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LongText Report for: 4FBL-pdb

Name Class
4FBL-pdb
HEADER    HYDROLASE                               23-MAY-12   4FBL              
TITLE     LIPS AND LIPT, TWO METAGENOME-DERIVED LIPOLYTIC ENZYMES INCREASE THE  
TITLE    2 DIVERSITY OF KNOWN LIPASE AND ESTERASE FAMILIES                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPS LIPOLYTIC ENZYME;                                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UNIDENTIFIED;                                   
SOURCE   3 ORGANISM_TAXID: 32644;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PETM11                                    
KEYWDS    THERMOSTABLE, STRUCTURAL GENOMICS, ENZYME FUNCTION INITIATIVE,        
KEYWDS   2 STRUCTURAL PROTEOMICS IN EUROPE, SPINE, ALPHA/BETA HYDROLASE,        
KEYWDS   3 LIPASE, HYDROLASE                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.CHOW,U.KRAUSS,Y.DALL ANTONIA,F.FERSINI,C.SCHMEISSER,M.SCHMIDT,      
AUTHOR   2 I.MENYES,U.BORNSCHEUER,B.LAUINGER,P.BONGEN,J.PIETRUSZKA,M.ECKSTEIN,  
AUTHOR   3 O.THUM,A.LIESE,J.MUELLER-DIECKMANN,K.-E.JAEGER,F.KOVACIC,W.R.STREIT, 
AUTHOR   4 STRUCTURAL PROTEOMICS IN EUROPE (SPINE)                              
REVDAT   1   10-OCT-12 4FBL    0                                                
JRNL        AUTH   J.CHOW,F.KOVACIC,Y.DALL ANTONIA,U.KRAUSS,F.FERSINI,          
JRNL        AUTH 2 C.SCHMEISSER,B.LAUINGER,P.BONGEN,J.PIETRUSZKA,M.SCHMIDT,     
JRNL        AUTH 3 I.MENYES,U.T.BORNSCHEUER,M.ECKSTEIN,O.THUM,A.LIESE,          
JRNL        AUTH 4 J.MUELLER-DIECKMANN,K.-E.JAEGER,W.R.STREIT                   
JRNL        TITL   THE METAGENOME-DERIVED ENZYMES LIPS AND LIPT INCREASE THE    
JRNL        TITL 2 DIVERSITY OF KNOWN LIPASES                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.99 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 85910                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4534                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.99                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.04                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6324                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.95                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 334                          
REMARK   3   BIN FREE R VALUE                    : 0.3190                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7418                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 608                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.74                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.90000                                              
REMARK   3    B22 (A**2) : 0.90000                                              
REMARK   3    B33 (A**2) : -1.80000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.138         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.135         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.100         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.687         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7659 ; 0.029 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10438 ; 2.193 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   985 ; 6.533 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   294 ;32.334 ;23.537       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1205 ;16.412 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    47 ;20.096 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1189 ; 0.163 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5807 ; 0.013 ; 0.022       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4921 ; 1.306 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7915 ; 2.160 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2738 ; 3.641 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2523 ; 5.658 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4FBL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072697.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : HORIZONTALLY DIFFRACTING           
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : MONOCHROMATOR (HORIZONTALLY SIDE   
REMARK 200                                   DIFFRACTING SILICON 111 CRYSTAL)   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 85910                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.990                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1TQH                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NAACETATE, 3 M NACL,0.01 M         
REMARK 280  SPERMIDINE, PH 4.5, VAPOR DIFFUSION, TEMPERATURE 292K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,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        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH D 500  LIES ON A SPECIAL POSITION.                          
