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Database: PDB
Entry: 3TNP
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Original site: 3TNP 
HEADER    TRANSFERASE                             01-SEP-11   3TNP              
TITLE     STRUCTURE AND ALLOSTERY OF THE PKA RIIB TETRAMERIC HOLOENZYME         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: C, F;                                                         
COMPND   4 SYNONYM: PKA C-ALPHA;                                                
COMPND   5 EC: 2.7.11.11;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE II-BETA REGULATORY      
COMPND   9 SUBUNIT;                                                             
COMPND  10 CHAIN: B, E;                                                         
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PKACA, PRKACA, RCG_51506;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  10 ORGANISM_COMMON: MOUSE;                                              
SOURCE  11 ORGANISM_TAXID: 10090;                                               
SOURCE  12 GENE: PRKAR2B;                                                       
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PKA RIIB TETRAMERIC HOLOENZYME, TRANSFERASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.ZHANG,E.V.SMITH-NGUYEN,M.M.KESHWANI,M.S.DEAL,A.P.KORNEV,S.S.TAYLOR  
REVDAT   3   27-FEB-13 3TNP    1       SOURCE                                   
REVDAT   2   12-SEP-12 3TNP    1       JRNL   REMARK                            
REVDAT   1   01-FEB-12 3TNP    0                                                
JRNL        AUTH   P.ZHANG,E.V.SMITH-NGUYEN,M.M.KESHWANI,M.S.DEAL,A.P.KORNEV,   
JRNL        AUTH 2 S.S.TAYLOR                                                   
JRNL        TITL   STRUCTURE AND ALLOSTERY OF THE PKA RIIBETA TETRAMERIC        
JRNL        TITL 2 HOLOENZYME                                                   
JRNL        REF    SCIENCE                       V. 335   712 2012              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   22323819                                                     
JRNL        DOI    10.1126/SCIENCE.1213979                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.1_357)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.90                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 82530                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4116                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.8995 -  4.9325    0.91     7570   394  0.1959 0.2079        
REMARK   3     2  4.9325 -  3.9249    0.91     7475   404  0.1776 0.1823        
REMARK   3     3  3.9249 -  3.4316    0.93     7678   396  0.2145 0.2062        
REMARK   3     4  3.4316 -  3.1192    0.97     7973   431  0.2386 0.2492        
REMARK   3     5  3.1192 -  2.8963    0.98     8000   445  0.2533 0.2752        
REMARK   3     6  2.8963 -  2.7260    0.98     8050   419  0.2589 0.2666        
REMARK   3     7  2.7260 -  2.5898    0.97     8030   387  0.2760 0.3172        
REMARK   3     8  2.5898 -  2.4773    0.97     7975   422  0.2661 0.2642        
REMARK   3     9  2.4773 -  2.3821    0.97     7971   395  0.2672 0.2724        
REMARK   3    10  2.3821 -  2.3000    0.94     7692   423  0.2843 0.3113        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 29.66                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.660           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.20630                                             
REMARK   3    B22 (A**2) : 0.48220                                              
REMARK   3    B33 (A**2) : -0.22740                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.35320                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010          10040                                  
REMARK   3   ANGLE     :  1.294          13530                                  
REMARK   3   CHIRALITY :  0.090           1456                                  
REMARK   3   PLANARITY :  0.005           1740                                  
REMARK   3   DIHEDRAL  : 14.297           3780                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain C and (resseq 14:138 or resseq 140:   
REMARK   3                          196 or resseq 198:337 or resseq 339:350 )   
REMARK   3     SELECTION          : chain F and (resseq 14:138 or resseq 140:   
REMARK   3                          196 or resseq 198:337 or resseq 339:350 )   
REMARK   3     ATOM PAIRS NUMBER  : 2756                                        
REMARK   3     RMSD               : 0.003                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain B and (resseq 104:121 or resseq       
REMARK   3                          130:324 or resseq 337:393 )                 
REMARK   3     SELECTION          : chain E and (resseq 104:121 or resseq       
REMARK   3                          130:324 or resseq 337:393 )                 
REMARK   3     ATOM PAIRS NUMBER  : 2131                                        
REMARK   3     RMSD               : 0.000                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3TNP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB067696.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 82530                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE RII   (R230K)2:C2 HOLOENZYME         
REMARK 280  COMPLEX WAS CRYSTALLIZED AT ROOM TEMPERATURE IN 10% PEG8000, 8%     
REMARK 280  ETHYLENE GLYCOL, PH7.5 HEPES BUFFER BY USING VAPOR DIFFUSION AT A   
REMARK 280  1:1 RATIO OF PROTEIN TO CRYSTALLIZATION SOLUTION. VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       75.98100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      106.63850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       75.98100            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000      106.63850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, B, F, E                            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, E                                  
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 C     1                                                      
REMARK 465     ASN C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     ALA C     6                                                      
REMARK 465     LYS C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     GLY C     9                                                      
