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Database: PDB
Entry: 4APC
LinkDB: 4APC
Original site: 4APC 
HEADER    TRANSFERASE                             02-APR-12   4APC              
TITLE     CRYSTAL STRUCTURE OF HUMAN NIMA-RELATED KINASE 1 (NEK1)               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE NEK1;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: KINASE DOMAIN, RESIDUES 1-238;                             
COMPND   5 SYNONYM: NEVER IN MITOSIS A-RELATED KINASE 1, NIMA-RELATED PROTEIN   
COMPND   6 KINASE 1, RENAL CARCINOMA ANTIGEN NY-REN-55;                         
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.ELKINS,T.D.M.HANCHUK,D.V.LOVATO,F.L.BASEI,G.V.MEIRELLES,J.KOBARG, 
AUTHOR   2 M.SZKLARZ,M.VOLLMAR,P.MAHAJAN,P.RELLOS,Y.ZHANG,T.KROJER,A.C.W.PIKE,  
AUTHOR   3 C.BOUNTRA,C.ARROWSMITH,A.EDWARDS,S.KNAPP                             
REVDAT   3   12-AUG-20 4APC    1       JRNL   REMARK                            
REVDAT   2   23-MAY-12 4APC    1       COMPND REMARK DBREF  SEQADV              
REVDAT   1   25-APR-12 4APC    0                                                
JRNL        AUTH   T.D.MELO-HANCHUK,P.F.SLEPICKA,G.V.MEIRELLES,F.L.BASEI,       
JRNL        AUTH 2 D.V.LOVATO,D.C.GRANATO,B.A.PAULETTI,R.R.DOMINGUES,           
JRNL        AUTH 3 A.F.P.LEME,A.L.PELEGRINI,G.LENZ,S.KNAPP,J.M.ELKINS,J.KOBARG  
JRNL        TITL   NEK1 KINASE DOMAIN STRUCTURE AND ITS DYNAMIC PROTEIN         
JRNL        TITL 2 INTERACTOME AFTER EXPOSURE TO CISPLATIN.                     
JRNL        REF    SCI REP                       V.   7  5445 2017              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   28710492                                                     
JRNL        DOI    10.1038/S41598-017-05325-W                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 81.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 38286                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2021                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2653                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 143                          
REMARK   3   BIN FREE R VALUE                    : 0.3180                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4692                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7                                       
REMARK   3   SOLVENT ATOMS            : 165                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.00000                                             
REMARK   3    B22 (A**2) : 1.63000                                              
REMARK   3    B33 (A**2) : -0.64000                                             
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): 0.235         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.189         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.133         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.061         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4835 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3343 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6529 ; 1.266 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8132 ; 0.973 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   597 ; 5.802 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   227 ;37.563 ;23.700       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   874 ;13.554 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    33 ;18.439 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   726 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5337 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1012 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A   -20    284       B   -20    284   11004  0.07  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4APC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-APR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290051961.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40349                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.410                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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 2JAV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM CHLORIDE, 20 %(W/V) PEG   
REMARK 280  3350, PH 7.5                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       81.97000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       81.97000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       44.95500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.40500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       44.95500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.40500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       81.97000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       44.95500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       46.40500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       81.97000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       44.95500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       46.40500            