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     GLY A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     CYS A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     CYS A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     ASN A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     ARG A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     ASP A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     GLN A    18                                                      
REMARK 465     GLN A    19                                                      
REMARK 465     ARG A    20                                                      
REMARK 465     PRO A    21                                                      
REMARK 465     ARG A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     GLY A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     GLY A    28                                                      
REMARK 465     MET A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     THR A    31                                                      
REMARK 465     THR A    32                                                      
REMARK 465     PRO A    33                                                      
REMARK 465     LEU A    34                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     CYS B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     CYS B     8                                                      
REMARK 465     ARG B     9                                                      
REMARK 465     ASN B    10                                                      
REMARK 465     PRO B    11                                                      
REMARK 465     PRO B    12                                                      
REMARK 465     ARG B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     ASP B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     GLN B    18                                                      
REMARK 465     GLN B    19                                                      
REMARK 465     ARG B    20                                                      
REMARK 465     PRO B    21                                                      
REMARK 465     ARG B    22                                                      
REMARK 465     GLU B    23                                                      
REMARK 465     ARG B    24                                                      
REMARK 465     SER B    25                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     GLY B    28                                                      
REMARK 465     MET B    29                                                      
REMARK 465     SER B    30                                                      
REMARK 465     THR B    31                                                      
REMARK 465     THR B    32                                                      
REMARK 465     PRO B    33                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     ALA C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     CYS C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     LYS C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     ASN C     7                                                      
REMARK 465     CYS C     8                                                      
REMARK 465     ARG C     9                                                      
REMARK 465     ASN C    10                                                      
REMARK 465     PRO C    11                                                      
REMARK 465     PRO C    12                                                      
REMARK 465     ARG C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     GLY C    15                                                      
REMARK 465     ASP C    16                                                      
REMARK 465     ALA C    17                                                      
REMARK 465     GLN C    18                                                      
