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LongText Report for: 5x61-pdb

Name Class
5x61-pdb
HEADER    HYDROLASE                               20-FEB-17   5X61              
TITLE     CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE CATALYTIC SUBUNIT OF THE    
TITLE    2 MALARIA VECTOR ANOPHELES GAMBIAE, 3.4 A                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 FRAGMENT: CATALYTIC SUBUNIT, UNP RESIDUES 162-714;                   
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ANOPHELES GAMBIAE;                              
SOURCE   3 ORGANISM_COMMON: AFRICAN MALARIA MOSQUITO;                           
SOURCE   4 ORGANISM_TAXID: 7165;                                                
SOURCE   5 GENE: ACE, ACE1, ACHE1, AGAP001356;                                  
SOURCE   6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPICZ* A                                  
KEYWDS    ALPHA/BETA HYDROLASE FOLD, HYDROLASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.HAN,H.ROBINSON,H.DING,D.M.WONG,P.C.H.LAM,M.M.TOTROV,P.R.CARLIER,    
AUTHOR   2 J.LI                                                                 
REVDAT   1   15-MAR-17 5X61    0                                                
JRNL        AUTH   Q.HAN,D.M.WONG,H.ROBINSON,H.DING,P.C.H.LAM,M.M.TOTROV,       
JRNL        AUTH 2 P.R.CARLIER,J.LI                                             
JRNL        TITL   CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE CATALYTIC SUBUNITS 
JRNL        TITL 2 OF THE MALARIA VECTOR ANOPHELES GAMBIAE                      
JRNL        REF    INSECT SCI.                                2017              
JRNL        REFN                   ISSN 1744-7917                               
JRNL        PMID   28247978                                                     
JRNL        DOI    10.1111/1744-7917.12450                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 36750                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1940                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2683                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.58                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2810                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 145                          
REMARK   3   BIN FREE R VALUE                    : 0.2910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8498                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 168                                     
REMARK   3   SOLVENT ATOMS            : 6                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.377         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.372         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.258         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.367        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.923                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8906 ; 0.004 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12170 ; 0.929 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1072 ; 4.811 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   424 ;33.251 ;23.302       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1324 ;15.303 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    70 ;12.220 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1308 ; 0.067 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6948 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5X61 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300002990.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38760                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 64.0                               
REMARK 200  DATA REDUNDANCY                : 20.30                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: 2HA2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 78.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES BUFFER, 1.6M AMMONIUM         
REMARK 280  SULFATE, 0.1M SODIUM CHLORIDE, PH 7.5, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.26533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      150.53067            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      112.89800            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      188.16333            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       37.63267            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -173.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A                                  