REMARK 290   SMTRY3   8  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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, THR 162 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, THR 162 TO ALA                        
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   -21                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     GLY A   -12                                                      
REMARK 465     VAL A   -11                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     PHE A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     SER A   285                                                      
REMARK 465     GLN A   286                                                      
REMARK 465     PRO A   287                                                      
REMARK 465     ILE A   288                                                      
REMARK 465     PRO A   289                                                      
REMARK 465     ALA A   290                                                      
REMARK 465     LYS A   291                                                      
REMARK 465     ARG A   292                                                      
REMARK 465     PRO A   293                                                      
REMARK 465     ALA A   294                                                      
REMARK 465     SER A   295                                                      
REMARK 465     GLY A   296                                                      
REMARK 465     GLN A   297                                                      
REMARK 465     ASN A   298                                                      
REMARK 465     SER A   299                                                      
REMARK 465     ILE A   300                                                      
REMARK 465     SER A   301                                                      
REMARK 465     VAL A   302                                                      
REMARK 465     MET A   303                                                      
REMARK 465     PRO A   304                                                      
REMARK 465     ALA A   305                                                      
REMARK 465     GLN A   306                                                      
REMARK 465     LYS A   307                                                      
REMARK 465     ILE A   308                                                      
REMARK 465     THR A   309                                                      
REMARK 465     LYS A   310                                                      
REMARK 465     PRO A   311                                                      
REMARK 465     ALA A   312                                                      
REMARK 465     ALA A   313                                                      
REMARK 465     LYS A   314                                                      
REMARK 465     TYR A   315                                                      
REMARK 465     GLY A   316                                                      
REMARK 465     ILE A   317                                                      
REMARK 465     PRO A   318                                                      
REMARK 465     LEU A   319                                                      
REMARK 465     ALA A   320                                                      
REMARK 465     TYR A   321                                                      
REMARK 465     LYS A   322                                                      
REMARK 465     LYS A   323                                                      
REMARK 465     TYR A   324                                                      
REMARK 465     GLY A   325                                                      
REMARK 465     ASP A   326                                                      
REMARK 465     LYS A   327                                                      
REMARK 465     LYS A   328                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     SER B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     GLY B   -12                                                      
REMARK 465     GLU B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     PHE B    15                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     SER B   285                                                      
REMARK 465     GLN B   286                                                      
REMARK 465     PRO B   287                                                      
REMARK 465     ILE B   288                                                      
REMARK 465     PRO B   289                                                      
REMARK 465     ALA B   290                                                      
REMARK 465     LYS B   291                                                      
REMARK 465     ARG B   292                                                      
