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Database: PDB
Entry: 5HFU
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HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       07-JAN-16   5HFU              
TITLE     CRYSTAL STRUCTURE OF HUMAN HEXOKINASE 2 WITH CMPD 27, A 2-AMIDO-6-    
TITLE    2 BENZENESULFONAMIDE GLUCOSAMINE                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEXOKINASE-2;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HEXOKINASE TYPE II,HK II,MUSCLE FORM HEXOKINASE;            
COMPND   5 EC: 2.7.1.1;                                                         
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: HK2;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    METABOLISM, INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE INHIBITOR      
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.CAMPOBASSO,B.ZHAO,A.SMALLWOOD                                       
REVDAT   1   30-MAR-16 5HFU    0                                                
JRNL        AUTH   H.LIN,J.ZENG,R.XIE,M.J.SCHULZ,R.TEDESCO,J.QU,K.F.ERHARD,     
JRNL        AUTH 2 J.F.MACK,K.RAHA,A.R.RENDINA,L.M.SZEWCZUK,P.M.KRATZ,          
JRNL        AUTH 3 A.J.JUREWICZ,T.CECCONIE,S.MARTENS,P.J.MCDEVITT,J.D.MARTIN,   
JRNL        AUTH 4 S.B.CHEN,Y.JIANG,L.NICKELS,B.J.SCHWARTZ,A.SMALLWOOD,B.ZHAO,  
JRNL        AUTH 5 N.CAMPOBASSO,Y.QIAN,J.BRIAND,C.M.ROMINGER,C.OLEYKOWSKI,      
JRNL        AUTH 6 M.A.HARDWICKE,J.I.LUENGO                                     
JRNL        TITL   DISCOVERY OF A NOVEL 2,6-DISUBSTITUTED GLUCOSAMINE SERIES OF 
JRNL        TITL 2 POTENT AND SELECTIVE HEXOKINASE 2 INHIBITORS.                
JRNL        REF    ACS MED.CHEM.LETT.            V.   7   217 2016              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   26985301                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.5B00214                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.92 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.92                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 113.64                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 49178                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.880                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2398                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.260           
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  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      :  0.009          14138                                  
REMARK   3   ANGLE     :  1.245          19063                                  
REMARK   3   CHIRALITY :  0.061           2133                                  
REMARK   3   PLANARITY :  0.007           2505                                  
REMARK   3   DIHEDRAL  : 14.545           8451                                  
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 5HFU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000216941.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5 - 6                              
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9787                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49230                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.920                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 113.640                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 10MGS/ML IN 50MM TRISHCL PH =   
REMARK 280  7.5, 250MM NACL, 2MM DTT, 2MM MGCL2 WELL SOLUTION: 0.1M NA          
REMARK 280  CITRATE PH = 6, 16 % PEG3350, 10 % ETHYLENE GLYCOL CRYO: 20 %       
REMARK 280  ETHYLENE GLYCOL IN WELL, PH 6, VAPOR DIFFUSION, TEMPERATURE 296K    
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       77.49300            
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                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     ASN A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     TYR A    12                                                      
REMARK 465     PHE A    13                                                      
REMARK 465     GLN A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     ARG A   912                                                      
REMARK 465     GLU A   913                                                      
REMARK 465     ALA A   914                                                      
REMARK 465     GLY A   915                                                      
REMARK 465     GLN A   916                                                      
REMARK 465     ARG A   917                                                      
REMARK 465     MET B    -5                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     SER B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     HIS B     1                                                      
REMARK 465     HIS B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     GLU B     9                                                      
REMARK 465     ASN B    10                                                      