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     ASN B   699                                                      
REMARK 465     LEU B   700                                                      
REMARK 465     PRO B   701                                                      
REMARK 465     GLY B   702                                                      
REMARK 465     PRO B   703                                                      
REMARK 465     ALA B   704                                                      
REMARK 465     PRO B   705                                                      
REMARK 465     PRO B   706                                                      
REMARK 465     SER B   707                                                      
REMARK 465     GLU B   708                                                      
REMARK 465     PRO B   709                                                      
REMARK 465     CYS B   710                                                      
REMARK 465     GLU B   711                                                      
REMARK 465     SER B   712                                                      
REMARK 465     SER B   713                                                      
REMARK 465     ALA B   714                                                      
REMARK 465     ASN A   699                                                      
REMARK 465     LEU A   700                                                      
REMARK 465     PRO A   701                                                      
REMARK 465     GLY A   702                                                      
REMARK 465     PRO A   703                                                      
REMARK 465     ALA A   704                                                      
REMARK 465     PRO A   705                                                      
REMARK 465     PRO A   706                                                      
REMARK 465     SER A   707                                                      
REMARK 465     GLU A   708                                                      
REMARK 465     PRO A   709                                                      
REMARK 465     CYS A   710                                                      
REMARK 465     GLU A   711                                                      
REMARK 465     SER A   712                                                      
REMARK 465     SER A   713                                                      
REMARK 465     ALA A   714                                                      
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           DISTANCE          
REMARK 500   ND2  ASN A   220     O5   NAG A   809              1.86            
REMARK 500   ND2  ASN B   220     O5   NAG B   809              1.91            
REMARK 500   O4   NAG B   809     O5   NAG B   810              1.93            
REMARK 500   C3   NAG B   809     C1   NAG B   810              2.01            
REMARK 500   OD1  ASN B   220     C1   NAG B   809              2.01            
REMARK 500   O3   NAG B   809     O5   NAG B   810              2.11            
REMARK 500   O7   NAG B   809     N2   NAG B   810              2.12            
REMARK 500   O3   NAG B   809     C2   NAG B   810              2.17            
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 206      -15.40     73.12                                   
REMARK 500    ASN B 220       98.59    -67.31                                   
REMARK 500    ASP B 238       50.03    -92.99                                   
REMARK 500    CYS B 255       -6.08   -141.96                                   
REMARK 500    ALA B 312     -157.12     58.48                                   
REMARK 500    PHE B 316       16.61   -142.39                                   
REMARK 500    ARG B 353       58.49   -117.11                                   
REMARK 500    SER B 360     -117.49     60.26                                   
REMARK 500    GLN B 380      -65.43   -103.32                                   
REMARK 500    PRO B 418        5.41    -68.52                                   