REMARK 465     PRO B   293                                                      
REMARK 465     ALA B   294                                                      
REMARK 465     SER B   295                                                      
REMARK 465     GLY B   296                                                      
REMARK 465     GLN B   297                                                      
REMARK 465     ASN B   298                                                      
REMARK 465     SER B   299                                                      
REMARK 465     ILE B   300                                                      
REMARK 465     SER B   301                                                      
REMARK 465     VAL B   302                                                      
REMARK 465     MET B   303                                                      
REMARK 465     PRO B   304                                                      
REMARK 465     ALA B   305                                                      
REMARK 465     GLN B   306                                                      
REMARK 465     LYS B   307                                                      
REMARK 465     ILE B   308                                                      
REMARK 465     THR B   309                                                      
REMARK 465     LYS B   310                                                      
REMARK 465     PRO B   311                                                      
REMARK 465     ALA B   312                                                      
REMARK 465     ALA B   313                                                      
REMARK 465     LYS B   314                                                      
REMARK 465     TYR B   315                                                      
REMARK 465     GLY B   316                                                      
REMARK 465     ILE B   317                                                      
REMARK 465     PRO B   318                                                      
REMARK 465     LEU B   319                                                      
REMARK 465     ALA B   320                                                      
REMARK 465     TYR B   321                                                      
REMARK 465     LYS B   322                                                      
REMARK 465     LYS B   323                                                      
REMARK 465     TYR B   324                                                      
REMARK 465     GLY B   325                                                      
REMARK 465     ASP B   326                                                      
REMARK 465     LYS B   327                                                      
REMARK 465     LYS B   328                                                      
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     HIS A -20    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP A -10    CG   OD1  OD2                                       
REMARK 470     LYS A   9    CD   CE   NZ                                        
REMARK 470     LYS A  17    CG   CD   CE   NZ                                   
REMARK 470     LYS A  22    CG   CD   CE   NZ                                   
REMARK 470     LYS A  33    NZ                                                  
REMARK 470     SER A  42    OG                                                  
REMARK 470     LYS A  43    CD   CE   NZ                                        
REMARK 470     GLU A  44    CD   OE1  OE2                                       
REMARK 470     GLU A  46    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  50    CZ   NH1  NH2                                       
REMARK 470     LYS A  59    CD   CE   NZ                                        
REMARK 470     LYS A  90    CE   NZ                                             
REMARK 470     LYS A  96    CE   NZ                                             
REMARK 470     LYS A 200    CE   NZ                                             
REMARK 470     GLU A 204    CD   OE1  OE2                                       
REMARK 470     ARG A 241    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 254    CD   OE1  OE2                                       
REMARK 470     VAL B -11    CG1  CG2                                            
REMARK 470     ASP B -10    CG   OD1  OD2                                       
REMARK 470     LYS B   9    CG   CD   CE   NZ                                   
REMARK 470     LYS B  17    CG   CD   CE   NZ                                   
REMARK 470     LYS B  22    CE   NZ                                             
REMARK 470     SER B  42    OG                                                  
REMARK 470     LYS B  43    CG   CD   CE   NZ                                   
REMARK 470     LYS B  59    CD   CE   NZ                                        
REMARK 470     LYS B  90    CD   CE   NZ                                        
REMARK 470     LYS B  96    CE   NZ                                             
