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Database: PDB
Entry: 3HBX
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Original site: 3HBX 
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HEADER    OXIDOREDUCTASE                          18-MAY-00   1F14              
TITLE     L-3-HYDROXYACYL-COA DEHYDROGENASE (APO)                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: L-3-HYDROXYACYL-COA DEHYDROGENASE;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: SCHAD;                                                      
COMPND   5 EC: 1.1.1.35;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: HEART;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28;                                    
SOURCE   9 OTHER_DETAILS: PROTEIN WAS EXPRESSED WITH A C-TERMINAL               
SOURCE  10 HEXAMERIC HISTIDINE TAG.                                             
KEYWDS    L-3-HYDROXYACYL-COA (APOENZYME), OXIDOREDUCTASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.J.BARYCKI,L.K.O'BRIEN,A.W.STRAUSS,L.J.BANASZAK                      
REVDAT   3   24-FEB-09 1F14    1       VERSN                                    
REVDAT   2   01-APR-03 1F14    1       JRNL                                     
REVDAT   1   27-SEP-00 1F14    0                                                
JRNL        AUTH   J.J.BARYCKI,L.K.O'BRIEN,A.W.STRAUSS,L.J.BANASZAK             
JRNL        TITL   SEQUESTRATION OF THE ACTIVE SITE BY INTERDOMAIN              
JRNL        TITL 2 SHIFTING. CRYSTALLOGRAPHIC AND SPECTROSCOPIC                 
JRNL        TITL 3 EVIDENCE FOR DISTINCT CONFORMATIONS OF                       
JRNL        TITL 4 L-3-HYDROXYACYL-COA DEHYDROGENASE.                           
JRNL        REF    J.BIOL.CHEM.                  V. 275 27186 2000              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   10840044                                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.J.BARYCKI,L.K.O'BRIEN,J.M.BRATT,R.ZHANG,                   
REMARK   1  AUTH 2 R.SANISHVILI,A.W.STRAUSS,L.J.BANASZAK                        
REMARK   1  TITL   BIOCHEMICAL CHARACTERIZATION AND CRYSTAL STRUCTURE           
REMARK   1  TITL 2 DETERMINATION OF HUMAN HEART SHORT CHAIN                     
REMARK   1  TITL 3 L-3-HYDROXYACYL-COA DEHYDROGENASE PROVIDE INSIGHTS           
REMARK   1  TITL 4 INTO CATALYTIC MECHANISM                                     
REMARK   1  REF    BIOCHEMISTRY                  V.  38  5786 1999              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  DOI    10.1021/BI9829027                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.3                                              
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1346566.550                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 32510                          
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) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1610                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4999                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2880                       
REMARK   3   BIN FREE R VALUE                    : 0.3270                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 280                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4462                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 287                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 47.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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) : 0.29                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.26                            
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) : 0.38                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.31                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.70                            
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) : 2.580 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.000 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.260 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.140 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1F14 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAY-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011115.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-FEB-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03321                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : APS-1                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33237                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 3.910                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.14600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: CNS 0.3                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM N-[2-ACETAMIDO]-2-                 
REMARK 280  IMINODIACETIC ACID WITHIN THE PRECIPITANT RANGE OF 14% TO 19%       
REMARK 280  POLYETHYLENE GLYCOL 4000 , PH 6.5, VAPOR DIFFUSION, HANGING         
REMARK 280  DROP, TEMPERATURE 291K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.22000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       84.14500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.48500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       84.14500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.22000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.48500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 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: 3220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     LYS A    11                                                      
REMARK 465     LEU A   303                                                      
REMARK 465     GLU A   304                                                      
REMARK 465     HIS A   305                                                      
REMARK 465     HIS A   306                                                      
REMARK 465     HIS A   307                                                      
REMARK 465     HIS A   308                                                      
REMARK 465     HIS A   309                                                      
REMARK 465     HIS A   310                                                      
REMARK 465     SER B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     LYS B    11                                                      
