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Database: PDB
Entry: 6ROL
LinkDB: 6ROL
Original site: 6ROL 
HEADER    RNA BINDING PROTEIN                     13-MAY-19   6ROL              
TITLE     STRUCTURE OF IMP2 KH34 DOMAINS                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INSULIN-LIKE GROWTH FACTOR 2 MRNA-BINDING PROTEIN 2;       
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: IMP-2,HEPATOCELLULAR CARCINOMA AUTOANTIGEN P62,IGF-II MRNA- 
COMPND   5 BINDING PROTEIN 2,VICKZ FAMILY MEMBER 2;                             
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: IGF2BP2, IMP2, VICKZ2;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SPECIFICITY, RNA BINDING PROTEIN                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.BHASKAR,J.BISWAS,R.H.SINGER,J.A.CHAO                                
REVDAT   1   16-OCT-19 6ROL    0                                                
JRNL        AUTH   J.BISWAS,V.L.PATEL,V.BHASKAR,J.A.CHAO,R.H.SINGER,            
JRNL        AUTH 2 C.ELISCOVICH                                                 
JRNL        TITL   THE STRUCTURAL BASIS FOR RNA SELECTIVITY BY THE IMP FAMILY   
JRNL        TITL 2 OF RNA-BINDING PROTEINS.                                     
JRNL        REF    NAT COMMUN                    V.  10  4440 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   31570709                                                     
JRNL        DOI    10.1038/S41467-019-12193-7                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.13_2998                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.80                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 46167                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1  2.1750 -  2.1000    0.00     4631   245  0.2694 0.3026        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.70                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6ROL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-MAY-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292102096.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 18-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46202                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.05660                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0500                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41140                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.050                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3KRM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 23% PEG-3350, 200MM AMMONIUM SULFATE,    
REMARK 280  100MM TRIS PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  295K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       31.19000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   423                                                      
REMARK 465     GLY A   424                                                      
REMARK 465     GLN A   587                                                      
REMARK 465     LYS A   588                                                      
REMARK 465     GLY B   423                                                      
REMARK 465     GLY B   424                                                      
REMARK 465     SER B   425                                                      
REMARK 465     GLN B   587                                                      
REMARK 465     LYS B   588                                                      
REMARK 465     GLY C   423                                                      
REMARK 465     GLY C   424                                                      
REMARK 465     SER C   425                                                      
REMARK 465     GLN C   587                                                      
