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Database: PDB
Entry: 2NZT
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Original site: 2NZT 
HEADER    TRANSFERASE                             25-NOV-06   2NZT              
TITLE     CRYSTAL STRUCTURE OF HUMAN HEXOKINASE II                              
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;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) CODON PLUS RIL;                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: P28A-LIC                                  
KEYWDS    GLUCOSE, GLUCOSE-6-PHOSPHATE, NON-PROTEIN KINASE, HEXOKINASE,         
KEYWDS   2 STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,            
KEYWDS   3 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.M.RABEH,H.ZHU,L.NEDYALKOVA,W.TEMPEL,G.WASNEY,R.LANDRY,M.VEDADI,     
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,M.SUNDSTROM,J.WEIGELT,A.BOCHKAREV,H.PARK, 
AUTHOR   3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   5   29-JUL-20 2NZT    1       COMPND REMARK HETNAM SITE                
REVDAT   4   15-JAN-20 2NZT    1       JRNL   SEQADV                            
REVDAT   3   18-OCT-17 2NZT    1       REMARK                                   
REVDAT   2   24-FEB-09 2NZT    1       VERSN                                    
REVDAT   1   05-DEC-06 2NZT    0                                                
JRNL        AUTH   M.H.NAWAZ,J.C.FERREIRA,L.NEDYALKOVA,H.ZHU,C.CARRASCO-LOPEZ,  
JRNL        AUTH 2 S.KIRMIZIALTIN,W.M.RABEH                                     
JRNL        TITL   THE CATALYTIC INACTIVATION OF THE N-HALF OF HUMAN HEXOKINASE 
JRNL        TITL 2 2 AND STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF ITS     
JRNL        TITL 3 MITOCHONDRIAL CONFORMATION.                                  
JRNL        REF    BIOSCI.REP.                   V.  38       2018              
JRNL        REFN                   ISSN 0144-8463                               
JRNL        PMID   29298880                                                     
JRNL        DOI    10.1042/BSR20171666                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC REFMAC_5.2.0019                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 83669                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : THIN SHELLS                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.490                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2083                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.51                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6156                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.48                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 0                            
REMARK   3   BIN FREE R VALUE                    : 0.3550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13309                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 140                                     
REMARK   3   SOLVENT ATOMS            : 97                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.44800                                              
REMARK   3    B22 (A**2) : -2.77700                                             
REMARK   3    B33 (A**2) : 1.32900                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.402         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.291         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.291         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.527        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13618 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  9241 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18350 ; 1.427 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22419 ; 1.349 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1725 ; 6.447 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   589 ;36.155 ;23.854       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2426 ;15.766 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   101 ;19.714 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2125 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15063 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2720 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3090 ; 0.215 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  9747 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6686 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  7619 ; 0.094 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   395 ; 0.165 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    10 ; 0.147 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    24 ; 0.333 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.195 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  8870 ; 0.713 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3588 ; 0.072 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13707 ; 1.180 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 11384 ; 0.587 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5343 ; 1.493 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  7068 ; 0.665 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4643 ; 2.336 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 11035 ; 1.120 ; 4.500       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    197       B     199      2                      
REMARK   3           1     A    197       A     199      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    B    (A):     17 ; 0.029 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):     22 ; 0.332 ; 0.500           
REMARK   3   TIGHT THERMAL      1    B (A**2):     17 ; 0.059 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    B (A**2):     22 ; 0.346 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    650       A     652      2                      
