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Database: PDB
Entry: 4Y83
LinkDB: 4Y83
Original site: 4Y83 
HEADER    TRANSFERASE                             16-FEB-15   4Y83              
TITLE     CRYSTAL STRUCTURE OF COT KINASE DOMAIN IN COMPLEX WITH 5-(2-AMINO-5-  
TITLE    2 (QUINOLIN-3-YL)PYRIDIN-3-YL)-1,3,4-OXADIAZOLE-2(3H)-THIONE           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 8;          
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: CANCER OSAKA THYROID ONCOGENE,PROTO-ONCOGENE C-COT,         
COMPND   5 SERINE/THREONINE-PROTEIN KINASE COT,TUMOR PROGRESSION LOCUS 2,TPL-2; 
COMPND   6 EC: 2.7.11.25;                                                       
COMPND   7 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: MAP3K8, COT, ESTF;                                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF21;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PFASTBAC1-HM                               
KEYWDS    COT, TPL-2, MAP3K8, KINASE, INHIBITOR, COMPLEX, TRANSFERASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.GUTMANN,A.HINNIGER                                                  
REVDAT   4   16-OCT-19 4Y83    1       REMARK                                   
REVDAT   3   24-JUN-15 4Y83    1       JRNL                                     
REVDAT   2   13-MAY-15 4Y83    1       JRNL                                     
REVDAT   1   06-MAY-15 4Y83    0                                                
JRNL        AUTH   S.GUTMANN,A.HINNIGER,G.FENDRICH,P.DRUCKES,S.ANTZ,H.MATTES,   
JRNL        AUTH 2 H.MOBITZ,S.OFNER,N.SCHMIEDEBERG,A.STOJANOVIC,S.RIEFFEL,      
JRNL        AUTH 3 A.STRAUSS,T.TROXLER,R.GLATTHAR,H.SPARRER                     
JRNL        TITL   THE CRYSTAL STRUCTURE OF CANCER OSAKA THYROID KINASE REVEALS 
JRNL        TITL 2 AN UNEXPECTED KINASE DOMAIN FOLD.                            
JRNL        REF    J.BIOL.CHEM.                  V. 290 15210 2015              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   25918157                                                     
JRNL        DOI    10.1074/JBC.M115.648097                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.89 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT BUSTER 2.11.5                             
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 88.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 28212                          
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)  : 0.204                          
REMARK   3   R VALUE            (WORKING SET)  : 0.202                          
REMARK   3   FREE R VALUE                      : 0.240                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1411                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 14                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.89                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.00                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.99                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3012                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2149                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2861                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2119                   
REMARK   3   BIN FREE R VALUE                        : 0.2700                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.01                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 151                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6124                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 167                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 76.04                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.21990                                              
REMARK   3    B22 (A**2) : 0.21990                                              
REMARK   3    B33 (A**2) : -0.43980                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.388               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.737               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.316               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.880               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.328               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.903                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.865                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6339   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 8665   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1846   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 85     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1005   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6339   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 888    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 6799   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.04                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.19                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.56                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -0.6497   -8.1952   -6.9520           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3412 T22:   -0.3417                                    
REMARK   3     T33:   -0.3837 T12:   -0.0272                                    
REMARK   3     T13:    0.0166 T23:   -0.0750                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.9825 L22:    1.2984                                    
REMARK   3     L33:    3.3430 L12:   -0.5338                                    
REMARK   3     L13:    0.9217 L23:   -0.2201                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2171 S12:    0.1632 S13:   -0.0500                     
REMARK   3     S21:   -0.0418 S22:    0.1839 S23:   -0.1926                     
REMARK   3     S31:    0.3065 S32:    0.0608 S33:    0.0332                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   43.5562  -33.8076  -24.1096           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3393 T22:   -0.4061                                    
REMARK   3     T33:   -0.3856 T12:   -0.0015                                    
REMARK   3     T13:    0.0748 T23:    0.0007                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4220 L22:    2.2807                                    
REMARK   3     L33:    3.7146 L12:   -0.8206                                    
REMARK   3     L13:    0.2857 L23:   -0.8943                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0131 S12:    0.1173 S13:    0.1203                     
REMARK   3     S21:    0.2481 S22:    0.0503 S23:    0.2157                     
REMARK   3     S31:    0.1875 S32:   -0.2137 S33:   -0.0371                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    8.8532  -62.5928   -7.7941           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.4984 T22:   -0.2758                                    
REMARK   3     T33:   -0.3359 T12:   -0.0245                                    
REMARK   3     T13:    0.1010 T23:   -0.0027                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.1698 L22:    3.2713                                    
REMARK   3     L33:    4.3283 L12:    0.3742                                    
REMARK   3     L13:    0.3669 L23:   -2.3109                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.4433 S12:   -0.1795 S13:   -0.5087                     
REMARK   3     S21:   -0.2562 S22:    0.0174 S23:   -0.0947                     