REMARK 465     LYS C   588                                                      
REMARK 465     GLY D   423                                                      
REMARK 465     GLY D   424                                                      
REMARK 465     SER D   425                                                      
REMARK 465     GLN D   585                                                      
REMARK 465     GLU D   586                                                      
REMARK 465     GLN D   587                                                      
REMARK 465     LYS D   588                                                      
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     SER A 425    OG                                                  
REMARK 470     ASP A 470    CG   OD1  OD2                                       
REMARK 470     GLN A 585    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 586    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 426    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 428    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 470    CG   OD1  OD2                                       
REMARK 470     LYS B 505    CG   CD   CE   NZ                                   
REMARK 470     LYS B 530    CG   CD   CE   NZ                                   
REMARK 470     VAL B 532    CG1  CG2                                            
REMARK 470     ASN B 533    CG   OD1  ND2                                       
REMARK 470     GLU B 534    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 537    CG   OD1  ND2                                       
REMARK 470     LYS B 583    CD   CE   NZ                                        
REMARK 470     GLN B 584    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 585    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 586    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 470    CG   OD1  OD2                                       
REMARK 470     GLN C 581    CD   OE1  NE2                                       
REMARK 470     LYS C 583    CD   CE   NZ                                        
REMARK 470     GLN C 584    CG   CD   OE1  NE2                                  
REMARK 470     GLN C 585    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 586    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 426    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 467    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 470    CG   OD1  OD2                                       
REMARK 470     ASN D 503    CG   OD1  ND2                                       
REMARK 470     LYS D 505    CG   CD   CE   NZ                                   
REMARK 470     LYS D 527    CG   CD   CE   NZ                                   
REMARK 470     LYS D 530    CG   CD   CE   NZ                                   
REMARK 470     ARG D 547    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS D 583    CG   CD   CE   NZ                                   
REMARK 470     GLN D 584    CG   CD   OE1  NE2                                  
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   HD2  PHE C   566     HZ2  LYS D   497              1.30            
REMARK 500   H    PHE D   566     O    HOH D   701              1.56            
REMARK 500   HO3  GOL A   603     O    HOH A   702              1.59            
REMARK 500   O    THR B   539     HG   SER B   540              1.60            
REMARK 500   O4   PEG D   605     O    HOH D   701              1.83            
REMARK 500   O    HOH C   715     O    HOH C   742              1.97            
REMARK 500   O2   SO4 C   613     O    HOH C   701              1.97            
REMARK 500   O    HOH A   702     O    HOH A   755              1.98            
REMARK 500   O    HOH C   742     O    HOH C   747              2.00            
REMARK 500   O    HOH C   805     O    HOH C   810              2.00            