REMARK 465     LEU B   303                                                      
REMARK 465     GLU B   304                                                      
REMARK 465     HIS B   305                                                      
REMARK 465     HIS B   306                                                      
REMARK 465     HIS B   307                                                      
REMARK 465     HIS B   308                                                      
REMARK 465     HIS B   309                                                      
REMARK 465     HIS B   310                                                      
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     GLU A  82    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  82    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 302    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   916     O    HOH A  1008              2.15            
REMARK 500   O    HOH A   916     O    HOH A  1010              2.16            
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    LYS A  67       -1.91    -58.26                                   
REMARK 500    PHE A  70       42.99   -106.80                                   
REMARK 500    ASN A 146        4.48    -68.70                                   
REMARK 500    PRO A 175       -5.44    -58.65                                   
REMARK 500    PHE A 205     -125.74     52.51                                   
REMARK 500    ILE A 206      -67.85    -99.84                                   
REMARK 500    ASP A 269       81.48   -158.64                                   
REMARK 500    GLU A 296      133.28   -176.28                                   
REMARK 500    LYS B  16      -38.25   -131.32                                   
REMARK 500    PHE B 205     -125.00     48.52                                   
REMARK 500    ILE B 206      -63.46    -99.53                                   
REMARK 500    ASP B 269       78.90   -173.37                                   
REMARK 500    ALA B 270        0.54    -67.43                                   
REMARK 500    GLU B 287       31.14    -84.39                                   
REMARK 500    LYS B 293       23.92    -73.35                                   
REMARK 500    THR B 294      -10.02   -156.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3HAD   RELATED DB: PDB                                   
REMARK 900 L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH NAD+                
REMARK 900 RELATED ID: 1F12   RELATED DB: PDB                                   
REMARK 900 L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH 3-                  
REMARK 900 HYDROXYBUTYRYL-COA                                                   
REMARK 900 RELATED ID: 1F17   RELATED DB: PDB                                   
REMARK 900 L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH NADH                
REMARK 900 RELATED ID: 1F0Y   RELATED DB: PDB                                   
REMARK 900 L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH                     
REMARK 900 ACETOACETYL-COA AND NAD+                                             
DBREF  1F14 A    1   302  UNP    Q16836   HCDH_HUMAN       7    308             
DBREF  1F14 B    1   302  UNP    Q16836   HCDH_HUMAN       7    308             
SEQADV 1F14 CYS A   80  UNP  Q16836    PHE    86 ENGINEERED                     
SEQADV 1F14 LEU A  303  UNP  Q16836              EXPRESSION TAG                 
SEQADV 1F14 GLU A  304  UNP  Q16836              EXPRESSION TAG                 
SEQADV 1F14 HIS A  305  UNP  Q16836              EXPRESSION TAG                 
SEQADV 1F14 HIS A  306  UNP  Q16836              EXPRESSION TAG                 
SEQADV 1F14 HIS A  307  UNP  Q16836              EXPRESSION TAG                 
SEQADV 1F14 HIS A  308  UNP  Q16836              EXPRESSION TAG                 
SEQADV 1F14 HIS A  309  UNP  Q16836              EXPRESSION TAG                 
SEQADV 1F14 HIS A  310  UNP  Q16836              EXPRESSION TAG                 
SEQADV 1F14 CYS B   80  UNP  Q16836    PHE    86 ENGINEERED                     
SEQADV 1F14 LEU B  303  UNP  Q16836              EXPRESSION TAG                 
SEQADV 1F14 GLU B  304  UNP  Q16836              EXPRESSION TAG                 
SEQADV 1F14 HIS B  305  UNP  Q16836              EXPRESSION TAG                 
SEQADV 1F14 HIS B  306  UNP  Q16836              EXPRESSION TAG                 
SEQADV 1F14 HIS B  307  UNP  Q16836              EXPRESSION TAG                 
SEQADV 1F14 HIS B  308  UNP  Q16836              EXPRESSION TAG                 
SEQADV 1F14 HIS B  309  UNP  Q16836              EXPRESSION TAG                 
SEQADV 1F14 HIS B  310  UNP  Q16836              EXPRESSION TAG                 
SEQRES   1 A  310  SER SER SER SER THR ALA SER ALA SER ALA LYS LYS ILE          
SEQRES   2 A  310  ILE VAL LYS HIS VAL THR VAL ILE GLY GLY GLY LEU MET          
SEQRES   3 A  310  GLY ALA GLY ILE ALA GLN VAL ALA ALA ALA THR GLY HIS          
SEQRES   4 A  310  THR VAL VAL LEU VAL ASP GLN THR GLU ASP ILE LEU ALA          
SEQRES   5 A  310  LYS SER LYS LYS GLY ILE GLU GLU SER LEU ARG LYS VAL          
SEQRES   6 A  310  ALA LYS LYS LYS PHE ALA GLU ASN PRO LYS ALA GLY ASP          
SEQRES   7 A  310  GLU CYS VAL GLU LYS THR LEU SER THR ILE ALA THR SER          
SEQRES   8 A  310  THR ASP ALA ALA SER VAL VAL HIS SER THR ASP LEU VAL          
SEQRES   9 A  310  VAL GLU ALA ILE VAL GLU ASN LEU LYS VAL LYS ASN GLU          
SEQRES  10 A  310  LEU PHE LYS ARG LEU ASP LYS PHE ALA ALA GLU HIS THR          
SEQRES  11 A  310  ILE PHE ALA SER ASN THR SER SER LEU GLN ILE THR SER          
SEQRES  12 A  310  ILE ALA ASN ALA THR THR ARG GLN ASP ARG PHE ALA GLY          
SEQRES  13 A  310  LEU HIS PHE PHE ASN PRO VAL PRO VAL MET LYS LEU VAL          
SEQRES  14 A  310  GLU VAL ILE LYS THR PRO MET THR SER GLN LYS THR PHE          
SEQRES  15 A  310  GLU SER LEU VAL ASP PHE SER LYS ALA LEU GLY LYS HIS          
SEQRES  16 A  310  PRO VAL SER CYS LYS ASP THR PRO GLY PHE ILE VAL ASN          
SEQRES  17 A  310  ARG LEU LEU VAL PRO TYR LEU MET GLU ALA ILE ARG LEU          
SEQRES  18 A  310  TYR GLU ARG GLY ASP ALA SER LYS GLU ASP ILE ASP THR          
SEQRES  19 A  310  ALA MET LYS LEU GLY ALA GLY TYR PRO MET GLY PRO PHE          
SEQRES  20 A  310  GLU LEU LEU ASP TYR VAL GLY LEU ASP THR THR LYS PHE          