REMARK 500    TYR B 494      -70.68    -76.42                                   
REMARK 500    LYS B 501       42.89    -75.85                                   
REMARK 500    PHE B 560      -78.38   -134.31                                   
REMARK 500    ALA B 647       77.75     60.88                                   
REMARK 500    SER B 672       16.60   -154.78                                   
REMARK 500    LYS B 688      -60.98   -108.17                                   
REMARK 500    PHE A 206      -21.28     75.59                                   
REMARK 500    CYS A 255       -1.35   -142.62                                   
REMARK 500    ASN A 269      106.61   -162.70                                   
REMARK 500    ALA A 312     -150.41     61.08                                   
REMARK 500    PHE A 316       21.56   -144.19                                   
REMARK 500    PRO A 351       -8.23    -58.69                                   
REMARK 500    SER A 360     -116.03     57.90                                   
REMARK 500    GLN A 380      -63.42    -94.93                                   
REMARK 500    ALA A 458      -65.01    -91.79                                   
REMARK 500    TYR A 535       49.67   -106.07                                   
REMARK 500    GLU A 540       80.79   -155.48                                   
REMARK 500    PHE A 560      -79.97   -133.83                                   
REMARK 500    ALA A 647       83.62     52.20                                   
REMARK 500    ASN A 670       56.11   -111.75                                   
REMARK 500    LYS A 688      -60.75   -101.20                                   
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 residue SO4 B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 808                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE B 812                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 808                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NH4 A 811                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 812                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  809 through NAG A 810 bound to ASN A 220                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  809 through NAG B 810                                               
DBREF  5X61 B  162   714  UNP    Q869C3   ACES_ANOGA     162    714             
DBREF  5X61 A  162   714  UNP    Q869C3   ACES_ANOGA     162    714             
SEQRES   1 B  553  ASP ASN ASP PRO LEU VAL VAL ASN THR ASP LYS GLY ARG          
SEQRES   2 B  553  ILE ARG GLY ILE THR VAL ASP ALA PRO SER GLY LYS LYS          
SEQRES   3 B  553  VAL ASP VAL TRP LEU GLY ILE PRO TYR ALA GLN PRO PRO          
SEQRES   4 B  553  VAL GLY PRO LEU ARG PHE ARG HIS PRO ARG PRO ALA GLU          
SEQRES   5 B  553  LYS TRP THR GLY VAL LEU ASN THR THR THR PRO PRO ASN          
SEQRES   6 B  553  SER CYS VAL GLN ILE VAL ASP THR VAL PHE GLY ASP PHE          
SEQRES   7 B  553  PRO GLY ALA THR MET TRP ASN PRO ASN THR PRO LEU SER          
SEQRES   8 B  553  GLU ASP CYS LEU TYR ILE ASN VAL VAL ALA PRO ARG PRO          
SEQRES   9 B  553  ARG PRO LYS ASN ALA ALA VAL MET LEU TRP ILE PHE GLY          
SEQRES  10 B  553  GLY GLY PHE TYR SER GLY THR ALA THR LEU ASP VAL TYR          
SEQRES  11 B  553  ASP HIS ARG ALA LEU ALA SER GLU GLU ASN VAL ILE VAL          
SEQRES  12 B  553  VAL SER LEU GLN TYR ARG VAL ALA SER LEU GLY PHE LEU          
SEQRES  13 B  553  PHE LEU GLY THR PRO GLU ALA PRO GLY ASN ALA GLY LEU          
SEQRES  14 B  553  PHE ASP GLN ASN LEU ALA LEU ARG TRP VAL ARG ASP ASN          
SEQRES  15 B  553  ILE HIS ARG PHE GLY GLY ASP PRO SER ARG VAL THR LEU          
SEQRES  16 B  553  PHE GLY GLU SER ALA GLY ALA VAL SER VAL SER LEU HIS          
SEQRES  17 B  553  LEU LEU SER ALA LEU SER ARG ASP LEU PHE GLN ARG ALA          
SEQRES  18 B  553  ILE LEU GLN SER GLY SER PRO THR ALA PRO TRP ALA LEU          
SEQRES  19 B  553  VAL SER ARG GLU GLU ALA THR LEU ARG ALA LEU ARG LEU          
SEQRES  20 B  553  ALA GLU ALA VAL GLY CYS PRO HIS GLU PRO SER LYS LEU          
SEQRES  21 B  553  SER ASP ALA VAL GLU CYS LEU ARG GLY LYS ASP PRO HIS          
SEQRES  22 B  553  VAL LEU VAL ASN ASN GLU TRP GLY THR LEU GLY ILE CYS          
SEQRES  23 B  553  GLU PHE PRO PHE VAL PRO VAL VAL ASP GLY ALA PHE LEU          