REMARK 465     GLN C    19                                                      
REMARK 465     ARG C    20                                                      
REMARK 465     PRO C    21                                                      
REMARK 465     ARG C    22                                                      
REMARK 465     GLU C    23                                                      
REMARK 465     ARG C    24                                                      
REMARK 465     SER C    25                                                      
REMARK 465     GLY C    26                                                      
REMARK 465     SER C    27                                                      
REMARK 465     GLY C    28                                                      
REMARK 465     MET C    29                                                      
REMARK 465     SER C    30                                                      
REMARK 465     THR C    31                                                      
REMARK 465     THR C    32                                                      
REMARK 465     PRO C    33                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     ALA D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     CYS D     2                                                      
REMARK 465     ARG D     3                                                      
REMARK 465     LYS D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     ARG D     6                                                      
REMARK 465     ASN D     7                                                      
REMARK 465     CYS D     8                                                      
REMARK 465     ARG D     9                                                      
REMARK 465     ASN D    10                                                      
REMARK 465     PRO D    11                                                      
REMARK 465     PRO D    12                                                      
REMARK 465     ARG D    13                                                      
REMARK 465     SER D    14                                                      
REMARK 465     GLY D    15                                                      
REMARK 465     ASP D    16                                                      
REMARK 465     ALA D    17                                                      
REMARK 465     GLN D    18                                                      
REMARK 465     GLN D    19                                                      
REMARK 465     ARG D    20                                                      
REMARK 465     PRO D    21                                                      
REMARK 465     ARG D    22                                                      
REMARK 465     GLU D    23                                                      
REMARK 465     ARG D    24                                                      
REMARK 465     SER D    25                                                      
REMARK 465     GLY D    26                                                      
REMARK 465     SER D    27                                                      
REMARK 465     GLY D    28                                                      
REMARK 465     MET D    29                                                      
REMARK 465     SER D    30                                                      
REMARK 465     THR D    31                                                      
REMARK 465     THR D    32                                                      
REMARK 465     PRO D    33                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG B  49    CG   CD   NE   CZ   NH1  NH2                        
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   NE2  HIS A   257     N10  SPD A   301              2.08            
REMARK 500   OG   SER D   126     NE2  HIS D   257              2.11            
REMARK 500   OG   SER C   126     NE2  HIS C   257              2.13            
REMARK 500   OG   SER B   126     NE2  HIS B   257              2.15            
