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LongText Report for: 2ZYR-pdb

Name Class
2ZYR-pdb
HEADER    HYDROLASE                               28-JAN-09   2ZYR              
TITLE     A. FULGIDUS LIPASE WITH FATTY ACID FRAGMENT AND MAGNESIUM             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE, PUTATIVE;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;                         
SOURCE   3 ORGANISM_TAXID: 2234;                                                
SOURCE   4 GENE: AF_1763;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-23A(+)                                
KEYWDS    LIPASE, ARCHAEOGLOBUS FULGIDUS, FATTY ACID, HYDROLASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.K.CHEN,T.P.KO,R.T.GUO,A.H.WANG                                      
REVDAT   1   16-JUN-09 2ZYR    0                                                
JRNL        AUTH   C.K.CHEN,G.C.LEE,T.P.KO,R.T.GUO,L.M.HUANG,H.J.LIU,           
JRNL        AUTH 2 Y.F.HO,J.F.SHAW,A.H.WANG                                     
JRNL        TITL   STRUCTURE OF THE ALKALOHYPERTHERMOPHILIC                     
JRNL        TITL 2 ARCHAEOGLOBUS FULGIDUS LIPASE CONTAINS A UNIQUE              
JRNL        TITL 3 C-TERMINAL DOMAIN ESSENTIAL FOR LONG-CHAIN                   
JRNL        TITL 4 SUBSTRATE BINDING.                                           
JRNL        REF    J.MOL.BIOL.                                2009              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   19447113                                                     
JRNL        DOI    10.1016/J.JMB.2009.05.017                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.77 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 90064                          
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) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4527                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.77                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.83                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 76.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2510                       
REMARK   3   BIN FREE R VALUE                    : 0.2780                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 396                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7246                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 1255                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.18                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.019                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.90                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2ZYR COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JAN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB028594.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 4.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NOIR-1                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 94247                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.770                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 23.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 2ZYH                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.16M MAGNESIUM CHLORIDE, 0.08M          
REMARK 280  TRIS HCL, 10% PEG4000, 20% GLYCEROL , PH 8.5, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, TEMPERATURE 298K                                      
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   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-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       26.14450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       87.94250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.33350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       87.94250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.14450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.33350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     VAL A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     VAL A    11                                                      
REMARK 465     PHE A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     GLN A    15                                                      