SEQRES  24 B  553  ASP GLU THR PRO GLN ARG SER LEU ALA SER GLY ARG PHE          
SEQRES  25 B  553  LYS LYS THR GLU ILE LEU THR GLY SER ASN THR GLU GLU          
SEQRES  26 B  553  GLY TYR TYR PHE ILE ILE TYR TYR LEU THR GLU LEU LEU          
SEQRES  27 B  553  ARG LYS GLU GLU GLY VAL THR VAL THR ARG GLU GLU PHE          
SEQRES  28 B  553  LEU GLN ALA VAL ARG GLU LEU ASN PRO TYR VAL ASN GLY          
SEQRES  29 B  553  ALA ALA ARG GLN ALA ILE VAL PHE GLU TYR THR ASP TRP          
SEQRES  30 B  553  THR GLU PRO ASP ASN PRO ASN SER ASN ARG ASP ALA LEU          
SEQRES  31 B  553  ASP LYS MET VAL GLY ASP TYR HIS PHE THR CYS ASN VAL          
SEQRES  32 B  553  ASN GLU PHE ALA GLN ARG TYR ALA GLU GLU GLY ASN ASN          
SEQRES  33 B  553  VAL TYR MET TYR LEU TYR THR HIS ARG SER LYS GLY ASN          
SEQRES  34 B  553  PRO TRP PRO ARG TRP THR GLY VAL MET HIS GLY ASP GLU          
SEQRES  35 B  553  ILE ASN TYR VAL PHE GLY GLU PRO LEU ASN PRO THR LEU          
SEQRES  36 B  553  GLY TYR THR GLU ASP GLU LYS ASP PHE SER ARG LYS ILE          
SEQRES  37 B  553  MET ARG TYR TRP SER ASN PHE ALA LYS THR GLY ASN PRO          
SEQRES  38 B  553  ASN PRO ASN THR ALA SER SER GLU PHE PRO GLU TRP PRO          
SEQRES  39 B  553  LYS HIS THR ALA HIS GLY ARG HIS TYR LEU GLU LEU GLY          
SEQRES  40 B  553  LEU ASN THR SER PHE VAL GLY ARG GLY PRO ARG LEU ARG          
SEQRES  41 B  553  GLN CYS ALA PHE TRP LYS LYS TYR LEU PRO GLN LEU VAL          
SEQRES  42 B  553  ALA ALA THR SER ASN LEU PRO GLY PRO ALA PRO PRO SER          
SEQRES  43 B  553  GLU PRO CYS GLU SER SER ALA                                  
SEQRES   1 A  553  ASP ASN ASP PRO LEU VAL VAL ASN THR ASP LYS GLY ARG          
SEQRES   2 A  553  ILE ARG GLY ILE THR VAL ASP ALA PRO SER GLY LYS LYS          
SEQRES   3 A  553  VAL ASP VAL TRP LEU GLY ILE PRO TYR ALA GLN PRO PRO          
SEQRES   4 A  553  VAL GLY PRO LEU ARG PHE ARG HIS PRO ARG PRO ALA GLU          
SEQRES   5 A  553  LYS TRP THR GLY VAL LEU ASN THR THR THR PRO PRO ASN          
SEQRES   6 A  553  SER CYS VAL GLN ILE VAL ASP THR VAL PHE GLY ASP PHE          
SEQRES   7 A  553  PRO GLY ALA THR MET TRP ASN PRO ASN THR PRO LEU SER          
SEQRES   8 A  553  GLU ASP CYS LEU TYR ILE ASN VAL VAL ALA PRO ARG PRO          
SEQRES   9 A  553  ARG PRO LYS ASN ALA ALA VAL MET LEU TRP ILE PHE GLY          
SEQRES  10 A  553  GLY GLY PHE TYR SER GLY THR ALA THR LEU ASP VAL TYR          
SEQRES  11 A  553  ASP HIS ARG ALA LEU ALA SER GLU GLU ASN VAL ILE VAL          
SEQRES  12 A  553  VAL SER LEU GLN TYR ARG VAL ALA SER LEU GLY PHE LEU          
SEQRES  13 A  553  PHE LEU GLY THR PRO GLU ALA PRO GLY ASN ALA GLY LEU          
SEQRES  14 A  553  PHE ASP GLN ASN LEU ALA LEU ARG TRP VAL ARG ASP ASN          
SEQRES  15 A  553  ILE HIS ARG PHE GLY GLY ASP PRO SER ARG VAL THR LEU          
SEQRES  16 A  553  PHE GLY GLU SER ALA GLY ALA VAL SER VAL SER LEU HIS          
SEQRES  17 A  553  LEU LEU SER ALA LEU SER ARG ASP LEU PHE GLN ARG ALA          
SEQRES  18 A  553  ILE LEU GLN SER GLY SER PRO THR ALA PRO TRP ALA LEU          
SEQRES  19 A  553  VAL SER ARG GLU GLU ALA THR LEU ARG ALA LEU ARG LEU          
SEQRES  20 A  553  ALA GLU ALA VAL GLY CYS PRO HIS GLU PRO SER LYS LEU          
SEQRES  21 A  553  SER ASP ALA VAL GLU CYS LEU ARG GLY LYS ASP PRO HIS          
SEQRES  22 A  553  VAL LEU VAL ASN ASN GLU TRP GLY THR LEU GLY ILE CYS          
SEQRES  23 A  553  GLU PHE PRO PHE VAL PRO VAL VAL ASP GLY ALA PHE LEU          
SEQRES  24 A  553  ASP GLU THR PRO GLN ARG SER LEU ALA SER GLY ARG PHE          
SEQRES  25 A  553  LYS LYS THR GLU ILE LEU THR GLY SER ASN THR GLU GLU          
SEQRES  26 A  553  GLY TYR TYR PHE ILE ILE TYR TYR LEU THR GLU LEU LEU          
SEQRES  27 A  553  ARG LYS GLU GLU GLY VAL THR VAL THR ARG GLU GLU PHE          
SEQRES  28 A  553  LEU GLN ALA VAL ARG GLU LEU ASN PRO TYR VAL ASN GLY          
SEQRES  29 A  553  ALA ALA ARG GLN ALA ILE VAL PHE GLU TYR THR ASP TRP          
SEQRES  30 A  553  THR GLU PRO ASP ASN PRO ASN SER ASN ARG ASP ALA LEU          
SEQRES  31 A  553  ASP LYS MET VAL GLY ASP TYR HIS PHE THR CYS ASN VAL          
SEQRES  32 A  553  ASN GLU PHE ALA GLN ARG TYR ALA GLU GLU GLY ASN ASN          
SEQRES  33 A  553  VAL TYR MET TYR LEU TYR THR HIS ARG SER LYS GLY ASN          
SEQRES  34 A  553  PRO TRP PRO ARG TRP THR GLY VAL MET HIS GLY ASP GLU          
SEQRES  35 A  553  ILE ASN TYR VAL PHE GLY GLU PRO LEU ASN PRO THR LEU          