REMARK   3     S31:    0.0001 S32:    0.4749 S33:    0.4259                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4Y83 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-FEB-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000207021.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28213                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.890                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 88.310                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.760                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.7200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.670                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR SOLUTION: 8% (W/V) PEG4000,    
REMARK 280  12% (V/V) ETHYLENE GLYCOL, 7% (V/V) ISO-PROPANOL, PH 7.6, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.10500            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       72.21000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    64                                                      
REMARK 465     PRO A    65                                                      
REMARK 465     SER A    66                                                      
REMARK 465     GLY A    67                                                      
REMARK 465     GLN A    68                                                      
REMARK 465     GLU A    69                                                      
REMARK 465     VAL A    70                                                      
REMARK 465     PRO A    71                                                      
REMARK 465     TRP A    72                                                      
REMARK 465     ILE A    91                                                      
REMARK 465     SER A    92                                                      
REMARK 465     ASN A    93                                                      
REMARK 465     THR A    94                                                      
REMARK 465     ALA A    95                                                      
REMARK 465     LYS A    96                                                      
REMARK 465     HIS A    97                                                      
REMARK 465     PHE A    98                                                      
REMARK 465     TYR A    99                                                      
REMARK 465     GLY A   100                                                      
REMARK 465     GLN A   101                                                      
REMARK 465     PRO A   332                                                      
REMARK 465     ARG A   333                                                      
REMARK 465     SER A   334                                                      
REMARK 465     ALA A   335                                                      
REMARK 465     TYR A   336                                                      
REMARK 465     PRO A   337                                                      
REMARK 465     SER A   338                                                      
REMARK 465     PRO A   390                                                      
REMARK 465     PRO A   391                                                      
REMARK 465     ARG A   392                                                      
REMARK 465     GLU A   393                                                      
REMARK 465     ASP A   394                                                      
REMARK 465     GLN A   395                                                      
REMARK 465     GLY B    64                                                      
REMARK 465     PRO B    65                                                      
REMARK 465     SER B    66                                                      
REMARK 465     GLY B    67                                                      
REMARK 465     GLN B    68                                                      
REMARK 465     GLU B    69                                                      
REMARK 465     VAL B    70                                                      
REMARK 465     PRO B    71                                                      
REMARK 465     TRP B    72                                                      
REMARK 465     ASN B    93                                                      
REMARK 465     THR B    94                                                      
REMARK 465     ALA B    95                                                      
REMARK 465     LYS B    96                                                      
REMARK 465     HIS B    97                                                      
REMARK 465     PHE B    98                                                      
REMARK 465     TYR B    99                                                      
REMARK 465     GLY B   100                                                      
REMARK 465     GLN B   101                                                      
REMARK 465     ARG B   102                                                      
REMARK 465     GLY B   147                                                      
REMARK 465     ALA B   148                                                      
REMARK 465     ARG B   333                                                      
REMARK 465     SER B   334                                                      
REMARK 465     ALA B   335                                                      
REMARK 465     TYR B   336                                                      
REMARK 465     PRO B   391                                                      
REMARK 465     ARG B   392                                                      
REMARK 465     GLU B   393                                                      
REMARK 465     ASP B   394                                                      
REMARK 465     GLN B   395                                                      
REMARK 465     GLY C    64                                                      
REMARK 465     PRO C    65                                                      
REMARK 465     SER C    66                                                      
REMARK 465     GLY C    67                                                      
REMARK 465     GLN C    68                                                      
REMARK 465     GLU C    69                                                      
REMARK 465     VAL C    70                                                      
REMARK 465     PRO C    71                                                      
REMARK 465     TRP C    72                                                      
REMARK 465     LEU C    73                                                      
REMARK 465     ILE C    91                                                      
REMARK 465     SER C    92                                                      
REMARK 465     ASN C    93                                                      
REMARK 465     THR C    94                                                      
REMARK 465     ALA C    95                                                      
REMARK 465     LYS C    96                                                      
REMARK 465     HIS C    97                                                      
REMARK 465     PHE C    98                                                      
REMARK 465     TYR C    99                                                      