REMARK 465     VAL A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     GLU A    20                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     VAL B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     VAL B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     VAL B    11                                                      
REMARK 465     PHE B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     VAL B    14                                                      
REMARK 465     GLN B    15                                                      
REMARK 465     VAL B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     GLU B    20                                                      
REMARK 465     VAL B   475                                                      
REMARK 465     ASP B   476                                                      
REMARK 465     LYS B   477                                                      
REMARK 465     LEU B   478                                                      
REMARK 465     ALA B   479                                                      
REMARK 465     ALA B   480                                                      
REMARK 465     ALA B   481                                                      
REMARK 465     LEU B   482                                                      
REMARK 465     GLU B   483                                                      
REMARK 465     HIS B   484                                                      
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   O    HOH A   787     O    HOH A   788              1.89            
REMARK 500   OG   SER B   136     O    HOH B   870              2.04            
REMARK 500   O    HOH A   829     O    HOH A   850              2.05            
REMARK 500   O    HOH A   653     O    HOH A  1084              2.09            
REMARK 500   OE2  GLU B    39     O    HOH B   513              2.10            
REMARK 500   O    HOH B   566     O    HOH B   812              2.10            
REMARK 500   O    HOH B   633     O    HOH B  1241              2.14            
REMARK 500   O    GLU B   437     O    HOH B   947              2.14            
REMARK 500   O    HOH B   604     O    HOH B  1113              2.15            
REMARK 500   O    HOH B   649     O    HOH B  1247              2.15            
REMARK 500   O    HOH A   535     O    HOH A  1139              2.16            
REMARK 500   O    HOH B   560     O    HOH B   561              2.17            
REMARK 500   OH   TYR B   473     O    HOH B  1202              2.18            
REMARK 500   O    HOH B   730     O    HOH B   731              2.18            
REMARK 500   O    HOH B   597     O    HOH B   905              2.18            
REMARK 500   O    HOH A   503     O    HOH A   991              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B  23   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    LEU B 213   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 136     -119.49     55.57                                   
REMARK 500    GLU A 194      146.44   -172.82                                   
REMARK 500    ALA A 255      -41.48     72.41                                   
REMARK 500    LEU A 336       72.08   -111.45                                   
REMARK 500    LYS A 363      112.34   -178.18                                   
REMARK 500    SER B 136     -119.79     54.34                                   
REMARK 500    LEU B 186       59.41   -148.66                                   
REMARK 500    ALA B 255      -36.11     69.30                                   
REMARK 500    LEU B 336       69.29   -116.58                                   
REMARK 500    LYS B 363      117.17   -172.39                                   
REMARK 500    ALA B 436       22.76    -77.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 539        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH A 559        DISTANCE =  6.85 ANGSTROMS                       
REMARK 525    HOH B 573        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH B 574        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH A 593        DISTANCE =  7.32 ANGSTROMS                       