REMARK   3           1     B    650       B     652      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):     18 ; 0.042 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  2    A    (A):     14 ; 0.187 ; 0.500           
REMARK   3   TIGHT THERMAL      2    A (A**2):     18 ; 0.128 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    A (A**2):     14 ; 0.290 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    669       A     671      2                      
REMARK   3           1     B    669       B     671      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):     17 ; 0.039 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  3    A    (A):     25 ; 0.271 ; 0.500           
REMARK   3   TIGHT THERMAL      3    A (A**2):     17 ; 0.087 ; 0.500           
REMARK   3   MEDIUM THERMAL     3    A (A**2):     25 ; 0.448 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    772       B     774      2                      
REMARK   3           1     A    772       A     774      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    B    (A):     18 ; 0.058 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  4    B    (A):     18 ; 0.393 ; 0.500           
REMARK   3   TIGHT THERMAL      4    B (A**2):     18 ; 0.254 ; 0.500           
REMARK   3   MEDIUM THERMAL     4    B (A**2):     18 ; 0.344 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK BULK SOLVENT                                    
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2NZT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000040507.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 85698                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67100                            
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: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1CZA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG3350, 0.2M SODIUM MALONATE,       
REMARK 280  0.1M BTP, 10% ETHYLENE GLYCOL, 0.001M DDT, PH 8.5, VAPOR            
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       47.44500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       93.61600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       64.66900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       93.61600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       47.44500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       64.66900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 SEQUENCE                                                             
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). THE BIOLOGICAL UNIT OF THE             
REMARK 300 PROTEIN IS NOT KNOWN                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 64950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     THR A    98                                                      
REMARK 465     ASP A    99                                                      
REMARK 465     ASN A   100                                                      
REMARK 465     GLY A   101                                                      
REMARK 465     LEU A   102                                                      
REMARK 465     GLN A   103                                                      
REMARK 465     LYS A   104                                                      
REMARK 465     ALA A   518                                                      
REMARK 465     THR A   519                                                      
REMARK 465     PRO A   520                                                      
REMARK 465     ASP A   521                                                      
REMARK 465     GLY A   522                                                      
REMARK 465     THR A   523                                                      
REMARK 465     GLU A   524                                                      
REMARK 465     LYS A   525                                                      
REMARK 465     ASN A   547                                                      
REMARK 465     GLY A   548                                                      
REMARK 465     LYS A   549                                                      
REMARK 465     TRP A   550                                                      
REMARK 465     GLY A   551                                                      
REMARK 465     LYS A   592                                                      
REMARK 465     GLY A   593                                                      
REMARK 465     VAL A   594                                                      
REMARK 465     GLU A   645                                                      
REMARK 465     GLU A   646                                                      
REMARK 465     PHE A   647                                                      
REMARK 465     ALA A   914                                                      
REMARK 465     GLY A   915                                                      
REMARK 465     GLN A   916                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     THR B    98                                                      
REMARK 465     ASP B    99                                                      
REMARK 465     ASN B   100                                                      
REMARK 465     GLY B   101                                                      
REMARK 465     LEU B   102                                                      
REMARK 465     GLN B   103                                                      
REMARK 465     LYS B   104                                                      
REMARK 465     LYS B   346                                                      
REMARK 465     GLU B   404                                                      