REMARK 470     LYS B 200    CE   NZ                                             
REMARK 470     GLU B 204    CD   OE1  OE2                                       
REMARK 470     ARG B 241    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B 263    CD   OE1  OE2                                       
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   ND1  HIS A   201     O    HOH A  2067              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU A    71     NH1  ARG B   244     7544     2.05            
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    HIS B -18   CG    HIS B -18   CD2     0.055                       
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    CYS A 163   CA  -  CB  -  SG  ANGL. DEV. =  11.1 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    HIS A -19       73.65   -153.73                                   
REMARK 500    GLN A   8      144.03   -170.97                                   
REMARK 500    ASP A  26       17.91   -143.49                                   
REMARK 500    ARG A  67      -60.21   -104.91                                   
REMARK 500    HIS B -19       70.68   -112.68                                   
REMARK 500    GLN B   8      144.76   -171.57                                   
REMARK 500    ASP B  26       18.67   -144.99                                   
REMARK 500    ARG B  67      -60.33   -106.87                                   
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 HIS A  -19     HIS A  -18                 -149.05                    
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 CL A 1285                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1286                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1287                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1288                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1285                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1286                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1287                 
DBREF  4APC A    1   328  UNP    Q96PY6   NEK1_HUMAN       1    328             
DBREF  4APC B    1   328  UNP    Q96PY6   NEK1_HUMAN       1    328             
SEQADV 4APC MET A  -21  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC HIS A  -20  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC HIS A  -19  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC HIS A  -18  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC HIS A  -17  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC HIS A  -16  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC HIS A  -15  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC SER A  -14  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC SER A  -13  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC GLY A  -12  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC VAL A  -11  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC ASP A  -10  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC LEU A   -9  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC GLY A   -8  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC THR A   -7  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC GLU A   -6  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC ASN A   -5  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC LEU A   -4  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC TYR A   -3  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC PHE A   -2  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC GLN A   -1  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC SER A    0  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC ALA A  162  UNP  Q96PY6    THR   162 ENGINEERED MUTATION            
SEQADV 4APC MET B  -21  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC HIS B  -20  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC HIS B  -19  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC HIS B  -18  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC HIS B  -17  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC HIS B  -16  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC HIS B  -15  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC SER B  -14  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC SER B  -13  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC GLY B  -12  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC VAL B  -11  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC ASP B  -10  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC LEU B   -9  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC GLY B   -8  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC THR B   -7  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC GLU B   -6  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC ASN B   -5  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC LEU B   -4  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC TYR B   -3  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC PHE B   -2  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC GLN B   -1  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC SER B    0  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4APC ALA B  162  UNP  Q96PY6    THR   162 ENGINEERED MUTATION            