REMARK 525    HOH A 598        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH A 600        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH B 612        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH B 616        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH A 626        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH B 636        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH B 644        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH A 665        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH B 696        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH A 766        DISTANCE =  5.52 ANGSTROMS                       
REMARK 525    HOH A 776        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH B 788        DISTANCE =  6.86 ANGSTROMS                       
REMARK 525    HOH B 801        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH A 806        DISTANCE =  6.53 ANGSTROMS                       
REMARK 525    HOH A 834        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH A 837        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH A 862        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH A 869        DISTANCE =  6.66 ANGSTROMS                       
REMARK 525    HOH B 925        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH B 931        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH B 937        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH B 951        DISTANCE =  6.99 ANGSTROMS                       
REMARK 525    HOH B 990        DISTANCE =  8.65 ANGSTROMS                       
REMARK 525    HOH B1014        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH B1093        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH A 929        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH B1107        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH B1111        DISTANCE =  7.93 ANGSTROMS                       
REMARK 525    HOH B1151        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH B1158        DISTANCE =  8.07 ANGSTROMS                       
REMARK 525    HOH B1162        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH A 971        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH B1173        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH B1179        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A 983        DISTANCE =  7.16 ANGSTROMS                       
REMARK 525    HOH B1204        DISTANCE =  7.38 ANGSTROMS                       
REMARK 525    HOH A1005        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH A1010        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH B1225        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH B1227        DISTANCE =  5.48 ANGSTROMS                       
REMARK 525    HOH B1232        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH A1024        DISTANCE =  7.00 ANGSTROMS                       
REMARK 525    HOH B1246        DISTANCE =  7.04 ANGSTROMS                       
REMARK 525    HOH B1250        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH A1075        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH A1082        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH A1127        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A1130        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH A1136        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH A1163        DISTANCE =  5.45 ANGSTROMS                       
REMARK 525    HOH A1164        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH A1253        DISTANCE =  5.16 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     1PE B  500                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 158   NE2                                                    
REMARK 620 2 HOH A 732   O    95.4                                              
REMARK 620 3 HOH A 680   O    95.8  82.4                                        
REMARK 620 4 HOH A 679   O   175.9  85.7  88.3                                  
REMARK 620 5 HOH A 682   O    89.1  97.2 175.1  86.8                            
REMARK 620 6 HOH A 681   O    90.1 174.5  96.2  89.0  83.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A2003  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 405   OD1                                                    