REMARK 465     GLY C   100                                                      
REMARK 465     GLN C   101                                                      
REMARK 465     ARG C   102                                                      
REMARK 465     LEU C   128                                                      
REMARK 465     GLY C   147                                                      
REMARK 465     ALA C   148                                                      
REMARK 465     PHE C   149                                                      
REMARK 465     THR C   278                                                      
REMARK 465     ARG C   333                                                      
REMARK 465     SER C   334                                                      
REMARK 465     ALA C   335                                                      
REMARK 465     ALA C   354                                                      
REMARK 465     ASP C   355                                                      
REMARK 465     ASP C   356                                                      
REMARK 465     PRO C   390                                                      
REMARK 465     PRO C   391                                                      
REMARK 465     ARG C   392                                                      
REMARK 465     GLU C   393                                                      
REMARK 465     ASP C   394                                                      
REMARK 465     GLN C   395                                                      
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     LEU A  73    CG   CD1  CD2                                       
REMARK 470     SER A  74    OG                                                  
REMARK 470     ARG A  77    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A  89    CG   OD1  ND2                                       
REMARK 470     HIS A  90    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 102    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 106    OG                                                  
REMARK 470     ILE A 108    CG1  CG2  CD1                                       
REMARK 470     LEU A 109    CG   CD1  CD2                                       
REMARK 470     MET A 112    CG   SD   CE                                        
REMARK 470     VAL A 113    CG1  CG2                                            
REMARK 470     ILE A 114    CG1  CG2  CD1                                       
REMARK 470     GLN A 117    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 118    CG   OD1  ND2                                       
REMARK 470     ILE A 123    CG1  CG2  CD1                                       
REMARK 470     ASP A 124    CG   OD1  OD2                                       
REMARK 470     SER A 125    OG                                                  
REMARK 470     VAL A 127    CG1  CG2                                            
REMARK 470     LEU A 128    CG   CD1  CD2                                       
REMARK 470     LEU A 129    CG   CD1  CD2                                       
REMARK 470     LYS A 133    CG   CD   CE   NZ                                   
REMARK 470     ILE A 158    CG1  CG2  CD1                                       
REMARK 470     LYS A 161    CG   CD   CE   NZ                                   
REMARK 470     LYS A 162    CG   CD   CE   NZ                                   
REMARK 470     ILE A 169    CG1  CG2  CD1                                       
REMARK 470     VAL A 171    CG1  CG2                                            
REMARK 470     ASP A 172    CG   OD1  OD2                                       
REMARK 470     GLN A 173    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 175    CG   CD   CE   NZ                                   
REMARK 470     VAL A 179    CG1  CG2                                            
REMARK 470     ILE A 181    CG1  CG2  CD1                                       
REMARK 470     GLU A 201    CG   CD   OE1  OE2                                  
REMARK 470     THR A 202    OG1  CG2                                            
REMARK 470     LYS A 218    CG   CD   CE   NZ                                   
REMARK 470     GLU A 227    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 231    CG1  CG2  CD1                                       
REMARK 470     LYS A 235    CG   CD   CE   NZ                                   
REMARK 470     ASP A 242    OD1  OD2                                            
REMARK 470     LYS A 248    CG   CD   CE   NZ                                   
REMARK 470     ILE A 254    CD1                                                 
REMARK 470     THR A 264    OG1  CG2                                            
REMARK 470     VAL A 267    CG1  CG2                                            
REMARK 470     VAL A 275    CG1  CG2                                            
REMARK 470     GLU A 279    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 280    CG   OD1  OD2                                       
REMARK 470     VAL A 281    CG1  CG2                                            
REMARK 470     LYS A 285    CG   CD   CE   NZ                                   
REMARK 470     ASP A 286    CG   OD1  OD2                                       
REMARK 470     ARG A 288    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 292    CG1  CG2  CD1                                       
REMARK 470     ILE A 299    CG1  CG2  CD1                                       
REMARK 470     LEU A 300    CG   CD1  CD2                                       
REMARK 470     ARG A 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 318    CG1  CG2  CD1                                       
REMARK 470     GLN A 321    CG   CD   OE1  NE2                                  
REMARK 470     THR A 322    OG1  CG2                                            
REMARK 470     THR A 324    OG1  CG2                                            
REMARK 470     PRO A 325    CG   CD                                             
REMARK 470     LYS A 329    CG   CD   CE   NZ                                   
REMARK 470     ARG A 330    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A 341    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     HIS A 344    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 345    CG   CD   CE   NZ                                   
REMARK 470     GLN A 346    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 350    CG   CD1  CD2                                       
REMARK 470     ASP A 355    CG   OD1  OD2                                       
REMARK 470     ASP A 356    CG   OD1  OD2                                       
REMARK 470     SER A 358    OG                                                  
REMARK 470     MET A 361    CG   SD   CE                                        
REMARK 470     GLU A 363    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 364    CG   CD1  CD2                                       
REMARK 470     ASN A 374    CG   OD1  ND2                                       
REMARK 470     GLU A 386    CG   CD   OE1  OE2                                  
REMARK 470     SER B  74    OG                                                  
REMARK 470     GLU B  82    CG   CD   OE1  OE2                                  
REMARK 470     LEU B  85    CG   CD1  CD2                                       
REMARK 470     HIS B  90    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE B  91    CG1  CG2  CD1                                       
REMARK 470     PRO B 103    CG   CD                                             