REMARK 500   OG   SER B   126     N10  SPD B   301              2.18            
REMARK 500   NE2  HIS B   257     N10  SPD B   301              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS C 117   CB    CYS C 117   SG     -0.131                       
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    LYS A 265   CD  -  CE  -  NZ  ANGL. DEV. = -22.0 DEGREES          
REMARK 500    ARG B 271   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG B 271   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    MET C  65   CG  -  SD  -  CE  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    ARG C  74   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG C  83   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    LEU C 173   CA  -  CB  -  CG  ANGL. DEV. =  16.8 DEGREES          
REMARK 500    ARG C 214   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG C 214   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG C 277   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG C 277   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 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    THR A  59       -5.33     74.12                                   
REMARK 500    THR A  89      -96.70   -136.04                                   
REMARK 500    SER A 126     -116.35     68.86                                   
REMARK 500    TYR A 256     -140.43    -99.75                                   
REMARK 500    THR B  59       -6.19     71.40                                   
REMARK 500    THR B  89      -92.10   -135.37                                   
REMARK 500    SER B 126     -114.39     67.71                                   
REMARK 500    ASP B 168       71.29   -117.30                                   
REMARK 500    PRO B 174      134.11    -30.88                                   
REMARK 500    SER B 178       41.49     72.07                                   
REMARK 500    VAL B 229      -51.92   -124.02                                   
REMARK 500    TYR B 256     -137.40   -103.39                                   
REMARK 500    THR C  89      -90.97   -123.83                                   
REMARK 500    SER C 126     -115.09     61.04                                   
REMARK 500    PRO C 174      142.16    -38.45                                   
REMARK 500    TYR C 256     -138.74    -96.99                                   
REMARK 500    THR D  59       -8.98     73.74                                   
REMARK 500    ALA D  75        5.02    -68.17                                   
REMARK 500    THR D  81       74.85   -119.76                                   
REMARK 500    THR D  89      -94.32   -131.58                                   
REMARK 500    SER D 126     -118.12     64.20                                   
REMARK 500    ALA D 152       72.73   -101.46                                   
REMARK 500    TYR D 256     -142.92    -96.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLU A  41        24.7      L          L   OUTSIDE RANGE           
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 553        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH C 511        DISTANCE =  6.90 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SPD A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SPD B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SPD C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 301                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FBM   RELATED DB: PDB                                   
DBREF  4FBL A   -1   279  PDB    4FBL     4FBL            -1    279             
DBREF  4FBL B   -1   279  PDB    4FBL     4FBL            -1    279             
DBREF  4FBL C   -1   279  PDB    4FBL     4FBL            -1    279             
DBREF  4FBL D   -1   279  PDB    4FBL     4FBL            -1    279             
SEQRES   1 A  281  GLY ALA MET CYS ARG LYS SER ARG ASN CYS ARG ASN PRO          
SEQRES   2 A  281  PRO ARG SER GLY ASP ALA GLN GLN ARG PRO ARG GLU ARG          
SEQRES   3 A  281  SER GLY SER GLY MET SER THR THR PRO LEU GLN VAL LEU          