SEQRES  21 A  310  ILE VAL ASP GLY TRP HIS GLU MET ASP ALA GLU ASN PRO          
SEQRES  22 A  310  LEU HIS GLN PRO SER PRO SER LEU ASN LYS LEU VAL ALA          
SEQRES  23 A  310  GLU ASN LYS PHE GLY LYS LYS THR GLY GLU GLY PHE TYR          
SEQRES  24 A  310  LYS TYR LYS LEU GLU HIS HIS HIS HIS HIS HIS                  
SEQRES   1 B  310  SER SER SER SER THR ALA SER ALA SER ALA LYS LYS ILE          
SEQRES   2 B  310  ILE VAL LYS HIS VAL THR VAL ILE GLY GLY GLY LEU MET          
SEQRES   3 B  310  GLY ALA GLY ILE ALA GLN VAL ALA ALA ALA THR GLY HIS          
SEQRES   4 B  310  THR VAL VAL LEU VAL ASP GLN THR GLU ASP ILE LEU ALA          
SEQRES   5 B  310  LYS SER LYS LYS GLY ILE GLU GLU SER LEU ARG LYS VAL          
SEQRES   6 B  310  ALA LYS LYS LYS PHE ALA GLU ASN PRO LYS ALA GLY ASP          
SEQRES   7 B  310  GLU CYS VAL GLU LYS THR LEU SER THR ILE ALA THR SER          
SEQRES   8 B  310  THR ASP ALA ALA SER VAL VAL HIS SER THR ASP LEU VAL          
SEQRES   9 B  310  VAL GLU ALA ILE VAL GLU ASN LEU LYS VAL LYS ASN GLU          
SEQRES  10 B  310  LEU PHE LYS ARG LEU ASP LYS PHE ALA ALA GLU HIS THR          
SEQRES  11 B  310  ILE PHE ALA SER ASN THR SER SER LEU GLN ILE THR SER          
SEQRES  12 B  310  ILE ALA ASN ALA THR THR ARG GLN ASP ARG PHE ALA GLY          
SEQRES  13 B  310  LEU HIS PHE PHE ASN PRO VAL PRO VAL MET LYS LEU VAL          
SEQRES  14 B  310  GLU VAL ILE LYS THR PRO MET THR SER GLN LYS THR PHE          
SEQRES  15 B  310  GLU SER LEU VAL ASP PHE SER LYS ALA LEU GLY LYS HIS          
SEQRES  16 B  310  PRO VAL SER CYS LYS ASP THR PRO GLY PHE ILE VAL ASN          
SEQRES  17 B  310  ARG LEU LEU VAL PRO TYR LEU MET GLU ALA ILE ARG LEU          
SEQRES  18 B  310  TYR GLU ARG GLY ASP ALA SER LYS GLU ASP ILE ASP THR          
SEQRES  19 B  310  ALA MET LYS LEU GLY ALA GLY TYR PRO MET GLY PRO PHE          
SEQRES  20 B  310  GLU LEU LEU ASP TYR VAL GLY LEU ASP THR THR LYS PHE          
SEQRES  21 B  310  ILE VAL ASP GLY TRP HIS GLU MET ASP ALA GLU ASN PRO          
SEQRES  22 B  310  LEU HIS GLN PRO SER PRO SER LEU ASN LYS LEU VAL ALA          
SEQRES  23 B  310  GLU ASN LYS PHE GLY LYS LYS THR GLY GLU GLY PHE TYR          
SEQRES  24 B  310  LYS TYR LYS LEU GLU HIS HIS HIS HIS HIS HIS                  
FORMUL   3  HOH   *287(H2 O)                                                    
HELIX    1   1 GLY A   24  THR A   37  1                                  14    
HELIX    2   2 THR A   47  PHE A   70  1                                  24    
HELIX    3   3 ASN A   73  THR A   87  1                                  15    
HELIX    4   4 ASP A   93  VAL A   97  5                                   5    
HELIX    5   5 VAL A   97  THR A  101  5                                   5    
HELIX    6   6 ASN A  111  ALA A  126  1                                  16    
HELIX    7   7 GLN A  140  ASN A  146  1                                   7    
HELIX    8   8 ARG A  150  ASP A  152  5                                   3    
HELIX    9   9 SER A  178  LEU A  192  1                                  15    
HELIX   10  10 ILE A  206  ARG A  224  1                                  19    
HELIX   11  11 SER A  228  GLY A  241  1                                  14    
HELIX   12  12 GLY A  245  GLY A  254  1                                  10    
HELIX   13  13 GLY A  254  ASP A  269  1                                  16    
HELIX   14  14 ASN A  272  GLN A  276  5                                   5    
HELIX   15  15 SER A  278  GLU A  287  1                                  10    
HELIX   16  16 GLY B   24  THR B   37  1                                  14    
HELIX   17  17 THR B   47  PHE B   70  1                                  24    
HELIX   18  18 ASN B   73  THR B   87  1                                  15    
HELIX   19  19 ASP B   93  VAL B   98  1                                   6    
HELIX   20  20 ASN B  111  ALA B  126  1                                  16    
HELIX   21  21 ILE B  141  ASN B  146  1                                   6    
HELIX   22  22 ARG B  150  ASP B  152  5                                   3    
HELIX   23  23 SER B  178  LEU B  192  1                                  15    
HELIX   24  24 ILE B  206  ARG B  224  1                                  19    
HELIX   25  25 SER B  228  GLY B  241  1                                  14    
HELIX   26  26 GLY B  245  GLY B  254  1                                  10    
HELIX   27  27 GLY B  254  ASP B  269  1                                  16    
HELIX   28  28 ASN B  272  GLN B  276  5                                   5    
HELIX   29  29 SER B  278  GLU B  287  1                                  10    
HELIX   30  30 LYS B  292  GLY B  295  5                                   4    
SHEET    1   A 8 ILE A  88  SER A  91  0                                        
SHEET    2   A 8 THR A  40  VAL A  44  1  O  VAL A  41   N  ALA A  89           
SHEET    3   A 8 HIS A  17  ILE A  21  1  N  VAL A  18   O  THR A  40           
SHEET    4   A 8 LEU A 103  GLU A 106  1  O  LEU A 103   N  THR A  19           
SHEET    5   A 8 ILE A 131  SER A 134  1  O  ILE A 131   N  VAL A 104           
SHEET    6   A 8 PHE A 154  HIS A 158  1  N  ALA A 155   O  PHE A 132           
SHEET    7   A 8 LEU A 168  LYS A 173 -1  O  GLU A 170   N  HIS A 158           
SHEET    8   A 8 HIS A 195  LYS A 200  1  O  HIS A 195   N  VAL A 169           
SHEET    1   B 8 ILE B  88  SER B  91  0                                        
SHEET    2   B 8 THR B  40  VAL B  44  1  O  VAL B  41   N  ALA B  89           
SHEET    3   B 8 HIS B  17  ILE B  21  1  N  VAL B  18   O  THR B  40           
SHEET    4   B 8 LEU B 103  GLU B 106  1  O  LEU B 103   N  THR B  19           
SHEET    5   B 8 ILE B 131  SER B 134  1  O  ILE B 131   N  VAL B 104           
SHEET    6   B 8 PHE B 154  HIS B 158  1  N  ALA B 155   O  PHE B 132           
SHEET    7   B 8 LEU B 168  LYS B 173 -1  O  GLU B 170   N  HIS B 158           
SHEET    8   B 8 HIS B 195  LYS B 200  1  O  HIS B 195   N  VAL B 169           
CISPEP   1 ASN A  161    PRO A  162          0        -0.74                     
CISPEP   2 ASN B  161    PRO B  162          0        -0.06                     
CRYST1   50.440   86.970  168.290  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019826  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011498  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005942        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
