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LongText Report for: 3HXK-pdb

Name Class
3HXK-pdb
HEADER    HYDROLASE                               20-JUN-09   3HXK              
TITLE     CRYSTAL STRUCTURE OF A SUGAR HYDROLASE (YEEB) FROM                    
TITLE    2 LACTOCOCCUS LACTIS, NORTHEAST STRUCTURAL GENOMICS                    
TITLE    3 CONSORTIUM TARGET KR108                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUGAR HYDROLASE;                                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOCOCCUS LACTIS SUBSP. LACTIS;               
SOURCE   3 ORGANISM_COMMON: STREPTOCOCCUS LACTIS;                               
SOURCE   4 ORGANISM_TAXID: 1360;                                                
SOURCE   5 STRAIN: IL1403;                                                      
SOURCE   6 GENE: L427, L42784, LL0430, YEEB;                                    
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+ MAGIC;                          
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET 21-23C                                
KEYWDS    ALPHA-BETA PROTEIN., STRUCTURAL GENOMICS, PSI-2, PROTEIN              
KEYWDS   2 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS                  
KEYWDS   3 CONSORTIUM, NESG, HYDROLASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.FOROUHAR,M.SU,J.SEETHARAMAN,M.MAO,R.XIAO,C.CICCOSANTI,              
AUTHOR   2 E.L.FOOTE,M.MAGLAQUI,L.ZHAO,J.K.EVERETT,R.NAIR,T.B.ACTON,            
AUTHOR   3 B.ROST,G.T.MONTELIONE,L.TONG,J.F.HUNT,NORTHEAST STRUCTURAL           
AUTHOR   4 GENOMICS CONSORTIUM (NESG)                                           
REVDAT   1   07-JUL-09 3HXK    0                                                
JRNL        AUTH   F.FOROUHAR,M.SU,J.SEETHARAMAN,M.MAO,R.XIAO,                  
JRNL        AUTH 2 C.CICCOSANTI,E.L.FOOTE,M.MAGLAQUI,L.ZHAO,                    
JRNL        AUTH 3 J.K.EVERETT,R.NAIR,T.B.ACTON,B.ROST,G.T.MONTELIONE,          
JRNL        AUTH 4 L.TONG,J.F.HUNT                                              
JRNL        TITL   CRYSTAL STRUCTURE OF A SUGAR HYDROLASE (YEEB) FROM           
JRNL        TITL 2 LACTOCOCCUS LACTIS, NORTHEAST STRUCTURAL GENOMICS            
JRNL        TITL 3 CONSORTIUM TARGET KR108                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2 & XTALVIEW                                   
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) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 350784.812                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 32873                          
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) : 0.256                           
REMARK   3   FREE R VALUE                     : 0.296                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3177                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.31                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2374                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3440                       
REMARK   3   BIN FREE R VALUE                    : 0.3720                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 225                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.025                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8080                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 61                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 54.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -14.28000                                            
REMARK   3    B22 (A**2) : -11.63000                                            
REMARK   3    B33 (A**2) : 25.91000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.47                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.61                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.55                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.66                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.10                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.87                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 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 : FLAT MODEL                                           
REMARK   3   KSOL        : 0.30                                                 
REMARK   3   BSOL        : 22.32                                                
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 3HXK COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053705.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97907                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36064                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : 0.08200                            
REMARK 200   FOR THE DATA SET  : 17.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.21100                            
REMARK 200   FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: BNP THEN SOLVE/RESOLVE                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 100MM NACL, 5MM        
REMARK 280  DTT, 0.02% NAN3, 10MM TRIS-HCL (PH 7.5) . RESERVOIR SOLUTION:       
REMARK 280  0.1 M TRIS (PH 9.1), 29% PEG400, AND 0.1M (MG)2SO4. ,               