SEQRES  36 A  553  GLY TYR THR GLU ASP GLU LYS ASP PHE SER ARG LYS ILE          
SEQRES  37 A  553  MET ARG TYR TRP SER ASN PHE ALA LYS THR GLY ASN PRO          
SEQRES  38 A  553  ASN PRO ASN THR ALA SER SER GLU PHE PRO GLU TRP PRO          
SEQRES  39 A  553  LYS HIS THR ALA HIS GLY ARG HIS TYR LEU GLU LEU GLY          
SEQRES  40 A  553  LEU ASN THR SER PHE VAL GLY ARG GLY PRO ARG LEU ARG          
SEQRES  41 A  553  GLN CYS ALA PHE TRP LYS LYS TYR LEU PRO GLN LEU VAL          
SEQRES  42 A  553  ALA ALA THR SER ASN LEU PRO GLY PRO ALA PRO PRO SER          
SEQRES  43 A  553  GLU PRO CYS GLU SER SER ALA                                  
MODRES 5X61 ASN A  220  ASN  GLYCOSYLATION SITE                                 
MODRES 5X61 ASN B  220  ASN  GLYCOSYLATION SITE                                 
HET    SO4  B 801       5                                                       
HET    SO4  B 802       5                                                       
HET    SO4  B 803       5                                                       
HET    SO4  B 804       5                                                       
HET    SO4  B 805       5                                                       
HET    SO4  B 806       5                                                       
HET    SO4  B 807       5                                                       
HET    SO4  B 808       5                                                       
HET    NAG  B 809      14                                                       
HET    NAG  B 810      14                                                       
HET    NH4  B 811       1                                                       
HET    EPE  B 812      15                                                       
HET    SO4  A 801       5                                                       
HET    SO4  A 802       5                                                       
HET    SO4  A 803       5                                                       
HET    SO4  A 804       5                                                       
HET    SO4  A 805       5                                                       
HET    SO4  A 806       5                                                       
HET    SO4  A 807       5                                                       
HET    SO4  A 808       5                                                       
HET    NAG  A 809      14                                                       
HET    NAG  A 810      14                                                       
HET    NH4  A 811       1                                                       
HET    EPE  A 812      15                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     NH4 AMMONIUM ION                                                     
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETSYN     EPE HEPES                                                            
FORMUL   3  SO4    16(O4 S 2-)                                                  
FORMUL  11  NAG    4(C8 H15 N O6)                                               
FORMUL  12  NH4    2(H4 N 1+)                                                   
FORMUL  13  EPE    2(C8 H18 N2 O4 S)                                            
FORMUL  25  HOH   *6(H2 O)                                                      
HELIX    1 AA1 VAL B  201  ARG B  205  5                                   5    
HELIX    2 AA2 PHE B  239  MET B  244  1                                   6    
HELIX    3 AA3 LEU B  288  ASP B  292  5                                   5    
HELIX    4 AA4 HIS B  293  ASN B  301  1                                   9    
HELIX    5 AA5 ALA B  312  LEU B  317  1                                   6    
HELIX    6 AA6 ASN B  327  ILE B  344  1                                  18    
HELIX    7 AA7 HIS B  345  PHE B  347  5                                   3    
HELIX    8 AA8 SER B  360  SER B  372  1                                  13    
HELIX    9 AA9 SER B  397  GLY B  413  1                                  17    
HELIX   10 AB1 LYS B  420  ARG B  429  1                                  10    
HELIX   11 AB2 ASP B  432  ASN B  438  1                                   7    
HELIX   12 AB3 THR B  463  SER B  470  1                                   8    
HELIX   13 AB4 GLY B  487  LEU B  495  1                                   9    