HEADER    LECTIN                                  12-APR-05   2BOI              
TITLE     1.1A STRUCTURE OF CHROMOBACTERIUM VIOLACEUM LECTIN CV2L IN            
TITLE    2 COMPLEX WITH ALPHA-METHYL-FUCOSIDE                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CV-IIL LECTIN;                                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CHROMOBACTERIUM VIOLACEUM;                      
SOURCE   3 ORGANISM_TAXID: 536;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: TUNER(DE3);                                
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET25(B)                                  
KEYWDS    LECTIN, FUCOSE, CHROMOBACTERIUM VIOLACEUM, PSEUDOMONAS                
KEYWDS   2 AERUGINOSA                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.POKORNA,G.CIOCI,S.PERRET,E.REBUFFET,J.ADAM,                         
AUTHOR   2 N.GILBOA-GARBER,E.P.MITCHELL,A.IMBERTY,M.WIMMEROVA                   
REVDAT   4   24-FEB-09 2BOI    1       VERSN                                    
REVDAT   3   21-JUN-06 2BOI    1       JRNL                                     
REVDAT   2   31-MAY-06 2BOI    1       AUTHOR JRNL                              
REVDAT   1   25-MAY-06 2BOI    0                                                
JRNL        AUTH   M.POKORNA,G.CIOCI,S.PERRET,E.REBUFFET,N.KOSTLANOVA,          
JRNL        AUTH 2 J.ADAM,N.GILBOA-GARBER,E.P.MITCHELL,A.IMBERTY,               
JRNL        AUTH 3 M.WIMMEROVA                                                  
JRNL        TITL   UNUSUAL ENTROPY DRIVEN AFFINITY OF CHROMOBACTER              
JRNL        TITL 2 VIOLACEUM LECTIN CV-IIL TOWARDS FUCOSE AND MANNOSE           
JRNL        REF    BIOCHEMISTRY                  V.  45  7501 2006              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   16768446                                                     
JRNL        DOI    10.1021/BI060214E                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.1  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.47                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 83099                          
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) : 0.102                           
REMARK   3   R VALUE            (WORKING SET) : 0.101                           
REMARK   3   FREE R VALUE                     : 0.117                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4389                            
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) : 1.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.13                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6038                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 327                          
REMARK   3   BIN FREE R VALUE                    : 0.1370                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1841                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 333                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.021         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.021         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.012         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.541         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.983                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.979                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1908 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1744 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2639 ; 1.634 ; 1.961       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4070 ; 0.844 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   271 ; 6.881 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    78 ;42.699 ;26.154       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   300 ;12.545 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;10.834 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   325 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2279 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   359 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   334 ; 0.269 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1752 ; 0.201 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   998 ; 0.162 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1204 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   192 ; 0.167 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    17 ; 0.050 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    13 ; 0.331 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    59 ; 0.290 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    41 ; 0.214 ; 0.200       
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):  1282 ; 1.606 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   522 ; 0.657 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2058 ; 2.143 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   682 ; 2.778 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   581 ; 4.001 ; 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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2BOI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-APR-05.                  
REMARK 100 THE PDBE ID CODE IS EBI-22376.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUL-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : DIAMOND AND GE DOUBLE CRYSTAL      
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 87549                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.380                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.140                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.3600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.13                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.04                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.340                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: ACORN                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1GZT                                       
REMARK 200                                                                      
REMARK 200 REMARK: MOLREP WAS USED WITH MODEL 1GZT TO FIND THE POSITIONS        
REMARK 200  OF 4 CA ATOMS IN THE A.U. PHASING WAS PERFORMED BY ACORN            
REMARK 200  STARTING FROM THE POSITIONS OF THESE CA ATOMS.                      