REMARK 280  MICROBATCH, UNDER OIL, TEMPERATURE 291K                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      109.42950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      109.42950            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       34.19550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       75.21250            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       34.19550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       75.21250            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      109.42950            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       34.19550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       75.21250            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      109.42950            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       34.19550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       75.21250            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     MSE A     1                                                      
REMARK 465     ILE A     2                                                      
REMARK 465     PHE A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     PHE A     8                                                      
REMARK 465     TRP A     9                                                      
REMARK 465     TYR A    10                                                      
REMARK 465     ASN A    11                                                      
REMARK 465     LYS A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     MSE A    14                                                      
REMARK 465     PRO A    35                                                      
REMARK 465     ARG A    36                                                      
REMARK 465     GLN A    37                                                      
REMARK 465     ASN A    38                                                      
REMARK 465     GLU A    39                                                      
REMARK 465     ASN A    40                                                      
REMARK 465     HIS A   271                                                      
REMARK 465     HIS A   272                                                      
REMARK 465     HIS A   273                                                      
REMARK 465     HIS A   274                                                      
REMARK 465     HIS A   275                                                      
REMARK 465     HIS A   276                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     ILE B     2                                                      
REMARK 465     PHE B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     PHE B     8                                                      
REMARK 465     TRP B     9                                                      
REMARK 465     TYR B    10                                                      
REMARK 465     ASN B    11                                                      
REMARK 465     LYS B    12                                                      
REMARK 465     LEU B    13                                                      
REMARK 465     MSE B    14                                                      
REMARK 465     PRO B    35                                                      
REMARK 465     ARG B    36                                                      
REMARK 465     GLN B    37                                                      
REMARK 465     ASN B    38                                                      
REMARK 465     GLU B    39                                                      
REMARK 465     ASN B    40                                                      
REMARK 465     HIS B   271                                                      
REMARK 465     HIS B   272                                                      
REMARK 465     HIS B   273                                                      
REMARK 465     HIS B   274                                                      
REMARK 465     HIS B   275                                                      
REMARK 465     HIS B   276                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     ILE C     2                                                      
REMARK 465     PHE C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     LEU C     7                                                      
REMARK 465     PHE C     8                                                      
REMARK 465     TRP C     9                                                      
REMARK 465     TYR C    10                                                      
REMARK 465     ASN C    11                                                      
REMARK 465     LYS C    12                                                      
REMARK 465     LEU C    13                                                      
REMARK 465     MSE C    14                                                      
REMARK 465     PRO C    35                                                      