SEQRES   4 A  281  PRO GLY ALA GLU PRO LEU TYR SER VAL GLY SER ARG ILE          
SEQRES   5 A  281  GLY VAL LEU VAL SER HIS GLY PHE THR GLY SER PRO GLN          
SEQRES   6 A  281  SER MET ARG PHE LEU ALA GLU GLY PHE ALA ARG ALA GLY          
SEQRES   7 A  281  TYR THR VAL ALA THR PRO ARG LEU THR GLY HIS GLY THR          
SEQRES   8 A  281  THR PRO ALA GLU MET ALA ALA SER THR ALA SER ASP TRP          
SEQRES   9 A  281  THR ALA ASP ILE VAL ALA ALA MET ARG TRP LEU GLU GLU          
SEQRES  10 A  281  ARG CYS ASP VAL LEU PHE MET THR GLY LEU SER MET GLY          
SEQRES  11 A  281  GLY ALA LEU THR VAL TRP ALA ALA GLY GLN PHE PRO GLU          
SEQRES  12 A  281  ARG PHE ALA GLY ILE MET PRO ILE ASN ALA ALA LEU ARG          
SEQRES  13 A  281  MET GLU SER PRO ASP LEU ALA ALA LEU ALA PHE ASN PRO          
SEQRES  14 A  281  ASP ALA PRO ALA GLU LEU PRO GLY ILE GLY SER ASP ILE          
SEQRES  15 A  281  LYS ALA GLU GLY VAL LYS GLU LEU ALA TYR PRO VAL THR          
SEQRES  16 A  281  PRO VAL PRO ALA ILE LYS HIS LEU ILE THR ILE GLY ALA          
SEQRES  17 A  281  VAL ALA GLU MET LEU LEU PRO ARG VAL LYS CYS PRO ALA          
SEQRES  18 A  281  LEU ILE ILE GLN SER ARG GLU ASP HIS VAL VAL PRO PRO          
SEQRES  19 A  281  HIS ASN GLY GLU LEU ILE TYR ASN GLY ILE GLY SER THR          
SEQRES  20 A  281  GLU LYS GLU LEU LEU TRP LEU GLU ASN SER TYR HIS VAL          
SEQRES  21 A  281  ALA THR LEU ASP ASN ASP LYS GLU LEU ILE LEU GLU ARG          
SEQRES  22 A  281  SER LEU ALA PHE ILE ARG LYS HIS                              
SEQRES   1 B  281  GLY ALA MET CYS ARG LYS SER ARG ASN CYS ARG ASN PRO          
SEQRES   2 B  281  PRO ARG SER GLY ASP ALA GLN GLN ARG PRO ARG GLU ARG          
SEQRES   3 B  281  SER GLY SER GLY MET SER THR THR PRO LEU GLN VAL LEU          
SEQRES   4 B  281  PRO GLY ALA GLU PRO LEU TYR SER VAL GLY SER ARG ILE          
SEQRES   5 B  281  GLY VAL LEU VAL SER HIS GLY PHE THR GLY SER PRO GLN          
SEQRES   6 B  281  SER MET ARG PHE LEU ALA GLU GLY PHE ALA ARG ALA GLY          
SEQRES   7 B  281  TYR THR VAL ALA THR PRO ARG LEU THR GLY HIS GLY THR          
SEQRES   8 B  281  THR PRO ALA GLU MET ALA ALA SER THR ALA SER ASP TRP          
SEQRES   9 B  281  THR ALA ASP ILE VAL ALA ALA MET ARG TRP LEU GLU GLU          
SEQRES  10 B  281  ARG CYS ASP VAL LEU PHE MET THR GLY LEU SER MET GLY          
SEQRES  11 B  281  GLY ALA LEU THR VAL TRP ALA ALA GLY GLN PHE PRO GLU          
SEQRES  12 B  281  ARG PHE ALA GLY ILE MET PRO ILE ASN ALA ALA LEU ARG          
SEQRES  13 B  281  MET GLU SER PRO ASP LEU ALA ALA LEU ALA PHE ASN PRO          
SEQRES  14 B  281  ASP ALA PRO ALA GLU LEU PRO GLY ILE GLY SER ASP ILE          
SEQRES  15 B  281  LYS ALA GLU GLY VAL LYS GLU LEU ALA TYR PRO VAL THR          
SEQRES  16 B  281  PRO VAL PRO ALA ILE LYS HIS LEU ILE THR ILE GLY ALA          
SEQRES  17 B  281  VAL ALA GLU MET LEU LEU PRO ARG VAL LYS CYS PRO ALA          
SEQRES  18 B  281  LEU ILE ILE GLN SER ARG GLU ASP HIS VAL VAL PRO PRO          
SEQRES  19 B  281  HIS ASN GLY GLU LEU ILE TYR ASN GLY ILE GLY SER THR          
SEQRES  20 B  281  GLU LYS GLU LEU LEU TRP LEU GLU ASN SER TYR HIS VAL          
SEQRES  21 B  281  ALA THR LEU ASP ASN ASP LYS GLU LEU ILE LEU GLU ARG          
SEQRES  22 B  281  SER LEU ALA PHE ILE ARG LYS HIS                              
SEQRES   1 C  281  GLY ALA MET CYS ARG LYS SER ARG ASN CYS ARG ASN PRO          
SEQRES   2 C  281  PRO ARG SER GLY ASP ALA GLN GLN ARG PRO ARG GLU ARG          
SEQRES   3 C  281  SER GLY SER GLY MET SER THR THR PRO LEU GLN VAL LEU          
SEQRES   4 C  281  PRO GLY ALA GLU PRO LEU TYR SER VAL GLY SER ARG ILE          
SEQRES   5 C  281  GLY VAL LEU VAL SER HIS GLY PHE THR GLY SER PRO GLN          
SEQRES   6 C  281  SER MET ARG PHE LEU ALA GLU GLY PHE ALA ARG ALA GLY          
SEQRES   7 C  281  TYR THR VAL ALA THR PRO ARG LEU THR GLY HIS GLY THR          
SEQRES   8 C  281  THR PRO ALA GLU MET ALA ALA SER THR ALA SER ASP TRP          
SEQRES   9 C  281  THR ALA ASP ILE VAL ALA ALA MET ARG TRP LEU GLU GLU          
SEQRES  10 C  281  ARG CYS ASP VAL LEU PHE MET THR GLY LEU SER MET GLY          
SEQRES  11 C  281  GLY ALA LEU THR VAL TRP ALA ALA GLY GLN PHE PRO GLU          
