7   7 ALA A 1206  PHE A 1208  5                                   3    
HELIX    8   8 SER A 1221  SER A 1233  1                                  13    
HELIX    9   9 THR A 1252  VAL A 1256  5                                   5    
HELIX   10  10 VAL A 1261  GLY A 1273  1                                  13    
HELIX   11  11 THR A 1278  GLN A 1288  1                                  11    
HELIX   12  12 THR A 1290  MET A 1301  1                                  12    
HELIX   13  13 ASP A 1311  SER A 1315  5                                   5    
HELIX   14  14 THR A 1331  ALA A 1337  1                                   7    
HELIX   15  15 TRP A 1357  MET A 1364  1                                   7    
HELIX   16  16 ASP A 1374  SER A 1385  1                                  12    
HELIX   17  17 SER A 1385  CYS A 1390  1                                   6    
HELIX   18  18 LEU A 1395  GLY A 1405  1                                  11    
HELIX   19  19 ASP A 1409  PHE A 1426  1                                  18    
HELIX   20  20 PHE A 1426  ALA A 1440  1                                  15    
HELIX   21  21 GLU A 1471  PHE A 1476  1                                   6    
HELIX   22  22 GLY A 1477  LEU A 1481  5                                   5    
HELIX   23  23 SER A 1486  GLY A 1507  1                                  22    
HELIX   24  24 LYS A 1540  ALA A 1552  1                                  13    
HELIX   25  25 LEU B 2060  ARG B 2064  5                                   5    
HELIX   26  26 ASP B 2090  THR B 2102  1                                  13    
HELIX   27  27 GLY B 2154  ASN B 2162  1                                   9    
HELIX   28  28 LEU B 2172  PHE B 2178  1                                   7    
HELIX   29  29 ASN B 2188  ILE B 2205  1                                  18    
HELIX   30  30 ALA B 2206  PHE B 2208  5                                   3    
HELIX   31  31 SER B 2221  SER B 2233  1                                  13    
HELIX   32  32 PRO B 2234  LYS B 2237  5                                   4    
HELIX   33  33 THR B 2252  VAL B 2256  5                                   5    
HELIX   34  34 VAL B 2261  ALA B 2272  1                                  12    
HELIX   35  35 THR B 2278  ARG B 2287  1                                  10    
HELIX   36  36 THR B 2290  LYS B 2302  1                                  13    
HELIX   37  37 THR B 2331  ALA B 2337  1                                   7    
HELIX   38  38 TRP B 2357  MET B 2364  1                                   7    
HELIX   39  39 PRO B 2367  GLY B 2371  5                                   5    
HELIX   40  40 ASP B 2374  SER B 2385  1                                  12    
HELIX   41  41 SER B 2385  CYS B 2390  1                                   6    
HELIX   42  42 LEU B 2395  GLY B 2405  1                                  11    
HELIX   43  43 ASP B 2409  PHE B 2426  1                                  18    
HELIX   44  44 PHE B 2426  ALA B 2440  1                                  15    
HELIX   45  45 GLU B 2471  PHE B 2476  1                                   6    
HELIX   46  46 GLY B 2477  LEU B 2481  5                                   5    
HELIX   47  47 SER B 2486  GLY B 2507  1                                  22    
HELIX   48  48 LYS B 2540  ALA B 2552  1                                  13    
HELIX   49  49 LEU C 3060  ARG C 3064  5                                   5    
HELIX   50  50 ASP C 3090  THR C 3102  1                                  13    
HELIX   51  51 GLY C 3154  ASN C 3162  1                                   9    
HELIX   52  52 LEU C 3172  PHE C 3178  1                                   7    
HELIX   53  53 ASN C 3188  ILE C 3205  1                                  18    
HELIX   54  54 ALA C 3206  PHE C 3208  5                                   3    
HELIX   55  55 SER C 3221  SER C 3233  1                                  13    
HELIX   56  56 ALA C 3236  PHE C 3240  5                                   5    
HELIX   57  57 THR C 3252  VAL C 3256  5                                   5    
HELIX   58  58 VAL C 3261  ALA C 3272  1                                  12    
HELIX   59  59 THR C 3278  GLN C 3288  1                                  11    
HELIX   60  60 THR C 3290  LYS C 3302  1                                  13    
HELIX   61  61 ASP C 3311  SER C 3315  5                                   5    
HELIX   62  62 THR C 3331  GLU C 3338  1                                   8    
HELIX   63  63 TRP C 3357  SER C 3365  1                                   8    
HELIX   64  64 ASP C 3374  SER C 3385  1                                  12    
HELIX   65  65 SER C 3385  CYS C 3390  1                                   6    
HELIX   66  66 LEU C 3395  GLY C 3405  1                                  11    
HELIX   67  67 ASP C 3409  PHE C 3426  1                                  18    
HELIX   68  68 PHE C 3426  ALA C 3440  1                                  15    
HELIX   69  69 GLU C 3471  PHE C 3476  1                                   6    
HELIX   70  70 GLY C 3477  LEU C 3481  5                                   5    
HELIX   71  71 SER C 3486  GLY C 3507  1                                  22    
HELIX   72  72 LYS C 3540  ALA C 3552  1                                  13    
SHEET    1   A 3 VAL A1025  THR A1028  0                                        
SHEET    2   A 3 GLY A1031  LEU A1034 -1  O  VAL A1033   N  VAL A1026           