REMARK 465     LEU B    11                                                      
REMARK 465     TYR B    12                                                      
REMARK 465     PHE B    13                                                      
REMARK 465     GLN B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     ALA B   914                                                      
REMARK 465     GLY B   915                                                      
REMARK 465     GLN B   916                                                      
REMARK 465     ARG B   917                                                      
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     THR A  88    OG1  CG2                                            
REMARK 470     ASN A  89    CG   OD1  ND2                                       
REMARK 470     ILE A 114    CG1  CG2  CD1                                       
REMARK 470     GLU A 116    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 120    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 132    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 136    CG   OD1  ND2                                       
REMARK 470     LYS A 173    CG   CD   CE   NZ                                   
REMARK 470     LYS A 176    CG   CD   CE   NZ                                   
REMARK 470     LYS A 191    CG   CD   CE   NZ                                   
REMARK 470     GLN A 279    OE1  NE2                                            
REMARK 470     GLU A 345    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 365    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 366    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 404    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 472    CG   CD   CE   NZ                                   
REMARK 470     LYS A 501    CD   CE   NZ                                        
REMARK 470     LYS A 525    CG   CD   CE   NZ                                   
REMARK 470     ILE A 562    CG1  CG2  CD1                                       
REMARK 470     GLU A 565    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 592    CB   CG   CD   CE   NZ                              
REMARK 470     LYS A 624    CG   CD   CE   NZ                                   
REMARK 470     GLU A 645    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 646    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 649    CD1  CD2                                            
REMARK 470     GLU A 668    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 697    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 774    OE1  OE2                                            
REMARK 470     LYS A 855    NZ                                                  
REMARK 470     LYS A 873    CD   CE   NZ                                        
REMARK 470     LYS A 880    NZ                                                  
REMARK 470     LYS B  21    CD   CE   NZ                                        
REMARK 470     LYS B  41    CD   CE   NZ                                        
REMARK 470     LYS B  45    CD   CE   NZ                                        
REMARK 470     GLU B 116    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 120    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 173    CD   CE   NZ                                        
REMARK 470     LYS B 176    CG   CD   CE   NZ                                   
REMARK 470     LYS B 346    CD   CE   NZ                                        
REMARK 470     GLU B 404    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 425    CD   CE   NZ                                        
REMARK 470     LYS B 472    CG   CD   CE   NZ                                   
REMARK 470     THR B 536    OG1  CG2                                            
REMARK 470     ASN B 537    CG   OD1  ND2                                       
REMARK 470     ARG B 544    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 549    CD   CE   NZ                                        
REMARK 470     GLU B 587    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 592    CB   CG   CD   CE   NZ                              
REMARK 470     LYS B 624    CG   CD   CE   NZ                                   
REMARK 470     GLU B 645    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 646    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 649    CD2                                                 
REMARK 470     GLU B 668    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 697    OE1  OE2                                            
REMARK 470     GLU B 700    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 769    NE   CZ   NH1  NH2                                  
REMARK 470     ARG B 771    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 805    CD   OE1  NE2                                       
REMARK 470     GLU B 810    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 873    CD   CE   NZ                                        