REMARK 465     ARG B   405                                                      
REMARK 465     ALA B   518                                                      
REMARK 465     THR B   519                                                      
REMARK 465     PRO B   520                                                      
REMARK 465     ASP B   521                                                      
REMARK 465     GLY B   522                                                      
REMARK 465     THR B   523                                                      
REMARK 465     GLU B   524                                                      
REMARK 465     LYS B   525                                                      
REMARK 465     ARG B   546                                                      
REMARK 465     ASN B   547                                                      
REMARK 465     GLY B   548                                                      
REMARK 465     LYS B   549                                                      
REMARK 465     TRP B   550                                                      
REMARK 465     GLY B   551                                                      
REMARK 465     GLY B   552                                                      
REMARK 465     GLU B   645                                                      
REMARK 465     GLU B   646                                                      
REMARK 465     PHE B   647                                                      
REMARK 465     ASP B   648                                                      
REMARK 465     LEU B   649                                                      
REMARK 465     ALA B   914                                                      
REMARK 465     GLY B   915                                                      
REMARK 465     GLN B   916                                                      
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     LYS A  41    CD   CE   NZ                                        
REMARK 470     LYS A  45    CD   CE   NZ                                        
REMARK 470     GLU A  79    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 249    CD   OE1  OE2                                       
REMARK 470     GLN A 279    OE1  NE2                                            
REMARK 470     LYS A 290    CE   NZ                                             
REMARK 470     GLU A 345    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 347    CG   OD1  OD2                                       
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     ARG A 405    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 406    CG   CD1  CD2                                       
REMARK 470     ARG A 468    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 472    CG   CD   CE   NZ                                   
REMARK 470     ARG A 546    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN A 564    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 565    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 568    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 618    CG   CD   CE   NZ                                   
REMARK 470     LYS A 624    CG   CD   CE   NZ                                   
REMARK 470     LEU A 649    CD1  CD2                                            
REMARK 470     GLU A 668    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 691    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 697    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 700    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 769    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 771    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 774    OE1  OE2                                            
REMARK 470     LYS A 777    CE   NZ                                             
REMARK 470     LYS A 785    CG   CD   CE   NZ                                   
REMARK 470     PHE A 786    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A 805    CD   OE1  NE2                                       
REMARK 470     LEU A 807    CD1  CD2                                            
REMARK 470     LYS A 855    CG   CD   CE   NZ                                   
REMARK 470     LYS A 873    CD   CE   NZ                                        
REMARK 470     LYS A 880    NZ                                                  
REMARK 470     GLU A 894    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 910    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  17    CG   OD1  OD2                                       
REMARK 470     LYS B  41    CG   CD   CE   NZ                                   
REMARK 470     LYS B  45    CD   CE   NZ                                        
REMARK 470     GLU B  79    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 120    NE   CZ   NH1  NH2                                  
REMARK 470     GLN B 125    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 140    CE   NZ                                             
REMARK 470     LYS B 290    CE   NZ                                             
REMARK 470     LYS B 323    CG   CD   CE   NZ                                   
REMARK 470     GLU B 345    CD   OE1  OE2                                       
REMARK 470     ARG B 350    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 365    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 366    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 406    CG   CD1  CD2                                       
REMARK 470     ARG B 407    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 472    CD   CE   NZ                                        
REMARK 470     LYS B 501    CD   CE   NZ                                        
REMARK 470     GLU B 502    CD   OE1  OE2                                       