SEQRES  12 C  281  ARG PHE ALA GLY ILE MET PRO ILE ASN ALA ALA LEU ARG          
SEQRES  13 C  281  MET GLU SER PRO ASP LEU ALA ALA LEU ALA PHE ASN PRO          
SEQRES  14 C  281  ASP ALA PRO ALA GLU LEU PRO GLY ILE GLY SER ASP ILE          
SEQRES  15 C  281  LYS ALA GLU GLY VAL LYS GLU LEU ALA TYR PRO VAL THR          
SEQRES  16 C  281  PRO VAL PRO ALA ILE LYS HIS LEU ILE THR ILE GLY ALA          
SEQRES  17 C  281  VAL ALA GLU MET LEU LEU PRO ARG VAL LYS CYS PRO ALA          
SEQRES  18 C  281  LEU ILE ILE GLN SER ARG GLU ASP HIS VAL VAL PRO PRO          
SEQRES  19 C  281  HIS ASN GLY GLU LEU ILE TYR ASN GLY ILE GLY SER THR          
SEQRES  20 C  281  GLU LYS GLU LEU LEU TRP LEU GLU ASN SER TYR HIS VAL          
SEQRES  21 C  281  ALA THR LEU ASP ASN ASP LYS GLU LEU ILE LEU GLU ARG          
SEQRES  22 C  281  SER LEU ALA PHE ILE ARG LYS HIS                              
SEQRES   1 D  281  GLY ALA MET CYS ARG LYS SER ARG ASN CYS ARG ASN PRO          
SEQRES   2 D  281  PRO ARG SER GLY ASP ALA GLN GLN ARG PRO ARG GLU ARG          
SEQRES   3 D  281  SER GLY SER GLY MET SER THR THR PRO LEU GLN VAL LEU          
SEQRES   4 D  281  PRO GLY ALA GLU PRO LEU TYR SER VAL GLY SER ARG ILE          
SEQRES   5 D  281  GLY VAL LEU VAL SER HIS GLY PHE THR GLY SER PRO GLN          
SEQRES   6 D  281  SER MET ARG PHE LEU ALA GLU GLY PHE ALA ARG ALA GLY          
SEQRES   7 D  281  TYR THR VAL ALA THR PRO ARG LEU THR GLY HIS GLY THR          
SEQRES   8 D  281  THR PRO ALA GLU MET ALA ALA SER THR ALA SER ASP TRP          
SEQRES   9 D  281  THR ALA ASP ILE VAL ALA ALA MET ARG TRP LEU GLU GLU          
SEQRES  10 D  281  ARG CYS ASP VAL LEU PHE MET THR GLY LEU SER MET GLY          
SEQRES  11 D  281  GLY ALA LEU THR VAL TRP ALA ALA GLY GLN PHE PRO GLU          
SEQRES  12 D  281  ARG PHE ALA GLY ILE MET PRO ILE ASN ALA ALA LEU ARG          
SEQRES  13 D  281  MET GLU SER PRO ASP LEU ALA ALA LEU ALA PHE ASN PRO          
SEQRES  14 D  281  ASP ALA PRO ALA GLU LEU PRO GLY ILE GLY SER ASP ILE          
SEQRES  15 D  281  LYS ALA GLU GLY VAL LYS GLU LEU ALA TYR PRO VAL THR          
SEQRES  16 D  281  PRO VAL PRO ALA ILE LYS HIS LEU ILE THR ILE GLY ALA          
SEQRES  17 D  281  VAL ALA GLU MET LEU LEU PRO ARG VAL LYS CYS PRO ALA          
SEQRES  18 D  281  LEU ILE ILE GLN SER ARG GLU ASP HIS VAL VAL PRO PRO          
SEQRES  19 D  281  HIS ASN GLY GLU LEU ILE TYR ASN GLY ILE GLY SER THR          
SEQRES  20 D  281  GLU LYS GLU LEU LEU TRP LEU GLU ASN SER TYR HIS VAL          
SEQRES  21 D  281  ALA THR LEU ASP ASN ASP LYS GLU LEU ILE LEU GLU ARG          
SEQRES  22 D  281  SER LEU ALA PHE ILE ARG LYS HIS                              
HET    SPD  A 301      10                                                       
HET     CL  A 302       1                                                       
HET    SPD  B 301      10                                                       
HET     CL  B 302       1                                                       
HET    SPD  C 301      10                                                       
HET     CL  C 302       1                                                       
HET     CL  D 301       1                                                       
HETNAM     SPD SPERMIDINE                                                       
HETNAM      CL CHLORIDE ION                                                     
HETSYN     SPD N-(2-AMINO-PROPYL)-1,4-DIAMINOBUTANE; PA(34)                     
FORMUL   5  SPD    3(C7 H19 N3)                                                 
FORMUL   6   CL    4(CL 1-)                                                     
FORMUL  12  HOH   *608(H2 O)                                                    
HELIX    1   1 SER A   61  SER A   64  5                                   4    
HELIX    2   2 MET A   65  ALA A   75  1                                  11    
HELIX    3   3 THR A   90  ALA A   96  1                                   7    
HELIX    4   4 THR A   98  CYS A  117  1                                  20    
HELIX    5   5 SER A  126  PHE A  139  1                                  14    