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000 10%, 0.1 M (NH4)2SO4            
REMARK 280  PH 5                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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 -1.000000  0.000000  0.000000       25.54650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.91800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.54650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.91800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 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 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       51.09300            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  2084  -  O    HOH B  2088              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500                                                                      
REMARK 500   O    HOH B  2001     O    HOH A  2127     2655      2.12           
REMARK 500   O    HOH B  2027     O    HOH A  2074     4455      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    GLU A  35   CG    GLU A  35   CD      0.106                       
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    GLU A  35   CG  -  CD  -  OE1 ANGL. DEV. =  12.0 DEGREES          
REMARK 500    GLU A  35   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.8 DEGREES          
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 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 200  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 100   OD1                                                    
REMARK 620 2 ASP A 103   OD1  76.1                                              
REMARK 620 3 GLU A  94   OE1  78.2 117.2                                        
REMARK 620 4 GLU A  94   OE2 130.4 131.1  53.1                                  
REMARK 620 5 ASP A 103   OD2 105.8  50.7  84.4  80.8                            
REMARK 620 6 ASP A  98   OD1  85.3 146.3  85.4  82.2 162.9                      
REMARK 620 7 MFU A 400   O3   76.1  71.8 149.5 144.5 118.3  76.5                
REMARK 620 8 MFU A 400   O2  141.5  80.7 140.2  87.9  81.5  97.9  67.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 300  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 100   OD1                                                    
REMARK 620 2 ASN A 102   OD1  70.5                                              
REMARK 620 3 ASP A 103   OD1  69.0  87.3                                        
REMARK 620 4 ASP A 100   OD2  45.6  76.1 114.6                                  
REMARK 620 5 GLY B 113   O   122.1  86.4 164.0  78.0                            
REMARK 620 6 ASN A  21   O   143.6  86.2  82.7 154.2  82.3                      
REMARK 620 7 MFU A 400   O4  130.1 159.0 102.9 114.7  78.9  77.2                
REMARK 620 8 MFU A 400   O3   64.4 134.9  76.7  73.1 117.7 131.7  65.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 500  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  94   OE1                                                    
REMARK 620 2 GLU B  94   OE2  53.5                                              
REMARK 620 3 ASP B  98   OD1  85.3  82.4                                        
REMARK 620 4 ASP B 100   OD1  77.9 130.5  85.3                                  
REMARK 620 5 ASP B 103   OD2  85.1  80.8 163.2 106.1                            
REMARK 620 6 ASP B 103   OD1 117.4 131.4 145.8  75.9  50.9                      
REMARK 620 7 MFU B 700   O2  140.5  87.9  98.2 141.5  80.7  80.5                
REMARK 620 8 MFU B 700   O3  148.9 144.0  75.7  76.2 118.5  72.1  67.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 600  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 100   OD1                                                    
REMARK 620 2 ASN B  21   O   143.8                                              
REMARK 620 3 ASP B 103   OD1  68.7  82.8                                        
REMARK 620 4 MFU B 700   O3   64.7 131.3  77.2                                  
REMARK 620 5 MFU B 700   O4  130.1  76.8 103.1  65.6                            
REMARK 620 6 GLY A 113   O   122.9  81.5 163.2 118.0  78.9                      
REMARK 620 7 ASP B 100   OD2  46.2 153.9 114.9  73.5 114.7  78.3                
REMARK 620 8 ASN B 102   OD1  70.7  86.4  87.1 135.4 158.9  86.2  76.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMIMATION METHOD: PROVIDED BY DEPOSITOR                          
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MFU A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MFU B 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B 600                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2BV4   RELATED DB: PDB                                   
REMARK 900  1.0A STRUCTURE OF CHROMOBACTERIUM VIOLACEUM                         
REMARK 900  LECTIN IN COMPLEX WITH ALPHA-METHYL-MANNOSIDE                       
DBREF  2BOI A    1   113  UNP    Q7NX84   Q7NX84_CHRVO     2    114             
DBREF  2BOI B    1   113  UNP    Q7NX84   Q7NX84_CHRVO     2    114             
SEQRES   1 A  113  ALA GLN GLN GLY VAL PHE THR LEU PRO ALA ARG ILE ASN          
SEQRES   2 A  113  PHE GLY VAL THR VAL LEU VAL ASN SER ALA ALA THR GLN          
SEQRES   3 A  113  HIS VAL GLU ILE PHE VAL ASP ASN GLU PRO ARG ALA ALA          
SEQRES   4 A  113  PHE SER GLY VAL GLY THR GLY ASP ASN ASN LEU GLY THR          
SEQRES   5 A  113  LYS VAL ILE ASN SER GLY SER GLY ASN VAL ARG VAL GLN          
SEQRES   6 A  113  ILE THR ALA ASN GLY ARG GLN SER ASP LEU VAL SER SER          
SEQRES   7 A  113  GLN LEU VAL LEU ALA ASN LYS LEU ASN LEU ALA VAL VAL          