REMARK 465     SEP C    10                                                      
REMARK 465     GLU C    11                                                      
REMARK 465     GLN C    12                                                      
REMARK 465     GLU C    13                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ILE B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     ILE B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     THR B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     LEU B    12                                                      
REMARK 465     LEU B    13                                                      
REMARK 465     GLN B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     PHE B    16                                                      
REMARK 465     THR B    17                                                      
REMARK 465     VAL B    18                                                      
REMARK 465     GLU B    19                                                      
REMARK 465     VAL B    20                                                      
REMARK 465     LEU B    21                                                      
REMARK 465     ARG B    22                                                      
REMARK 465     HIS B    23                                                      
REMARK 465     GLN B    24                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     ALA B    26                                                      
REMARK 465     ASP B    27                                                      
REMARK 465     LEU B    28                                                      
REMARK 465     LEU B    29                                                      
REMARK 465     GLU B    30                                                      
REMARK 465     PHE B    31                                                      
REMARK 465     ALA B    32                                                      
REMARK 465     LEU B    33                                                      
REMARK 465     GLN B    34                                                      
REMARK 465     HIS B    35                                                      
REMARK 465     PHE B    36                                                      
REMARK 465     THR B    37                                                      
REMARK 465     ARG B    38                                                      
REMARK 465     LEU B    39                                                      
REMARK 465     GLN B    40                                                      
REMARK 465     GLN B    41                                                      
REMARK 465     GLU B    42                                                      
REMARK 465     ASN B    43                                                      
REMARK 465     GLU B    44                                                      
REMARK 465     ARG B    45                                                      
REMARK 465     LYS B    46                                                      
REMARK 465     GLY B    47                                                      
REMARK 465     ALA B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     ARG B    50                                                      
REMARK 465     PHE B    51                                                      
REMARK 465     GLY B    52                                                      
REMARK 465     HIS B    53                                                      
REMARK 465     GLU B    54                                                      
REMARK 465     GLY B    55                                                      
REMARK 465     ARG B    56                                                      
REMARK 465     THR B    57                                                      
REMARK 465     TRP B    58                                                      
REMARK 465     GLY B    59                                                      
REMARK 465     ASP B    60                                                      
REMARK 465     ALA B    61                                                      
REMARK 465     GLY B    62                                                      
REMARK 465     ALA B    63                                                      
REMARK 465     ALA B    64                                                      
REMARK 465     ALA B    65                                                      
REMARK 465     GLY B    66                                                      
REMARK 465     GLY B    67                                                      
REMARK 465     GLY B    68                                                      
REMARK 465     ILE B    69                                                      
REMARK 465     PRO B    70                                                      
REMARK 465     SER B    71                                                      
REMARK 465     LYS B    72                                                      
REMARK 465     GLY B    73                                                      
REMARK 465     VAL B    74                                                      
REMARK 465     ASN B    75                                                      
REMARK 465     PHE B    76                                                      
REMARK 465     ALA B    77                                                      
REMARK 465     GLU B    78                                                      
REMARK 465     GLU B    79                                                      
REMARK 465     PRO B    80                                                      
REMARK 465     MET B    81                                                      
REMARK 465     ARG B    82                                                      
REMARK 465     SER B    83                                                      
REMARK 465     ASP B    84                                                      
REMARK 465     SER B    85                                                      
REMARK 465     GLU B    86                                                      
REMARK 465     ASN B    87                                                      