REMARK 470     GLU B 565    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 580    CD   OE1  NE2                                       
REMARK 470     LYS B 592    CG   CD   CE   NZ                                   
REMARK 470     LYS B 618    CG   CD   CE   NZ                                   
REMARK 470     LYS B 624    CG   CD   CE   NZ                                   
REMARK 470     ARG B 769    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 777    CE   NZ                                             
REMARK 470     LEU B 807    CD1  CD2                                            
REMARK 470     GLU B 810    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 873    CD   CE   NZ                                        
REMARK 470     LYS B 880    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    VAL B   696     UNK  UNX B     5              2.11            
REMARK 500   O    GLY B   250     UNK  UNX B  1013              2.11            
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    LEU A  26       44.56   -100.66                                   
REMARK 500    ASP A 164       33.88    -91.44                                   
REMARK 500    LYS A 173     -128.30     56.87                                   
REMARK 500    LYS A 176       62.13   -163.80                                   
REMARK 500    ARG A 196      -61.29   -101.61                                   
REMARK 500    ASP A 198      -44.42    -26.10                                   
REMARK 500    ASP A 202     -138.91    -88.88                                   
REMARK 500    HIS A 222       -8.75    -59.70                                   
REMARK 500    GLN A 365      -37.93    -36.15                                   
REMARK 500    GLU A 565      -79.55    -48.72                                   
REMARK 500    LYS A 621     -128.56     60.54                                   
REMARK 500    LYS A 624       63.31   -153.69                                   
REMARK 500    ASP A 650       73.49   -112.95                                   
REMARK 500    VAL A 651       90.67    -65.45                                   
REMARK 500    PRO A 670      -35.81    -30.60                                   
REMARK 500    ARG A 769       23.80     43.47                                   
REMARK 500    SER A 773      130.25    -38.78                                   
REMARK 500    ARG A 912       31.18    -84.21                                   
REMARK 500    LEU B  26       52.93    -95.93                                   
REMARK 500    ILE B 143       41.70    -93.51                                   
REMARK 500    SER B 166      114.62   -167.21                                   
REMARK 500    LYS B 173     -126.05     58.39                                   
REMARK 500    LYS B 176       55.32   -155.01                                   
REMARK 500    ASP B 198      -40.50    -27.39                                   
REMARK 500    ASP B 202     -114.81    -89.60                                   
REMARK 500    ILE B 297      -51.65   -122.58                                   
REMARK 500    ALA B 370      -70.31    -57.73                                   
REMARK 500    MET B 591       42.22   -154.85                                   
REMARK 500    LYS B 621     -132.93     56.07                                   
REMARK 500    LYS B 624       20.32   -155.50                                   
REMARK 500    VAL B 651       90.26    -67.24                                   
REMARK 500    ASN B 735       61.96   -114.83                                   
REMARK 500    SER B 773      132.68    -34.62                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2NZT A   17   916  UNP    P52789   HXK2_HUMAN      17    916             
DBREF  2NZT B   17   916  UNP    P52789   HXK2_HUMAN      17    916             
SEQADV 2NZT GLY A   15  UNP  P52789              CLONING ARTIFACT               
SEQADV 2NZT SER A   16  UNP  P52789              CLONING ARTIFACT               
SEQADV 2NZT GLY B   15  UNP  P52789              CLONING ARTIFACT               
SEQADV 2NZT SER B   16  UNP  P52789              CLONING ARTIFACT               
SEQRES   1 A  902  GLY SER ASP GLN VAL GLN LYS VAL ASP GLN TYR LEU TYR          
SEQRES   2 A  902  HIS MET ARG LEU SER ASP GLU THR LEU LEU GLU ILE SER          
SEQRES   3 A  902  LYS ARG PHE ARG LYS GLU MET GLU LYS GLY LEU GLY ALA          
SEQRES   4 A  902  THR THR HIS PRO THR ALA ALA VAL LYS MET LEU PRO THR          
SEQRES   5 A  902  PHE VAL ARG SER THR PRO ASP GLY THR GLU HIS GLY GLU          
SEQRES   6 A  902  PHE LEU ALA LEU ASP LEU GLY GLY THR ASN PHE ARG VAL          
SEQRES   7 A  902  LEU TRP VAL LYS VAL THR ASP ASN GLY LEU GLN LYS VAL          
SEQRES   8 A  902  GLU MET GLU ASN GLN ILE TYR ALA ILE PRO GLU ASP ILE          
SEQRES   9 A  902  MET ARG GLY SER GLY THR GLN LEU PHE ASP HIS ILE ALA          
SEQRES  10 A  902  GLU CYS LEU ALA ASN PHE MET ASP LYS LEU GLN ILE LYS          
SEQRES  11 A  902  ASP LYS LYS LEU PRO LEU GLY PHE THR PHE SER PHE PRO          
SEQRES  12 A  902  CYS HIS GLN THR LYS LEU ASP GLU SER PHE LEU VAL SER          
SEQRES  13 A  902  TRP THR LYS GLY PHE LYS SER SER GLY VAL GLU GLY ARG          
SEQRES  14 A  902  ASP VAL VAL ALA LEU ILE ARG LYS ALA ILE GLN ARG ARG          
SEQRES  15 A  902  GLY ASP PHE ASP ILE ASP ILE VAL ALA VAL VAL ASN ASP          
SEQRES  16 A  902  THR VAL GLY THR MET MET THR CYS GLY TYR ASP ASP HIS          
SEQRES  17 A  902  ASN CYS GLU ILE GLY LEU ILE VAL GLY THR GLY SER ASN          
SEQRES  18 A  902  ALA CYS TYR MET GLU GLU MET ARG HIS ILE ASP MET VAL          
SEQRES  19 A  902  GLU GLY ASP GLU GLY ARG MET CYS ILE ASN MET GLU TRP          
SEQRES  20 A  902  GLY ALA PHE GLY ASP ASP GLY SER LEU ASN ASP ILE ARG          
SEQRES  21 A  902  THR GLU PHE ASP GLN GLU ILE ASP MET GLY SER LEU ASN          
SEQRES  22 A  902  PRO GLY LYS GLN LEU PHE GLU LYS MET ILE SER GLY MET          