HELIX   14 AB5 THR B  508  ASN B  520  1                                  13    
HELIX   15 AB6 GLY B  525  TYR B  535  1                                  11    
HELIX   16 AB7 ASN B  543  PHE B  560  1                                  18    
HELIX   17 AB8 PHE B  560  GLU B  574  1                                  15    
HELIX   18 AB9 PRO B  593  GLY B  597  5                                   5    
HELIX   19 AC1 GLU B  603  PHE B  608  1                                   6    
HELIX   20 AC2 ASN B  613  GLY B  617  5                                   5    
HELIX   21 AC3 THR B  619  GLY B  640  1                                  22    
HELIX   22 AC4 ARG B  679  LYS B  688  1                                  10    
HELIX   23 AC5 LYS B  688  SER B  698  1                                  11    
HELIX   24 AC6 VAL A  201  ARG A  205  5                                   5    
HELIX   25 AC7 PHE A  239  MET A  244  1                                   6    
HELIX   26 AC8 ASP A  292  ASN A  301  1                                  10    
HELIX   27 AC9 ALA A  312  LEU A  317  1                                   6    
HELIX   28 AD1 ASN A  327  ILE A  344  1                                  18    
HELIX   29 AD2 HIS A  345  PHE A  347  5                                   3    
HELIX   30 AD3 SER A  360  SER A  372  1                                  13    
HELIX   31 AD4 SER A  375  PHE A  379  5                                   5    
HELIX   32 AD5 SER A  397  VAL A  412  1                                  16    
HELIX   33 AD6 LYS A  420  LYS A  431  1                                  12    
HELIX   34 AD7 ASP A  432  ASN A  439  1                                   8    
HELIX   35 AD8 THR A  463  SER A  470  1                                   8    
HELIX   36 AD9 GLY A  487  TYR A  494  1                                   8    
HELIX   37 AE1 THR A  508  ASN A  520  1                                  13    
HELIX   38 AE2 GLY A  525  TYR A  535  1                                  11    
HELIX   39 AE3 ASN A  543  PHE A  560  1                                  18    
HELIX   40 AE4 PHE A  560  GLU A  573  1                                  14    
HELIX   41 AE5 PRO A  593  GLY A  597  5                                   5    
HELIX   42 AE6 GLU A  603  PHE A  608  1                                   6    
HELIX   43 AE7 THR A  619  GLY A  640  1                                  22    
HELIX   44 AE8 ARG A  679  LYS A  688  1                                  10    
HELIX   45 AE9 LYS A  688  THR A  697  1                                  10    
SHEET    1 AA1 3 VAL B 167  VAL B 168  0                                        
SHEET    2 AA1 3 ARG B 174  ARG B 176 -1  O  ILE B 175   N  VAL B 168           
SHEET    3 AA1 3 VAL B 218  ASN B 220  1  O  LEU B 219   N  ARG B 176           
SHEET    1 AA211 ILE B 178  ASP B 181  0                                        
SHEET    2 AA211 LYS B 187  PRO B 195 -1  O  VAL B 188   N  VAL B 180           
SHEET    3 AA211 TYR B 257  PRO B 263 -1  O  ALA B 262   N  ASP B 189           
SHEET    4 AA211 ILE B 303  LEU B 307 -1  O  SER B 306   N  ASN B 259           
SHEET    5 AA211 ALA B 270  ILE B 276  1  N  TRP B 275   O  VAL B 305           
SHEET    6 AA211 GLY B 349  GLU B 359  1  O  THR B 355   N  VAL B 272           
SHEET    7 AA211 ARG B 381  GLN B 385  1  O  ILE B 383   N  LEU B 356           
SHEET    8 AA211 ILE B 478  ASN B 483  1  O  LEU B 479   N  LEU B 384           
SHEET    9 AA211 VAL B 578  TYR B 583  1  O  TYR B 583   N  SER B 482           
SHEET   10 AA211 HIS B 663  LEU B 667  1  O  LEU B 667   N  LEU B 582           
SHEET   11 AA211 VAL B 674  ARG B 676 -1  O  GLY B 675   N  TYR B 664           
SHEET    1 AA3 2 ALA B 197  GLN B 198  0                                        
SHEET    2 AA3 2 ARG B 210  PRO B 211 -1  O  ARG B 210   N  GLN B 198           
SHEET    1 AA4 2 SER B 227  CYS B 228  0                                        
SHEET    2 AA4 2 LEU B 251  SER B 252  1  O  SER B 252   N  SER B 227           
SHEET    1 AA5 3 VAL A 167  THR A 170  0                                        
SHEET    2 AA5 3 GLY A 173  ARG A 176 -1  O  ILE A 175   N  VAL A 168           
SHEET    3 AA5 3 VAL A 218  ASN A 220  1  O  LEU A 219   N  ARG A 176           
SHEET    1 AA611 ILE A 178  ASP A 181  0                                        