REMARK 500   O4   SO4 C   614     O    HOH C   702              2.00            
REMARK 500   O    HOH C   713     O    HOH C   772              2.02            
REMARK 500   O1   PEG D   606     O    HOH D   702              2.02            
REMARK 500   OE2  GLU B   577     O    HOH B   701              2.03            
REMARK 500   O    HOH A   790     O    HOH A   797              2.06            
REMARK 500   N    PHE D   566     O    HOH D   701              2.07            
REMARK 500   O    HOH C   757     O    HOH C   814              2.07            
REMARK 500   O    HOH C   704     O    HOH C   807              2.07            
REMARK 500   O    HOH C   796     O    HOH C   811              2.08            
REMARK 500   O4   PEG D   605     O    HOH D   703              2.09            
REMARK 500   OE2  GLU A   428     NH1  ARG A   576              2.10            
REMARK 500   O    HOH B   702     O    HOH B   728              2.10            
REMARK 500   OE1  GLN B   452     O    HOH B   702              2.11            
REMARK 500   O    PHE A   501     O2   GOL A   601              2.12            
REMARK 500   O1   PEG B   603     O    HOH B   703              2.12            
REMARK 500   O    HOH C   701     O    HOH C   710              2.12            
REMARK 500   O3   GOL C   605     O    HOH C   703              2.14            
REMARK 500   O    HOH A   747     O    HOH A   795              2.14            
REMARK 500   NH2  ARG A   547     O    HOH A   701              2.14            
REMARK 500   NH1  ARG C   573     O2   GOL D   602              2.16            
REMARK 500   O3   GOL A   603     O    HOH A   702              2.18            
REMARK 500   OE1  GLU C   428     O    HOH C   704              2.19            
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   OD1  ASN A   503     H    GLY C   528     2645     1.53            
REMARK 500   O    HOH A   714     O    HOH C   746     2645     2.02            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A 501       43.08    -96.27                                   
REMARK 500    SER A 540       -5.09     73.56                                   
REMARK 500    SER B 540       -6.73     76.48                                   
REMARK 500    LYS B 583        1.05    -64.07                                   
REMARK 500    SER C 540       -4.62     73.75                                   
REMARK 500    PRO D 504       -4.97    -56.98                                   
REMARK 500    SER D 540       -4.70     75.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 606                 
DBREF  6ROL A  426   588  UNP    Q9Y6M1   IF2B2_HUMAN    426    588             
DBREF  6ROL B  426   588  UNP    Q9Y6M1   IF2B2_HUMAN    426    588             
DBREF  6ROL C  426   588  UNP    Q9Y6M1   IF2B2_HUMAN    426    588             
DBREF  6ROL D  426   588  UNP    Q9Y6M1   IF2B2_HUMAN    426    588             
SEQADV 6ROL GLY A  423  UNP  Q9Y6M1              EXPRESSION TAG                 
SEQADV 6ROL GLY A  424  UNP  Q9Y6M1              EXPRESSION TAG                 
SEQADV 6ROL SER A  425  UNP  Q9Y6M1              EXPRESSION TAG                 
SEQADV 6ROL GLY B  423  UNP  Q9Y6M1              EXPRESSION TAG                 
SEQADV 6ROL GLY B  424  UNP  Q9Y6M1              EXPRESSION TAG                 
SEQADV 6ROL SER B  425  UNP  Q9Y6M1              EXPRESSION TAG                 
SEQADV 6ROL GLY C  423  UNP  Q9Y6M1              EXPRESSION TAG                 
SEQADV 6ROL GLY C  424  UNP  Q9Y6M1              EXPRESSION TAG                 
SEQADV 6ROL SER C  425  UNP  Q9Y6M1              EXPRESSION TAG                 
SEQADV 6ROL GLY D  423  UNP  Q9Y6M1              EXPRESSION TAG                 
SEQADV 6ROL GLY D  424  UNP  Q9Y6M1              EXPRESSION TAG                 
SEQADV 6ROL SER D  425  UNP  Q9Y6M1              EXPRESSION TAG                 
SEQRES   1 A  166  GLY GLY SER GLU GLN GLU ILE VAL ASN LEU PHE ILE PRO          