REMARK 620 2 ARG A 406   O    84.1                                              
REMARK 620 3 ASP A 409   OD2  80.1  89.3                                        
REMARK 620 4 LYS A 411   O    98.2 177.3  89.6                                  
REMARK 620 5 ASP A 431   OD1  92.3  91.3 172.2  90.1                            
REMARK 620 6 HOH A 845   O   151.2  84.5  73.5  92.8 114.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2005  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 158   NE2                                                    
REMARK 620 2 HOH B 867   O   170.4                                              
REMARK 620 3 HOH B 727   O    87.6 101.0                                        
REMARK 620 4 HOH B1235   O    96.8  85.5 103.9                                  
REMARK 620 5 HOH B1236   O    93.0  78.1 175.6  80.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2004  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 405   OD1                                                    
REMARK 620 2 ARG B 406   O    96.0                                              
REMARK 620 3 LYS B 411   O    85.5 177.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A2002  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 873   O                                                      
REMARK 620 2 HOH A1138   O    96.7                                              
REMARK 620 3 HOH A 870   O   114.3  89.0                                        
REMARK 620 4 HOH A 872   O   158.9  92.6  84.7                                  
REMARK 620 5 HOH A 874   O    89.9 173.4  87.5  81.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 500                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A2001                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A2002                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A2003                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 500                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B2004                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B2005                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ZYH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZYI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZYS   RELATED DB: PDB                                   
DBREF  2ZYR A    1   474  UNP    O28511   O28511_ARCFU     1    474             
DBREF  2ZYR B    1   474  UNP    O28511   O28511_ARCFU     1    474             
SEQADV 2ZYR VAL A  475  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR ASP A  476  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR LYS A  477  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR LEU A  478  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR ALA A  479  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR ALA A  480  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR ALA A  481  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR LEU A  482  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR GLU A  483  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR HIS A  484  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR VAL B  475  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR ASP B  476  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR LYS B  477  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR LEU B  478  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR ALA B  479  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR ALA B  480  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR ALA B  481  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR LEU B  482  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR GLU B  483  UNP  O28511              EXPRESSION TAG                 
SEQADV 2ZYR HIS B  484  UNP  O28511              EXPRESSION TAG                 
SEQRES   1 A  484  MET ARG GLY LEU ALA VAL LEU VAL LEU LEU VAL PHE ALA          
SEQRES   2 A  484  VAL GLN VAL ALA ALA ALA GLU ASP PHE ARG PRO VAL VAL          
SEQRES   3 A  484  PHE VAL HIS GLY LEU ALA GLY SER ALA GLY GLN PHE GLU          
SEQRES   4 A  484  SER GLN GLY MET ARG PHE ALA ALA ASN GLY TYR PRO ALA          