REMARK 470     LYS B 880    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   OE1  GLU B   673     NH2  ARG B   849              2.14            
REMARK 500   O    ASP A   793     NZ   LYS A   820              2.17            
REMARK 500   OD1  ASN B    89     O    HOH B  1101              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 494   CD    GLU A 494   OE1    -0.067                       
REMARK 500    GLU A 502   CD    GLU A 502   OE1    -0.079                       
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    GLN A 142   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500    ARG A 307   CG  -  CD  -  NE  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    PHE A 423   CB  -  CG  -  CD1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    PRO A 508   C   -  N   -  CD  ANGL. DEV. = -14.7 DEGREES          
REMARK 500    ASP A 669   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG B 407   CG  -  CD  -  NE  ANGL. DEV. = -12.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  88      -16.50     67.06                                   
REMARK 500    GLN A 142      -21.49     87.57                                   
REMARK 500    GLU A 446      -68.83    -93.04                                   
REMARK 500    TRP A 550     -135.77     57.98                                   
REMARK 500    CYS A 628      -62.09   -107.12                                   
REMARK 500    GLU A 645       81.38     60.25                                   
REMARK 500    GLN A 739       38.40     70.12                                   
REMARK 500    LEU A 795     -117.36     52.10                                   
REMARK 500    GLU A 894       81.63     68.02                                   
REMARK 500    ASP A 895       39.25     72.70                                   
REMARK 500    SER A 897      -72.92    -53.40                                   
REMARK 500    VAL B 180      -53.74   -129.35                                   
REMARK 500    ASP B 202     -153.67    -91.79                                   
REMARK 500    ILE B 297      -59.40   -121.07                                   
REMARK 500    LYS B 549      -34.39     74.25                                   
REMARK 500    GLU B 645      -25.32     72.59                                   
REMARK 500    ASP B 669      131.08   -174.33                                   
REMARK 500    LEU B 795     -126.76     56.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN A  142     ILE A  143                 -149.25                    
REMARK 500 LEU A  150     GLY A  151                   34.61                    
REMARK 500 GLY A  679     THR A  680                  146.97                    
REMARK 500 PHE B  154     SER B  155                  144.96                    
REMARK 500 GLU B  646     PHE B  647                 -149.77                    
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 603 A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 603 A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 603 B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 603 B 1002                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5HEX   RELATED DB: PDB                                   
DBREF  5HFU A   17   917  UNP    P52789   HXK2_HUMAN      17    917             
DBREF  5HFU B   17   917  UNP    P52789   HXK2_HUMAN      17    917             
SEQADV 5HFU MET A   -5  UNP  P52789              INITIATING METHIONINE          
SEQADV 5HFU GLY A   -4  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU SER A   -3  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU SER A   -2  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU HIS A   -1  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU HIS A    0  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU HIS A    1  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU HIS A    2  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU HIS A    3  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU HIS A    4  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU SER A    5  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU SER A    6  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU GLY A    7  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU LEU A    8  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU GLU A    9  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU ASN A   10  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU LEU A   11  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU TYR A   12  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU PHE A   13  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU GLN A   14  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU GLY A   15  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU SER A   16  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU MET B   -5  UNP  P52789              INITIATING METHIONINE          