REMARK 465     ARG C    36                                                      
REMARK 465     GLN C    37                                                      
REMARK 465     ASN C    38                                                      
REMARK 465     GLU C    39                                                      
REMARK 465     ASN C    40                                                      
REMARK 465     HIS C   271                                                      
REMARK 465     HIS C   272                                                      
REMARK 465     HIS C   273                                                      
REMARK 465     HIS C   274                                                      
REMARK 465     HIS C   275                                                      
REMARK 465     HIS C   276                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     ILE D     2                                                      
REMARK 465     PHE D     3                                                      
REMARK 465     LEU D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     THR D     6                                                      
REMARK 465     LEU D     7                                                      
REMARK 465     PHE D     8                                                      
REMARK 465     TRP D     9                                                      
REMARK 465     TYR D    10                                                      
REMARK 465     ASN D    11                                                      
REMARK 465     LYS D    12                                                      
REMARK 465     LEU D    13                                                      
REMARK 465     MSE D    14                                                      
REMARK 465     PRO D    35                                                      
REMARK 465     ARG D    36                                                      
REMARK 465     GLN D    37                                                      
REMARK 465     ASN D    38                                                      
REMARK 465     GLU D    39                                                      
REMARK 465     ASN D    40                                                      
REMARK 465     HIS D   271                                                      
REMARK 465     HIS D   272                                                      
REMARK 465     HIS D   273                                                      
REMARK 465     HIS D   274                                                      
REMARK 465     HIS D   275                                                      
REMARK 465     HIS D   276                                                      
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    LEU A  21      -76.07   -109.90                                   
REMARK 500    ASN A  22     -165.67   -119.89                                   
REMARK 500    ALA A  25       93.47   -176.99                                   
REMARK 500    THR A  42       79.78   -153.41                                   
REMARK 500    TYR A  54       -5.52     62.36                                   
REMARK 500    HIS A  56     -155.15   -135.23                                   
REMARK 500    SER A  58      103.91    -50.69                                   
REMARK 500    ARG A  60       14.69    -69.19                                   
REMARK 500    SER A  62     -112.71   -114.83                                   
REMARK 500    LYS A  86       46.44   -144.31                                   
REMARK 500    ASN A  89      -80.24   -121.14                                   
REMARK 500    ASN A  91       82.64    -67.27                                   
REMARK 500    PHE A  92        3.86    -64.12                                   
REMARK 500    SER A 127     -141.10     52.16                                   
REMARK 500    ASN A 138      145.53    172.49                                   
REMARK 500    SER A 139       71.62     73.83                                   
REMARK 500    GLN A 141     -115.69   -137.16                                   
REMARK 500    ILE A 142       42.92    -78.74                                   
REMARK 500    HIS A 143       16.17   -143.06                                   
REMARK 500    TYR A 152       63.96     30.98                                   
REMARK 500    PHE A 159       76.45   -109.91                                   
REMARK 500    HIS A 167      -93.08   -142.75                                   
REMARK 500    PHE A 168        9.56    -69.05                                   
REMARK 500    GLU A 171     -137.68     82.63                                   
REMARK 500    ILE A 172       94.83     59.92                                   
REMARK 500    ASN A 174       95.98    -50.89                                   
REMARK 500    LYS A 183       27.34    -66.82                                   
REMARK 500    ASP A 198        3.83   -176.96                                   
REMARK 500    LEU A 208      -70.16    -51.71                                   
REMARK 500    ARG A 213       30.27    -72.25                                   