REMARK 465     GLY B    88                                                      
REMARK 465     GLU B    89                                                      
REMARK 465     GLU B    90                                                      
REMARK 465     GLU B    91                                                      
REMARK 465     GLU B    92                                                      
REMARK 465     ALA B    93                                                      
REMARK 465     ALA B    94                                                      
REMARK 465     GLU B    95                                                      
REMARK 465     ALA B    96                                                      
REMARK 465     GLY B    97                                                      
REMARK 465     ALA B    98                                                      
REMARK 465     PHE B    99                                                      
REMARK 465     ASN B   100                                                      
REMARK 465     ALA B   101                                                      
REMARK 465     PRO B   102                                                      
REMARK 465     VAL B   103                                                      
REMARK 465     GLU B   122                                                      
REMARK 465     GLU B   123                                                      
REMARK 465     GLU B   124                                                      
REMARK 465     ASP B   125                                                      
REMARK 465     ASP B   126                                                      
REMARK 465     ALA B   127                                                      
REMARK 465     GLU B   128                                                      
REMARK 465     SER B   129                                                      
REMARK 465     ARG B   325                                                      
REMARK 465     LYS B   326                                                      
REMARK 465     GLY B   327                                                      
REMARK 465     LYS B   328                                                      
REMARK 465     SER B   329                                                      
REMARK 465     GLU B   330                                                      
REMARK 465     VAL B   331                                                      
REMARK 465     GLU B   332                                                      
REMARK 465     GLU B   333                                                      
REMARK 465     ASN B   334                                                      
REMARK 465     GLY B   335                                                      
REMARK 465     ALA B   336                                                      
REMARK 465     ILE B   394                                                      
REMARK 465     ALA B   395                                                      
REMARK 465     THR B   396                                                      
REMARK 465     TYR B   397                                                      
REMARK 465     GLU B   398                                                      
REMARK 465     GLU B   399                                                      
REMARK 465     GLN B   400                                                      
REMARK 465     LEU B   401                                                      
REMARK 465     VAL B   402                                                      
REMARK 465     ALA B   403                                                      
REMARK 465     LEU B   404                                                      
REMARK 465     PHE B   405                                                      
REMARK 465     GLY B   406                                                      
REMARK 465     THR B   407                                                      
REMARK 465     ASN B   408                                                      
REMARK 465     MET B   409                                                      
REMARK 465     ASP B   410                                                      
REMARK 465     ILE B   411                                                      
REMARK 465     VAL B   412                                                      
REMARK 465     GLU B   413                                                      
REMARK 465     PRO B   414                                                      
REMARK 465     THR B   415                                                      
REMARK 465     ALA B   416                                                      
REMARK 465     GLY F     1                                                      
REMARK 465     ASN F     2                                                      
REMARK 465     ALA F     3                                                      
REMARK 465     ALA F     4                                                      
REMARK 465     ALA F     5                                                      
REMARK 465     ALA F     6                                                      
REMARK 465     LYS F     7                                                      
REMARK 465     LYS F     8                                                      
REMARK 465     GLY F     9                                                      
REMARK 465     SEP F    10                                                      
REMARK 465     GLU F    11                                                      
REMARK 465     GLN F    12                                                      
REMARK 465     GLU F    13                                                      
REMARK 465     MET E     1                                                      
REMARK 465     SER E     2                                                      
REMARK 465     ILE E     3                                                      
REMARK 465     GLU E     4                                                      
REMARK 465     ILE E     5                                                      
REMARK 465     PRO E     6                                                      
REMARK 465     ALA E     7                                                      
REMARK 465     GLY E     8                                                      