SHEET    2 AA611 LYS A 187  PRO A 195 -1  O  VAL A 188   N  VAL A 180           
SHEET    3 AA611 TYR A 257  PRO A 263 -1  O  ALA A 262   N  ASP A 189           
SHEET    4 AA611 ILE A 303  LEU A 307 -1  O  SER A 306   N  ASN A 259           
SHEET    5 AA611 ALA A 270  ILE A 276  1  N  TRP A 275   O  VAL A 305           
SHEET    6 AA611 GLY A 349  GLU A 359  1  O  THR A 355   N  VAL A 272           
SHEET    7 AA611 ARG A 381  GLN A 385  1  O  ILE A 383   N  LEU A 356           
SHEET    8 AA611 ILE A 478  ASN A 483  1  O  LEU A 479   N  LEU A 384           
SHEET    9 AA611 VAL A 578  TYR A 583  1  O  TYR A 583   N  SER A 482           
SHEET   10 AA611 HIS A 663  LEU A 667  1  O  LEU A 667   N  LEU A 582           
SHEET   11 AA611 VAL A 674  ARG A 676 -1  O  GLY A 675   N  TYR A 664           
SSBOND   1 CYS B  228    CYS B  255                          1555   1555  2.04  
SSBOND   2 CYS B  414    CYS B  427                          1555   1555  2.04  
SSBOND   3 CYS B  562    CYS B  683                          1555   1555  2.05  
SSBOND   4 CYS A  228    CYS A  255                          1555   1555  2.04  
SSBOND   5 CYS A  414    CYS A  427                          1555   1555  2.04  
SSBOND   6 CYS A  562    CYS A  683                          1555   1555  2.04  
LINK         ND2 ASN A 220                 C1  NAG A 809     1555   1555  1.57  
LINK         O3  NAG B 809                 C1  NAG B 810     1555   1555  1.18  
LINK         O3  NAG A 809                 C1  NAG A 810     1555   1555  1.39  
LINK         ND2 ASN B 220                 C1  NAG B 809     1555   1555  1.97  
CISPEP   1 ARG B  264    PRO B  265          0         2.08                     
CISPEP   2 GLY B  677    PRO B  678          0         2.54                     
CISPEP   3 ARG A  264    PRO A  265          0         3.02                     
CISPEP   4 GLY A  677    PRO A  678          0        -0.60                     
SITE     1 AC1  3 ARG B 376  LYS B 474  LYS B 475                               
SITE     1 AC2  2 ARG B 353  LYS B 638                                          
SITE     1 AC3  3 PRO A 203  SER B 470  ARG B 472                               
SITE     1 AC4  4 SER B 397  ARG B 398  GLU B 399  HOH B 904                    
SITE     1 AC5  2 LYS B 187  ARG B 264                                          
SITE     1 AC6  2 LEU B 582  ARG B 679                                          
SITE     1 AC7  3 ARG B 174  THR B 216  GLY B 217                               
SITE     1 AC8  4 TRP B 441  GLY B 442  LEU B 444  EPE B 812                    
SITE     1 AC9  3 TYR B 282  TRP B 441  SO4 B 808                               
SITE     1 AD1  3 SER A 470  ARG A 472  PRO B 203                               
SITE     1 AD2  2 ARG A 353  LYS A 638                                          
SITE     1 AD3  2 GLY A 504  ARG A 594                                          
SITE     1 AD4  2 ASN A 524  ARG A 528                                          
SITE     1 AD5  3 SER A 397  ARG A 398  GLU A 399                               
SITE     1 AD6  5 THR A 536  ASP A 537  TRP A 538  THR A 539                    
SITE     2 AD6  5 ARG B 681                                                     
SITE     1 AD7  2 GLY A 525  ARG A 528                                          
SITE     1 AD8  4 THR A 658  HIS A 660  GLY A 661  HIS A 663                    
SITE     1 AD9  1 TRP A 245                                                     
SITE     1 AE1  2 TYR A 282  TRP A 441                                          
SITE     1 AE2  2 ARG A 176  ASN A 220                                          
SITE     1 AE3  2 ARG B 176  ASN B 220                                          
CRYST1  148.723  148.723  225.796  90.00  90.00 120.00 P 61         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      0.006724  0.003882  0.000000        0.00000                         
SCALE2      0.000000  0.007764  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004429        0.00000                         
TER    4250      SER B 698                                                      
TER    8500      SER A 698                                                      
MASTER      437    0   24   45   32    0   22    6 8672    2  180   86          
END                                                                             

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