SEQADV 5HFU GLY B   -4  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU SER B   -3  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU SER B   -2  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU HIS B   -1  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU HIS B    0  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU HIS B    1  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU HIS B    2  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU HIS B    3  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU HIS B    4  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU SER B    5  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU SER B    6  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU GLY B    7  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU LEU B    8  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU GLU B    9  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU ASN B   10  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU LEU B   11  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU TYR B   12  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU PHE B   13  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU GLN B   14  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU GLY B   15  UNP  P52789              EXPRESSION TAG                 
SEQADV 5HFU SER B   16  UNP  P52789              EXPRESSION TAG                 
SEQRES   1 A  923  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  923  LEU GLU ASN LEU TYR PHE GLN GLY SER ASP GLN VAL GLN          
SEQRES   3 A  923  LYS VAL ASP GLN TYR LEU TYR HIS MET ARG LEU SER ASP          
SEQRES   4 A  923  GLU THR LEU LEU GLU ILE SER LYS ARG PHE ARG LYS GLU          
SEQRES   5 A  923  MET GLU LYS GLY LEU GLY ALA THR THR HIS PRO THR ALA          
SEQRES   6 A  923  ALA VAL LYS MET LEU PRO THR PHE VAL ARG SER THR PRO          
SEQRES   7 A  923  ASP GLY THR GLU HIS GLY GLU PHE LEU ALA LEU ASP LEU          
SEQRES   8 A  923  GLY GLY THR ASN PHE ARG VAL LEU TRP VAL LYS VAL THR          
SEQRES   9 A  923  ASP ASN GLY LEU GLN LYS VAL GLU MET GLU ASN GLN ILE          
SEQRES  10 A  923  TYR ALA ILE PRO GLU ASP ILE MET ARG GLY SER GLY THR          
SEQRES  11 A  923  GLN LEU PHE ASP HIS ILE ALA GLU CYS LEU ALA ASN PHE          
SEQRES  12 A  923  MET ASP LYS LEU GLN ILE LYS ASP LYS LYS LEU PRO LEU          
SEQRES  13 A  923  GLY PHE THR PHE SER PHE PRO CYS HIS GLN THR LYS LEU          
SEQRES  14 A  923  ASP GLU SER PHE LEU VAL SER TRP THR LYS GLY PHE LYS          
SEQRES  15 A  923  SER SER GLY VAL GLU GLY ARG ASP VAL VAL ALA LEU ILE          
SEQRES  16 A  923  ARG LYS ALA ILE GLN ARG ARG GLY ASP PHE ASP ILE ASP          
SEQRES  17 A  923  ILE VAL ALA VAL VAL ASN ASP THR VAL GLY THR MET MET          
SEQRES  18 A  923  THR CYS GLY TYR ASP ASP HIS ASN CYS GLU ILE GLY LEU          
SEQRES  19 A  923  ILE VAL GLY THR GLY SER ASN ALA CYS TYR MET GLU GLU          
SEQRES  20 A  923  MET ARG HIS ILE ASP MET VAL GLU GLY ASP GLU GLY ARG          
SEQRES  21 A  923  MET CYS ILE ASN MET GLU TRP GLY ALA PHE GLY ASP ASP          
SEQRES  22 A  923  GLY SER LEU ASN ASP ILE ARG THR GLU PHE ASP GLN GLU          
SEQRES  23 A  923  ILE ASP MET GLY SER LEU ASN PRO GLY LYS GLN LEU PHE          
SEQRES  24 A  923  GLU LYS MET ILE SER GLY MET TYR MET GLY GLU LEU VAL          
SEQRES  25 A  923  ARG LEU ILE LEU VAL LYS MET ALA LYS GLU GLU LEU LEU          
SEQRES  26 A  923  PHE GLY GLY LYS LEU SER PRO GLU LEU LEU ASN THR GLY          
SEQRES  27 A  923  ARG PHE GLU THR LYS ASP ILE SER ASP ILE GLU GLY GLU          
SEQRES  28 A  923  LYS ASP GLY ILE ARG LYS ALA ARG GLU VAL LEU MET ARG          
SEQRES  29 A  923  LEU GLY LEU ASP PRO THR GLN GLU ASP CYS VAL ALA THR          
SEQRES  30 A  923  HIS ARG ILE CYS GLN ILE VAL SER THR ARG SER ALA SER          
SEQRES  31 A  923  LEU CYS ALA ALA THR LEU ALA ALA VAL LEU GLN ARG ILE          
SEQRES  32 A  923  LYS GLU ASN LYS GLY GLU GLU ARG LEU ARG SER THR ILE          
SEQRES  33 A  923  GLY VAL ASP GLY SER VAL TYR LYS LYS HIS PRO HIS PHE          
SEQRES  34 A  923  ALA LYS ARG LEU HIS LYS THR VAL ARG ARG LEU VAL PRO          
SEQRES  35 A  923  GLY CYS ASP VAL ARG PHE LEU ARG SER GLU ASP GLY SER          
SEQRES  36 A  923  GLY LYS GLY ALA ALA MET VAL THR ALA VAL ALA TYR ARG          
SEQRES  37 A  923  LEU ALA ASP GLN HIS ARG ALA ARG GLN LYS THR LEU GLU          
SEQRES  38 A  923  HIS LEU GLN LEU SER HIS ASP GLN LEU LEU GLU VAL LYS          
SEQRES  39 A  923  ARG ARG MET LYS VAL GLU MET GLU ARG GLY LEU SER LYS          
SEQRES  40 A  923  GLU THR HIS ALA SER ALA PRO VAL LYS MET LEU PRO THR          
SEQRES  41 A  923  TYR VAL CYS ALA THR PRO ASP GLY THR GLU LYS GLY ASP          
SEQRES  42 A  923  PHE LEU ALA LEU ASP LEU GLY GLY THR ASN PHE ARG VAL          
SEQRES  43 A  923  LEU LEU VAL ARG VAL ARG ASN GLY LYS TRP GLY GLY VAL          
SEQRES  44 A  923  GLU MET HIS ASN LYS ILE TYR ALA ILE PRO GLN GLU VAL          
SEQRES  45 A  923  MET HIS GLY THR GLY ASP GLU LEU PHE ASP HIS ILE VAL          
SEQRES  46 A  923  GLN CYS ILE ALA ASP PHE LEU GLU TYR MET GLY MET LYS          
SEQRES  47 A  923  GLY VAL SER LEU PRO LEU GLY PHE THR PHE SER PHE PRO          
SEQRES  48 A  923  CYS GLN GLN ASN SER LEU ASP GLU SER ILE LEU LEU LYS          