SEQRES   1 A  350  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  350  GLY THR GLU ASN LEU TYR PHE GLN SER MET GLU LYS TYR          
SEQRES   3 A  350  VAL ARG LEU GLN LYS ILE GLY GLU GLY SER PHE GLY LYS          
SEQRES   4 A  350  ALA ILE LEU VAL LYS SER THR GLU ASP GLY ARG GLN TYR          
SEQRES   5 A  350  VAL ILE LYS GLU ILE ASN ILE SER ARG MET SER SER LYS          
SEQRES   6 A  350  GLU ARG GLU GLU SER ARG ARG GLU VAL ALA VAL LEU ALA          
SEQRES   7 A  350  ASN MET LYS HIS PRO ASN ILE VAL GLN TYR ARG GLU SER          
SEQRES   8 A  350  PHE GLU GLU ASN GLY SER LEU TYR ILE VAL MET ASP TYR          
SEQRES   9 A  350  CYS GLU GLY GLY ASP LEU PHE LYS ARG ILE ASN ALA GLN          
SEQRES  10 A  350  LYS GLY VAL LEU PHE GLN GLU ASP GLN ILE LEU ASP TRP          
SEQRES  11 A  350  PHE VAL GLN ILE CYS LEU ALA LEU LYS HIS VAL HIS ASP          
SEQRES  12 A  350  ARG LYS ILE LEU HIS ARG ASP ILE LYS SER GLN ASN ILE          
SEQRES  13 A  350  PHE LEU THR LYS ASP GLY THR VAL GLN LEU GLY ASP PHE          
SEQRES  14 A  350  GLY ILE ALA ARG VAL LEU ASN SER THR VAL GLU LEU ALA          
SEQRES  15 A  350  ARG ALA CYS ILE GLY THR PRO TYR TYR LEU SER PRO GLU          
SEQRES  16 A  350  ILE CYS GLU ASN LYS PRO TYR ASN ASN LYS SER ASP ILE          
SEQRES  17 A  350  TRP ALA LEU GLY CYS VAL LEU TYR GLU LEU CYS THR LEU          
SEQRES  18 A  350  LYS HIS ALA PHE GLU ALA GLY SER MET LYS ASN LEU VAL          
SEQRES  19 A  350  LEU LYS ILE ILE SER GLY SER PHE PRO PRO VAL SER LEU          
SEQRES  20 A  350  HIS TYR SER TYR ASP LEU ARG SER LEU VAL SER GLN LEU          
SEQRES  21 A  350  PHE LYS ARG ASN PRO ARG ASP ARG PRO SER VAL ASN SER          
SEQRES  22 A  350  ILE LEU GLU LYS GLY PHE ILE ALA LYS ARG ILE GLU LYS          
SEQRES  23 A  350  PHE LEU SER PRO GLN LEU ILE ALA GLU GLU PHE CYS LEU          
SEQRES  24 A  350  LYS THR PHE SER LYS PHE GLY SER GLN PRO ILE PRO ALA          
SEQRES  25 A  350  LYS ARG PRO ALA SER GLY GLN ASN SER ILE SER VAL MET          
SEQRES  26 A  350  PRO ALA GLN LYS ILE THR LYS PRO ALA ALA LYS TYR GLY          
SEQRES  27 A  350  ILE PRO LEU ALA TYR LYS LYS TYR GLY ASP LYS LYS              
SEQRES   1 B  350  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  350  GLY THR GLU ASN LEU TYR PHE GLN SER MET GLU LYS TYR          
SEQRES   3 B  350  VAL ARG LEU GLN LYS ILE GLY GLU GLY SER PHE GLY LYS          
SEQRES   4 B  350  ALA ILE LEU VAL LYS SER THR GLU ASP GLY ARG GLN TYR          
SEQRES   5 B  350  VAL ILE LYS GLU ILE ASN ILE SER ARG MET SER SER LYS          
SEQRES   6 B  350  GLU ARG GLU GLU SER ARG ARG GLU VAL ALA VAL LEU ALA          
SEQRES   7 B  350  ASN MET LYS HIS PRO ASN ILE VAL GLN TYR ARG GLU SER          
SEQRES   8 B  350  PHE GLU GLU ASN GLY SER LEU TYR ILE VAL MET ASP TYR          
SEQRES   9 B  350  CYS GLU GLY GLY ASP LEU PHE LYS ARG ILE ASN ALA GLN          
SEQRES  10 B  350  LYS GLY VAL LEU PHE GLN GLU ASP GLN ILE LEU ASP TRP          
SEQRES  11 B  350  PHE VAL GLN ILE CYS LEU ALA LEU LYS HIS VAL HIS ASP          
SEQRES  12 B  350  ARG LYS ILE LEU HIS ARG ASP ILE LYS SER GLN ASN ILE          
SEQRES  13 B  350  PHE LEU THR LYS ASP GLY THR VAL GLN LEU GLY ASP PHE          
SEQRES  14 B  350  GLY ILE ALA ARG VAL LEU ASN SER THR VAL GLU LEU ALA          
SEQRES  15 B  350  ARG ALA CYS ILE GLY THR PRO TYR TYR LEU SER PRO GLU          
SEQRES  16 B  350  ILE CYS GLU ASN LYS PRO TYR ASN ASN LYS SER ASP ILE          
SEQRES  17 B  350  TRP ALA LEU GLY CYS VAL LEU TYR GLU LEU CYS THR LEU          
SEQRES  18 B  350  LYS HIS ALA PHE GLU ALA GLY SER MET LYS ASN LEU VAL          
SEQRES  19 B  350  LEU LYS ILE ILE SER GLY SER PHE PRO PRO VAL SER LEU          
SEQRES  20 B  350  HIS TYR SER TYR ASP LEU ARG SER LEU VAL SER GLN LEU          
SEQRES  21 B  350  PHE LYS ARG ASN PRO ARG ASP ARG PRO SER VAL ASN SER          
SEQRES  22 B  350  ILE LEU GLU LYS GLY PHE ILE ALA LYS ARG ILE GLU LYS          
SEQRES  23 B  350  PHE LEU SER PRO GLN LEU ILE ALA GLU GLU PHE CYS LEU          
SEQRES  24 B  350  LYS THR PHE SER LYS PHE GLY SER GLN PRO ILE PRO ALA          
SEQRES  25 B  350  LYS ARG PRO ALA SER GLY GLN ASN SER ILE SER VAL MET          
SEQRES  26 B  350  PRO ALA GLN LYS ILE THR LYS PRO ALA ALA LYS TYR GLY          
SEQRES  27 B  350  ILE PRO LEU ALA TYR LYS LYS TYR GLY ASP LYS LYS              
HET     CL  A1285       1                                                       
HET     CL  A1286       1                                                       
HET     CL  A1287       1                                                       
HET     CL  A1288       1                                                       
HET     CL  B1285       1                                                       
HET     CL  B1286       1                                                       
HET     CL  B1287       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   CL    7(CL 1-)                                                     