HELIX    6   6 SER A  157  ALA A  162  1                                   6    
HELIX    7   7 ALA A  197  LEU A  212  1                                  16    
HELIX    8   8 PRO A  213  VAL A  215  5                                   3    
HELIX    9   9 PRO A  232  ILE A  242  1                                  11    
HELIX   10  10 VAL A  258  ASP A  262  5                                   5    
HELIX   11  11 ASP A  264  LYS A  278  1                                  15    
HELIX   12  12 SER B   61  SER B   64  5                                   4    
HELIX   13  13 MET B   65  ALA B   75  1                                  11    
HELIX   14  14 THR B   90  ALA B   96  1                                   7    
HELIX   15  15 THR B   98  CYS B  117  1                                  20    
HELIX   16  16 SER B  126  PHE B  139  1                                  14    
HELIX   17  17 SER B  157  ALA B  162  1                                   6    
HELIX   18  18 ALA B  197  LEU B  212  1                                  16    
HELIX   19  19 PRO B  213  VAL B  215  5                                   3    
HELIX   20  20 PRO B  232  ILE B  242  1                                  11    
HELIX   21  21 VAL B  258  ASP B  262  5                                   5    
HELIX   22  22 ASP B  264  HIS B  279  1                                  16    
HELIX   23  23 SER C   61  SER C   64  5                                   4    
HELIX   24  24 MET C   65  ALA C   75  1                                  11    
HELIX   25  25 THR C   90  ALA C   96  1                                   7    
HELIX   26  26 THR C   98  CYS C  117  1                                  20    
HELIX   27  27 SER C  126  PHE C  139  1                                  14    
HELIX   28  28 SER C  157  ALA C  162  1                                   6    
HELIX   29  29 ALA C  197  LEU C  212  1                                  16    
HELIX   30  30 PRO C  213  VAL C  215  5                                   3    
HELIX   31  31 PRO C  232  ILE C  242  1                                  11    
HELIX   32  32 VAL C  258  ASP C  262  5                                   5    
HELIX   33  33 ASP C  264  LYS C  278  1                                  15    
HELIX   34  34 SER D   61  SER D   64  5                                   4    
HELIX   35  35 MET D   65  ALA D   75  1                                  11    
HELIX   36  36 THR D   90  ALA D   96  1                                   7    
HELIX   37  37 THR D   98  GLU D  115  1                                  18    
HELIX   38  38 SER D  126  PHE D  139  1                                  14    
HELIX   39  39 SER D  157  ALA D  162  1                                   6    
HELIX   40  40 ALA D  197  LEU D  212  1                                  16    
HELIX   41  41 PRO D  213  VAL D  215  5                                   3    
HELIX   42  42 PRO D  232  ILE D  242  1                                  11    
HELIX   43  43 VAL D  258  ASP D  262  5                                   5    
HELIX   44  44 ASP D  264  LYS D  278  1                                  15    
SHEET    1   A 5 LEU A  43  SER A  45  0                                        
SHEET    2   A 5 THR A  78  THR A  81 -1  O  VAL A  79   N  SER A  45           
SHEET    3   A 5 ILE A  50  SER A  55  1  N  VAL A  54   O  ALA A  80           
SHEET    4   A 5 VAL A 119  LEU A 125  1  O  VAL A 119   N  GLY A  51           
SHEET    5   A 5 GLY A 145  ILE A 149  1  O  ILE A 149   N  GLY A 124           
SHEET    1   B 2 GLU A 172  PRO A 174  0                                        
SHEET    2   B 2 VAL A 192  PRO A 194 -1  O  THR A 193   N  LEU A 173           
SHEET    1   C 2 ALA A 219  SER A 224  0                                        
SHEET    2   C 2 LYS A 247  LEU A 252  1  O  GLU A 248   N  ILE A 221           
SHEET    1   D 5 LEU B  43  SER B  45  0                                        
SHEET    2   D 5 THR B  78  THR B  81 -1  O  THR B  81   N  LEU B  43           
SHEET    3   D 5 ILE B  50  SER B  55  1  N  VAL B  54   O  ALA B  80           
SHEET    4   D 5 VAL B 119  LEU B 125  1  O  VAL B 119   N  GLY B  51           