REMARK 470     GLU B 105    CG   CD   OE1  OE2                                  
REMARK 470     SER B 106    OG                                                  
REMARK 470     ASN B 111    CG   OD1  ND2                                       
REMARK 470     MET B 112    CE                                                  
REMARK 470     VAL B 113    CG1  CG2                                            
REMARK 470     ILE B 114    CG1  CG2  CD1                                       
REMARK 470     PRO B 116    CG   CD                                             
REMARK 470     GLN B 117    CG   CD   OE1  NE2                                  
REMARK 470     ASN B 118    CG   OD1  ND2                                       
REMARK 470     ARG B 120    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 122    CG   CD   OE1  NE2                                  
REMARK 470     ILE B 123    CG1  CG2  CD1                                       
REMARK 470     SER B 125    OG                                                  
REMARK 470     LEU B 128    CG   CD1  CD2                                       
REMARK 470     LEU B 129    CG   CD1  CD2                                       
REMARK 470     ILE B 130    CG1  CG2  CD1                                       
REMARK 470     PRO B 131    CG   CD                                             
REMARK 470     LYS B 133    CG   CD   CE   NZ                                   
REMARK 470     SER B 141    OG                                                  
REMARK 470     PHE B 149    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 151    CD   CE   NZ                                        
REMARK 470     ILE B 158    CG1  CG2  CD1                                       
REMARK 470     LYS B 159    CG   CD   CE   NZ                                   
REMARK 470     LYS B 161    CG   CD   CE   NZ                                   
REMARK 470     ILE B 169    CG1  CG2  CD1                                       
REMARK 470     VAL B 171    CG1  CG2                                            
REMARK 470     ASP B 172    CG   OD1  OD2                                       
REMARK 470     GLN B 173    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 175    CG   CD   CE   NZ                                   
REMARK 470     PRO B 176    CG   CD                                             
REMARK 470     SER B 177    OG                                                  
REMARK 470     GLU B 180    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 181    CG1  CG2  CD1                                       
REMARK 470     GLU B 201    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 203    CG1  CG2                                            
REMARK 470     LEU B 216    CG   CD1  CD2                                       
REMARK 470     LYS B 218    CG   CD   CE   NZ                                   
REMARK 470     LEU B 219    CG   CD1  CD2                                       
REMARK 470     GLU B 227    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 233    CG1  CG2                                            
REMARK 470     ASP B 242    OD1  OD2                                            
REMARK 470     LEU B 244    CD1  CD2                                            
REMARK 470     VAL B 249    CG1  CG2                                            
REMARK 470     ILE B 259    CG1  CG2  CD1                                       
REMARK 470     MET B 262    CG   SD   CE                                        
REMARK 470     SER B 263    OG                                                  
REMARK 470     VAL B 275    CG1  CG2                                            
REMARK 470     THR B 278    OG1  CG2                                            
REMARK 470     GLU B 279    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 280    CG   OD1  OD2                                       
REMARK 470     LYS B 285    CG   CD   CE   NZ                                   
REMARK 470     ASP B 286    CG   OD1  OD2                                       
REMARK 470     LEU B 287    CG   CD1  CD2                                       
REMARK 470     SER B 295    OG                                                  
REMARK 470     ILE B 299    CG1  CG2  CD1                                       
REMARK 470     LEU B 300    CG   CD1  CD2                                       
REMARK 470     ARG B 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 305    OG                                                  
REMARK 470     LEU B 313    CG   CD1  CD2                                       
REMARK 470     THR B 316    CG2                                                 
REMARK 470     ILE B 318    CG1  CG2  CD1                                       
REMARK 470     GLN B 321    CG   CD   OE1  NE2                                  
REMARK 470     THR B 322    CG2                                                 
REMARK 470     VAL B 328    CG1  CG2                                            
REMARK 470     LYS B 329    CG   CD   CE   NZ                                   
REMARK 470     SER B 338    OG                                                  
REMARK 470     LEU B 340    CG   CD1  CD2                                       
REMARK 470     TYR B 341    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE B 342    CG1  CG2  CD1                                       
REMARK 470     ILE B 343    CG1  CG2  CD1                                       
REMARK 470     HIS B 344    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 345    CG   CD   CE   NZ                                   
REMARK 470     GLN B 346    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 351    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 356    CG   OD1  OD2                                       
REMARK 470     SER B 358    OG                                                  
REMARK 470     MET B 361    CG   SD   CE                                        
REMARK 470     GLU B 363    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 365    CG1  CG2  CD1                                       
REMARK 470     GLU B 366    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 371    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 372    OD1  ND2                                            
REMARK 470     LYS B 384    CG   CD   CE   NZ                                   
REMARK 470     ASN B 389    CG   OD1  ND2                                       
REMARK 470     SER C  74    OG                                                  
REMARK 470     ARG C  77    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C  82    CG   CD   OE1  OE2                                  
REMARK 470     LEU C  84    CG   CD1  CD2                                       
REMARK 470     LEU C  85    CG   CD1  CD2                                       
REMARK 470     HIS C  90    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PRO C 103    CG   CD                                             
REMARK 470     GLN C 104    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 105    CG   CD   OE1  OE2                                  
REMARK 470     SER C 106    OG                                                  
REMARK 470     ILE C 108    CG1  CG2  CD1                                       
REMARK 470     MET C 112    CE                                                  
REMARK 470     VAL C 113    CG1  CG2                                            
REMARK 470     THR C 115    OG1  CG2                                            
REMARK 470     GLN C 117    CG   CD   OE1  NE2                                  