SEQRES   8 A  113  GLY SER GLU ASP GLY THR ASP MET ASP TYR ASN ASP SER          
SEQRES   9 A  113  ILE VAL ILE LEU ASN TRP PRO LEU GLY                          
SEQRES   1 B  113  ALA GLN GLN GLY VAL PHE THR LEU PRO ALA ARG ILE ASN          
SEQRES   2 B  113  PHE GLY VAL THR VAL LEU VAL ASN SER ALA ALA THR GLN          
SEQRES   3 B  113  HIS VAL GLU ILE PHE VAL ASP ASN GLU PRO ARG ALA ALA          
SEQRES   4 B  113  PHE SER GLY VAL GLY THR GLY ASP ASN ASN LEU GLY THR          
SEQRES   5 B  113  LYS VAL ILE ASN SER GLY SER GLY ASN VAL ARG VAL GLN          
SEQRES   6 B  113  ILE THR ALA ASN GLY ARG GLN SER ASP LEU VAL SER SER          
SEQRES   7 B  113  GLN LEU VAL LEU ALA ASN LYS LEU ASN LEU ALA VAL VAL          
SEQRES   8 B  113  GLY SER GLU ASP GLY THR ASP MET ASP TYR ASN ASP SER          
SEQRES   9 B  113  ILE VAL ILE LEU ASN TRP PRO LEU GLY                          
HET    MFU  A 400      12                                                       
HET    MFU  B 700      12                                                       
HET     CA  A 200       1                                                       
HET     CA  A 300       1                                                       
HET     CA  B 500       1                                                       
HET     CA  B 600       1                                                       
HETNAM     MFU ALPHA-L-METHYL-FUCOSE                                            
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  MFU    2(C7 H14 O5)                                                 
FORMUL   5   CA    4(CA 2+)                                                     
FORMUL   9  HOH   *333(H2 O1)                                                   
SHEET    1  AA 4 VAL A   5  THR A   7  0                                        
SHEET    2  AA 4 ASN A  61  ALA A  68 -1  O  VAL A  62   N  PHE A   6           
SHEET    3  AA 4 GLN A  26  VAL A  32 -1  O  HIS A  27   N  THR A  67           
SHEET    4  AA 4 GLU A  35  GLY A  42 -1  O  ALA A  38   N  ILE A  30           
SHEET    1  AB 5 PRO A  36  ILE A  55  0                                        
SHEET    2  AB 5 PHE A  14  ASN A  21 -1  O  VAL A  16   N  LYS A  53           
SHEET    3  AB 5 SER A 104  TRP A 110 -1  O  ILE A 107   N  THR A  17           
SHEET    4  AB 5 LEU A  86  SER A  93 -1  O  VAL A  91   N  VAL A 106           
SHEET    5  AB 5 ASP A  74  LEU A  82 -1  O  SER A  78   N  VAL A  90           
SHEET    1  BA 4 VAL B   5  THR B   7  0                                        
SHEET    2  BA 4 ASN B  61  ALA B  68 -1  O  VAL B  62   N  PHE B   6           
SHEET    3  BA 4 GLN B  26  VAL B  32 -1  O  HIS B  27   N  THR B  67           
SHEET    4  BA 4 GLU B  35  GLY B  42 -1  O  ALA B  38   N  ILE B  30           
SHEET    1  BB 5 PRO B  36  ILE B  55  0                                        
SHEET    2  BB 5 PHE B  14  ASN B  21 -1  O  VAL B  16   N  LYS B  53           
SHEET    3  BB 5 SER B 104  TRP B 110 -1  O  ILE B 107   N  THR B  17           
SHEET    4  BB 5 LEU B  86  SER B  93 -1  O  VAL B  91   N  VAL B 106           
SHEET    5  BB 5 ASP B  74  LEU B  82 -1  O  SER B  78   N  VAL B  90           
LINK        CA    CA A 200                 OD1 ASP A 100     1555   1555  2.37  
LINK        CA    CA A 200                 OD1 ASP A 103     1555   1555  2.66  
LINK        CA    CA A 200                 OE1 GLU A  94     1555   1555  2.49  
LINK        CA    CA A 200                 OE2 GLU A  94     1555   1555  2.40  
LINK        CA    CA A 200                 OD2 ASP A 103     1555   1555  2.43  
LINK        CA    CA A 200                 OD1 ASP A  98     1555   1555  2.36  
LINK        CA    CA A 200                 O3  MFU A 400     1555   1555  2.45  
LINK        CA    CA A 200                 O2  MFU A 400     1555   1555  2.51  
LINK        CA    CA A 300                 OD1 ASP A 100     1555   1555  3.04  
LINK        CA    CA A 300                 OD1 ASN A 102     1555   1555  2.35  
LINK        CA    CA A 300                 OD1 ASP A 103     1555   1555  2.36  
LINK        CA    CA A 300                 OD2 ASP A 100     1555   1555  2.41  
LINK        CA    CA A 300                 O   GLY B 113     1555   1555  2.40  
LINK        CA    CA A 300                 O   ASN A  21     1555   1555  2.35  
LINK        CA    CA A 300                 O4  MFU A 400     1555   1555  2.50  
LINK        CA    CA A 300                 O3  MFU A 400     1555   1555  2.47  
LINK        CA    CA B 500                 OE2 GLU B  94     1555   1555  2.41  
LINK        CA    CA B 500                 OD1 ASP B  98     1555   1555  2.35  
LINK        CA    CA B 500                 OD1 ASP B 100     1555   1555  2.36  
LINK        CA    CA B 500                 OD2 ASP B 103     1555   1555  2.42  
LINK        CA    CA B 500                 OD1 ASP B 103     1555   1555  2.65  
LINK        CA    CA B 500                 O2  MFU B 700     1555   1555  2.50  
LINK        CA    CA B 500                 O3  MFU B 700     1555   1555  2.47  
LINK        CA    CA B 500                 OE1 GLU B  94     1555   1555  2.46  
LINK        CA    CA B 600                 O   ASN B  21     1555   1555  2.34  
LINK        CA    CA B 600                 OD1 ASP B 103     1555   1555  2.36  
LINK        CA    CA B 600                 O3  MFU B 700     1555   1555  2.47  
LINK        CA    CA B 600                 O4  MFU B 700     1555   1555  2.51  
LINK        CA    CA B 600                 O   GLY A 113     1555   1555  2.40  
LINK        CA    CA B 600                 OD2 ASP B 100     1555   1555  2.42  
LINK        CA    CA B 600                 OD1 ASN B 102     1555   1555  2.35  