SEQRES   5 A  484  GLU TYR VAL LYS THR PHE GLU TYR ASP THR ILE SER TRP          
SEQRES   6 A  484  ALA LEU VAL VAL GLU THR ASP MET LEU PHE SER GLY LEU          
SEQRES   7 A  484  GLY SER GLU PHE GLY LEU ASN ILE SER GLN ILE ILE ASP          
SEQRES   8 A  484  PRO GLU THR LEU ASP LYS ILE LEU SER LYS SER ARG GLU          
SEQRES   9 A  484  ARG LEU ILE ASP GLU THR PHE SER ARG LEU ASP ARG VAL          
SEQRES  10 A  484  ILE ASP GLU ALA LEU ALA GLU SER GLY ALA ASP LYS VAL          
SEQRES  11 A  484  ASP LEU VAL GLY HIS SER MET GLY THR PHE PHE LEU VAL          
SEQRES  12 A  484  ARG TYR VAL ASN SER SER PRO GLU ARG ALA ALA LYS VAL          
SEQRES  13 A  484  ALA HIS LEU ILE LEU LEU ASP GLY VAL TRP GLY VAL ASP          
SEQRES  14 A  484  ALA PRO GLU GLY ILE PRO THR LEU ALA VAL PHE GLY ASN          
SEQRES  15 A  484  PRO LYS ALA LEU PRO ALA LEU GLY LEU PRO GLU GLU LYS          
SEQRES  16 A  484  VAL VAL TYR ASN ALA THR ASN VAL TYR PHE ASN ASN MET          
SEQRES  17 A  484  THR HIS VAL GLN LEU CYS THR SER PRO GLU THR PHE ALA          
SEQRES  18 A  484  VAL MET PHE GLU PHE ILE ASN GLY TYR LYS PRO ALA THR          
SEQRES  19 A  484  THR ASP ILE VAL PRO GLN ASP GLY ASP TYR VAL LYS VAL          
SEQRES  20 A  484  LYS GLY LYS PHE LEU ALA PHE ALA THR ASN GLY ASP VAL          
SEQRES  21 A  484  SER GLY TRP LEU SER ILE TYR PRO ILE ASP GLU ASN GLY          
SEQRES  22 A  484  LYS ARG LEU THR ARG LEU PRO VAL LYS PHE MET ARG VAL          
SEQRES  23 A  484  LYS GLY ASP PHE GLU VAL ARG LEU ARG LYS GLY GLN LEU          
SEQRES  24 A  484  TYR GLU PHE GLN PHE ARG LYS ASP PHE SER PRO ILE ILE          
SEQRES  25 A  484  TYR HIS TYR TYR ARG ALA PRO PHE VAL ARG ASP ASP LEU          
SEQRES  26 A  484  TRP ALA ARG PHE LEU VAL SER LYS PRO PRO LEU ASP VAL          
SEQRES  27 A  484  GLU LEU LEU ILE LEU PRO GLU ARG LEU SER PRO ALA ALA          
SEQRES  28 A  484  LYS GLU THR SER GLY LEU LEU LEU ILE ARG TYR LYS GLU          
SEQRES  29 A  484  MET ILE GLY GLU TYR ASP GLU GLU ILE GLY GLY VAL ASP          
SEQRES  30 A  484  GLU VAL TYR VAL ASN GLY VAL ASN VAL CYS THR GLU ARG          
SEQRES  31 A  484  ILE CYS PRO ILE GLU ARG ALA VAL ASN GLY LEU TRP VAL          
SEQRES  32 A  484  PHE ASP ARG GLY ALA ASP GLY LYS SER ASP LEU ASP ARG          
SEQRES  33 A  484  GLU VAL VAL ARG TYR SER ILE MET PRO PHE MET SER ALA          
SEQRES  34 A  484  ALA ASP LEU VAL VAL PRO ALA GLU GLY THR ILE SER ILE          
SEQRES  35 A  484  ALA VAL LYS SER ARG THR GLY GLY GLU GLU SER PHE THR          
SEQRES  36 A  484  ILE PRO ALA TRP SER ALA ASP ARG HIS SER ILE ILE VAL          
SEQRES  37 A  484  GLN PHE SER ASP TYR ILE VAL ASP LYS LEU ALA ALA ALA          
SEQRES  38 A  484  LEU GLU HIS                                                  
SEQRES   1 B  484  MET ARG GLY LEU ALA VAL LEU VAL LEU LEU VAL PHE ALA          
SEQRES   2 B  484  VAL GLN VAL ALA ALA ALA GLU ASP PHE ARG PRO VAL VAL          
SEQRES   3 B  484  PHE VAL HIS GLY LEU ALA GLY SER ALA GLY GLN PHE GLU          
SEQRES   4 B  484  SER GLN GLY MET ARG PHE ALA ALA ASN GLY TYR PRO ALA          
SEQRES   5 B  484  GLU TYR VAL LYS THR PHE GLU TYR ASP THR ILE SER TRP          
SEQRES   6 B  484  ALA LEU VAL VAL GLU THR ASP MET LEU PHE SER GLY LEU          
SEQRES   7 B  484  GLY SER GLU PHE GLY LEU ASN ILE SER GLN ILE ILE ASP          
SEQRES   8 B  484  PRO GLU THR LEU ASP LYS ILE LEU SER LYS SER ARG GLU          
SEQRES   9 B  484  ARG LEU ILE ASP GLU THR PHE SER ARG LEU ASP ARG VAL          
SEQRES  10 B  484  ILE ASP GLU ALA LEU ALA GLU SER GLY ALA ASP LYS VAL          
SEQRES  11 B  484  ASP LEU VAL GLY HIS SER MET GLY THR PHE PHE LEU VAL          
SEQRES  12 B  484  ARG TYR VAL ASN SER SER PRO GLU ARG ALA ALA LYS VAL          
SEQRES  13 B  484  ALA HIS LEU ILE LEU LEU ASP GLY VAL TRP GLY VAL ASP          
SEQRES  14 B  484  ALA PRO GLU GLY ILE PRO THR LEU ALA VAL PHE GLY ASN          
SEQRES  15 B  484  PRO LYS ALA LEU PRO ALA LEU GLY LEU PRO GLU GLU LYS          
SEQRES  16 B  484  VAL VAL TYR ASN ALA THR ASN VAL TYR PHE ASN ASN MET          
SEQRES  17 B  484  THR HIS VAL GLN LEU CYS THR SER PRO GLU THR PHE ALA          
SEQRES  18 B  484  VAL MET PHE GLU PHE ILE ASN GLY TYR LYS PRO ALA THR          
SEQRES  19 B  484  THR ASP ILE VAL PRO GLN ASP GLY ASP TYR VAL LYS VAL          