SEQRES   2 A  166  THR GLN ALA VAL GLY ALA ILE ILE GLY LYS LYS GLY ALA          
SEQRES   3 A  166  HIS ILE LYS GLN LEU ALA ARG PHE ALA GLY ALA SER ILE          
SEQRES   4 A  166  LYS ILE ALA PRO ALA GLU GLY PRO ASP VAL SER GLU ARG          
SEQRES   5 A  166  MET VAL ILE ILE THR GLY PRO PRO GLU ALA GLN PHE LYS          
SEQRES   6 A  166  ALA GLN GLY ARG ILE PHE GLY LYS LEU LYS GLU GLU ASN          
SEQRES   7 A  166  PHE PHE ASN PRO LYS GLU GLU VAL LYS LEU GLU ALA HIS          
SEQRES   8 A  166  ILE ARG VAL PRO SER SER THR ALA GLY ARG VAL ILE GLY          
SEQRES   9 A  166  LYS GLY GLY LYS THR VAL ASN GLU LEU GLN ASN LEU THR          
SEQRES  10 A  166  SER ALA GLU VAL ILE VAL PRO ARG ASP GLN THR PRO ASP          
SEQRES  11 A  166  GLU ASN GLU GLU VAL ILE VAL ARG ILE ILE GLY HIS PHE          
SEQRES  12 A  166  PHE ALA SER GLN THR ALA GLN ARG LYS ILE ARG GLU ILE          
SEQRES  13 A  166  VAL GLN GLN VAL LYS GLN GLN GLU GLN LYS                      
SEQRES   1 B  166  GLY GLY SER GLU GLN GLU ILE VAL ASN LEU PHE ILE PRO          
SEQRES   2 B  166  THR GLN ALA VAL GLY ALA ILE ILE GLY LYS LYS GLY ALA          
SEQRES   3 B  166  HIS ILE LYS GLN LEU ALA ARG PHE ALA GLY ALA SER ILE          
SEQRES   4 B  166  LYS ILE ALA PRO ALA GLU GLY PRO ASP VAL SER GLU ARG          
SEQRES   5 B  166  MET VAL ILE ILE THR GLY PRO PRO GLU ALA GLN PHE LYS          
SEQRES   6 B  166  ALA GLN GLY ARG ILE PHE GLY LYS LEU LYS GLU GLU ASN          
SEQRES   7 B  166  PHE PHE ASN PRO LYS GLU GLU VAL LYS LEU GLU ALA HIS          
SEQRES   8 B  166  ILE ARG VAL PRO SER SER THR ALA GLY ARG VAL ILE GLY          
SEQRES   9 B  166  LYS GLY GLY LYS THR VAL ASN GLU LEU GLN ASN LEU THR          
SEQRES  10 B  166  SER ALA GLU VAL ILE VAL PRO ARG ASP GLN THR PRO ASP          
SEQRES  11 B  166  GLU ASN GLU GLU VAL ILE VAL ARG ILE ILE GLY HIS PHE          
SEQRES  12 B  166  PHE ALA SER GLN THR ALA GLN ARG LYS ILE ARG GLU ILE          
SEQRES  13 B  166  VAL GLN GLN VAL LYS GLN GLN GLU GLN LYS                      
SEQRES   1 C  166  GLY GLY SER GLU GLN GLU ILE VAL ASN LEU PHE ILE PRO          
SEQRES   2 C  166  THR GLN ALA VAL GLY ALA ILE ILE GLY LYS LYS GLY ALA          
SEQRES   3 C  166  HIS ILE LYS GLN LEU ALA ARG PHE ALA GLY ALA SER ILE          
SEQRES   4 C  166  LYS ILE ALA PRO ALA GLU GLY PRO ASP VAL SER GLU ARG          
SEQRES   5 C  166  MET VAL ILE ILE THR GLY PRO PRO GLU ALA GLN PHE LYS          
SEQRES   6 C  166  ALA GLN GLY ARG ILE PHE GLY LYS LEU LYS GLU GLU ASN          
SEQRES   7 C  166  PHE PHE ASN PRO LYS GLU GLU VAL LYS LEU GLU ALA HIS          
SEQRES   8 C  166  ILE ARG VAL PRO SER SER THR ALA GLY ARG VAL ILE GLY          
SEQRES   9 C  166  LYS GLY GLY LYS THR VAL ASN GLU LEU GLN ASN LEU THR          
SEQRES  10 C  166  SER ALA GLU VAL ILE VAL PRO ARG ASP GLN THR PRO ASP          
SEQRES  11 C  166  GLU ASN GLU GLU VAL ILE VAL ARG ILE ILE GLY HIS PHE          
SEQRES  12 C  166  PHE ALA SER GLN THR ALA GLN ARG LYS ILE ARG GLU ILE          
SEQRES  13 C  166  VAL GLN GLN VAL LYS GLN GLN GLU GLN LYS                      
SEQRES   1 D  166  GLY GLY SER GLU GLN GLU ILE VAL ASN LEU PHE ILE PRO          
SEQRES   2 D  166  THR GLN ALA VAL GLY ALA ILE ILE GLY LYS LYS GLY ALA          
SEQRES   3 D  166  HIS ILE LYS GLN LEU ALA ARG PHE ALA GLY ALA SER ILE          
SEQRES   4 D  166  LYS ILE ALA PRO ALA GLU GLY PRO ASP VAL SER GLU ARG          
SEQRES   5 D  166  MET VAL ILE ILE THR GLY PRO PRO GLU ALA GLN PHE LYS          
SEQRES   6 D  166  ALA GLN GLY ARG ILE PHE GLY LYS LEU LYS GLU GLU ASN          
SEQRES   7 D  166  PHE PHE ASN PRO LYS GLU GLU VAL LYS LEU GLU ALA HIS          
SEQRES   8 D  166  ILE ARG VAL PRO SER SER THR ALA GLY ARG VAL ILE GLY          
SEQRES   9 D  166  LYS GLY GLY LYS THR VAL ASN GLU LEU GLN ASN LEU THR          
SEQRES  10 D  166  SER ALA GLU VAL ILE VAL PRO ARG ASP GLN THR PRO ASP          