LINK        CA    CA B 600                 OD1 ASP B 100     1555   1555  3.03  
CISPEP   1 TRP A  110    PRO A  111          0       -13.50                     
CISPEP   2 TRP B  110    PRO B  111          0       -13.19                     
SITE     1 AC1 12 ASN A  21  SER A  22  ALA A  23  GLU A  94                    
SITE     2 AC1 12 ASP A  95  ASP A  98  ASP A 100  ASP A 103                    
SITE     3 AC1 12  CA A 200   CA A 300  HOH A2150  GLY B 113                    
SITE     1 AC2 12 GLY A 113  ASN B  21  SER B  22  ALA B  23                    
SITE     2 AC2 12 GLU B  94  ASP B  95  ASP B  98  ASP B 100                    
SITE     3 AC2 12 ASP B 103   CA B 500   CA B 600  HOH B2166                    
SITE     1 AC3  5 GLU A  94  ASP A  98  ASP A 100  ASP A 103                    
SITE     2 AC3  5 MFU A 400                                                     
SITE     1 AC4  6 ASN A  21  ASP A 100  ASN A 102  ASP A 103                    
SITE     2 AC4  6 MFU A 400  GLY B 113                                          
SITE     1 AC5  5 GLU B  94  ASP B  98  ASP B 100  ASP B 103                    
SITE     2 AC5  5 MFU B 700                                                     
SITE     1 AC6  6 GLY A 113  ASN B  21  ASP B 100  ASN B 102                    
SITE     2 AC6  6 ASP B 103  MFU B 700                                          
CRYST1   51.093   89.836   46.479  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019572  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011131  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021515        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
HEADER    CYTOKINE                                28-JAN-09   2KEC              
TITLE     STRUCTURE OF SDF-1/CXCL12                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: STROMAL CELL-DERIVED FACTOR 1-ALPHA;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SDF-1, C-X-C MOTIF CHEMOKINE 12, PRE-B CELL                 
COMPND   5 GROWTH-STIMULATING FACTOR, PBSF, HIRH, SDF-1-ALPHA(3-67);            
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CXCL12, SDF1, SDF1A, SDF1B;                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PQE30                                      
KEYWDS    STROMAL CELL DERIVED FACTOR-1, SDF1-ALPHA, CXCL12,                    
KEYWDS   2 CHEMOKINE, ALTERNATIVE SPLICING, CHEMOTAXIS, CYTOKINE,               
KEYWDS   3 GROWTH FACTOR, SECRETED                                              
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    B.F.VOLKMAN,C.T.VELDKAMP,F.C.PETERSON                                 
REVDAT   1   29-SEP-09 2KEC    0                                                
JRNL        AUTH   C.T.VELDKAMP,J.J.ZIAREK,J.SU,H.BASNET,R.LENNERTZ,            
JRNL        AUTH 2 J.J.WEINER,F.C.PETERSON,J.E.BAKER,B.F.VOLKMAN                
JRNL        TITL   MONOMERIC STRUCTURE OF THE CARDIOPROTECTIVE                  
JRNL        TITL 2 CHEMOKINE SDF-1/CXCL12                                       
JRNL        REF    PROTEIN SCI.                  V.  18  1359 2009              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   19551879                                                     
JRNL        DOI    10.1002/PRO.167                                              
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : XPLOR-NIH 2.9.3                                      
REMARK   3   AUTHORS     : SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,           
REMARK   3                 CLORE,G.M.                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: AUTOMATED METHODS WERE USED FOR           
REMARK   3  BACKBONE CHEMICAL SHIFT ASSIGNMENT AND ITERATIVE NOE                
REMARK   3  REFINEMENT. FINAL STRUCTURES WERE OBTAINED BY MOLECULAR             
REMARK   3  DYNAMICS IN EXPLICIT SOLVENT, CXCL12 STRUCTURES ARE BASED ON A      
REMARK   3  TOTAL OF 1196 NOE CONSTRAINTS (336 INTRA, 251 SEQUENTIAL, 218       
REMARK   3  MEDIUM, 391 LONG RANGE) AND 72 PHI AND PSI DIHEDRAL ANGLE           
REMARK   3  CONSTRAINTS.                                                        
REMARK   4                                                                      
REMARK   4 2KEC COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB101015.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 5.5                                
REMARK 210  IONIC STRENGTH                 : 50                                 
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 1.56 MM [U-100% 13C; U-100%        
REMARK 210                                   15N] CXCL12/SDF1-ALPHA, 90%        
REMARK 210                                   H2O, 10% D2O                       
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D_15N-SEPARATED_NOESY; 3D_        
REMARK 210                                   13C-SEPARATED_NOESY; 3D_13C-       
REMARK 210                                   SEPARATED_NOESY (AROMATIC)         
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ                            
REMARK 210  SPECTROMETER MODEL             : AVANCE                             
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : XWINNMR 3.5, NMRPIPE 2004,         
REMARK 210                                   XEASY 1.3, GARANT 2.1, CYANA       
REMARK 210                                   2.1                                
REMARK 210   METHOD USED                   : MOLECULAR DYNAMICS                 
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : TARGET FUNCTION                    