SEQRES  49 A  923  TRP THR LYS GLY PHE LYS ALA SER GLY CYS GLU GLY GLU          
SEQRES  50 A  923  ASP VAL VAL THR LEU LEU LYS GLU ALA ILE HIS ARG ARG          
SEQRES  51 A  923  GLU GLU PHE ASP LEU ASP VAL VAL ALA VAL VAL ASN ASP          
SEQRES  52 A  923  THR VAL GLY THR MET MET THR CYS GLY PHE GLU ASP PRO          
SEQRES  53 A  923  HIS CYS GLU VAL GLY LEU ILE VAL GLY THR GLY SER ASN          
SEQRES  54 A  923  ALA CYS TYR MET GLU GLU MET ARG ASN VAL GLU LEU VAL          
SEQRES  55 A  923  GLU GLY GLU GLU GLY ARG MET CYS VAL ASN MET GLU TRP          
SEQRES  56 A  923  GLY ALA PHE GLY ASP ASN GLY CYS LEU ASP ASP PHE ARG          
SEQRES  57 A  923  THR GLU PHE ASP VAL ALA VAL ASP GLU LEU SER LEU ASN          
SEQRES  58 A  923  PRO GLY LYS GLN ARG PHE GLU LYS MET ILE SER GLY MET          
SEQRES  59 A  923  TYR LEU GLY GLU ILE VAL ARG ASN ILE LEU ILE ASP PHE          
SEQRES  60 A  923  THR LYS ARG GLY LEU LEU PHE ARG GLY ARG ILE SER GLU          
SEQRES  61 A  923  ARG LEU LYS THR ARG GLY ILE PHE GLU THR LYS PHE LEU          
SEQRES  62 A  923  SER GLN ILE GLU SER ASP CYS LEU ALA LEU LEU GLN VAL          
SEQRES  63 A  923  ARG ALA ILE LEU GLN HIS LEU GLY LEU GLU SER THR CYS          
SEQRES  64 A  923  ASP ASP SER ILE ILE VAL LYS GLU VAL CYS THR VAL VAL          
SEQRES  65 A  923  ALA ARG ARG ALA ALA GLN LEU CYS GLY ALA GLY MET ALA          
SEQRES  66 A  923  ALA VAL VAL ASP ARG ILE ARG GLU ASN ARG GLY LEU ASP          
SEQRES  67 A  923  ALA LEU LYS VAL THR VAL GLY VAL ASP GLY THR LEU TYR          
SEQRES  68 A  923  LYS LEU HIS PRO HIS PHE ALA LYS VAL MET HIS GLU THR          
SEQRES  69 A  923  VAL LYS ASP LEU ALA PRO LYS CYS ASP VAL SER PHE LEU          
SEQRES  70 A  923  GLN SER GLU ASP GLY SER GLY LYS GLY ALA ALA LEU ILE          
SEQRES  71 A  923  THR ALA VAL ALA CYS ARG ILE ARG GLU ALA GLY GLN ARG          
SEQRES   1 B  923  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  923  LEU GLU ASN LEU TYR PHE GLN GLY SER ASP GLN VAL GLN          
SEQRES   3 B  923  LYS VAL ASP GLN TYR LEU TYR HIS MET ARG LEU SER ASP          
SEQRES   4 B  923  GLU THR LEU LEU GLU ILE SER LYS ARG PHE ARG LYS GLU          
SEQRES   5 B  923  MET GLU LYS GLY LEU GLY ALA THR THR HIS PRO THR ALA          
SEQRES   6 B  923  ALA VAL LYS MET LEU PRO THR PHE VAL ARG SER THR PRO          
SEQRES   7 B  923  ASP GLY THR GLU HIS GLY GLU PHE LEU ALA LEU ASP LEU          
SEQRES   8 B  923  GLY GLY THR ASN PHE ARG VAL LEU TRP VAL LYS VAL THR          
SEQRES   9 B  923  ASP ASN GLY LEU GLN LYS VAL GLU MET GLU ASN GLN ILE          
SEQRES  10 B  923  TYR ALA ILE PRO GLU ASP ILE MET ARG GLY SER GLY THR          
SEQRES  11 B  923  GLN LEU PHE ASP HIS ILE ALA GLU CYS LEU ALA ASN PHE          
SEQRES  12 B  923  MET ASP LYS LEU GLN ILE LYS ASP LYS LYS LEU PRO LEU          
SEQRES  13 B  923  GLY PHE THR PHE SER PHE PRO CYS HIS GLN THR LYS LEU          
SEQRES  14 B  923  ASP GLU SER PHE LEU VAL SER TRP THR LYS GLY PHE LYS          
SEQRES  15 B  923  SER SER GLY VAL GLU GLY ARG ASP VAL VAL ALA LEU ILE          
SEQRES  16 B  923  ARG LYS ALA ILE GLN ARG ARG GLY ASP PHE ASP ILE ASP          
SEQRES  17 B  923  ILE VAL ALA VAL VAL ASN ASP THR VAL GLY THR MET MET          
SEQRES  18 B  923  THR CYS GLY TYR ASP ASP HIS ASN CYS GLU ILE GLY LEU          
SEQRES  19 B  923  ILE VAL GLY THR GLY SER ASN ALA CYS TYR MET GLU GLU          
SEQRES  20 B  923  MET ARG HIS ILE ASP MET VAL GLU GLY ASP GLU GLY ARG          
SEQRES  21 B  923  MET CYS ILE ASN MET GLU TRP GLY ALA PHE GLY ASP ASP          
SEQRES  22 B  923  GLY SER LEU ASN ASP ILE ARG THR GLU PHE ASP GLN GLU          
SEQRES  23 B  923  ILE ASP MET GLY SER LEU ASN PRO GLY LYS GLN LEU PHE          
SEQRES  24 B  923  GLU LYS MET ILE SER GLY MET TYR MET GLY GLU LEU VAL          
SEQRES  25 B  923  ARG LEU ILE LEU VAL LYS MET ALA LYS GLU GLU LEU LEU          
SEQRES  26 B  923  PHE GLY GLY LYS LEU SER PRO GLU LEU LEU ASN THR GLY          
SEQRES  27 B  923  ARG PHE GLU THR LYS ASP ILE SER ASP ILE GLU GLY GLU          
SEQRES  28 B  923  LYS ASP GLY ILE ARG LYS ALA ARG GLU VAL LEU MET ARG          
SEQRES  29 B  923  LEU GLY LEU ASP PRO THR GLN GLU ASP CYS VAL ALA THR          
SEQRES  30 B  923  HIS ARG ILE CYS GLN ILE VAL SER THR ARG SER ALA SER          
SEQRES  31 B  923  LEU CYS ALA ALA THR LEU ALA ALA VAL LEU GLN ARG ILE          
SEQRES  32 B  923  LYS GLU ASN LYS GLY GLU GLU ARG LEU ARG SER THR ILE          
SEQRES  33 B  923  GLY VAL ASP GLY SER VAL TYR LYS LYS HIS PRO HIS PHE          
SEQRES  34 B  923  ALA LYS ARG LEU HIS LYS THR VAL ARG ARG LEU VAL PRO          
SEQRES  35 B  923  GLY CYS ASP VAL ARG PHE LEU ARG SER GLU ASP GLY SER          
SEQRES  36 B  923  GLY LYS GLY ALA ALA MET VAL THR ALA VAL ALA TYR ARG          
SEQRES  37 B  923  LEU ALA ASP GLN HIS ARG ALA ARG GLN LYS THR LEU GLU          
SEQRES  38 B  923  HIS LEU GLN LEU SER HIS ASP GLN LEU LEU GLU VAL LYS          
SEQRES  39 B  923  ARG ARG MET LYS VAL GLU MET GLU ARG GLY LEU SER LYS          
SEQRES  40 B  923  GLU THR HIS ALA SER ALA PRO VAL LYS MET LEU PRO THR          
SEQRES  41 B  923  TYR VAL CYS ALA THR PRO ASP GLY THR GLU LYS GLY ASP          