SEQRES  11 D  166  GLU ASN GLU GLU VAL ILE VAL ARG ILE ILE GLY HIS PHE          
SEQRES  12 D  166  PHE ALA SER GLN THR ALA GLN ARG LYS ILE ARG GLU ILE          
SEQRES  13 D  166  VAL GLN GLN VAL LYS GLN GLN GLU GLN LYS                      
HET    GOL  A 601      14                                                       
HET    GOL  A 602      14                                                       
HET    GOL  A 603      14                                                       
HET    GOL  A 604      14                                                       
HET    GOL  A 605      14                                                       
HET    GOL  A 606      14                                                       
HET    PEG  A 607      17                                                       
HET    SO4  A 608       5                                                       
HET    SO4  A 609       5                                                       
HET    GOL  B 601      14                                                       
HET    GOL  B 602      14                                                       
HET    PEG  B 603      17                                                       
HET    GOL  C 601      14                                                       
HET    GOL  C 602      14                                                       
HET    GOL  C 603      14                                                       
HET    GOL  C 604      14                                                       
HET    GOL  C 605      14                                                       
HET    GOL  C 606      14                                                       
HET    GOL  C 607      14                                                       
HET    PEG  C 608      17                                                       
HET    PEG  C 609      17                                                       
HET    PEG  C 610      17                                                       
HET    PEG  C 611      17                                                       
HET    PEG  C 612      17                                                       
HET    SO4  C 613       5                                                       
HET    SO4  C 614       5                                                       
HET    GOL  D 601      14                                                       
HET    GOL  D 602      14                                                       
HET    GOL  D 603      14                                                       
HET    PEG  D 604      17                                                       
HET    PEG  D 605      17                                                       
HET    PEG  D 606      17                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  GOL    18(C3 H8 O3)                                                 
FORMUL  11  PEG    10(C4 H10 O3)                                                
FORMUL  12  SO4    4(O4 S 2-)                                                   
FORMUL  37  HOH   *335(H2 O)                                                    
HELIX    1 AA1 ALA A  438  GLY A  444  1                                   7    
HELIX    2 AA2 GLY A  447  GLY A  458  1                                  12    
HELIX    3 AA3 PRO A  481  GLU A  499  1                                  19    
HELIX    4 AA4 THR A  520  GLY A  526  1                                   7    
HELIX    5 AA5 GLY A  529  SER A  540  1                                  12    
HELIX    6 AA6 HIS A  564  GLN A  585  1                                  22    
HELIX    7 AA7 ALA B  438  GLY B  444  1                                   7    
HELIX    8 AA8 GLY B  447  GLY B  458  1                                  12    
HELIX    9 AA9 PRO B  481  GLU B  499  1                                  19    
HELIX   10 AB1 SER B  518  GLY B  526  1                                   9    