REMARK 500    SER A 234     -119.16     58.55                                   
REMARK 500    ALA A 236       15.42     59.39                                   
REMARK 500    ARG A 238        4.82    -64.49                                   
REMARK 500    ALA A 241      119.16    178.63                                   
REMARK 500    SER A 243     -167.81   -108.49                                   
REMARK 500    ASN A 268       45.69    -84.24                                   
REMARK 500    LEU B  21      -74.61   -110.23                                   
REMARK 500    ASN B  22     -165.01   -120.82                                   
REMARK 500    ALA B  25       92.79   -177.37                                   
REMARK 500    THR B  42       77.41   -154.41                                   
REMARK 500    TYR B  54       -5.35     59.92                                   
REMARK 500    HIS B  56     -154.94   -133.88                                   
REMARK 500    SER B  58      103.57    -49.61                                   
REMARK 500    ARG B  60       15.83    -69.09                                   
REMARK 500    SER B  62     -112.73   -114.00                                   
REMARK 500    LYS B  86       45.17   -142.90                                   
REMARK 500    ASN B  89      -80.90   -120.76                                   
REMARK 500    ASN B  91       83.04    -66.95                                   
REMARK 500    PHE B  92        3.55    -63.90                                   
REMARK 500    SER B 127     -140.62     52.49                                   
REMARK 500    ASN B 138      145.98    171.87                                   
REMARK 500    SER B 139       71.20     73.55                                   
REMARK 500    GLN B 141     -114.53   -136.19                                   
REMARK 500    ILE B 142       42.50    -79.45                                   
REMARK 500    HIS B 143       17.02   -142.89                                   
REMARK 500    LYS B 146       -8.95    -59.73                                   
REMARK 500    TYR B 152       62.93     29.14                                   
REMARK 500    PHE B 159       75.78   -109.20                                   
REMARK 500    HIS B 167      -93.05   -143.58                                   
REMARK 500    PHE B 168        9.28    -68.93                                   
REMARK 500    GLU B 171     -138.18     80.93                                   
REMARK 500    ILE B 172       95.60     60.98                                   
REMARK 500    ASN B 174       94.48    -51.30                                   
REMARK 500    ILE B 180        7.38    -69.84                                   
REMARK 500    LYS B 183       27.34    -66.62                                   
REMARK 500    ASP B 198        3.25   -176.58                                   
REMARK 500    ARG B 213       29.15    -71.47                                   
REMARK 500    SER B 234     -119.06     55.10                                   
REMARK 500    ARG B 238        2.74    -63.91                                   
REMARK 500    ALA B 241      117.49   -178.35                                   
REMARK 500    SER B 243     -168.67   -108.04                                   
REMARK 500    ASN B 268       49.90    -72.41                                   
REMARK 500    LEU B 269     -147.86   -138.78                                   
REMARK 500    LEU C  21      -76.17   -108.76                                   
REMARK 500    ASN C  22     -164.56   -119.73                                   
REMARK 500    ALA C  25       93.39   -178.29                                   
REMARK 500    THR C  42       79.45   -153.83                                   
REMARK 500    TYR C  54       -4.37     62.08                                   
REMARK 500    HIS C  56     -155.10   -134.33                                   
REMARK 500    SER C  58      102.33    -50.05                                   
REMARK 500    ARG C  60       15.70    -69.82                                   
REMARK 500    SER C  62     -113.46   -113.68                                   
REMARK 500    LYS C  86       45.71   -143.38                                   
REMARK 500    ASN C  89      -82.03   -119.93                                   
REMARK 500    ASN C  91       81.96    -65.93                                   
REMARK 500    PHE C  92        3.51    -63.48                                   
REMARK 500    SER C 127     -140.22     52.26                                   
REMARK 500    ASN C 138      145.86    171.39                                   
REMARK 500    SER C 139       70.30     72.73                                   
REMARK 500    GLN C 141     -114.36   -136.99                                   
REMARK 500    ILE C 142       42.37    -79.86                                   
REMARK 500    HIS C 143       16.57   -143.04                                   
REMARK 500    TYR C 152       63.34     29.18                                   
REMARK 500    PHE C 159       77.46   -110.40                                   
REMARK 500    HIS C 167      -92.92   -144.16                                   