REMARK 470     ASN C 118    CG   OD1  ND2                                       
REMARK 470     ARG C 120    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR C 121    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN C 122    CG   CD   OE1  NE2                                  
REMARK 470     ILE C 123    CG1  CG2  CD1                                       
REMARK 470     ASP C 124    CG   OD1  OD2                                       
REMARK 470     SER C 125    OG                                                  
REMARK 470     ASP C 126    CG   OD1  OD2                                       
REMARK 470     VAL C 127    CG1  CG2                                            
REMARK 470     LEU C 129    CG   CD1  CD2                                       
REMARK 470     ILE C 130    CG1  CG2  CD1                                       
REMARK 470     LYS C 133    CG   CD   CE   NZ                                   
REMARK 470     LEU C 134    CG   CD1  CD2                                       
REMARK 470     THR C 135    OG1  CG2                                            
REMARK 470     TYR C 136    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG C 137    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN C 138    CG   OD1  ND2                                       
REMARK 470     ILE C 139    CG1  CG2  CD1                                       
REMARK 470     SER C 141    OG                                                  
REMARK 470     ASP C 142    CG   OD1  OD2                                       
REMARK 470     PHE C 143    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C 151    CG   CD   CE   NZ                                   
REMARK 470     GLN C 156    CG   CD   OE1  NE2                                  
REMARK 470     ILE C 158    CG1  CG2  CD1                                       
REMARK 470     LYS C 159    CG   CD   CE   NZ                                   
REMARK 470     LYS C 161    CG   CD   CE   NZ                                   
REMARK 470     LYS C 162    CG   CD   CE   NZ                                   
REMARK 470     LYS C 167    CG   CD   CE   NZ                                   
REMARK 470     LEU C 168    CG   CD1  CD2                                       
REMARK 470     ILE C 169    CG1  CG2  CD1                                       
REMARK 470     VAL C 171    CG1  CG2                                            
REMARK 470     ASP C 172    CG   OD1  OD2                                       
REMARK 470     GLN C 173    CG   CD   OE1  NE2                                  
REMARK 470     PHE C 174    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C 175    CG   CD   CE   NZ                                   
REMARK 470     PRO C 176    CG   CD                                             
REMARK 470     SER C 177    OG                                                  
REMARK 470     ASP C 178    CG   OD1  OD2                                       
REMARK 470     VAL C 179    CG1  CG2                                            
REMARK 470     GLU C 180    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 181    CG1  CG2  CD1                                       
REMARK 470     GLN C 182    OE1  NE2                                            
REMARK 470     ARG C 186    NE   CZ   NH1  NH2                                  
REMARK 470     ILE C 190    CG1  CG2  CD1                                       
REMARK 470     GLU C 192    OE1  OE2                                            
REMARK 470     LEU C 193    CG   CD1  CD2                                       
REMARK 470     VAL C 197    CG1  CG2                                            
REMARK 470     LEU C 198    CG   CD1  CD2                                       
REMARK 470     TRP C 199    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP C 199    CZ3  CH2                                            
REMARK 470     GLU C 201    CG   CD   OE1  OE2                                  
REMARK 470     THR C 202    OG1  CG2                                            
REMARK 470     VAL C 203    CG1  CG2                                            
REMARK 470     LEU C 205    CG   CD1  CD2                                       
REMARK 470     PHE C 206    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER C 214    OG                                                  
REMARK 470     LEU C 216    CG   CD1  CD2                                       
REMARK 470     GLU C 217    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 218    CG   CD   CE   NZ                                   
REMARK 470     LEU C 219    CG   CD1  CD2                                       
REMARK 470     SER C 221    OG                                                  
REMARK 470     PRO C 224    CG   CD                                             
REMARK 470     GLU C 227    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 229    CG   CD   OE1  OE2                                  
REMARK 470     VAL C 233    CG1  CG2                                            
REMARK 470     THR C 234    OG1  CG2                                            
REMARK 470     LYS C 235    CG   CD   CE   NZ                                   
REMARK 470     VAL C 237    CG1  CG2                                            
REMARK 470     LEU C 244    CG   CD1  CD2                                       
REMARK 470     LYS C 248    CG   CD   CE   NZ                                   
REMARK 470     ILE C 250    CG1  CG2  CD1                                       
REMARK 470     ILE C 254    CG1  CG2  CD1                                       
REMARK 470     LYS C 255    CG   CD   CE   NZ                                   
REMARK 470     ILE C 259    CG1  CG2  CD1                                       
REMARK 470     VAL C 260    CG1  CG2                                            
REMARK 470     THR C 264    OG1  CG2                                            
REMARK 470     LYS C 265    CE   NZ                                             
REMARK 470     VAL C 267    CG1  CG2                                            
REMARK 470     VAL C 269    CG1  CG2                                            
REMARK 470     ASP C 270    CG   OD1  OD2                                       
REMARK 470     SER C 274    OG                                                  
REMARK 470     VAL C 275    CG1  CG2                                            
REMARK 470     GLN C 276    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 279    CG   CD   OE1  OE2                                  
REMARK 470     VAL C 281    CG1  CG2                                            
REMARK 470     TYR C 282    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE C 283    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C 285    CG   CD   CE   NZ                                   
REMARK 470     ASP C 286    CG   OD1  OD2                                       
REMARK 470     LEU C 287    CG   CD1  CD2                                       
REMARK 470     ARG C 288    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE C 292    CG1  CG2  CD1                                       
REMARK 470     GLU C 297    CG   CD   OE1  OE2                                  
REMARK 470     VAL C 298    CG1  CG2                                            
REMARK 470     ILE C 299    CG1  CG2  CD1                                       
REMARK 470     LEU C 300    CG   CD1  CD2                                       
REMARK 470     CYS C 301    SG                                                  
REMARK 470     ARG C 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS C 304    ND1  CD2  CE1  NE2                                  