HELIX   11 AB2 GLY B  529  SER B  540  1                                  12    
HELIX   12 AB3 PHE B  565  LYS B  583  1                                  19    
HELIX   13 AB4 GLN B  584  GLU B  586  5                                   3    
HELIX   14 AB5 ALA C  438  GLY C  444  1                                   7    
HELIX   15 AB6 GLY C  447  GLY C  458  1                                  12    
HELIX   16 AB7 PRO C  481  GLU C  499  1                                  19    
HELIX   17 AB8 SER C  518  GLY C  526  1                                   9    
HELIX   18 AB9 GLY C  529  SER C  540  1                                  12    
HELIX   19 AC1 HIS C  564  GLU C  586  1                                  23    
HELIX   20 AC2 ALA D  438  GLY D  444  1                                   7    
HELIX   21 AC3 GLY D  447  GLY D  458  1                                  12    
HELIX   22 AC4 PRO D  481  GLU D  499  1                                  19    
HELIX   23 AC5 SER D  518  GLY D  526  1                                   9    
HELIX   24 AC6 GLY D  529  SER D  540  1                                  12    
HELIX   25 AC7 HIS D  564  LYS D  583  1                                  20    
SHEET    1 AA1 6 SER A 460  ILE A 463  0                                        
SHEET    2 AA1 6 GLU A 473  GLY A 480 -1  O  ILE A 477   N  LYS A 462           
SHEET    3 AA1 6 GLU A 428  PRO A 435 -1  N  LEU A 432   O  VAL A 476           
SHEET    4 AA1 6 LEU A 510  PRO A 517 -1  O  HIS A 513   N  ASN A 431           
SHEET    5 AA1 6 GLU A 556  GLY A 563 -1  O  VAL A 557   N  VAL A 516           
SHEET    6 AA1 6 GLU A 542  ILE A 544 -1  N  ILE A 544   O  ARG A 560           
SHEET    1 AA2 6 SER B 460  ILE B 463  0                                        
SHEET    2 AA2 6 GLU B 473  GLY B 480 -1  O  ILE B 477   N  LYS B 462           
SHEET    3 AA2 6 GLU B 428  PRO B 435 -1  N  LEU B 432   O  VAL B 476           
SHEET    4 AA2 6 LYS B 509  PRO B 517 -1  O  HIS B 513   N  ASN B 431           
SHEET    5 AA2 6 GLU B 556  HIS B 564 -1  O  VAL B 557   N  VAL B 516           
SHEET    6 AA2 6 GLU B 542  ILE B 544 -1  N  ILE B 544   O  ARG B 560           
SHEET    1 AA3 6 SER C 460  ILE C 463  0                                        
SHEET    2 AA3 6 GLU C 473  GLY C 480 -1  O  ILE C 477   N  LYS C 462           
SHEET    3 AA3 6 GLU C 428  PRO C 435 -1  N  LEU C 432   O  VAL C 476           
SHEET    4 AA3 6 LEU C 510  PRO C 517 -1  O  HIS C 513   N  ASN C 431           
SHEET    5 AA3 6 GLU C 556  GLY C 563 -1  O  ILE C 561   N  ALA C 512           
SHEET    6 AA3 6 GLU C 542  ILE C 544 -1  N  ILE C 544   O  ARG C 560           
SHEET    1 AA4 6 SER D 460  ILE D 463  0                                        
SHEET    2 AA4 6 GLU D 473  GLY D 480 -1  O  ILE D 477   N  LYS D 462           
SHEET    3 AA4 6 GLU D 428  PRO D 435 -1  N  LEU D 432   O  VAL D 476           
SHEET    4 AA4 6 LEU D 510  PRO D 517 -1  O  HIS D 513   N  ASN D 431           
SHEET    5 AA4 6 GLU D 556  GLY D 563 -1  O  VAL D 557   N  VAL D 516           
SHEET    6 AA4 6 GLU D 542  ILE D 544 -1  N  GLU D 542   O  ILE D 562           
SITE     1 AC1  6 PRO A 435  PHE A 501  PHE A 502  LYS A 509                    
SITE     2 AC1  6 HOH A 725  HOH A 730                                          
SITE     1 AC2  7 ALA A 441  GLY A 444  LYS A 445  HIS A 449                    
SITE     2 AC2  7 LYS A 495  HOH A 708  HOH A 750                               
SITE     1 AC3  7 ILE A 450  LYS A 451  ALA A 454  SER A 460                    
SITE     2 AC3  7 ILE A 461  LYS A 462  HOH A 702                               
SITE     1 AC4  4 GLU A 473  GLU A 511  HIS A 513  HOH A 709                    
SITE     1 AC5  8 GLU A 428  PRO A 482  GLN A 485  PHE A 486                    
SITE     2 AC5  8 GLN A 569  GLN A 572  ARG A 576  HOH A 723                    
SITE     1 AC6  8 LYS A 497  GLU A 507  VAL A 508  HIS A 564                    