SEQRES  42 B  923  PHE LEU ALA LEU ASP LEU GLY GLY THR ASN PHE ARG VAL          
SEQRES  43 B  923  LEU LEU VAL ARG VAL ARG ASN GLY LYS TRP GLY GLY VAL          
SEQRES  44 B  923  GLU MET HIS ASN LYS ILE TYR ALA ILE PRO GLN GLU VAL          
SEQRES  45 B  923  MET HIS GLY THR GLY ASP GLU LEU PHE ASP HIS ILE VAL          
SEQRES  46 B  923  GLN CYS ILE ALA ASP PHE LEU GLU TYR MET GLY MET LYS          
SEQRES  47 B  923  GLY VAL SER LEU PRO LEU GLY PHE THR PHE SER PHE PRO          
SEQRES  48 B  923  CYS GLN GLN ASN SER LEU ASP GLU SER ILE LEU LEU LYS          
SEQRES  49 B  923  TRP THR LYS GLY PHE LYS ALA SER GLY CYS GLU GLY GLU          
SEQRES  50 B  923  ASP VAL VAL THR LEU LEU LYS GLU ALA ILE HIS ARG ARG          
SEQRES  51 B  923  GLU GLU PHE ASP LEU ASP VAL VAL ALA VAL VAL ASN ASP          
SEQRES  52 B  923  THR VAL GLY THR MET MET THR CYS GLY PHE GLU ASP PRO          
SEQRES  53 B  923  HIS CYS GLU VAL GLY LEU ILE VAL GLY THR GLY SER ASN          
SEQRES  54 B  923  ALA CYS TYR MET GLU GLU MET ARG ASN VAL GLU LEU VAL          
SEQRES  55 B  923  GLU GLY GLU GLU GLY ARG MET CYS VAL ASN MET GLU TRP          
SEQRES  56 B  923  GLY ALA PHE GLY ASP ASN GLY CYS LEU ASP ASP PHE ARG          
SEQRES  57 B  923  THR GLU PHE ASP VAL ALA VAL ASP GLU LEU SER LEU ASN          
SEQRES  58 B  923  PRO GLY LYS GLN ARG PHE GLU LYS MET ILE SER GLY MET          
SEQRES  59 B  923  TYR LEU GLY GLU ILE VAL ARG ASN ILE LEU ILE ASP PHE          
SEQRES  60 B  923  THR LYS ARG GLY LEU LEU PHE ARG GLY ARG ILE SER GLU          
SEQRES  61 B  923  ARG LEU LYS THR ARG GLY ILE PHE GLU THR LYS PHE LEU          
SEQRES  62 B  923  SER GLN ILE GLU SER ASP CYS LEU ALA LEU LEU GLN VAL          
SEQRES  63 B  923  ARG ALA ILE LEU GLN HIS LEU GLY LEU GLU SER THR CYS          
SEQRES  64 B  923  ASP ASP SER ILE ILE VAL LYS GLU VAL CYS THR VAL VAL          
SEQRES  65 B  923  ALA ARG ARG ALA ALA GLN LEU CYS GLY ALA GLY MET ALA          
SEQRES  66 B  923  ALA VAL VAL ASP ARG ILE ARG GLU ASN ARG GLY LEU ASP          
SEQRES  67 B  923  ALA LEU LYS VAL THR VAL GLY VAL ASP GLY THR LEU TYR          
SEQRES  68 B  923  LYS LEU HIS PRO HIS PHE ALA LYS VAL MET HIS GLU THR          
SEQRES  69 B  923  VAL LYS ASP LEU ALA PRO LYS CYS ASP VAL SER PHE LEU          
SEQRES  70 B  923  GLN SER GLU ASP GLY SER GLY LYS GLY ALA ALA LEU ILE          
SEQRES  71 B  923  THR ALA VAL ALA CYS ARG ILE ARG GLU ALA GLY GLN ARG          
HET    603  A1001      37                                                       
HET    603  A1002      37                                                       
HET    603  B1001      37                                                       
HET    603  B1002      37                                                       
HETNAM     603 ~{N}-[(2~{S},3~{R},4~{R},5~{S},6~{R})-6-[[(4-                    
HETNAM   2 603  CYANOPHENYL)SULFONYLAMINO]METHYL]-2,4,5-                        
HETNAM   3 603  TRIS(OXIDANYL)OXAN-3-YL]-3-PHENYL-BENZAMIDE                     
FORMUL   3  603    4(C26 H25 N3 O7 S)                                           
FORMUL   7  HOH   *57(H2 O)                                                     
HELIX    1 AA1 ASP A   17  LEU A   26  1                                  10    
HELIX    2 AA2 TYR A   27  ARG A   30  5                                   4    
HELIX    3 AA3 SER A   32  GLY A   52  1                                  21    
HELIX    4 AA4 THR A   55  ALA A   59  5                                   5    
HELIX    5 AA5 PRO A  115  ARG A  120  1                                   6    
HELIX    6 AA6 SER A  122  LEU A  141  1                                  20    
HELIX    7 AA7 ASP A  184  GLY A  197  1                                  14    
HELIX    8 AA8 ASN A  208  ASP A  221  1                                  14    
HELIX    9 AA9 ARG A  243  ILE A  245  5                                   3    
HELIX   10 AB1 GLU A  260  PHE A  264  5                                   5    
HELIX   11 AB2 THR A  275  GLY A  284  1                                  10    
HELIX   12 AB3 GLN A  291  SER A  298  1                                   8    
HELIX   13 AB4 SER A  298  GLU A  316  1                                  19    
HELIX   14 AB5 LEU A  319  LYS A  323  5                                   5    
HELIX   15 AB6 GLU A  335  GLU A  345  1                                  11    
HELIX   16 AB7 ASP A  347  LEU A  359  1                                  13    
HELIX   17 AB8 THR A  364  GLY A  402  1                                  39    
HELIX   18 AB9 GLY A  414  HIS A  420  1                                   7    
HELIX   19 AC1 HIS A  422  VAL A  435  1                                  14    
HELIX   20 AC2 GLY A  448  LEU A  474  1                                  27    
HELIX   21 AC3 SER A  480  SER A  500  1                                  21    
HELIX   22 AC4 PRO A  563  HIS A  568  1                                   6    
HELIX   23 AC5 THR A  570  MET A  589  1                                  20    
HELIX   24 AC6 ASP A  632  ARG A  643  1                                  12    