REMARK 470     SER C 305    OG                                                  
REMARK 470     THR C 306    OG1  CG2                                            
REMARK 470     LYS C 307    CG   CD   CE   NZ                                   
REMARK 470     ILE C 310    CG1  CG2  CD1                                       
REMARK 470     SER C 312    OG                                                  
REMARK 470     THR C 316    CG2                                                 
REMARK 470     ILE C 318    CG1  CG2  CD1                                       
REMARK 470     GLN C 321    CD   OE1  NE2                                       
REMARK 470     THR C 322    OG1  CG2                                            
REMARK 470     THR C 324    OG1  CG2                                            
REMARK 470     VAL C 328    CG1  CG2                                            
REMARK 470     LYS C 329    CG   CD   CE   NZ                                   
REMARK 470     TYR C 331    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR C 336    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER C 338    OG                                                  
REMARK 470     TYR C 339    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU C 340    CG   CD1  CD2                                       
REMARK 470     ILE C 342    CG1  CG2  CD1                                       
REMARK 470     ILE C 343    CG1  CG2  CD1                                       
REMARK 470     LYS C 345    CG   CD   CE   NZ                                   
REMARK 470     GLU C 351    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 352    CG   OD1  OD2                                       
REMARK 470     GLU C 363    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 364    CG   CD1  CD2                                       
REMARK 470     ILE C 365    CG1  CG2  CD1                                       
REMARK 470     GLU C 366    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 369    CG   CD1  CD2                                       
REMARK 470     GLU C 370    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 371    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN C 372    CG   OD1  ND2                                       
REMARK 470     ASN C 374    CG   OD1  ND2                                       
REMARK 470     HIS C 375    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PRO C 377    CG   CD                                             
REMARK 470     ARG C 378    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 381    CG   OD1  OD2                                       
REMARK 470     LEU C 382    CG   CD1  CD2                                       
REMARK 470     LYS C 384    CG   CD   CE   NZ                                   
REMARK 470     LEU C 388    CG   CD1  CD2                                       
REMARK 470     ASN C 389    CG   OD1  ND2                                       
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    ASP A 124       -6.63     67.09                                   
REMARK 500    PHE A 149       43.05    -98.43                                   
REMARK 500    HIS A 252       -1.41     76.28                                   
REMARK 500    ASP A 253       52.48   -150.60                                   
REMARK 500    MET A 262     -167.55   -120.83                                   
REMARK 500    ASP A 270       92.70     65.19                                   
REMARK 500    CYS A 301       15.08     58.81                                   
REMARK 500    TRP A 327      -42.72     77.93                                   
REMARK 500    ASP B 124       -7.54     67.98                                   
REMARK 500    HIS B 252        5.72    -65.30                                   
REMARK 500    MET B 262     -166.08   -121.85                                   
REMARK 500    ASP B 270       91.08     58.04                                   
REMARK 500    CYS B 301       14.75     58.34                                   
REMARK 500    TRP B 327      -42.39     77.32                                   
REMARK 500    ASP C 124       -1.37     65.32                                   
REMARK 500    HIS C 252        5.59    -64.95                                   
REMARK 500    MET C 262     -167.13   -120.60                                   
REMARK 500    ASP C 270       91.32     58.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    THR B 115        -10.05                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 557        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A 558        DISTANCE =  6.58 ANGSTROMS                       
REMARK 525    HOH A 559        DISTANCE =  6.76 ANGSTROMS                       
REMARK 525    HOH A 560        DISTANCE =  6.77 ANGSTROMS                       
REMARK 525    HOH A 561        DISTANCE =  6.89 ANGSTROMS                       
REMARK 525    HOH A 562        DISTANCE =  6.97 ANGSTROMS                       
REMARK 525    HOH A 563        DISTANCE =  7.08 ANGSTROMS                       
REMARK 525    HOH A 564        DISTANCE =  7.79 ANGSTROMS                       
REMARK 525    HOH A 565        DISTANCE =  8.15 ANGSTROMS                       
REMARK 525    HOH A 566        DISTANCE =  8.34 ANGSTROMS                       
REMARK 525    HOH A 567        DISTANCE =  8.38 ANGSTROMS                       
REMARK 525    HOH A 568        DISTANCE =  9.08 ANGSTROMS                       
REMARK 525    HOH A 569        DISTANCE = 10.05 ANGSTROMS                       
REMARK 525    HOH B 557        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH B 558        DISTANCE =  7.12 ANGSTROMS                       
REMARK 525    HOH B 559        DISTANCE =  7.17 ANGSTROMS                       
REMARK 525    HOH B 560        DISTANCE =  8.04 ANGSTROMS                       
REMARK 525    HOH C 537        DISTANCE =  9.94 ANGSTROMS                       
REMARK 525    HOH C 538        DISTANCE = 11.94 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 49B A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 49B B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 49B C 401                 
DBREF  4Y83 A   66   395  UNP    P41279   M3K8_HUMAN      66    395             
DBREF  4Y83 B   66   395  UNP    P41279   M3K8_HUMAN      66    395             
DBREF  4Y83 C   66   395  UNP    P41279   M3K8_HUMAN      66    395             
SEQADV 4Y83 GLY A   64  UNP  P41279              EXPRESSION TAG                 
SEQADV 4Y83 PRO A   65  UNP  P41279              EXPRESSION TAG                 
SEQADV 4Y83 GLY B   64  UNP  P41279              EXPRESSION TAG                 
SEQADV 4Y83 PRO B   65  UNP  P41279              EXPRESSION TAG                 
SEQADV 4Y83 GLY C   64  UNP  P41279              EXPRESSION TAG                 
SEQADV 4Y83 PRO C   65  UNP  P41279              EXPRESSION TAG                 
SEQRES   1 A  332  GLY PRO SER GLY GLN GLU VAL PRO TRP LEU SER SER VAL          
SEQRES   2 A  332  ARG TYR GLY THR VAL GLU ASP LEU LEU ALA PHE ALA ASN          
SEQRES   3 A  332  HIS ILE SER ASN THR ALA LYS HIS PHE TYR GLY GLN ARG          
SEQRES   4 A  332  PRO GLN GLU SER GLY ILE LEU LEU ASN MET VAL ILE THR          
SEQRES   5 A  332  PRO GLN ASN GLY ARG TYR GLN ILE ASP SER ASP VAL LEU          
SEQRES   6 A  332  LEU ILE PRO TRP LYS LEU THR TYR ARG ASN ILE GLY SER          
SEQRES   7 A  332  ASP PHE ILE PRO ARG GLY ALA PHE GLY LYS VAL TYR LEU          
SEQRES   8 A  332  ALA GLN ASP ILE LYS THR LYS LYS ARG MET ALA CYS LYS          
SEQRES   9 A  332  LEU ILE PRO VAL ASP GLN PHE LYS PRO SER ASP VAL GLU          