REMARK 465     LEU E     9                                                      
REMARK 465     THR E    10                                                      
REMARK 465     GLU E    11                                                      
REMARK 465     LEU E    12                                                      
REMARK 465     LEU E    13                                                      
REMARK 465     GLN E    14                                                      
REMARK 465     GLY E    15                                                      
REMARK 465     PHE E    16                                                      
REMARK 465     THR E    17                                                      
REMARK 465     VAL E    18                                                      
REMARK 465     GLU E    19                                                      
REMARK 465     VAL E    20                                                      
REMARK 465     LEU E    21                                                      
REMARK 465     ARG E    22                                                      
REMARK 465     HIS E    23                                                      
REMARK 465     GLN E    24                                                      
REMARK 465     PRO E    25                                                      
REMARK 465     ALA E    26                                                      
REMARK 465     ASP E    27                                                      
REMARK 465     LEU E    28                                                      
REMARK 465     LEU E    29                                                      
REMARK 465     GLU E    30                                                      
REMARK 465     PHE E    31                                                      
REMARK 465     ALA E    32                                                      
REMARK 465     LEU E    33                                                      
REMARK 465     GLN E    34                                                      
REMARK 465     HIS E    35                                                      
REMARK 465     PHE E    36                                                      
REMARK 465     THR E    37                                                      
REMARK 465     ARG E    38                                                      
REMARK 465     LEU E    39                                                      
REMARK 465     GLN E    40                                                      
REMARK 465     GLN E    41                                                      
REMARK 465     GLU E    42                                                      
REMARK 465     ASN E    43                                                      
REMARK 465     GLU E    44                                                      
REMARK 465     ARG E    45                                                      
REMARK 465     LYS E    46                                                      
REMARK 465     GLY E    47                                                      
REMARK 465     ALA E    48                                                      
REMARK 465     ALA E    49                                                      
REMARK 465     ARG E    50                                                      
REMARK 465     PHE E    51                                                      
REMARK 465     GLY E    52                                                      
REMARK 465     HIS E    53                                                      
REMARK 465     GLU E    54                                                      
REMARK 465     GLY E    55                                                      
REMARK 465     ARG E    56                                                      
REMARK 465     THR E    57                                                      
REMARK 465     TRP E    58                                                      
REMARK 465     GLY E    59                                                      
REMARK 465     ASP E    60                                                      
REMARK 465     ALA E    61                                                      
REMARK 465     GLY E    62                                                      
REMARK 465     ALA E    63                                                      
REMARK 465     ALA E    64                                                      
REMARK 465     ALA E    65                                                      
REMARK 465     GLY E    66                                                      
REMARK 465     GLY E    67                                                      
REMARK 465     GLY E    68                                                      
REMARK 465     ILE E    69                                                      
REMARK 465     PRO E    70                                                      
REMARK 465     SER E    71                                                      
REMARK 465     LYS E    72                                                      
REMARK 465     GLY E    73                                                      
REMARK 465     VAL E    74                                                      
REMARK 465     ASN E    75                                                      
REMARK 465     PHE E    76                                                      
REMARK 465     ALA E    77                                                      
REMARK 465     GLU E    78                                                      
REMARK 465     GLU E    79                                                      
REMARK 465     PRO E    80                                                      
REMARK 465     MET E    81                                                      
REMARK 465     ARG E    82                                                      
REMARK 465     SER E    83                                                      
REMARK 465     ASP E    84                                                      
REMARK 465     SER E    85                                                      
REMARK 465     GLU E    86                                                      
REMARK 465     ASN E    87                                                      