SEQRES  20 B  484  LYS GLY LYS PHE LEU ALA PHE ALA THR ASN GLY ASP VAL          
SEQRES  21 B  484  SER GLY TRP LEU SER ILE TYR PRO ILE ASP GLU ASN GLY          
SEQRES  22 B  484  LYS ARG LEU THR ARG LEU PRO VAL LYS PHE MET ARG VAL          
SEQRES  23 B  484  LYS GLY ASP PHE GLU VAL ARG LEU ARG LYS GLY GLN LEU          
SEQRES  24 B  484  TYR GLU PHE GLN PHE ARG LYS ASP PHE SER PRO ILE ILE          
SEQRES  25 B  484  TYR HIS TYR TYR ARG ALA PRO PHE VAL ARG ASP ASP LEU          
SEQRES  26 B  484  TRP ALA ARG PHE LEU VAL SER LYS PRO PRO LEU ASP VAL          
SEQRES  27 B  484  GLU LEU LEU ILE LEU PRO GLU ARG LEU SER PRO ALA ALA          
SEQRES  28 B  484  LYS GLU THR SER GLY LEU LEU LEU ILE ARG TYR LYS GLU          
SEQRES  29 B  484  MET ILE GLY GLU TYR ASP GLU GLU ILE GLY GLY VAL ASP          
SEQRES  30 B  484  GLU VAL TYR VAL ASN GLY VAL ASN VAL CYS THR GLU ARG          
SEQRES  31 B  484  ILE CYS PRO ILE GLU ARG ALA VAL ASN GLY LEU TRP VAL          
SEQRES  32 B  484  PHE ASP ARG GLY ALA ASP GLY LYS SER ASP LEU ASP ARG          
SEQRES  33 B  484  GLU VAL VAL ARG TYR SER ILE MET PRO PHE MET SER ALA          
SEQRES  34 B  484  ALA ASP LEU VAL VAL PRO ALA GLU GLY THR ILE SER ILE          
SEQRES  35 B  484  ALA VAL LYS SER ARG THR GLY GLY GLU GLU SER PHE THR          
SEQRES  36 B  484  ILE PRO ALA TRP SER ALA ASP ARG HIS SER ILE ILE VAL          
SEQRES  37 B  484  GLN PHE SER ASP TYR ILE VAL ASP LYS LEU ALA ALA ALA          
SEQRES  38 B  484  LEU GLU HIS                                                  
HET    1PE  A 500      16                                                       
HET     MG  A2001       1                                                       
HET     MG  A2002       1                                                       
HET     MG  A2003       1                                                       
HET    1PE  B 500      13                                                       
HET     MG  B2004       1                                                       
HET     MG  B2005       1                                                       
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     1PE PEG400                                                           
FORMUL   3  1PE    2(C10 H22 O6)                                                
FORMUL   4   MG    5(MG 2+)                                                     
FORMUL  10  HOH   *1255(H2 O)                                                   
HELIX    1   1 SER A   34  GLN A   37  5                                   4    
HELIX    2   2 PHE A   38  ASN A   48  1                                  11    
HELIX    3   3 PRO A   51  GLU A   53  5                                   3    
HELIX    4   4 ASP A   61  VAL A   69  1                                   9    
HELIX    5   5 GLY A   77  GLY A   79  5                                   3    
HELIX    6   6 SER A   80  SER A   87  1                                   8    
HELIX    7   7 GLN A   88  ILE A   90  5                                   3    
HELIX    8   8 ASP A   91  SER A  100  1                                  10    
HELIX    9   9 SER A  102  GLY A  126  1                                  25    
HELIX   10  10 SER A  136  SER A  148  1                                  13    
HELIX   11  11 SER A  149  LYS A  155  1                                   7    
HELIX   12  12 PRO A  183  LEU A  186  5                                   4    
HELIX   13  13 THR A  209  SER A  216  1                                   8    
HELIX   14  14 SER A  216  GLY A  229  1                                  14    
HELIX   15  15 ASP A  337  LEU A  341  5                                   5    
HELIX   16  16 ILE A  342  LEU A  347  1                                   6    
HELIX   17  17 SER A  348  GLU A  353  5                                   6    
HELIX   18  18 PRO A  393  ALA A  397  5                                   5    
HELIX   19  19 ASP A  405  ASP A  409  5                                   5    
HELIX   20  20 VAL A  418  SER A  422  5                                   5    
HELIX   21  21 ASP A  476  HIS A  484  1                                   9    
HELIX   22  22 SER B   34  GLN B   37  5                                   4    
HELIX   23  23 PHE B   38  ASN B   48  1                                  11    