SEQRES  23 A  902  TYR MET GLY GLU LEU VAL ARG LEU ILE LEU VAL LYS MET          
SEQRES  24 A  902  ALA LYS GLU GLU LEU LEU PHE GLY GLY LYS LEU SER PRO          
SEQRES  25 A  902  GLU LEU LEU ASN THR GLY ARG PHE GLU THR LYS ASP ILE          
SEQRES  26 A  902  SER ASP ILE GLU GLY GLU LYS ASP GLY ILE ARG LYS ALA          
SEQRES  27 A  902  ARG GLU VAL LEU MET ARG LEU GLY LEU ASP PRO THR GLN          
SEQRES  28 A  902  GLU ASP CYS VAL ALA THR HIS ARG ILE CYS GLN ILE VAL          
SEQRES  29 A  902  SER THR ARG SER ALA SER LEU CYS ALA ALA THR LEU ALA          
SEQRES  30 A  902  ALA VAL LEU GLN ARG ILE LYS GLU ASN LYS GLY GLU GLU          
SEQRES  31 A  902  ARG LEU ARG SER THR ILE GLY VAL ASP GLY SER VAL TYR          
SEQRES  32 A  902  LYS LYS HIS PRO HIS PHE ALA LYS ARG LEU HIS LYS THR          
SEQRES  33 A  902  VAL ARG ARG LEU VAL PRO GLY CYS ASP VAL ARG PHE LEU          
SEQRES  34 A  902  ARG SER GLU ASP GLY SER GLY LYS GLY ALA ALA MET VAL          
SEQRES  35 A  902  THR ALA VAL ALA TYR ARG LEU ALA ASP GLN HIS ARG ALA          
SEQRES  36 A  902  ARG GLN LYS THR LEU GLU HIS LEU GLN LEU SER HIS ASP          
SEQRES  37 A  902  GLN LEU LEU GLU VAL LYS ARG ARG MET LYS VAL GLU MET          
SEQRES  38 A  902  GLU ARG GLY LEU SER LYS GLU THR HIS ALA SER ALA PRO          
SEQRES  39 A  902  VAL LYS MET LEU PRO THR TYR VAL CYS ALA THR PRO ASP          
SEQRES  40 A  902  GLY THR GLU LYS GLY ASP PHE LEU ALA LEU ASP LEU GLY          
SEQRES  41 A  902  GLY THR ASN PHE ARG VAL LEU LEU VAL ARG VAL ARG ASN          
SEQRES  42 A  902  GLY LYS TRP GLY GLY VAL GLU MET HIS ASN LYS ILE TYR          
SEQRES  43 A  902  ALA ILE PRO GLN GLU VAL MET HIS GLY THR GLY ASP GLU          
SEQRES  44 A  902  LEU PHE ASP HIS ILE VAL GLN CYS ILE ALA ASP PHE LEU          
SEQRES  45 A  902  GLU TYR MET GLY MET LYS GLY VAL SER LEU PRO LEU GLY          
SEQRES  46 A  902  PHE THR PHE SER PHE PRO CYS GLN GLN ASN SER LEU ASP          
SEQRES  47 A  902  GLU SER ILE LEU LEU LYS TRP THR LYS GLY PHE LYS ALA          
SEQRES  48 A  902  SER GLY CYS GLU GLY GLU ASP VAL VAL THR LEU LEU LYS          
SEQRES  49 A  902  GLU ALA ILE HIS ARG ARG GLU GLU PHE ASP LEU ASP VAL          
SEQRES  50 A  902  VAL ALA VAL VAL ASN ASP THR VAL GLY THR MET MET THR          
SEQRES  51 A  902  CYS GLY PHE GLU ASP PRO HIS CYS GLU VAL GLY LEU ILE          
SEQRES  52 A  902  VAL GLY THR GLY SER ASN ALA CYS TYR MET GLU GLU MET          
SEQRES  53 A  902  ARG ASN VAL GLU LEU VAL GLU GLY GLU GLU GLY ARG MET          
SEQRES  54 A  902  CYS VAL ASN MET GLU TRP GLY ALA PHE GLY ASP ASN GLY          
SEQRES  55 A  902  CYS LEU ASP ASP PHE ARG THR GLU PHE ASP VAL ALA VAL          
SEQRES  56 A  902  ASP GLU LEU SER LEU ASN PRO GLY LYS GLN ARG PHE GLU          
SEQRES  57 A  902  LYS MET ILE SER GLY MET TYR LEU GLY GLU ILE VAL ARG          
SEQRES  58 A  902  ASN ILE LEU ILE ASP PHE THR LYS ARG GLY LEU LEU PHE          
SEQRES  59 A  902  ARG GLY ARG ILE SER GLU ARG LEU LYS THR ARG GLY ILE          
SEQRES  60 A  902  PHE GLU THR LYS PHE LEU SER GLN ILE GLU SER ASP CYS          
SEQRES  61 A  902  LEU ALA LEU LEU GLN VAL ARG ALA ILE LEU GLN HIS LEU          
SEQRES  62 A  902  GLY LEU GLU SER THR CYS ASP ASP SER ILE ILE VAL LYS          
SEQRES  63 A  902  GLU VAL CYS THR VAL VAL ALA ARG ARG ALA ALA GLN LEU          
SEQRES  64 A  902  CYS GLY ALA GLY MET ALA ALA VAL VAL ASP ARG ILE ARG          
SEQRES  65 A  902  GLU ASN ARG GLY LEU ASP ALA LEU LYS VAL THR VAL GLY          
SEQRES  66 A  902  VAL ASP GLY THR LEU TYR LYS LEU HIS PRO HIS PHE ALA          
SEQRES  67 A  902  LYS VAL MET HIS GLU THR VAL LYS ASP LEU ALA PRO LYS          
SEQRES  68 A  902  CYS ASP VAL SER PHE LEU GLN SER GLU ASP GLY SER GLY          
SEQRES  69 A  902  LYS GLY ALA ALA LEU ILE THR ALA VAL ALA CYS ARG ILE          
SEQRES  70 A  902  ARG GLU ALA GLY GLN                                          
SEQRES   1 B  902  GLY SER ASP GLN VAL GLN LYS VAL ASP GLN TYR LEU TYR          
SEQRES   2 B  902  HIS MET ARG LEU SER ASP GLU THR LEU LEU GLU ILE SER          
SEQRES   3 B  902  LYS ARG PHE ARG LYS GLU MET GLU LYS GLY LEU GLY ALA          
SEQRES   4 B  902  THR THR HIS PRO THR ALA ALA VAL LYS MET LEU PRO THR          
SEQRES   5 B  902  PHE VAL ARG SER THR PRO ASP GLY THR GLU HIS GLY GLU          
SEQRES   6 B  902  PHE LEU ALA LEU ASP LEU GLY GLY THR ASN PHE ARG VAL          
SEQRES   7 B  902  LEU TRP VAL LYS VAL THR ASP ASN GLY LEU GLN LYS VAL          
SEQRES   8 B  902  GLU MET GLU ASN GLN ILE TYR ALA ILE PRO GLU ASP ILE          
SEQRES   9 B  902  MET ARG GLY SER GLY THR GLN LEU PHE ASP HIS ILE ALA          
SEQRES  10 B  902  GLU CYS LEU ALA ASN PHE MET ASP LYS LEU GLN ILE LYS          
SEQRES  11 B  902  ASP LYS LYS LEU PRO LEU GLY PHE THR PHE SER PHE PRO          
SEQRES  12 B  902  CYS HIS GLN THR LYS LEU ASP GLU SER PHE LEU VAL SER          
SEQRES  13 B  902  TRP THR LYS GLY PHE LYS SER SER GLY VAL GLU GLY ARG          
SEQRES  14 B  902  ASP VAL VAL ALA LEU ILE ARG LYS ALA ILE GLN ARG ARG          
SEQRES  15 B  902  GLY ASP PHE ASP ILE ASP ILE VAL ALA VAL VAL ASN ASP          
SEQRES  16 B  902  THR VAL GLY THR MET MET THR CYS GLY TYR ASP ASP HIS          
SEQRES  17 B  902  ASN CYS GLU ILE GLY LEU ILE VAL GLY THR GLY SER ASN          
SEQRES  18 B  902  ALA CYS TYR MET GLU GLU MET ARG HIS ILE ASP MET VAL          
SEQRES  19 B  902  GLU GLY ASP GLU GLY ARG MET CYS ILE ASN MET GLU TRP          
SEQRES  20 B  902  GLY ALA PHE GLY ASP ASP GLY SER LEU ASN ASP ILE ARG          
SEQRES  21 B  902  THR GLU PHE ASP GLN GLU ILE ASP MET GLY SER LEU ASN          
SEQRES  22 B  902  PRO GLY LYS GLN LEU PHE GLU LYS MET ILE SER GLY MET          
SEQRES  23 B  902  TYR MET GLY GLU LEU VAL ARG LEU ILE LEU VAL LYS MET          
SEQRES  24 B  902  ALA LYS GLU GLU LEU LEU PHE GLY GLY LYS LEU SER PRO          
SEQRES  25 B  902  GLU LEU LEU ASN THR GLY ARG PHE GLU THR LYS ASP ILE          