REMARK 465     GLY E    88                                                      
REMARK 465     GLU E    89                                                      
REMARK 465     GLU E    90                                                      
REMARK 465     GLU E    91                                                      
REMARK 465     GLU E    92                                                      
REMARK 465     ALA E    93                                                      
REMARK 465     ALA E    94                                                      
REMARK 465     GLU E    95                                                      
REMARK 465     ALA E    96                                                      
REMARK 465     GLY E    97                                                      
REMARK 465     ALA E    98                                                      
REMARK 465     PHE E    99                                                      
REMARK 465     ASN E   100                                                      
REMARK 465     ALA E   101                                                      
REMARK 465     PRO E   102                                                      
REMARK 465     VAL E   103                                                      
REMARK 465     GLU E   122                                                      
REMARK 465     GLU E   123                                                      
REMARK 465     GLU E   124                                                      
REMARK 465     ASP E   125                                                      
REMARK 465     ASP E   126                                                      
REMARK 465     ALA E   127                                                      
REMARK 465     GLU E   128                                                      
REMARK 465     SER E   129                                                      
REMARK 465     ARG E   325                                                      
REMARK 465     LYS E   326                                                      
REMARK 465     GLY E   327                                                      
REMARK 465     LYS E   328                                                      
REMARK 465     SER E   329                                                      
REMARK 465     GLU E   330                                                      
REMARK 465     VAL E   331                                                      
REMARK 465     GLU E   332                                                      
REMARK 465     GLU E   333                                                      
REMARK 465     ASN E   334                                                      
REMARK 465     GLY E   335                                                      
REMARK 465     ALA E   336                                                      
REMARK 465     ILE E   394                                                      
REMARK 465     ALA E   395                                                      
REMARK 465     THR E   396                                                      
REMARK 465     TYR E   397                                                      
REMARK 465     GLU E   398                                                      
REMARK 465     GLU E   399                                                      
REMARK 465     GLN E   400                                                      
REMARK 465     LEU E   401                                                      
REMARK 465     VAL E   402                                                      
REMARK 465     ALA E   403                                                      
REMARK 465     LEU E   404                                                      
REMARK 465     PHE E   405                                                      
REMARK 465     GLY E   406                                                      
REMARK 465     THR E   407                                                      
REMARK 465     ASN E   408                                                      
REMARK 465     MET E   409                                                      
REMARK 465     ASP E   410                                                      
REMARK 465     ILE E   411                                                      
REMARK 465     VAL E   412                                                      
REMARK 465     GLU E   413                                                      
REMARK 465     PRO E   414                                                      
REMARK 465     THR E   415                                                      
REMARK 465     ALA E   416                                                      
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     ILE B 104    N                                                   
REMARK 470     ILE E 104    N                                                   
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   CG   ASP F   290     O    HOH F   418              1.27            
REMARK 500   NH1  ARG E   140     O    HOH E   443              1.36            
REMARK 500   OD2  ASP F   290     O    HOH F   418              1.53            
REMARK 500   NZ   LYS C    47     O    HOH C   358              1.54            
REMARK 500   OD1  ASP F   290     O    HOH F   418              1.61            
REMARK 500   O    ASP B   185     O    HOH B   423              1.61            
REMARK 500   N    GLY C    55     O    HOH C   432              1.79            
REMARK 500   OE2  GLU E   266     O    HOH E   450              1.79            
REMARK 500   O    HOH E   476     O    HOH E   501              1.90            
REMARK 500   N    THR E   249     O    HOH E   451              1.97            
REMARK 500   OD1  ASP B   185     O    HOH B   431              1.98            
REMARK 500   NZ   LYS F   319     O    HOH F   353              2.00            
REMARK 500   NH2  ARG E   216     O    HOH E   503              2.00            
REMARK 500   O    GLY B   345     O    HOH B   496              2.08            
REMARK 500   CD2  LEU B   143     O    HOH B   490              2.13            
REMARK 500   NE   ARG C    45     O    HOH C   412              2.13            
REMARK 500   NH1  ARG F   134     O    HOH F   378              2.14            
REMARK 500   NZ   LYS E   370     O    HOH E   500              2.14            