REMARK 500    PHE C 168        9.56    -69.28                                   
REMARK 500    GLU C 171     -137.67     82.12                                   
REMARK 500    ILE C 172       94.78     60.60                                   
REMARK 500    ASN C 174       93.92    -50.65                                   
REMARK 500    LYS C 183       27.38    -65.82                                   
REMARK 500    ASP C 198        4.70   -175.97                                   
REMARK 500    LEU C 208      -72.04    -52.48                                   
REMARK 500    ARG C 213       29.97    -73.52                                   
REMARK 500    SER C 234     -117.93     56.51                                   
REMARK 500    ARG C 238        4.03    -62.00                                   
REMARK 500    ALA C 241      118.90    179.46                                   
REMARK 500    SER C 243     -167.54   -107.65                                   
REMARK 500    ASN C 268       31.72    -81.11                                   
REMARK 500    LEU D  21      -76.21   -110.90                                   
REMARK 500    ASN D  22     -163.25   -119.71                                   
REMARK 500    ALA D  25       94.05   -175.37                                   
REMARK 500    THR D  42       79.23   -153.34                                   
REMARK 500    TYR D  54       -5.92     61.13                                   
REMARK 500    HIS D  56     -154.65   -134.66                                   
REMARK 500    SER D  58      103.55    -51.35                                   
REMARK 500    ARG D  60       14.14    -68.65                                   
REMARK 500    SER D  62     -113.21   -113.27                                   
REMARK 500    LYS D  86       44.53   -144.21                                   
REMARK 500    ASN D  89      -81.76   -120.54                                   
REMARK 500    ASN D  91       83.78    -66.76                                   
REMARK 500    PHE D  92        3.29    -65.13                                   
REMARK 500    SER D 127     -142.03     52.62                                   
REMARK 500    ASN D 138      144.93    172.95                                   
REMARK 500    SER D 139       70.79     74.37                                   
REMARK 500    GLN D 141     -115.19   -136.56                                   
REMARK 500    ILE D 142       42.83    -79.42                                   
REMARK 500    HIS D 143       15.75   -142.59                                   
REMARK 500    LYS D 146       -9.40    -58.54                                   
REMARK 500    TYR D 152       65.22     29.17                                   
REMARK 500    PHE D 159       78.21   -110.74                                   
REMARK 500    HIS D 167      -92.35   -143.90                                   
REMARK 500    PHE D 168        9.33    -69.37                                   
REMARK 500    GLU D 171     -138.20     82.02                                   
REMARK 500    ILE D 172       95.49     60.71                                   
REMARK 500    ASN D 174       94.78    -49.53                                   
REMARK 500    ILE D 180        5.76    -68.88                                   
REMARK 500    LYS D 183       27.36    -66.96                                   
REMARK 500    ASP D 198        4.82   -176.34                                   
REMARK 500    ARG D 213       28.50    -72.79                                   
REMARK 500    SER D 234     -120.21     54.40                                   
REMARK 500    ARG D 238        4.56    -62.57                                   
REMARK 500    ALA D 241      120.94    179.96                                   
REMARK 500    SER D 243     -167.83   -108.82                                   
REMARK 500    LEU D 269      -73.88   -113.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: KR108   RELATED DB: TARGETDB                             
DBREF  3HXK A    1   268  UNP    Q9CID4   Q9CID4_LACLA     1    268             
DBREF  3HXK B    1   268  UNP    Q9CID4   Q9CID4_LACLA     1    268             
DBREF  3HXK C    1   268  UNP    Q9CID4   Q9CID4_LACLA     1    268             
DBREF  3HXK D    1   268  UNP    Q9CID4   Q9CID4_LACLA     1    268             
SEQADV 3HXK LEU A  269  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK GLU A  270  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS A  271  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS A  272  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS A  273  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS A  274  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS A  275  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS A  276  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK LEU B  269  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK GLU B  270  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS B  271  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS B  272  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS B  273  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS B  274  