FORMUL  10  HOH   *165(H2 O)                                                    
HELIX    1   1 SER A   41  MET A   58  1                                  18    
HELIX    2   2 ASP A   87  GLN A   95  1                                   9    
HELIX    3   3 GLN A  101  ARG A  122  1                                  22    
HELIX    4   4 LYS A  130  GLN A  132  5                                   3    
HELIX    5   5 ASN A  154  GLY A  165  1                                  12    
HELIX    6   6 SER A  171  GLU A  176  1                                   6    
HELIX    7   7 ASN A  181  LEU A  199  1                                  19    
HELIX    8   8 SER A  207  GLY A  218  1                                  12    
HELIX    9   9 SER A  228  PHE A  239  1                                  12    
HELIX   10  10 ASN A  242  ARG A  246  5                                   5    
HELIX   11  11 SER A  248  GLU A  254  1                                   7    
HELIX   12  12 LYS A  255  LYS A  260  1                                   6    
HELIX   13  13 ARG A  261  PHE A  265  5                                   5    
HELIX   14  14 SER A  267  CYS A  276  1                                  10    
HELIX   15  15 SER B   41  MET B   58  1                                  18    
HELIX   16  16 ASP B   87  GLN B   95  1                                   9    
HELIX   17  17 GLN B  101  ARG B  122  1                                  22    
HELIX   18  18 LYS B  130  GLN B  132  5                                   3    
HELIX   19  19 ASN B  154  GLY B  165  1                                  12    
HELIX   20  20 SER B  171  GLU B  176  1                                   6    
HELIX   21  21 ASN B  181  LEU B  199  1                                  19    
HELIX   22  22 SER B  207  GLY B  218  1                                  12    
HELIX   23  23 SER B  228  PHE B  239  1                                  12    
HELIX   24  24 ASN B  242  ARG B  246  5                                   5    
HELIX   25  25 SER B  248  LYS B  255  1                                   8    
HELIX   26  26 LYS B  255  LYS B  260  1                                   6    
HELIX   27  27 ARG B  261  PHE B  265  5                                   5    
HELIX   28  28 SER B  267  CYS B  276  1                                  10    
SHEET    1  AA 5 TYR A   4  LYS A   9  0                                        
SHEET    2  AA 5 ALA A  18  SER A  23 -1  O  LEU A  20   N  LEU A   7           
SHEET    3  AA 5 GLN A  29  ASN A  36 -1  O  TYR A  30   N  VAL A  21           
SHEET    4  AA 5 SER A  75  ASP A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5  AA 5 TYR A  66  GLU A  72 -1  N  ARG A  67   O  VAL A  79           
SHEET    1  AB 2 LEU A 125  HIS A 126  0                                        
SHEET    2  AB 2 ILE A 149  ALA A 150 -1  O  ALA A 150   N  LEU A 125           
SHEET    1  AC 2 ILE A 134  LEU A 136  0                                        
SHEET    2  AC 2 VAL A 142  LEU A 144 -1  O  GLN A 143   N  PHE A 135           
SHEET    1  BA 5 TYR B   4  LYS B   9  0                                        
SHEET    2  BA 5 ALA B  18  SER B  23 -1  O  LEU B  20   N  LEU B   7           
SHEET    3  BA 5 GLN B  29  ASN B  36 -1  O  TYR B  30   N  VAL B  21           
SHEET    4  BA 5 SER B  75  ASP B  81 -1  O  LEU B  76   N  ILE B  35           
SHEET    5  BA 5 TYR B  66  GLU B  72 -1  N  ARG B  67   O  VAL B  79           
SHEET    1  BB 2 LEU B 125  HIS B 126  0                                        
SHEET    2  BB 2 ILE B 149  ALA B 150 -1  O  ALA B 150   N  LEU B 125           
SHEET    1  BC 2 ILE B 134  LEU B 136  0                                        
SHEET    2  BC 2 VAL B 142  LEU B 144 -1  O  GLN B 143   N  PHE B 135           
SSBOND   1 CYS A  163    CYS B  276                          1555   1555  2.09  
SSBOND   2 CYS A  276    CYS B  163                          1555   6555  2.56  
SITE     1 AC1  4 MET A  80  GLY A 145  ASP A 146  PHE A 147                    
SITE     1 AC2  1 GLN A 101                                                     
SITE     1 AC3  3 HIS A 120  ASN A 182  VAL A 249                               
SITE     1 AC4  2 ASN A 242  ARG A 244                                          
SITE     1 AC5  4 HIS B 120  ASN B 182  SER B 248  VAL B 249                    
SITE     1 AC6  2 ASN B  -5  GLY B  74                                          
SITE     1 AC7  3 ASN B 242  PRO B 243  ARG B 244                               
CRYST1   89.910   92.810  163.940  90.00  90.00  90.00 C 2 2 21     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011122  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010775  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006100        0.00000                         
MTRIX1   1  0.048540  0.998820  0.000850       -3.03855    1                    
MTRIX2   1 -0.998140  0.048540 -0.036970       41.88874    1                    
MTRIX3   1 -0.036970  0.000950  0.999320       41.92957    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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