SEQRES  26 B  902  SER ASP ILE GLU GLY GLU LYS ASP GLY ILE ARG LYS ALA          
SEQRES  27 B  902  ARG GLU VAL LEU MET ARG LEU GLY LEU ASP PRO THR GLN          
SEQRES  28 B  902  GLU ASP CYS VAL ALA THR HIS ARG ILE CYS GLN ILE VAL          
SEQRES  29 B  902  SER THR ARG SER ALA SER LEU CYS ALA ALA THR LEU ALA          
SEQRES  30 B  902  ALA VAL LEU GLN ARG ILE LYS GLU ASN LYS GLY GLU GLU          
SEQRES  31 B  902  ARG LEU ARG SER THR ILE GLY VAL ASP GLY SER VAL TYR          
SEQRES  32 B  902  LYS LYS HIS PRO HIS PHE ALA LYS ARG LEU HIS LYS THR          
SEQRES  33 B  902  VAL ARG ARG LEU VAL PRO GLY CYS ASP VAL ARG PHE LEU          
SEQRES  34 B  902  ARG SER GLU ASP GLY SER GLY LYS GLY ALA ALA MET VAL          
SEQRES  35 B  902  THR ALA VAL ALA TYR ARG LEU ALA ASP GLN HIS ARG ALA          
SEQRES  36 B  902  ARG GLN LYS THR LEU GLU HIS LEU GLN LEU SER HIS ASP          
SEQRES  37 B  902  GLN LEU LEU GLU VAL LYS ARG ARG MET LYS VAL GLU MET          
SEQRES  38 B  902  GLU ARG GLY LEU SER LYS GLU THR HIS ALA SER ALA PRO          
SEQRES  39 B  902  VAL LYS MET LEU PRO THR TYR VAL CYS ALA THR PRO ASP          
SEQRES  40 B  902  GLY THR GLU LYS GLY ASP PHE LEU ALA LEU ASP LEU GLY          
SEQRES  41 B  902  GLY THR ASN PHE ARG VAL LEU LEU VAL ARG VAL ARG ASN          
SEQRES  42 B  902  GLY LYS TRP GLY GLY VAL GLU MET HIS ASN LYS ILE TYR          
SEQRES  43 B  902  ALA ILE PRO GLN GLU VAL MET HIS GLY THR GLY ASP GLU          
SEQRES  44 B  902  LEU PHE ASP HIS ILE VAL GLN CYS ILE ALA ASP PHE LEU          
SEQRES  45 B  902  GLU TYR MET GLY MET LYS GLY VAL SER LEU PRO LEU GLY          
SEQRES  46 B  902  PHE THR PHE SER PHE PRO CYS GLN GLN ASN SER LEU ASP          
SEQRES  47 B  902  GLU SER ILE LEU LEU LYS TRP THR LYS GLY PHE LYS ALA          
SEQRES  48 B  902  SER GLY CYS GLU GLY GLU ASP VAL VAL THR LEU LEU LYS          
SEQRES  49 B  902  GLU ALA ILE HIS ARG ARG GLU GLU PHE ASP LEU ASP VAL          
SEQRES  50 B  902  VAL ALA VAL VAL ASN ASP THR VAL GLY THR MET MET THR          
SEQRES  51 B  902  CYS GLY PHE GLU ASP PRO HIS CYS GLU VAL GLY LEU ILE          
SEQRES  52 B  902  VAL GLY THR GLY SER ASN ALA CYS TYR MET GLU GLU MET          
SEQRES  53 B  902  ARG ASN VAL GLU LEU VAL GLU GLY GLU GLU GLY ARG MET          
SEQRES  54 B  902  CYS VAL ASN MET GLU TRP GLY ALA PHE GLY ASP ASN GLY          
SEQRES  55 B  902  CYS LEU ASP ASP PHE ARG THR GLU PHE ASP VAL ALA VAL          
SEQRES  56 B  902  ASP GLU LEU SER LEU ASN PRO GLY LYS GLN ARG PHE GLU          
SEQRES  57 B  902  LYS MET ILE SER GLY MET TYR LEU GLY GLU ILE VAL ARG          
SEQRES  58 B  902  ASN ILE LEU ILE ASP PHE THR LYS ARG GLY LEU LEU PHE          
SEQRES  59 B  902  ARG GLY ARG ILE SER GLU ARG LEU LYS THR ARG GLY ILE          
SEQRES  60 B  902  PHE GLU THR LYS PHE LEU SER GLN ILE GLU SER ASP CYS          
SEQRES  61 B  902  LEU ALA LEU LEU GLN VAL ARG ALA ILE LEU GLN HIS LEU          
SEQRES  62 B  902  GLY LEU GLU SER THR CYS ASP ASP SER ILE ILE VAL LYS          
SEQRES  63 B  902  GLU VAL CYS THR VAL VAL ALA ARG ARG ALA ALA GLN LEU          
SEQRES  64 B  902  CYS GLY ALA GLY MET ALA ALA VAL VAL ASP ARG ILE ARG          
SEQRES  65 B  902  GLU ASN ARG GLY LEU ASP ALA LEU LYS VAL THR VAL GLY          
SEQRES  66 B  902  VAL ASP GLY THR LEU TYR LYS LEU HIS PRO HIS PHE ALA          
SEQRES  67 B  902  LYS VAL MET HIS GLU THR VAL LYS ASP LEU ALA PRO LYS          
SEQRES  68 B  902  CYS ASP VAL SER PHE LEU GLN SER GLU ASP GLY SER GLY          
SEQRES  69 B  902  LYS GLY ALA ALA LEU ILE THR ALA VAL ALA CYS ARG ILE          
SEQRES  70 B  902  ARG GLU ALA GLY GLN                                          
HET    GLC  A1001      12                                                       
HET    BG6  A1002      16                                                       
HET    GLC  A1003      12                                                       
HET    BG6  A1004      16                                                       
HET    UNX  A   1       1                                                       
HET    UNX  A   4       1                                                       
HET    UNX  A   6       1                                                       
HET    UNX  A   8       1                                                       
HET    UNX  A   9       1                                                       
HET    UNX  A  10       1                                                       
HET    UNX  A  11       1                                                       
HET    UNX  A1005       1                                                       
HET    UNX  A1006       1                                                       
HET    UNX  A1007       1                                                       
HET    UNX  A1008       1                                                       
HET    UNX  A1009       1                                                       
HET    GLC  B1001      12                                                       
HET    BG6  B1002      16                                                       
HET    GLC  B1003      12                                                       
HET    BG6  B1004      16                                                       
HET    UNX  B   2       1                                                       
HET    UNX  B   3       1                                                       
HET    UNX  B   5       1                                                       
HET    UNX  B   7       1                                                       
HET    UNX  B  12       1                                                       
HET    UNX  B  13       1                                                       
HET    UNX  B  14       1                                                       
HET    UNX  B1005       1                                                       