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS B  275  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS B  276  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK LEU C  269  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK GLU C  270  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS C  271  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS C  272  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS C  273  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS C  274  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS C  275  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS C  276  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK LEU D  269  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK GLU D  270  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS D  271  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS D  272  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS D  273  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS D  274  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS D  275  UNP  Q9CID4              EXPRESSION TAG                 
SEQADV 3HXK HIS D  276  UNP  Q9CID4              EXPRESSION TAG                 
SEQRES   1 A  276  MSE ILE PHE LEU SER THR LEU PHE TRP TYR ASN LYS LEU          
SEQRES   2 A  276  MSE ASN LYS SER THR PHE SER LEU ASN ASP THR ALA TRP          
SEQRES   3 A  276  VAL ASP PHE TYR GLN LEU GLN ASN PRO ARG GLN ASN GLU          
SEQRES   4 A  276  ASN TYR THR PHE PRO ALA ILE ILE ILE CYS PRO GLY GLY          
SEQRES   5 A  276  GLY TYR GLN HIS ILE SER GLN ARG GLU SER ASP PRO LEU          
SEQRES   6 A  276  ALA LEU ALA PHE LEU ALA GLN GLY TYR GLN VAL LEU LEU          
SEQRES   7 A  276  LEU ASN TYR THR VAL MSE ASN LYS GLY THR ASN TYR ASN          
SEQRES   8 A  276  PHE LEU SER GLN ASN LEU GLU GLU VAL GLN ALA VAL PHE          
SEQRES   9 A  276  SER LEU ILE HIS GLN ASN HIS LYS GLU TRP GLN ILE ASN          
SEQRES  10 A  276  PRO GLU GLN VAL PHE LEU LEU GLY CYS SER ALA GLY GLY          
SEQRES  11 A  276  HIS LEU ALA ALA TRP TYR GLY ASN SER GLU GLN ILE HIS          
SEQRES  12 A  276  ARG PRO LYS GLY VAL ILE LEU CYS TYR PRO VAL THR SER          
SEQRES  13 A  276  PHE THR PHE GLY TRP PRO SER ASP LEU SER HIS PHE ASN          
SEQRES  14 A  276  PHE GLU ILE GLU ASN ILE SER GLU TYR ASN ILE SER GLU          
SEQRES  15 A  276  LYS VAL THR SER SER THR PRO PRO THR PHE ILE TRP HIS          
SEQRES  16 A  276  THR ALA ASP ASP GLU GLY VAL PRO ILE TYR ASN SER LEU          
SEQRES  17 A  276  LYS TYR CYS ASP ARG LEU SER LYS HIS GLN VAL PRO PHE          
SEQRES  18 A  276  GLU ALA HIS PHE PHE GLU SER GLY PRO HIS GLY VAL SER          
SEQRES  19 A  276  LEU ALA ASN ARG THR THR ALA PRO SER ASP ALA TYR CYS          
SEQRES  20 A  276  LEU PRO SER VAL HIS ARG TRP VAL SER TRP ALA SER ASP          
SEQRES  21 A  276  TRP LEU GLU ARG GLN ILE LYS ASN LEU GLU HIS HIS HIS          
SEQRES  22 A  276  HIS HIS HIS                                                  
SEQRES   1 B  276  MSE ILE PHE LEU SER THR LEU PHE TRP TYR ASN LYS LEU          
SEQRES   2 B  276  MSE ASN LYS SER THR PHE SER LEU ASN ASP THR ALA TRP          
SEQRES   3 B  276  VAL ASP PHE TYR GLN LEU GLN ASN PRO ARG GLN ASN GLU          
SEQRES   4 B  276  ASN TYR THR PHE PRO ALA ILE ILE ILE CYS PRO GLY GLY          
SEQRES   5 B  276  GLY TYR GLN HIS ILE SER GLN ARG GLU SER ASP PRO LEU          
SEQRES   6 B  276  ALA LEU ALA PHE LEU ALA GLN GLY TYR GLN VAL LEU LEU          
SEQRES   7 B  276  LEU ASN TYR THR VAL MSE ASN LYS GLY THR ASN TYR ASN          
SEQRES   8 B  276  PHE LEU SER GLN ASN LEU GLU GLU VAL GLN ALA VAL PHE          
SEQRES   9 B  276  SER LEU ILE HIS GLN ASN HIS LYS GLU TRP GLN ILE ASN          
SEQRES  10 B  276  PRO GLU GLN VAL PHE LEU LEU GLY CYS SER ALA GLY GLY          
SEQRES  11 B  276  HIS LEU ALA ALA TRP TYR GLY ASN SER GLU GLN ILE HIS          
SEQRES  12 B  276  ARG PRO LYS GLY VAL ILE LEU CYS TYR PRO VAL THR SER          
SEQRES  13 B  276  PHE THR PHE GLY TRP PRO SER ASP LEU SER HIS PHE ASN          
SEQRES  14 B  276  PHE GLU ILE GLU ASN ILE SER GLU TYR ASN ILE SER GLU          
SEQRES  15 B  276  LYS VAL THR SER SER THR PRO PRO THR PHE ILE TRP HIS          
SEQRES  16 B  276  THR ALA ASP ASP GLU GLY VAL PRO ILE TYR ASN SER LEU          
SEQRES  17 B  276  LYS TYR CYS ASP ARG LEU SER LYS HIS GLN VAL PRO PHE          
SEQRES  18 B  276  GLU ALA HIS PHE PHE GLU SER GLY PRO HIS GLY VAL SER          
SEQRES  19 B  276  LEU ALA ASN ARG THR THR ALA PRO SER ASP ALA TYR CYS          
SEQRES  20 B  276  LEU PRO SER VAL HIS ARG TRP VAL SER TRP ALA SER ASP          
SEQRES  21 B  276  TRP LEU GLU ARG GLN ILE LYS ASN LEU GLU HIS HIS HIS          
SEQRES  22 B  276  HIS HIS HIS                                                  
SEQRES   1 C  276  MSE ILE PHE LEU SER THR LEU PHE TRP TYR ASN LYS LEU          
SEQRES   2 C  276  MSE ASN LYS SER THR PHE SER LEU ASN ASP THR ALA TRP          
SEQRES   3 C  276  VAL ASP PHE TYR GLN LEU GLN ASN PRO ARG GLN ASN GLU          
SEQRES   4 C  276  ASN TYR THR PHE PRO ALA ILE ILE ILE CYS PRO GLY GLY          
SEQRES   5 C  276  GLY TYR GLN HIS ILE SER GLN ARG GLU SER ASP PRO LEU          
SEQRES   6 C  276  ALA LEU ALA PHE LEU ALA GLN GLY TYR GLN VAL LEU LEU          