SITE     2 AC6  8 HOH A 703  HOH A 753  PHE B 566  PEG B 603                    
SITE     1 AC7  6 GLN A 452  PHE A 456  ARG A 491  ARG B 573                    
SITE     2 AC7  6 GLU B 577  HOH B 701                                          
SITE     1 AC8  5 ARG A 523  GLY A 526  LYS A 527  HOH A 728                    
SITE     2 AC8  5 HOH A 748                                                     
SITE     1 AC9  5 ASN A 431  MET A 475  HIS A 513  ARG A 515                    
SITE     2 AC9  5 ILE A 558                                                     
SITE     1 AD1  4 ASN B 431  HIS B 513  ARG B 515  ILE B 558                    
SITE     1 AD2  4 ALA B 454  SER B 460  ILE B 461  HOH B 708                    
SITE     1 AD3 10 LYS A 497  GOL A 606  GLU B 507  VAL B 508                    
SITE     2 AD3 10 HIS B 564  PHE B 565  PHE B 566  ALA B 567                    
SITE     3 AD3 10 HOH B 703  HOH B 705                                          
SITE     1 AD4  9 LYS C 497  GLU C 507  HIS C 564  PHE C 565                    
SITE     2 AD4  9 PHE C 566  HOH C 768  HOH C 776  LYS D 497                    
SITE     3 AD4  9 GLU D 507                                                     
SITE     1 AD5  2 GLU C 467  VAL C 471                                          
SITE     1 AD6  3 GLU C 473  GLU C 511  PEG C 612                               
SITE     1 AD7  8 PRO C 435  PHE C 501  ASN C 503  GLU C 507                    
SITE     2 AD7  8 VAL C 508  LYS C 509  GOL C 605  HOH C 733                    
SITE     1 AD8  4 ASN C 503  LYS C 509  GOL C 604  HOH C 703                    
SITE     1 AD9  4 ILE C 450  ALA C 454  ILE C 461  LYS C 462                    
SITE     1 AE1  5 ARG C 523  GLY C 526  LYS C 527  HOH C 709                    
SITE     2 AE1  5 HOH C 751                                                     
SITE     1 AE2  5 PRO C 517  SER C 518  SER C 519  GLU C 555                    
SITE     2 AE2  5 HOH C 800                                                     
SITE     1 AE3  3 GLN C 452  ARG C 455  PHE C 456                               
SITE     1 AE4  7 HIS C 449  GLN C 452  LYS C 495  GLU C 498                    
SITE     2 AE4  7 HOH C 752  ARG D 573  GLU D 577                               
SITE     1 AE5  7 ASN C 500  PHE C 502  ASN C 503  GLU C 506                    
SITE     2 AE5  7 HOH C 713  HOH C 761  HOH C 772                               
SITE     1 AE6  6 GLU C 511  HIS C 513  ILE C 558  ARG C 560                    
SITE     2 AE6  6 GOL C 603  HOH C 812                                          
SITE     1 AE7  7 ASN C 503  LYS C 505  GLU C 507  LYS C 509                    
SITE     2 AE7  7 HIS C 564  HOH C 701  HOH C 710                               
SITE     1 AE8  6 VAL C 545  PRO C 546  ASP C 548  GLN C 549                    
SITE     2 AE8  6 HOH C 702  HOH C 725                                          
SITE     1 AE9  4 ALA D 454  SER D 460  ILE D 461  LYS D 462                    
SITE     1 AF1  6 ARG C 573  LYS C 574  GLU C 577  LYS D 495                    
SITE     2 AF1  6 GLU D 498  HOH D 726                                          
SITE     1 AF2  3 PHE D 433  GLU D 473  GLU D 511                               
SITE     1 AF3  4 ILE D 463  PRO D 465  ALA D 466  ARG D 474                    
SITE     1 AF4  6 LYS C 497  THR D 539  HIS D 564  ALA D 567                    
SITE     2 AF4  6 HOH D 701  HOH D 703                                          
SITE     1 AF5  4 ASN D 431  HIS D 513  ARG D 515  HOH D 702                    
CRYST1   76.880   62.380   85.740  90.00  91.32  90.00 P 1 21 1      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      0.013007  0.000000  0.000300        0.00000                         
SCALE2      0.000000  0.016031  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011666        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system