HET    UNX  B1006       1                                                       
HET    UNX  B1007       1                                                       
HET    UNX  B1008       1                                                       
HET    UNX  B1009       1                                                       
HET    UNX  B1010       1                                                       
HET    UNX  B1011       1                                                       
HET    UNX  B1012       1                                                       
HET    UNX  B1013       1                                                       
HETNAM     GLC ALPHA-D-GLUCOPYRANOSE                                            
HETNAM     BG6 6-O-PHOSPHONO-BETA-D-GLUCOPYRANOSE                               
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   3  GLC    4(C6 H12 O6)                                                 
FORMUL   4  BG6    4(C6 H13 O9 P)                                               
FORMUL   7  UNX    28(X)                                                        
FORMUL  39  HOH   *97(H2 O)                                                     
HELIX    1   1 GLN A   18  LEU A   26  1                                   9    
HELIX    2   2 TYR A   27  ARG A   30  5                                   4    
HELIX    3   3 SER A   32  GLY A   52  1                                  21    
HELIX    4   4 THR A   55  ALA A   59  5                                   5    
HELIX    5   5 PRO A  115  ARG A  120  1                                   6    
HELIX    6   6 SER A  122  GLN A  142  1                                  21    
HELIX    7   7 ASP A  184  ARG A  195  1                                  12    
HELIX    8   8 ASN A  208  TYR A  219  1                                  12    
HELIX    9   9 ARG A  243  ILE A  245  5                                   3    
HELIX   10  10 GLU A  260  PHE A  264  5                                   5    
HELIX   11  11 THR A  275  GLY A  284  1                                  10    
HELIX   12  12 GLN A  291  MET A  296  1                                   6    
HELIX   13  13 TYR A  301  GLU A  316  1                                  16    
HELIX   14  14 LEU A  319  LYS A  323  5                                   5    
HELIX   15  15 SER A  325  ASN A  330  1                                   6    
HELIX   16  16 GLU A  335  GLU A  345  1                                  11    
HELIX   17  17 ASP A  347  LEU A  359  1                                  13    
HELIX   18  18 THR A  364  GLY A  402  1                                  39    
HELIX   19  19 GLY A  414  HIS A  420  1                                   7    
HELIX   20  20 HIS A  422  VAL A  435  1                                  14    
HELIX   21  21 GLY A  448  GLU A  475  1                                  28    
HELIX   22  22 HIS A  476  GLN A  478  5                                   3    
HELIX   23  23 SER A  480  SER A  500  1                                  21    
HELIX   24  24 SER A  500  ALA A  505  1                                   6    
HELIX   25  25 PRO A  563  GLY A  569  1                                   7    
HELIX   26  26 THR A  570  MET A  589  1                                  20    
HELIX   27  27 ASP A  632  ARG A  643  1                                  12    
HELIX   28  28 ASN A  656  PHE A  667  1                                  12    
HELIX   29  29 GLU A  708  PHE A  712  5                                   5    
HELIX   30  30 THR A  723  LEU A  732  1                                  10    
HELIX   31  31 PHE A  741  ILE A  745  5                                   5    
HELIX   32  32 TYR A  749  ARG A  764  1                                  16    
HELIX   33  33 LEU A  767  ARG A  771  5                                   5    
HELIX   34  34 THR A  784  GLN A  789  1                                   6    
HELIX   35  35 ALA A  796  LEU A  807  1                                  12    
HELIX   36  36 THR A  812  ARG A  849  1                                  38    
HELIX   37  37 GLY A  862  HIS A  868  1                                   7    
HELIX   38  38 HIS A  870  ALA A  883  1                                  14    
HELIX   39  39 GLY A  896  ARG A  912  1                                  17    
HELIX   40  40 GLN B   18  LEU B   26  1                                   9    
HELIX   41  41 SER B   32  GLY B   52  1                                  21    
HELIX   42  42 THR B   55  ALA B   59  5                                   5    
HELIX   43  43 PRO B  115  ARG B  120  1                                   6    
HELIX   44  44 SER B  122  LEU B  141  1                                  20    
HELIX   45  45 ASP B  184  GLY B  197  1                                  14    
HELIX   46  46 ASN B  208  ASP B  221  1                                  14    
HELIX   47  47 ARG B  243  ILE B  245  5                                   3    
HELIX   48  48 GLU B  260  PHE B  264  5                                   5    
HELIX   49  49 THR B  275  GLY B  284  1                                  10    
HELIX   50  50 PHE B  293  ILE B  297  5                                   5    
HELIX   51  51 SER B  298  GLU B  316  1                                  19    
HELIX   52  52 LEU B  319  LYS B  323  5                                   5    
HELIX   53  53 SER B  325  ASN B  330  1                                   6    
HELIX   54  54 GLU B  335  GLU B  345  1                                  11    
HELIX   55  55 ASP B  347  LEU B  359  1                                  13    
HELIX   56  56 GLU B  366  GLY B  402  1                                  37    
HELIX   57  57 GLY B  414  HIS B  420  1                                   7    
HELIX   58  58 HIS B  422  VAL B  435  1                                  14    
HELIX   59  59 GLY B  448  GLU B  475  1                                  28    