HELIX   24  24 PRO B   51  GLU B   53  5                                   3    
HELIX   25  25 ASP B   61  VAL B   69  1                                   9    
HELIX   26  26 GLY B   79  GLN B   88  1                                  10    
HELIX   27  27 ASP B   91  SER B  100  1                                  10    
HELIX   28  28 SER B  102  GLY B  126  1                                  25    
HELIX   29  29 SER B  136  SER B  148  1                                  13    
HELIX   30  30 SER B  149  LYS B  155  1                                   7    
HELIX   31  31 ASN B  182  GLY B  190  5                                   9    
HELIX   32  32 THR B  209  SER B  216  1                                   8    
HELIX   33  33 SER B  216  GLY B  229  1                                  14    
HELIX   34  34 ASP B  337  LEU B  341  5                                   5    
HELIX   35  35 ILE B  342  LEU B  347  1                                   6    
HELIX   36  36 SER B  348  GLU B  353  5                                   6    
HELIX   37  37 PRO B  393  ALA B  397  5                                   5    
HELIX   38  38 ASP B  405  ASP B  409  5                                   5    
HELIX   39  39 VAL B  418  SER B  422  5                                   5    
SHEET    1   A 6 VAL A  55  PHE A  58  0                                        
SHEET    2   A 6 VAL A  25  VAL A  28  1  N  VAL A  25   O  LYS A  56           
SHEET    3   A 6 VAL A 130  HIS A 135  1  O  VAL A 133   N  VAL A  28           
SHEET    4   A 6 VAL A 156  LEU A 162  1  O  LEU A 162   N  GLY A 134           
SHEET    5   A 6 THR A 176  GLY A 181  1  O  LEU A 177   N  LEU A 161           
SHEET    6   A 6 THR A 201  PHE A 205  1  O  PHE A 205   N  PHE A 180           
SHEET    1   B 3 ASP A 289  ARG A 295  0                                        
SHEET    2   B 3 TYR A 244  ALA A 253 -1  N  VAL A 247   O  VAL A 292           
SHEET    3   B 3 ASP A 324  VAL A 331  1  O  PHE A 329   N  LYS A 250           
SHEET    1   C 8 LYS A 282  LYS A 287  0                                        
SHEET    2   C 8 SER A 261  PRO A 268 -1  N  GLY A 262   O  VAL A 286           
SHEET    3   C 8 TYR A 300  LYS A 306 -1  O  GLN A 303   N  SER A 265           
SHEET    4   C 8 ILE A 312  ARG A 317 -1  O  TYR A 315   N  PHE A 302           
SHEET    5   C 8 HIS A 464  GLN A 469  1  O  GLN A 469   N  TYR A 316           
SHEET    6   C 8 LEU A 357  MET A 365  1  N  ILE A 360   O  VAL A 468           
SHEET    7   C 8 VAL A 398  PHE A 404 -1  O  VAL A 403   N  LEU A 357           
SHEET    8   C 8 MET A 427  ASP A 431  1  O  ALA A 430   N  TRP A 402           
SHEET    1   D 4 VAL A 384  ASN A 385  0                                        
SHEET    2   D 4 GLU A 378  VAL A 381 -1  N  VAL A 381   O  VAL A 384           
SHEET    3   D 4 THR A 439  LYS A 445 -1  O  ALA A 443   N  TYR A 380           
SHEET    4   D 4 GLU A 451  PRO A 457 -1  O  PHE A 454   N  ILE A 442           
SHEET    1   E 6 VAL B  55  PHE B  58  0                                        
SHEET    2   E 6 VAL B  25  VAL B  28  1  N  VAL B  25   O  LYS B  56           
SHEET    3   E 6 VAL B 130  HIS B 135  1  O  VAL B 133   N  VAL B  28           
SHEET    4   E 6 VAL B 156  LEU B 162  1  O  ALA B 157   N  VAL B 130           
SHEET    5   E 6 THR B 176  PHE B 180  1  O  LEU B 177   N  LEU B 161           
SHEET    6   E 6 THR B 201  TYR B 204  1  O  THR B 201   N  ALA B 178           
SHEET    1   F 3 ASP B 289  ARG B 295  0                                        
SHEET    2   F 3 TYR B 244  ALA B 253 -1  N  VAL B 245   O  LEU B 294           
SHEET    3   F 3 ASP B 324  VAL B 331  1  O  PHE B 329   N  LYS B 250           
SHEET    1   G 8 LYS B 282  LYS B 287  0                                        
SHEET    2   G 8 SER B 261  PRO B 268 -1  N  LEU B 264   O  MET B 284           
SHEET    3   G 8 TYR B 300  LYS B 306 -1  O  GLN B 303   N  SER B 265           
SHEET    4   G 8 ILE B 312  ARG B 317 -1  O  TYR B 313   N  PHE B 304           
SHEET    5   G 8 HIS B 464  GLN B 469  1  O  ILE B 467   N  TYR B 316           
SHEET    6   G 8 LEU B 357  ILE B 360  1  N  ILE B 360   O  VAL B 468           
SHEET    7   G 8 GLY B 400  PHE B 404 -1  O  VAL B 403   N  LEU B 357           