SEQRES  10 A  332  ILE GLN ALA CYS PHE ARG HIS GLU ASN ILE ALA GLU LEU          
SEQRES  11 A  332  TYR GLY ALA VAL LEU TRP GLY GLU THR VAL HIS LEU PHE          
SEQRES  12 A  332  MET GLU ALA GLY GLU GLY GLY SER VAL LEU GLU LYS LEU          
SEQRES  13 A  332  GLU SER CYS GLY PRO MET ARG GLU PHE GLU ILE ILE TRP          
SEQRES  14 A  332  VAL THR LYS HIS VAL LEU LYS GLY LEU ASP PHE LEU HIS          
SEQRES  15 A  332  SER LYS LYS VAL ILE HIS HIS ASP ILE LYS PRO SER ASN          
SEQRES  16 A  332  ILE VAL PHE MET SER THR LYS ALA VAL LEU VAL ASP PHE          
SEQRES  17 A  332  GLY LEU SER VAL GLN MET THR GLU ASP VAL TYR PHE PRO          
SEQRES  18 A  332  LYS ASP LEU ARG GLY THR GLU ILE TYR MET SER PRO GLU          
SEQRES  19 A  332  VAL ILE LEU CYS ARG GLY HIS SER THR LYS ALA ASP ILE          
SEQRES  20 A  332  TYR SER LEU GLY ALA THR LEU ILE HIS MET GLN THR GLY          
SEQRES  21 A  332  THR PRO PRO TRP VAL LYS ARG TYR PRO ARG SER ALA TYR          
SEQRES  22 A  332  PRO SER TYR LEU TYR ILE ILE HIS LYS GLN ALA PRO PRO          
SEQRES  23 A  332  LEU GLU ASP ILE ALA ASP ASP CYS SER PRO GLY MET ARG          
SEQRES  24 A  332  GLU LEU ILE GLU ALA SER LEU GLU ARG ASN PRO ASN HIS          
SEQRES  25 A  332  ARG PRO ARG ALA ALA ASP LEU LEU LYS HIS GLU ALA LEU          
SEQRES  26 A  332  ASN PRO PRO ARG GLU ASP GLN                                  
SEQRES   1 B  332  GLY PRO SER GLY GLN GLU VAL PRO TRP LEU SER SER VAL          
SEQRES   2 B  332  ARG TYR GLY THR VAL GLU ASP LEU LEU ALA PHE ALA ASN          
SEQRES   3 B  332  HIS ILE SER ASN THR ALA LYS HIS PHE TYR GLY GLN ARG          
SEQRES   4 B  332  PRO GLN GLU SER GLY ILE LEU LEU ASN MET VAL ILE THR          
SEQRES   5 B  332  PRO GLN ASN GLY ARG TYR GLN ILE ASP SER ASP VAL LEU          
SEQRES   6 B  332  LEU ILE PRO TRP LYS LEU THR TYR ARG ASN ILE GLY SER          
SEQRES   7 B  332  ASP PHE ILE PRO ARG GLY ALA PHE GLY LYS VAL TYR LEU          
SEQRES   8 B  332  ALA GLN ASP ILE LYS THR LYS LYS ARG MET ALA CYS LYS          
SEQRES   9 B  332  LEU ILE PRO VAL ASP GLN PHE LYS PRO SER ASP VAL GLU          
SEQRES  10 B  332  ILE GLN ALA CYS PHE ARG HIS GLU ASN ILE ALA GLU LEU          
SEQRES  11 B  332  TYR GLY ALA VAL LEU TRP GLY GLU THR VAL HIS LEU PHE          
SEQRES  12 B  332  MET GLU ALA GLY GLU GLY GLY SER VAL LEU GLU LYS LEU          
SEQRES  13 B  332  GLU SER CYS GLY PRO MET ARG GLU PHE GLU ILE ILE TRP          
SEQRES  14 B  332  VAL THR LYS HIS VAL LEU LYS GLY LEU ASP PHE LEU HIS          
SEQRES  15 B  332  SER LYS LYS VAL ILE HIS HIS ASP ILE LYS PRO SER ASN          
SEQRES  16 B  332  ILE VAL PHE MET SER THR LYS ALA VAL LEU VAL ASP PHE          
SEQRES  17 B  332  GLY LEU SER VAL GLN MET THR GLU ASP VAL TYR PHE PRO          
SEQRES  18 B  332  LYS ASP LEU ARG GLY THR GLU ILE TYR MET SER PRO GLU          
SEQRES  19 B  332  VAL ILE LEU CYS ARG GLY HIS SER THR LYS ALA ASP ILE          
SEQRES  20 B  332  TYR SER LEU GLY ALA THR LEU ILE HIS MET GLN THR GLY          
SEQRES  21 B  332  THR PRO PRO TRP VAL LYS ARG TYR PRO ARG SER ALA TYR          
SEQRES  22 B  332  PRO SER TYR LEU TYR ILE ILE HIS LYS GLN ALA PRO PRO          
SEQRES  23 B  332  LEU GLU ASP ILE ALA ASP ASP CYS SER PRO GLY MET ARG          
SEQRES  24 B  332  GLU LEU ILE GLU ALA SER LEU GLU ARG ASN PRO ASN HIS          
SEQRES  25 B  332  ARG PRO ARG ALA ALA ASP LEU LEU LYS HIS GLU ALA LEU          
SEQRES  26 B  332  ASN PRO PRO ARG GLU ASP GLN                                  
SEQRES   1 C  332  GLY PRO SER GLY GLN GLU VAL PRO TRP LEU SER SER VAL          
SEQRES   2 C  332  ARG TYR GLY THR VAL GLU ASP LEU LEU ALA PHE ALA ASN          
SEQRES   3 C  332  HIS ILE SER ASN THR ALA LYS HIS PHE TYR GLY GLN ARG          
SEQRES   4 C  332  PRO GLN GLU SER GLY ILE LEU LEU ASN MET VAL ILE THR          
SEQRES   5 C  332  PRO GLN ASN GLY ARG TYR GLN ILE ASP SER ASP VAL LEU          
SEQRES   6 C  332  LEU ILE PRO TRP LYS LEU THR TYR ARG ASN ILE GLY SER          
SEQRES   7 C  332  ASP PHE ILE PRO ARG GLY ALA PHE GLY LYS VAL TYR LEU          
SEQRES   8 C  332  ALA GLN ASP ILE LYS THR LYS LYS ARG MET ALA CYS LYS          
SEQRES   9 C  332  LEU ILE PRO VAL ASP GLN PHE LYS PRO SER ASP VAL GLU          
SEQRES  10 C  332  ILE GLN ALA CYS PHE ARG HIS GLU ASN ILE ALA GLU LEU          
SEQRES  11 C  332  TYR GLY ALA VAL LEU TRP GLY GLU THR VAL HIS LEU PHE          
SEQRES  12 C  332  MET GLU ALA GLY GLU GLY GLY SER VAL LEU GLU LYS LEU          
SEQRES  13 C  332  GLU SER CYS GLY PRO MET ARG GLU PHE GLU ILE ILE TRP          
SEQRES  14 C  332  VAL THR LYS HIS VAL LEU LYS GLY LEU ASP PHE LEU HIS          
SEQRES  15 C  332  SER LYS LYS VAL ILE HIS HIS ASP ILE LYS PRO SER ASN          
SEQRES  16 C  332  ILE VAL PHE MET SER THR LYS ALA VAL LEU VAL ASP PHE          
SEQRES  17 C  332  GLY LEU SER VAL GLN MET THR GLU ASP VAL TYR PHE PRO          
SEQRES  18 C  332  LYS ASP LEU ARG GLY THR GLU ILE TYR MET SER PRO GLU          
SEQRES  19 C  332  VAL ILE LEU CYS ARG GLY HIS SER THR LYS ALA ASP ILE          
SEQRES  20 C  332  TYR SER LEU GLY ALA THR LEU ILE HIS MET GLN THR GLY          
SEQRES  21 C  332  THR PRO PRO TRP VAL LYS ARG TYR PRO ARG SER ALA TYR          
SEQRES  22 C  332  PRO SER TYR LEU TYR ILE ILE HIS LYS GLN ALA PRO PRO          
SEQRES  23 C  332  LEU GLU ASP ILE ALA ASP ASP CYS SER PRO GLY MET ARG          
SEQRES  24 C  332  GLU LEU ILE GLU ALA SER LEU GLU ARG ASN PRO ASN HIS          
SEQRES  25 C  332  ARG PRO ARG ALA ALA ASP LEU LEU LYS HIS GLU ALA LEU          
SEQRES  26 C  332  ASN PRO PRO ARG GLU ASP GLN                                  
HET    49B  A 401      23                                                       
HET    49B  B 401      23                                                       
HET    49B  C 401      23                                                       
HETNAM     49B 5-[2-AMINO-5-(QUINOLIN-3-YL)PYRIDIN-3-YL]-1,3,4-                 
HETNAM   2 49B  OXADIAZOLE-2(3H)-THIONE                                         
FORMUL   4  49B    3(C16 H11 N5 O S)                                            
FORMUL   7  HOH   *167(H2 O)                                                    
HELIX    1 AA1 THR A   80  HIS A   90  1                                  11    
HELIX    2 AA2 THR A  135  ASN A  138  5                                   4    
HELIX    3 AA3 ASP A  172  LYS A  175  5                                   4    
HELIX    4 AA4 PRO A  176  PHE A  185  1                                  10    
HELIX    5 AA5 SER A  214  GLY A  223  1                                  10    
HELIX    6 AA6 ARG A  226  LYS A  247  1                                  22    
HELIX    7 AA7 LYS A  255  SER A  257  5                                   3    
HELIX    8 AA8 THR A  290  MET A  294  5                                   5    
HELIX    9 AA9 SER A  295  CYS A  301  1                                   7    
HELIX   10 AB1 THR A  306  GLY A  323  1                                  18    
HELIX   11 AB2 LEU A  340  GLN A  346  1                                   7    
HELIX   12 AB3 PRO A  349  ILE A  353  5                                   5    
HELIX   13 AB4 SER A  358  LEU A  369  1                                  12    
HELIX   14 AB5 ARG A  378  LYS A  384  1                                   7    
HELIX   15 AB6 THR B   80  SER B   92  1                                  13    
HELIX   16 AB7 THR B  135  ASN B  138  5                                   4    
HELIX   17 AB8 ASP B  172  LYS B  175  5                                   4    
HELIX   18 AB9 PRO B  176  PHE B  185  1                                  10    
HELIX   19 AC1 SER B  214  GLY B  223  1                                  10    