HELIX   60  60 HIS B  476  GLN B  478  5                                   3    
HELIX   61  61 SER B  480  SER B  500  1                                  21    
HELIX   62  62 PRO B  563  HIS B  568  1                                   6    
HELIX   63  63 THR B  570  MET B  589  1                                  20    
HELIX   64  64 ASP B  632  ARG B  643  1                                  12    
HELIX   65  65 ASN B  656  PHE B  667  1                                  12    
HELIX   66  66 GLU B  708  PHE B  712  5                                   5    
HELIX   67  67 THR B  723  LEU B  732  1                                  10    
HELIX   68  68 PHE B  741  ILE B  745  5                                   5    
HELIX   69  69 TYR B  749  ARG B  764  1                                  16    
HELIX   70  70 LEU B  767  ARG B  771  5                                   5    
HELIX   71  71 GLU B  783  GLU B  791  1                                   9    
HELIX   72  72 ALA B  796  GLY B  808  1                                  13    
HELIX   73  73 THR B  812  ASN B  848  1                                  37    
HELIX   74  74 GLY B  862  HIS B  868  1                                   7    
HELIX   75  75 HIS B  870  ALA B  883  1                                  14    
HELIX   76  76 GLY B  896  ARG B  912  1                                  17    
SHEET    1   A 6 LEU A  64  PRO A  65  0                                        
SHEET    2   A 6 ARG A 254  ASN A 258 -1  O  ASN A 258   N  LEU A  64           
SHEET    3   A 6 SER A 234  GLU A 241 -1  N  TYR A 238   O  ILE A 257           
SHEET    4   A 6 CYS A 224  VAL A 230 -1  N  ILE A 229   O  ASN A 235           
SHEET    5   A 6 LEU A 406  ASP A 413  1  O  GLY A 411   N  LEU A 228           
SHEET    6   A 6 CYS A 438  ARG A 444  1  O  ASP A 439   N  LEU A 406           
SHEET    1   B 5 GLU A 106  TYR A 112  0                                        
SHEET    2   B 5 PHE A  90  VAL A  97 -1  N  PHE A  90   O  TYR A 112           
SHEET    3   B 5 GLY A  78  LEU A  85 -1  N  PHE A  80   O  VAL A  95           
SHEET    4   B 5 LEU A 148  PHE A 154  1  O  THR A 153   N  LEU A  83           
SHEET    5   B 5 ILE A 201  VAL A 207  1  O  ALA A 205   N  PHE A 152           
SHEET    1   C 2 CYS A 158  HIS A 159  0                                        
SHEET    2   C 2 PHE A 167  LEU A 168 -1  O  PHE A 167   N  HIS A 159           
SHEET    1   D 6 LEU A 512  PRO A 513  0                                        
SHEET    2   D 6 ARG A 702  ASN A 706 -1  O  ASN A 706   N  LEU A 512           
SHEET    3   D 6 SER A 682  GLU A 689 -1  N  TYR A 686   O  VAL A 705           
SHEET    4   D 6 CYS A 672  VAL A 678 -1  N  GLY A 675   O  CYS A 685           
SHEET    5   D 6 LEU A 854  ASP A 861  1  O  GLY A 859   N  VAL A 674           
SHEET    6   D 6 CYS A 886  GLN A 892  1  O  ASP A 887   N  LEU A 854           
SHEET    1   E 5 GLU A 554  ILE A 559  0                                        
SHEET    2   E 5 ARG A 539  ARG A 544 -1  N  ARG A 544   O  GLU A 554           
SHEET    3   E 5 ASP A 527  LEU A 533 -1  N  PHE A 528   O  VAL A 543           
SHEET    4   E 5 PRO A 597  PHE A 602  1  O  THR A 601   N  LEU A 533           
SHEET    5   E 5 ASP A 650  VAL A 655  1  O  VAL A 655   N  PHE A 600           
SHEET    1   F 2 CYS A 606  SER A 610  0                                        
SHEET    2   F 2 GLU A 613  LEU A 616 -1  O  ILE A 615   N  GLN A 607           
SHEET    1   G 6 LEU B  64  PRO B  65  0                                        
SHEET    2   G 6 ARG B 254  ASN B 258 -1  O  ASN B 258   N  LEU B  64           
SHEET    3   G 6 SER B 234  GLU B 241 -1  N  TYR B 238   O  ILE B 257           
SHEET    4   G 6 CYS B 224  VAL B 230 -1  N  GLY B 227   O  CYS B 237           
SHEET    5   G 6 THR B 409  ASP B 413  1  O  GLY B 411   N  LEU B 228           
SHEET    6   G 6 ARG B 441  ARG B 444  1  O  LEU B 443   N  ILE B 410           
SHEET    1   H 5 GLU B 106  TYR B 112  0                                        
SHEET    2   H 5 PHE B  90  VAL B  97 -1  N  PHE B  90   O  TYR B 112           
SHEET    3   H 5 GLY B  78  LEU B  85 -1  N  PHE B  80   O  VAL B  95           
SHEET    4   H 5 LYS B 147  PHE B 154  1  O  PRO B 149   N  LEU B  81           
SHEET    5   H 5 ASP B 200  VAL B 207  1  O  ALA B 205   N  PHE B 152           
SHEET    1   I 2 CYS B 158  HIS B 159  0                                        
SHEET    2   I 2 PHE B 167  LEU B 168 -1  O  PHE B 167   N  HIS B 159           
SHEET    1   J 6 LEU B 512  PRO B 513  0                                        
SHEET    2   J 6 ARG B 702  ASN B 706 -1  O  ASN B 706   N  LEU B 512           
SHEET    3   J 6 SER B 682  GLU B 689 -1  N  GLU B 688   O  MET B 703           
SHEET    4   J 6 CYS B 672  VAL B 678 -1  N  GLY B 675   O  CYS B 685           
SHEET    5   J 6 LEU B 854  ASP B 861  1  O  GLY B 859   N  VAL B 674           
SHEET    6   J 6 CYS B 886  GLN B 892  1  O  LEU B 891   N  VAL B 858           
SHEET    1   K 5 GLU B 554  TYR B 560  0                                        
SHEET    2   K 5 PHE B 538  ARG B 544 -1  N  ARG B 544   O  GLU B 554           
SHEET    3   K 5 ASP B 527  LEU B 533 -1  N  PHE B 528   O  VAL B 543           
SHEET    4   K 5 LEU B 598  PHE B 602  1  O  THR B 601   N  LEU B 533           
SHEET    5   K 5 VAL B 651  VAL B 655  1  O  ALA B 653   N  PHE B 600           
SHEET    1   L 2 CYS B 606  SER B 610  0                                        
SHEET    2   L 2 GLU B 613  LEU B 616 -1  O  ILE B 615   N  GLN B 607           
CRYST1   94.890  129.338  187.232  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010540  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007730  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005340        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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