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465   MODELS 1-20                                                        
REMARK 465     RES C SSSEQI                                                     
REMARK 465     GLY A    -1                                                      
REMARK 465     MET A     0                                                      
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  2 ARG A  12      -69.72    -97.25                                   
REMARK 500  3 LEU A   5       35.39    -93.42                                   
REMARK 500  3 ASN A  46       -2.13     66.38                                   
REMARK 500  3 PRO A  53        3.69    -69.60                                   
REMARK 500  4 VAL A   3      -57.12   -125.50                                   
REMARK 500  4 SER A   4       95.93     46.80                                   
REMARK 500  4 ALA A  35     -164.94    -75.45                                   
REMARK 500  4 ASN A  46       -0.72     65.37                                   
REMARK 500  5 SER A   4      -36.41     73.13                                   
REMARK 500  5 ALA A  35     -163.20    -78.21                                   
REMARK 500  7 SER A   4     -162.70     66.45                                   
REMARK 500  7 ARG A  12      -62.56    -94.64                                   
REMARK 500  7 ASN A  46       -1.54     71.76                                   
REMARK 500  8 SER A   4       24.59   -149.54                                   
REMARK 500  8 LEU A   5      -42.40     71.82                                   
REMARK 500  8 ALA A  35     -163.86    -73.48                                   
REMARK 500  9 VAL A   3       94.89     65.71                                   
REMARK 500  9 SER A   6       92.25     65.04                                   
REMARK 500 10 VAL A   3       18.54   -141.28                                   
REMARK 500 10 SER A   6       40.19    -79.77                                   
REMARK 500 10 TYR A   7      179.08     67.51                                   
REMARK 500 11 PRO A   2       88.11    -68.27                                   
REMARK 500 12 ARG A  12      -74.06    -94.60                                   
REMARK 500 12 ALA A  35      -89.03    -76.23                                   
REMARK 500 13 ASN A  46       -3.42     64.96                                   
REMARK 500 14 VAL A   3      102.17     72.73                                   
REMARK 500 14 ALA A  35     -164.08    -75.96                                   
REMARK 500 15 VAL A   3      117.58     47.32                                   
REMARK 500 16 ALA A  35     -167.93    -71.97                                   
REMARK 500 17 LEU A   5       92.54     69.99                                   
REMARK 500 17 TYR A   7      149.29     68.32                                   
REMARK 500 17 ASN A  46       -2.28     66.76                                   
REMARK 500 17 ASN A  67       57.95   -142.28                                   
REMARK 500 18 ALA A  35      -86.92    -76.14                                   
REMARK 500 18 ASN A  46       -1.04     67.62                                   
REMARK 500 19 SER A   4       82.88     59.04                                   
REMARK 500 19 LEU A   5       98.30    -68.09                                   
REMARK 500 19 ALA A  35      -77.88    -77.69                                   
REMARK 500 19 ASN A  46       -4.57     62.81                                   
REMARK 500 19 PRO A  53        0.18    -66.24                                   
REMARK 500 20 LYS A  24      -70.11    -78.62                                   
REMARK 500 20 ASN A  46       -0.47     63.94                                   
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 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: (11X,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  15 VAL A   3        24.6      L          L   OUTSIDE RANGE          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 16142   RELATED DB: BMRB                                 
REMARK 900 RELATED ID: 2KED   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2KEE   RELATED DB: PDB                                   
DBREF  2KEC A    1    68  UNP    P48061   SDF1_HUMAN      22     89             
SEQADV 2KEC GLY A   -1  UNP  P48061              EXPRESSION TAG                 
SEQADV 2KEC MET A    0  UNP  P48061              EXPRESSION TAG                 
SEQRES   1 A   70  GLY MET LYS PRO VAL SER LEU SER TYR ARG CYS PRO CYS          
SEQRES   2 A   70  ARG PHE PHE GLU SER HIS VAL ALA ARG ALA ASN VAL LYS          
SEQRES   3 A   70  HIS LEU LYS ILE LEU ASN THR PRO ASN CYS ALA LEU GLN          
SEQRES   4 A   70  ILE VAL ALA ARG LEU LYS ASN ASN ASN ARG GLN VAL CYS          
SEQRES   5 A   70  ILE ASP PRO LYS LEU LYS TRP ILE GLN GLU TYR LEU GLU          
SEQRES   6 A   70  LYS ALA LEU ASN LYS                                          
HELIX    1   1 ALA A   19  ALA A   21  5                                   3    
HELIX    2   2 LEU A   55  LYS A   68  1                                  14    
SHEET    1   A 3 VAL A  23  ASN A  30  0                                        
SHEET    2   A 3 LEU A  36  LEU A  42 -1  O  ARG A  41   N  LYS A  24           
SHEET    3   A 3 GLN A  48  ILE A  51 -1  O  VAL A  49   N  ALA A  40           
SSBOND   1 CYS A    9    CYS A   34                          1555   1555  2.02  
SSBOND   2 CYS A   11    CYS A   50                          1555   1555  2.02  
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)

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