HELIX   25 AC7 ASN A  656  ASP A  669  1                                  14    
HELIX   26 AC8 ARG A  691  VAL A  693  5                                   3    
HELIX   27 AC9 GLU A  708  PHE A  712  5                                   5    
HELIX   28 AD1 THR A  723  SER A  733  1                                  11    
HELIX   29 AD2 GLN A  739  SER A  746  1                                   8    
HELIX   30 AD3 MET A  748  ARG A  764  1                                  17    
HELIX   31 AD4 LEU A  767  ARG A  771  5                                   5    
HELIX   32 AD5 SER A  773  THR A  778  1                                   6    
HELIX   33 AD6 GLU A  783  ASP A  793  1                                  11    
HELIX   34 AD7 LEU A  797  LEU A  807  1                                  11    
HELIX   35 AD8 THR A  812  GLY A  850  1                                  39    
HELIX   36 AD9 GLY A  862  HIS A  868  1                                   7    
HELIX   37 AE1 HIS A  870  ALA A  883  1                                  14    
HELIX   38 AE2 GLY A  898  ARG A  910  1                                  13    
HELIX   39 AE3 GLN B   18  LEU B   26  1                                   9    
HELIX   40 AE4 TYR B   27  ARG B   30  5                                   4    
HELIX   41 AE5 SER B   32  GLY B   52  1                                  21    
HELIX   42 AE6 PRO B  115  GLY B  121  1                                   7    
HELIX   43 AE7 SER B  122  LEU B  141  1                                  20    
HELIX   44 AE8 ASP B  184  GLY B  197  1                                  14    
HELIX   45 AE9 ASP B  209  ASP B  221  1                                  13    
HELIX   46 AF1 ARG B  243  ILE B  245  5                                   3    
HELIX   47 AF2 GLU B  260  PHE B  264  5                                   5    
HELIX   48 AF3 THR B  275  GLY B  284  1                                  10    
HELIX   49 AF4 PHE B  293  ILE B  297  5                                   5    
HELIX   50 AF5 TYR B  301  GLU B  316  1                                  16    
HELIX   51 AF6 LEU B  319  LYS B  323  5                                   5    
HELIX   52 AF7 GLU B  335  GLY B  344  1                                  10    
HELIX   53 AF8 GLY B  348  LEU B  359  1                                  12    
HELIX   54 AF9 THR B  364  GLY B  402  1                                  39    
HELIX   55 AG1 GLY B  414  HIS B  420  1                                   7    
HELIX   56 AG2 HIS B  422  VAL B  435  1                                  14    
HELIX   57 AG3 GLY B  448  GLU B  475  1                                  28    
HELIX   58 AG4 HIS B  476  GLN B  478  5                                   3    
HELIX   59 AG5 SER B  480  SER B  500  1                                  21    
HELIX   60 AG6 PRO B  563  HIS B  568  1                                   6    
HELIX   61 AG7 THR B  570  TYR B  588  1                                  19    
HELIX   62 AG8 ASP B  632  ARG B  643  1                                  12    
HELIX   63 AG9 ASN B  656  PHE B  667  1                                  12    
HELIX   64 AH1 GLU B  708  PHE B  712  5                                   5    
HELIX   65 AH2 LEU B  718  ARG B  722  5                                   5    
HELIX   66 AH3 THR B  723  LEU B  732  1                                  10    
HELIX   67 AH4 PHE B  741  SER B  746  1                                   6    
HELIX   68 AH5 SER B  746  ARG B  764  1                                  19    
HELIX   69 AH6 LEU B  767  ARG B  771  5                                   5    
HELIX   70 AH7 GLU B  774  THR B  778  5                                   5    
HELIX   71 AH8 GLU B  783  ASP B  793  1                                  11    
HELIX   72 AH9 LEU B  797  LEU B  807  1                                  11    
HELIX   73 AI1 THR B  812  ARG B  849  1                                  38    
HELIX   74 AI2 GLY B  862  HIS B  868  1                                   7    
HELIX   75 AI3 HIS B  870  ALA B  883  1                                  14    
HELIX   76 AI4 GLY B  898  ARG B  912  1                                  15    
SHEET    1 AA1 6 LEU A  64  PRO A  65  0                                        
SHEET    2 AA1 6 ARG A 254  ASN A 258 -1  O  ASN A 258   N  LEU A  64           
SHEET    3 AA1 6 SER A 234  GLU A 241 -1  N  GLU A 240   O  MET A 255           
SHEET    4 AA1 6 CYS A 224  VAL A 230 -1  N  ILE A 229   O  ASN A 235           
SHEET    5 AA1 6 LEU A 406  ASP A 413  1  O  GLY A 411   N  ILE A 226           
SHEET    6 AA1 6 CYS A 438  ARG A 444  1  O  ASP A 439   N  LEU A 406           
SHEET    1 AA2 5 GLU A 106  TYR A 112  0                                        
SHEET    2 AA2 5 PHE A  90  VAL A  97 -1  N  LYS A  96   O  GLU A 106           
SHEET    3 AA2 5 GLY A  78  LEU A  85 -1  N  GLY A  78   O  VAL A  97           
SHEET    4 AA2 5 LEU A 148  PHE A 154  1  O  GLY A 151   N  LEU A  83           
SHEET    5 AA2 5 ILE A 201  VAL A 206  1  O  ASP A 202   N  LEU A 148           
SHEET    1 AA3 2 CYS A 158  LYS A 162  0                                        