SEQRES   7 C  276  LEU ASN TYR THR VAL MSE ASN LYS GLY THR ASN TYR ASN          
SEQRES   8 C  276  PHE LEU SER GLN ASN LEU GLU GLU VAL GLN ALA VAL PHE          
SEQRES   9 C  276  SER LEU ILE HIS GLN ASN HIS LYS GLU TRP GLN ILE ASN          
SEQRES  10 C  276  PRO GLU GLN VAL PHE LEU LEU GLY CYS SER ALA GLY GLY          
SEQRES  11 C  276  HIS LEU ALA ALA TRP TYR GLY ASN SER GLU GLN ILE HIS          
SEQRES  12 C  276  ARG PRO LYS GLY VAL ILE LEU CYS TYR PRO VAL THR SER          
SEQRES  13 C  276  PHE THR PHE GLY TRP PRO SER ASP LEU SER HIS PHE ASN          
SEQRES  14 C  276  PHE GLU ILE GLU ASN ILE SER GLU TYR ASN ILE SER GLU          
SEQRES  15 C  276  LYS VAL THR SER SER THR PRO PRO THR PHE ILE TRP HIS          
SEQRES  16 C  276  THR ALA ASP ASP GLU GLY VAL PRO ILE TYR ASN SER LEU          
SEQRES  17 C  276  LYS TYR CYS ASP ARG LEU SER LYS HIS GLN VAL PRO PHE          
SEQRES  18 C  276  GLU ALA HIS PHE PHE GLU SER GLY PRO HIS GLY VAL SER          
SEQRES  19 C  276  LEU ALA ASN ARG THR THR ALA PRO SER ASP ALA TYR CYS          
SEQRES  20 C  276  LEU PRO SER VAL HIS ARG TRP VAL SER TRP ALA SER ASP          
SEQRES  21 C  276  TRP LEU GLU ARG GLN ILE LYS ASN LEU GLU HIS HIS HIS          
SEQRES  22 C  276  HIS HIS HIS                                                  
SEQRES   1 D  276  MSE ILE PHE LEU SER THR LEU PHE TRP TYR ASN LYS LEU          
SEQRES   2 D  276  MSE ASN LYS SER THR PHE SER LEU ASN ASP THR ALA TRP          
SEQRES   3 D  276  VAL ASP PHE TYR GLN LEU GLN ASN PRO ARG GLN ASN GLU          
SEQRES   4 D  276  ASN TYR THR PHE PRO ALA ILE ILE ILE CYS PRO GLY GLY          
SEQRES   5 D  276  GLY TYR GLN HIS ILE SER GLN ARG GLU SER ASP PRO LEU          
SEQRES   6 D  276  ALA LEU ALA PHE LEU ALA GLN GLY TYR GLN VAL LEU LEU          
SEQRES   7 D  276  LEU ASN TYR THR VAL MSE ASN LYS GLY THR ASN TYR ASN          
SEQRES   8 D  276  PHE LEU SER GLN ASN LEU GLU GLU VAL GLN ALA VAL PHE          
SEQRES   9 D  276  SER LEU ILE HIS GLN ASN HIS LYS GLU TRP GLN ILE ASN          
SEQRES  10 D  276  PRO GLU GLN VAL PHE LEU LEU GLY CYS SER ALA GLY GLY          
SEQRES  11 D  276  HIS LEU ALA ALA TRP TYR GLY ASN SER GLU GLN ILE HIS          
SEQRES  12 D  276  ARG PRO LYS GLY VAL ILE LEU CYS TYR PRO VAL THR SER          
SEQRES  13 D  276  PHE THR PHE GLY TRP PRO SER ASP LEU SER HIS PHE ASN          
SEQRES  14 D  276  PHE GLU ILE GLU ASN ILE SER GLU TYR ASN ILE SER GLU          
SEQRES  15 D  276  LYS VAL THR SER SER THR PRO PRO THR PHE ILE TRP HIS          
SEQRES  16 D  276  THR ALA ASP ASP GLU GLY VAL PRO ILE TYR ASN SER LEU          
SEQRES  17 D  276  LYS TYR CYS ASP ARG LEU SER LYS HIS GLN VAL PRO PHE          
SEQRES  18 D  276  GLU ALA HIS PHE PHE GLU SER GLY PRO HIS GLY VAL SER          
SEQRES  19 D  276  LEU ALA ASN ARG THR THR ALA PRO SER ASP ALA TYR CYS          
SEQRES  20 D  276  LEU PRO SER VAL HIS ARG TRP VAL SER TRP ALA SER ASP          
SEQRES  21 D  276  TRP LEU GLU ARG GLN ILE LYS ASN LEU GLU HIS HIS HIS          
SEQRES  22 D  276  HIS HIS HIS                                                  
MODRES 3HXK MSE A   84  MET  SELENOMETHIONINE                                   
MODRES 3HXK MSE B   84  MET  SELENOMETHIONINE                                   
MODRES 3HXK MSE C   84  MET  SELENOMETHIONINE                                   
MODRES 3HXK MSE D   84  MET  SELENOMETHIONINE                                   
HET    MSE  A  84       8                                                       
HET    MSE  B  84       8                                                       
HET    MSE  C  84       8                                                       
HET    MSE  D  84       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   5  HOH   *61(H2 O)                                                     
HELIX    1   1 SER A   58  GLU A   61  5                                   4    
HELIX    2   2 SER A   62  GLN A   72  1                                  11    
HELIX    3   3 PHE A   92  HIS A  111  1                                  20    
HELIX    4   4 ALA A  128  GLY A  137  1                                  10    
HELIX    5   5 ILE A  175  ASN A  179  5                                   5    
HELIX    6   6 ILE A  204  LYS A  216  1                                  13    
HELIX    7   7 LEU A  248  ARG A  253  1                                   6    
HELIX    8   8 ARG A  253  ASN A  268  1                                  16    
HELIX    9   9 SER B   58  GLU B   61  5                                   4    
HELIX   10  10 SER B   62  GLN B   72  1                                  11    
HELIX   11  11 PHE B   92  HIS B  111  1                                  20    
HELIX   12  12 ALA B  128  GLY B  137  1                                  10    
HELIX   13  13 ILE B  175  ASN B  179  5                                   5    
HELIX   14  14 ILE B  204  LYS B  216  1                                  13    
HELIX   15  15 LEU B  248  ASN B  268  1                                  21    
HELIX   16  16 SER C   58  GLU C   61  5                                   4    
HELIX   17  17 SER C   62  GLN C   72  1                                  11    
HELIX   18  18 PHE C   92  HIS C  111  1                                  20    