SHEET    5   D 5 GLY B 145  ILE B 149  1  O  ILE B 149   N  GLY B 124           
SHEET    1   E 2 GLU B 172  PRO B 174  0                                        
SHEET    2   E 2 VAL B 192  PRO B 194 -1  O  THR B 193   N  LEU B 173           
SHEET    1   F 2 ALA B 219  SER B 224  0                                        
SHEET    2   F 2 LYS B 247  LEU B 252  1  O  GLU B 248   N  ILE B 221           
SHEET    1   G 5 LEU C  43  SER C  45  0                                        
SHEET    2   G 5 THR C  78  THR C  81 -1  O  THR C  81   N  LEU C  43           
SHEET    3   G 5 ILE C  50  SER C  55  1  N  VAL C  54   O  ALA C  80           
SHEET    4   G 5 VAL C 119  LEU C 125  1  O  VAL C 119   N  GLY C  51           
SHEET    5   G 5 GLY C 145  ILE C 149  1  O  ILE C 149   N  GLY C 124           
SHEET    1   H 2 GLU C 172  PRO C 174  0                                        
SHEET    2   H 2 VAL C 192  PRO C 194 -1  O  THR C 193   N  LEU C 173           
SHEET    1   I 2 ALA C 219  SER C 224  0                                        
SHEET    2   I 2 LYS C 247  LEU C 252  1  O  LEU C 252   N  GLN C 223           
SHEET    1   J 5 LEU D  43  SER D  45  0                                        
SHEET    2   J 5 THR D  78  THR D  81 -1  O  VAL D  79   N  SER D  45           
SHEET    3   J 5 ILE D  50  SER D  55  1  N  VAL D  54   O  ALA D  80           
SHEET    4   J 5 VAL D 119  LEU D 125  1  O  VAL D 119   N  GLY D  51           
SHEET    5   J 5 GLY D 145  ILE D 149  1  O  ILE D 149   N  GLY D 124           
SHEET    1   K 2 GLU D 172  PRO D 174  0                                        
SHEET    2   K 2 VAL D 192  PRO D 194 -1  O  THR D 193   N  LEU D 173           
SHEET    1   L 2 ALA D 219  SER D 224  0                                        
SHEET    2   L 2 LYS D 247  LEU D 252  1  O  LEU D 250   N  ILE D 221           
SITE     1 AC1 12 GLY A  57  PHE A  58  THR A  59  SER A 126                    
SITE     2 AC1 12 ILE A 176  GLY A 177  GLU A 187  ALA A 189                    
SITE     3 AC1 12 TYR A 190  HIS A 257   CL A 302  HOH A 423                    
SITE     1 AC2  5 PHE A  58  SER A 126  MET A 127  SPD A 301                    
SITE     2 AC2  5 HOH A 495                                                     
SITE     1 AC3 15 GLY B  57  PHE B  58  THR B  59  GLY B  60                    
SITE     2 AC3 15 SER B 126  ILE B 176  GLY B 177  SER B 178                    
SITE     3 AC3 15 ASP B 179  GLU B 187  VAL B 229  HIS B 257                    
SITE     4 AC3 15 VAL B 258   CL B 302  HOH B 419                               
SITE     1 AC4  5 PHE B  58  SER B 126  MET B 127  SPD B 301                    
SITE     2 AC4  5 HOH B 488                                                     
SITE     1 AC5 13 PHE C  58  GLY C  60  SER C 126  ILE C 176                    
SITE     2 AC5 13 GLY C 177  SER C 178  ASP C 179  GLU C 187                    
SITE     3 AC5 13 VAL C 229  HIS C 257  VAL C 258   CL C 302                    
SITE     4 AC5 13 HOH C 441                                                     
SITE     1 AC6  5 PHE C  58  SER C 126  MET C 127  SPD C 301                    
SITE     2 AC6  5 HOH C 568                                                     
SITE     1 AC7  4 PHE D  58  SER D 126  MET D 127  HOH D 464                    
CRYST1  105.270  105.270  120.980  90.00  90.00  90.00 P 4          16          
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      0.009499  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009499  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008266        0.00000                         
TER    1851      HIS A 279                                                      
TER    3713      HIS B 279                                                      
TER    5581      HIS C 279                                                      
TER    7449      HIS D 279                                                      
MASTER      576    0    7   44   36    0   18    6 8060    4   30   88          
END                                                                             

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