HELIX   20 AC2 ARG B  226  LYS B  247  1                                  22    
HELIX   21 AC3 LYS B  255  SER B  257  5                                   3    
HELIX   22 AC4 THR B  290  MET B  294  5                                   5    
HELIX   23 AC5 SER B  295  CYS B  301  1                                   7    
HELIX   24 AC6 THR B  306  GLY B  323  1                                  18    
HELIX   25 AC7 TYR B  339  GLN B  346  1                                   8    
HELIX   26 AC8 PRO B  349  ILE B  353  5                                   5    
HELIX   27 AC9 SER B  358  LEU B  369  1                                  12    
HELIX   28 AD1 ARG B  378  LYS B  384  1                                   7    
HELIX   29 AD2 THR C   80  HIS C   90  1                                  11    
HELIX   30 AD3 ASP C  172  LYS C  175  5                                   4    
HELIX   31 AD4 PRO C  176  PHE C  185  1                                  10    
HELIX   32 AD5 VAL C  215  CYS C  222  1                                   8    
HELIX   33 AD6 ARG C  226  LYS C  247  1                                  22    
HELIX   34 AD7 THR C  290  MET C  294  5                                   5    
HELIX   35 AD8 SER C  295  CYS C  301  1                                   7    
HELIX   36 AD9 THR C  306  GLY C  323  1                                  18    
HELIX   37 AE1 PRO C  325  TYR C  331  1                                   7    
HELIX   38 AE2 TYR C  339  GLN C  346  1                                   8    
HELIX   39 AE3 PRO C  349  ILE C  353  5                                   5    
HELIX   40 AE4 SER C  358  LEU C  369  1                                  12    
HELIX   41 AE5 ARG C  378  LYS C  384  1                                   7    
SHEET    1 AA1 7 VAL A  76  TYR A  78  0                                        
SHEET    2 AA1 7 GLU A 105  LEU A 109  1  O  GLY A 107   N  ARG A  77           
SHEET    3 AA1 7 LEU A 193  TRP A 199 -1  O  LEU A 198   N  SER A 106           
SHEET    4 AA1 7 THR A 202  GLU A 208 -1  O  HIS A 204   N  VAL A 197           
SHEET    5 AA1 7 ARG A 163  PRO A 170 -1  N  ALA A 165   O  MET A 207           
SHEET    6 AA1 7 LYS A 151  ASP A 157 -1  N  ALA A 155   O  MET A 164           
SHEET    7 AA1 7 VAL A 127  ILE A 130 -1  N  LEU A 128   O  GLN A 156           
SHEET    1 AA2 7 VAL A  76  TYR A  78  0                                        
SHEET    2 AA2 7 GLU A 105  LEU A 109  1  O  GLY A 107   N  ARG A  77           
SHEET    3 AA2 7 LEU A 193  TRP A 199 -1  O  LEU A 198   N  SER A 106           
SHEET    4 AA2 7 THR A 202  GLU A 208 -1  O  HIS A 204   N  VAL A 197           
SHEET    5 AA2 7 ARG A 163  PRO A 170 -1  N  ALA A 165   O  MET A 207           
SHEET    6 AA2 7 LYS A 151  ASP A 157 -1  N  ALA A 155   O  MET A 164           
SHEET    7 AA2 7 PHE A 143  PRO A 145 -1  N  ILE A 144   O  VAL A 152           
SHEET    1 AA3 2 TRP A 132  LYS A 133  0                                        
SHEET    2 AA3 2 GLY A 140  SER A 141 -1  O  SER A 141   N  TRP A 132           
SHEET    1 AA4 2 VAL A 249  ILE A 250  0                                        
SHEET    2 AA4 2 VAL A 275  GLN A 276 -1  O  VAL A 275   N  ILE A 250           
SHEET    1 AA5 2 ILE A 259  PHE A 261  0                                        
SHEET    2 AA5 2 ALA A 266  LEU A 268 -1  O  VAL A 267   N  VAL A 260           
SHEET    1 AA6 7 VAL B  76  TYR B  78  0                                        
SHEET    2 AA6 7 GLU B 105  LEU B 109  1  O  GLY B 107   N  ARG B  77           
SHEET    3 AA6 7 LEU B 193  TRP B 199 -1  O  LEU B 198   N  SER B 106           
SHEET    4 AA6 7 THR B 202  GLU B 208 -1  O  HIS B 204   N  VAL B 197           
SHEET    5 AA6 7 ARG B 163  PRO B 170 -1  N  ALA B 165   O  MET B 207           
SHEET    6 AA6 7 LYS B 151  ASP B 157 -1  N  ALA B 155   O  MET B 164           
SHEET    7 AA6 7 VAL B 127  ILE B 130 -1  N  LEU B 128   O  GLN B 156           
SHEET    1 AA7 7 VAL B  76  TYR B  78  0                                        
SHEET    2 AA7 7 GLU B 105  LEU B 109  1  O  GLY B 107   N  ARG B  77           
SHEET    3 AA7 7 LEU B 193  TRP B 199 -1  O  LEU B 198   N  SER B 106           
SHEET    4 AA7 7 THR B 202  GLU B 208 -1  O  HIS B 204   N  VAL B 197           
SHEET    5 AA7 7 ARG B 163  PRO B 170 -1  N  ALA B 165   O  MET B 207           
SHEET    6 AA7 7 LYS B 151  ASP B 157 -1  N  ALA B 155   O  MET B 164           
SHEET    7 AA7 7 PHE B 143  PRO B 145 -1  N  ILE B 144   O  VAL B 152           
SHEET    1 AA8 2 TRP B 132  LYS B 133  0                                        
SHEET    2 AA8 2 GLY B 140  SER B 141 -1  O  SER B 141   N  TRP B 132           
SHEET    1 AA9 2 VAL B 249  ILE B 250  0                                        
SHEET    2 AA9 2 VAL B 275  GLN B 276 -1  O  VAL B 275   N  ILE B 250           
SHEET    1 AB1 2 ILE B 259  PHE B 261  0                                        
SHEET    2 AB1 2 ALA B 266  LEU B 268 -1  O  VAL B 267   N  VAL B 260           
SHEET    1 AB2 7 VAL C  76  TYR C  78  0                                        
SHEET    2 AB2 7 GLU C 105  LEU C 109  1  O  LEU C 109   N  ARG C  77           
SHEET    3 AB2 7 LEU C 193  TRP C 199 -1  O  LEU C 198   N  SER C 106           
SHEET    4 AB2 7 THR C 202  GLU C 208 -1  O  HIS C 204   N  VAL C 197           
SHEET    5 AB2 7 ARG C 163  PRO C 170 -1  N  ILE C 169   O  VAL C 203           
SHEET    6 AB2 7 LYS C 151  GLN C 156 -1  N  ALA C 155   O  MET C 164           
SHEET    7 AB2 7 PHE C 143  ILE C 144 -1  N  ILE C 144   O  VAL C 152           
SHEET    1 AB3 2 TRP C 132  LEU C 134  0                                        
SHEET    2 AB3 2 ILE C 139  SER C 141 -1  O  SER C 141   N  TRP C 132           
SHEET    1 AB4 3 GLY C 213  SER C 214  0                                        
SHEET    2 AB4 3 ILE C 259  PHE C 261 -1  O  PHE C 261   N  GLY C 213           
SHEET    3 AB4 3 ALA C 266  LEU C 268 -1  O  VAL C 267   N  VAL C 260           
SHEET    1 AB5 2 VAL C 249  ILE C 250  0                                        
SHEET    2 AB5 2 VAL C 275  GLN C 276 -1  O  VAL C 275   N  ILE C 250           
CISPEP   1 ALA A  347    PRO A  348          0         3.01                     
CISPEP   2 ALA B  347    PRO B  348          0         3.23                     
CISPEP   3 ALA C  347    PRO C  348          0         2.08                     
SITE     1 AC1 14 TRP A 132  ILE A 144  ARG A 146  VAL A 152                    
SITE     2 AC1 14 ALA A 165  LYS A 167  MET A 207  GLU A 208                    
SITE     3 AC1 14 GLY A 210  GLY A 213  SER A 214  GLU A 217                    
SITE     4 AC1 14 VAL A 260  ASP A 270                                          
SITE     1 AC2 15 TRP B 132  LEU B 134  ILE B 144  ARG B 146                    
SITE     2 AC2 15 ALA B 165  LYS B 167  MET B 207  GLU B 208                    
SITE     3 AC2 15 GLY B 210  GLY B 213  SER B 214  GLU B 217                    
SITE     4 AC2 15 VAL B 260  VAL B 269  HOH B 511                               
SITE     1 AC3 11 TRP C 132  ILE C 144  ARG C 146  VAL C 152                    
SITE     2 AC3 11 ALA C 165  MET C 207  GLU C 208  GLY C 210                    
SITE     3 AC3 11 GLY C 213  VAL C 269  ASP C 270                               
CRYST1  101.952  101.952  108.315  90.00  90.00 120.00 P 31          9          
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      0.009809  0.005663  0.000000        0.00000                         
SCALE2      0.000000  0.011326  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009232        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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