HELIX   19  19 ALA C  128  GLY C  137  1                                  10    
HELIX   20  20 ILE C  175  ASN C  179  5                                   5    
HELIX   21  21 ILE C  204  LYS C  216  1                                  13    
HELIX   22  22 LEU C  248  ASN C  268  1                                  21    
HELIX   23  23 SER D   58  GLU D   61  5                                   4    
HELIX   24  24 SER D   62  GLN D   72  1                                  11    
HELIX   25  25 PHE D   92  HIS D  111  1                                  20    
HELIX   26  26 SER D  127  GLY D  137  1                                  11    
HELIX   27  27 ILE D  175  ASN D  179  5                                   5    
HELIX   28  28 ILE D  204  LYS D  216  1                                  13    
HELIX   29  29 LEU D  248  ASN D  268  1                                  21    
SHEET    1   A16 LYS A  16  THR A  18  0                                        
SHEET    2   A16 TRP A  26  TYR A  30 -1  O  PHE A  29   N  SER A  17           
SHEET    3   A16 GLN A  75  ASN A  80 -1  O  VAL A  76   N  TYR A  30           
SHEET    4   A16 ALA A  45  CYS A  49  1  N  ILE A  46   O  GLN A  75           
SHEET    5   A16 PHE A 122  SER A 127  1  O  PHE A 122   N  ILE A  47           
SHEET    6   A16 GLY A 147  PRO A 153  1  O  CYS A 151   N  SER A 127           
SHEET    7   A16 THR A 191  THR A 196  1  O  PHE A 192   N  LEU A 150           
SHEET    8   A16 PHE A 221  PHE A 226  1  O  GLU A 222   N  ILE A 193           
SHEET    9   A16 PHE B 221  PHE B 226 -1  O  ALA B 223   N  PHE A 225           
SHEET   10   A16 THR B 191  THR B 196  1  N  ILE B 193   O  GLU B 222           
SHEET   11   A16 VAL B 148  PRO B 153  1  N  LEU B 150   O  PHE B 192           
SHEET   12   A16 PHE B 122  SER B 127  1  N  SER B 127   O  CYS B 151           
SHEET   13   A16 ALA B  45  CYS B  49  1  N  ILE B  47   O  PHE B 122           
SHEET   14   A16 GLN B  75  ASN B  80  1  O  GLN B  75   N  ILE B  46           
SHEET   15   A16 TRP B  26  TYR B  30 -1  N  TYR B  30   O  VAL B  76           
SHEET   16   A16 LYS B  16  THR B  18 -1  N  SER B  17   O  PHE B  29           
SHEET    1   B16 LYS C  16  THR C  18  0                                        
SHEET    2   B16 TRP C  26  TYR C  30 -1  O  PHE C  29   N  SER C  17           
SHEET    3   B16 GLN C  75  ASN C  80 -1  O  VAL C  76   N  TYR C  30           
SHEET    4   B16 ALA C  45  CYS C  49  1  N  ILE C  46   O  GLN C  75           
SHEET    5   B16 PHE C 122  SER C 127  1  O  PHE C 122   N  ILE C  47           
SHEET    6   B16 GLY C 147  PRO C 153  1  O  CYS C 151   N  SER C 127           
SHEET    7   B16 THR C 191  THR C 196  1  O  PHE C 192   N  LEU C 150           
SHEET    8   B16 PHE C 221  PHE C 226  1  O  GLU C 222   N  ILE C 193           
SHEET    9   B16 PHE D 221  PHE D 226 -1  O  ALA D 223   N  PHE C 225           
SHEET   10   B16 THR D 191  THR D 196  1  N  ILE D 193   O  GLU D 222           
SHEET   11   B16 VAL D 148  CYS D 151  1  N  LEU D 150   O  PHE D 192           
SHEET   12   B16 PHE D 122  CYS D 126  1  N  GLY D 125   O  CYS D 151           
SHEET   13   B16 ALA D  45  CYS D  49  1  N  ILE D  47   O  PHE D 122           
SHEET   14   B16 GLN D  75  ASN D  80  1  O  LEU D  77   N  ILE D  48           
SHEET   15   B16 TRP D  26  TYR D  30 -1  N  TYR D  30   O  VAL D  76           
SHEET   16   B16 LYS D  16  THR D  18 -1  N  SER D  17   O  PHE D  29           
LINK         C   VAL A  83                 N   MSE A  84     1555   1555  1.33  
LINK         C   MSE A  84                 N   ASN A  85     1555   1555  1.33  
LINK         C   VAL B  83                 N   MSE B  84     1555   1555  1.34  
LINK         C   MSE B  84                 N   ASN B  85     1555   1555  1.33  
LINK         C   VAL C  83                 N   MSE C  84     1555   1555  1.34  
LINK         C   MSE C  84                 N   ASN C  85     1555   1555  1.33  
LINK         C   VAL D  83                 N   MSE D  84     1555   1555  1.34  
LINK         C   MSE D  84                 N   ASN D  85     1555   1555  1.33  
CISPEP   1 TRP A  161    PRO A  162          0         0.21                     
CISPEP   2 TRP B  161    PRO B  162          0        -0.63                     
CISPEP   3 TRP C  161    PRO C  162          0         1.24                     
CISPEP   4 TRP D  161    PRO D  162          0         0.16                     
CRYST1   68.391  150.425  218.859  90.00  90.00  90.00 C 2 2 21     32          
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      0.014622  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006648  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004569        0.00000                         
TER    2021      GLU A 270                                                      
TER    4042      GLU B 270                                                      
TER    6063      GLU C 270                                                      
TER    8084      GLU D 270                                                      
MASTER      507    0    4   29   32    0    0    6 8141    4   40   88          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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