SHEET    2 AA3 2 GLU A 165  LEU A 168 -1  O  PHE A 167   N  HIS A 159           
SHEET    1 AA4 6 LEU A 512  PRO A 513  0                                        
SHEET    2 AA4 6 ARG A 702  ASN A 706 -1  O  ASN A 706   N  LEU A 512           
SHEET    3 AA4 6 SER A 682  GLU A 689 -1  N  GLU A 688   O  MET A 703           
SHEET    4 AA4 6 CYS A 672  VAL A 678 -1  N  ILE A 677   O  ASN A 683           
SHEET    5 AA4 6 LEU A 854  ASP A 861  1  O  GLY A 859   N  VAL A 674           
SHEET    6 AA4 6 CYS A 886  GLN A 892  1  O  ASP A 887   N  LEU A 854           
SHEET    1 AA5 5 GLY A 552  ALA A 561  0                                        
SHEET    2 AA5 5 ASN A 537  ARG A 546 -1  N  LEU A 542   O  HIS A 556           
SHEET    3 AA5 5 GLY A 526  LEU A 533 -1  N  PHE A 528   O  VAL A 543           
SHEET    4 AA5 5 PRO A 597  PHE A 602  1  O  THR A 601   N  LEU A 533           
SHEET    5 AA5 5 ASP A 650  VAL A 655  1  O  ASP A 650   N  LEU A 598           
SHEET    1 AA6 2 CYS A 606  GLN A 607  0                                        
SHEET    2 AA6 2 ILE A 615  LEU A 616 -1  O  ILE A 615   N  GLN A 607           
SHEET    1 AA7 6 LEU B  64  PRO B  65  0                                        
SHEET    2 AA7 6 ARG B 254  ASN B 258 -1  O  ASN B 258   N  LEU B  64           
SHEET    3 AA7 6 SER B 234  GLU B 241 -1  N  GLU B 240   O  MET B 255           
SHEET    4 AA7 6 CYS B 224  VAL B 230 -1  N  GLY B 227   O  CYS B 237           
SHEET    5 AA7 6 LEU B 406  ASP B 413  1  O  GLY B 411   N  LEU B 228           
SHEET    6 AA7 6 CYS B 438  ARG B 444  1  O  ARG B 441   N  ILE B 410           
SHEET    1 AA8 5 VAL B 105  ALA B 113  0                                        
SHEET    2 AA8 5 ASN B  89  VAL B  97 -1  N  TRP B  94   O  GLU B 108           
SHEET    3 AA8 5 GLY B  78  LEU B  85 -1  N  ASP B  84   O  ARG B  91           
SHEET    4 AA8 5 LEU B 148  PHE B 154  1  O  GLY B 151   N  LEU B  83           
SHEET    5 AA8 5 ILE B 201  ASN B 208  1  O  VAL B 207   N  PHE B 152           
SHEET    1 AA9 2 CYS B 158  LYS B 162  0                                        
SHEET    2 AA9 2 GLU B 165  LEU B 168 -1  O  PHE B 167   N  HIS B 159           
SHEET    1 AB1 6 LEU B 512  PRO B 513  0                                        
SHEET    2 AB1 6 ARG B 702  ASN B 706 -1  O  ASN B 706   N  LEU B 512           
SHEET    3 AB1 6 SER B 682  GLU B 689 -1  N  TYR B 686   O  VAL B 705           
SHEET    4 AB1 6 CYS B 672  VAL B 678 -1  N  ILE B 677   O  ASN B 683           
SHEET    5 AB1 6 LEU B 854  ASP B 861  1  O  GLY B 859   N  VAL B 674           
SHEET    6 AB1 6 CYS B 886  GLN B 892  1  O  ASP B 887   N  LEU B 854           
SHEET    1 AB2 5 VAL B 553  ALA B 561  0                                        
SHEET    2 AB2 5 ASN B 537  VAL B 545 -1  N  LEU B 542   O  HIS B 556           
SHEET    3 AB2 5 GLY B 526  LEU B 533 -1  N  ALA B 530   O  LEU B 541           
SHEET    4 AB2 5 PRO B 597  PHE B 602  1  O  PRO B 597   N  LEU B 529           
SHEET    5 AB2 5 ASP B 650  VAL B 655  1  O  ASP B 650   N  LEU B 598           
SHEET    1 AB3 2 CYS B 606  SER B 610  0                                        
SHEET    2 AB3 2 GLU B 613  LEU B 616 -1  O  ILE B 615   N  GLN B 607           
CISPEP   1 GLU A  645    GLU A  646          0        28.01                     
CISPEP   2 ASN B  547    GLY B  548          0         8.33                     
SITE     1 AC1 13 LYS A  62  SER A 155  PRO A 157  CYS A 158                    
SITE     2 AC1 13 ASN A 208  ASP A 209  THR A 232  GLY A 233                    
SITE     3 AC1 13 SER A 234  ASN A 235  GLU A 260  GLN A 291                    
SITE     4 AC1 13 GLU A 294                                                     
SITE     1 AC2 13 LYS A 510  LYS A 621  ASN A 656  ASP A 657                    
SITE     2 AC2 13 THR A 658  ILE A 677  THR A 680  GLY A 681                    
SITE     3 AC2 13 SER A 682  ASN A 683  GLU A 708  GLN A 739                    
SITE     4 AC2 13 GLU A 742                                                     
SITE     1 AC3 15 LYS B  62  LEU B  64  SER B 155  PRO B 157                    
SITE     2 AC3 15 CYS B 158  THR B 172  ASN B 208  ASP B 209                    
SITE     3 AC3 15 ILE B 229  THR B 232  GLY B 233  SER B 234                    
SITE     4 AC3 15 ASN B 235  GLU B 260  GLU B 294                               
SITE     1 AC4 13 LEU B 512  SER B 603  LYS B 621  ASN B 656                    
SITE     2 AC4 13 ASP B 657  THR B 658  THR B 680  GLY B 681                    
SITE     3 AC4 13 SER B 682  ASN B 683  GLU B 708  GLU B 742                    
SITE     4 AC4 13 HOH B1119                                                     
CRYST1   65.883  154.986  114.205  90.00  95.70  90.00 P 1 21 1      4          
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      0.015178  0.000000  0.001515        0.00000                         
SCALE2      0.000000  0.006452  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008800        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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