SHEET    8   G 8 MET B 427  ASP B 431  1  O  ALA B 430   N  TRP B 402           
SHEET    1   H 4 VAL B 384  ASN B 385  0                                        
SHEET    2   H 4 GLU B 378  VAL B 381 -1  N  VAL B 381   O  VAL B 384           
SHEET    3   H 4 THR B 439  LYS B 445 -1  O  ALA B 443   N  TYR B 380           
SHEET    4   H 4 GLU B 451  PRO B 457 -1  O  PHE B 454   N  ILE B 442           
LINK         NE2 HIS A 158                MG    MG A2001     1555   1555  2.24  
LINK         OD1 ASP A 405                MG    MG A2003     1555   1555  2.35  
LINK         O   ARG A 406                MG    MG A2003     1555   1555  2.34  
LINK         OD2 ASP A 409                MG    MG A2003     1555   1555  2.48  
LINK         O   LYS A 411                MG    MG A2003     1555   1555  2.33  
LINK         OD1 ASP A 431                MG    MG A2003     1555   1555  2.49  
LINK         NE2 HIS B 158                MG    MG B2005     1555   1555  2.31  
LINK         OD1 ASP B 405                MG    MG B2004     1555   1555  2.15  
LINK         O   ARG B 406                MG    MG B2004     1555   1555  2.16  
LINK         O   LYS B 411                MG    MG B2004     1555   1555  2.10  
LINK        MG    MG A2001                 O   HOH A 732     1555   1555  1.76  
LINK        MG    MG A2001                 O   HOH A 680     1555   1555  2.23  
LINK        MG    MG A2001                 O   HOH A 679     1555   1555  2.21  
LINK        MG    MG A2001                 O   HOH A 682     1555   1555  2.21  
LINK        MG    MG A2001                 O   HOH A 681     1555   1555  2.14  
LINK        MG    MG A2002                 O   HOH A 873     1555   1555  1.87  
LINK        MG    MG A2002                 O   HOH A1138     1555   1555  2.12  
LINK        MG    MG A2002                 O   HOH A 870     1555   1555  2.37  
LINK        MG    MG A2002                 O   HOH A 872     1555   1555  2.08  
LINK        MG    MG A2002                 O   HOH A 874     1555   1555  2.01  
LINK        MG    MG A2003                 O   HOH A 845     1555   1555  2.44  
LINK        MG    MG B2005                 O   HOH B 867     1555   1555  2.21  
LINK        MG    MG B2005                 O   HOH B 727     1555   1555  2.11  
LINK        MG    MG B2005                 O   HOH B1235     1555   1555  2.17  
LINK        MG    MG B2005                 O   HOH B1236     1555   1555  1.88  
CISPEP   1 PRO A  334    PRO A  335          0         0.91                     
CISPEP   2 PRO B  334    PRO B  335          0         0.28                     
SITE     1 AC1  7 LEU A  31  HIS A 135  PHE A 254  LEU A 330                    
SITE     2 AC1  7 SER A 332  GLU A 339  PHE A 426                               
SITE     1 AC2  6 HIS A 158  HOH A 679  HOH A 680  HOH A 681                    
SITE     2 AC2  6 HOH A 682  HOH A 732                                          
SITE     1 AC3  5 HOH A 870  HOH A 872  HOH A 873  HOH A 874                    
SITE     2 AC3  5 HOH A1138                                                     
SITE     1 AC4  6 ASP A 405  ARG A 406  ASP A 409  LYS A 411                    
SITE     2 AC4  6 ASP A 431  HOH A 845                                          
SITE     1 AC5  5 LEU B  31  ALA B  32  VAL B 338  PHE B 426                    
SITE     2 AC5  5 HOH B 871                                                     
SITE     1 AC6  6 ASP B 405  ARG B 406  ASP B 409  LYS B 411                    
SITE     2 AC6  6 ASP B 431  HOH B 804                                          
SITE     1 AC7  6 HIS B 158  HOH B 726  HOH B 727  HOH B 867                    
SITE     2 AC7  6 HOH B1235  HOH B1236                                          
CRYST1   52.289  106.667  175.885  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019124  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009375  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005686        0.00000                         
TER    3661      HIS A 484                                                      
TER    7248      ILE B 474                                                      
MASTER      509    0    7   39   42    0   14    6 8535    2   63   76          
END                                                                             

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