SHEET    3   A 3 VAL A1077  ASN A1079  1  O  LYS A1078   N  LYS A1032           
SHEET    1   B11 LYS A1036  VAL A1038  0                                        
SHEET    2   B11 VAL A1047  PRO A1054 -1  O  ILE A1049   N  LYS A1036           
SHEET    3   B11 TYR A1118  THR A1123 -1  O  THR A1123   N  ALA A1048           
SHEET    4   B11 VAL A1164  ILE A1168 -1  O  VAL A1165   N  TYR A1122           
SHEET    5   B11 LEU A1133  ILE A1139  1  N  MET A1136   O  VAL A1164           
SHEET    6   B11 GLY A1210  GLU A1220  1  O  THR A1216   N  VAL A1135           
SHEET    7   B11 ARG A1242  GLU A1246  1  O  GLU A1246   N  GLY A1219           
SHEET    8   B11 TYR A1346  ASN A1351  1  O  MET A1347   N  SER A1245           
SHEET    9   B11 THR A1444  PHE A1449  1  O  TYR A1445   N  VAL A1348           
SHEET   10   B11 GLY A1525  ILE A1529  1  O  LEU A1527   N  MET A1446           
SHEET   11   B11 GLN A1534  GLN A1537 -1  O  GLN A1534   N  GLN A1528           
SHEET    1   C 2 MET A1086  CYS A1087  0                                        
SHEET    2   C 2 LEU A1112  SER A1113  1  O  SER A1113   N  MET A1086           
SHEET    1   D 3 VAL B2025  THR B2028  0                                        
SHEET    2   D 3 GLY B2031  LEU B2034 -1  O  VAL B2033   N  VAL B2026           
SHEET    3   D 3 VAL B2077  ASN B2079  1  O  LYS B2078   N  LEU B2034           
SHEET    1   E11 LYS B2036  VAL B2038  0                                        
SHEET    2   E11 VAL B2047  PRO B2054 -1  O  ILE B2049   N  LYS B2036           
SHEET    3   E11 TYR B2118  THR B2123 -1  O  ILE B2121   N  PHE B2050           
SHEET    4   E11 VAL B2164  ILE B2168 -1  O  VAL B2165   N  TYR B2122           
SHEET    5   E11 LEU B2133  ILE B2139  1  N  TRP B2138   O  VAL B2166           
SHEET    6   E11 GLY B2210  GLU B2220  1  O  THR B2216   N  VAL B2135           
SHEET    7   E11 ARG B2242  GLU B2246  1  O  GLU B2246   N  GLY B2219           
SHEET    8   E11 TYR B2346  ASN B2351  1  O  MET B2347   N  ALA B2243           
SHEET    9   E11 THR B2444  PHE B2449  1  O  TYR B2445   N  VAL B2348           
SHEET   10   E11 GLY B2525  ILE B2529  1  O  LEU B2527   N  GLU B2448           
SHEET   11   E11 GLN B2534  GLN B2537 -1  O  GLN B2534   N  GLN B2528           
SHEET    1   F 2 MET B2086  CYS B2087  0                                        
SHEET    2   F 2 LEU B2112  SER B2113  1  O  SER B2113   N  MET B2086           
SHEET    1   G 3 VAL C3025  THR C3028  0                                        
SHEET    2   G 3 GLY C3031  LEU C3034 -1  O  VAL C3033   N  VAL C3026           
SHEET    3   G 3 VAL C3077  ASN C3079  1  O  LYS C3078   N  LYS C3032           
SHEET    1   H11 LYS C3036  VAL C3038  0                                        
SHEET    2   H11 VAL C3047  PRO C3054 -1  O  VAL C3047   N  VAL C3038           
SHEET    3   H11 TYR C3118  THR C3123 -1  O  THR C3123   N  ALA C3048           
SHEET    4   H11 VAL C3164  ILE C3168 -1  O  VAL C3165   N  TYR C3122           
SHEET    5   H11 LEU C3133  ILE C3139  1  N  TRP C3138   O  VAL C3166           
SHEET    6   H11 GLY C3210  GLU C3220  1  O  THR C3216   N  VAL C3135           
SHEET    7   H11 ARG C3242  GLU C3246  1  O  ILE C3244   N  ILE C3217           
SHEET    8   H11 TYR C3346  ASN C3351  1  O  MET C3347   N  ALA C3243           
SHEET    9   H11 THR C3444  GLN C3450  1  O  TYR C3445   N  VAL C3348           
SHEET   10   H11 GLY C3525  GLY C3530  1  O  ILE C3529   N  GLN C3450           
SHEET   11   H11 GLN C3534  GLN C3537 -1  O  ALA C3536   N  TYR C3526           
SHEET    1   I 2 MET C3086  CYS C3087  0                                        
SHEET    2   I 2 LEU C3112  SER C3113  1  O  SER C3113   N  MET C3086           
SSBOND   1 CYS A 1087    CYS A 1116                                             
SSBOND   2 CYS A 1274    CYS A 1285                                             
SSBOND   3 CYS B 2087    CYS B 2116                                             
SSBOND   4 CYS B 2274    CYS B 2285                                             
SSBOND   5 CYS C 3087    CYS C 3116                                             
SSBOND   6 CYS C 3274    CYS C 3285                                             
LINK         OG  SER A1221                 P1  NTJ     1                        
LINK         OG  SER B2221                 P1  NTJ     2                        
LINK         OG  SER C3221                 P1  NTJ     3                        
LINK         ND2 ASN B2079                 C1  NAG B 279                        
LINK         ND2 ASN A1079                 C2  NAG A 179                        
LINK         ND2 ASN A1079                 C1  NAG A 179                        
LINK         ND2 ASN C3079                 C1  NAG C 379                        
CRYST1   55.570  181.050  202.920  90.00  90.00  90.00 P 21 21 21   12          
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      0.017995  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005523  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004928        0.00000                         
TER    4131      LYS A1553                                                      
TER    8256      LYS B2553                                                      
TER   12382      LYS C3553                                                      
MASTER      328    0   17   72   48    0    0    613429    3  241  123          
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.
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