REMARK 500   OD1  ASP B   246     O    HOH B   459              2.15            
REMARK 500   N    THR B   368     O    HOH B   487              2.16            
REMARK 500   O    PHE C    18     O    HOH C   406              2.18            
REMARK 500   O    ASP B   185     O    HOH B   417              2.18            
REMARK 500   OE2  GLU C   349     O    HOH C   409              2.18            
REMARK 500   O    HOH B   464     O    HOH B   494              2.18            
REMARK 500   O    ALA B   259     O    ARG B   262              2.19            
REMARK 500   O    ALA E   259     O    ARG E   262              2.19            
REMARK 500   CD   GLU E   266     O    HOH E   450              2.19            
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    ASN C  36       69.40     36.84                                   
REMARK 500    ALA C  38     -169.61   -162.08                                   
REMARK 500    SER C  53       -8.56    -53.94                                   
REMARK 500    ASN C  99      108.36   -165.48                                   
REMARK 500    ASP C 112     -155.62   -139.82                                   
REMARK 500    ASP C 166       36.74   -142.31                                   
REMARK 500    ASN C 216     -119.80   -123.70                                   
REMARK 500    LYS C 319     -142.83    -91.46                                   
REMARK 500    ASN B 105       60.80   -108.80                                   
REMARK 500    CYS B 114      119.90   -167.94                                   
REMARK 500    ASP B 185      133.80    -33.43                                   
REMARK 500    ASN B 215       10.84     57.55                                   
REMARK 500    SER B 267      -11.30     77.32                                   
REMARK 500    ASP B 297      117.07    -38.19                                   
REMARK 500    ASN B 356       35.69    -99.12                                   
REMARK 500    ARG B 392      -99.74    -88.74                                   
REMARK 500    ASN F  36       69.42     36.80                                   
REMARK 500    ALA F  38     -169.56   -162.05                                   
REMARK 500    SER F  53       -8.62    -53.92                                   
REMARK 500    ASN F  99      108.32   -165.46                                   
REMARK 500    ASP F 112     -155.64   -139.82                                   
REMARK 500    ASP F 166       36.72   -142.33                                   
REMARK 500    ASN F 216     -119.77   -123.65                                   
REMARK 500    LYS F 319     -142.86    -91.45                                   
REMARK 500    ASN E 105       60.76   -108.73                                   
REMARK 500    CYS E 114      119.87   -167.96                                   
REMARK 500    ASP E 185      133.77    -33.38                                   
REMARK 500    ASN E 215       10.87     57.48                                   
REMARK 500    SER E 267      -11.32     77.33                                   
REMARK 500    ASP E 297      117.04    -38.17                                   
REMARK 500    ASN E 356       35.62    -99.07                                   
REMARK 500    ARG E 392      -99.73    -88.75                                   
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 SER B  267     PHE B  268                  132.98                    
REMARK 500 SER E  267     PHE E  268                  132.99                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR C 183        24.6      L          L   OUTSIDE RANGE           
REMARK 500    THR F 183        24.6      L          L   OUTSIDE RANGE           
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 E 497        DISTANCE =  5.27 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3TNQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3TNR   RELATED DB: PDB                                   
DBREF  3TNP C    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  3TNP B    1   416  UNP    P31324   KAP3_MOUSE       1    416             
DBREF  3TNP F    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  3TNP E    1   416  UNP    P31324   KAP3_MOUSE       1    416             
SEQADV 3TNP LYS B  230  UNP  P31324    ARG   230 ENGINEERED MUTATION            
SEQADV 3TNP LYS E  230  UNP  P31324    ARG   230 ENGINEERED MUTATION            
SEQRES   1 C  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SEP GLU GLN GLU          
SEQRES   2 C  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 C  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 C  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 C  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 C  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 C  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 C  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 C  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 C  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 C  350  HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU PRO HIS ALA          
SEQRES  12 C  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 C  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 C  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 C  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 C  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 C  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 C  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 C  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 C  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 C  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 C  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 C  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 C  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 C  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 C  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 C  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
SEQRES   1 B  416  MET SER ILE GLU ILE PRO ALA GLY LEU THR GLU LEU LEU          
SEQRES   2 B  416  GLN GLY PHE THR VAL GLU VAL LEU ARG HIS GLN PRO ALA          
SEQRES   3 B  416  ASP LEU LEU GLU PHE ALA LEU GLN HIS PHE THR ARG LEU          
SEQRES   4 B  416  GLN GLN GLU ASN GLU ARG LYS GLY ALA ALA ARG PHE GLY          
SEQRES   5 B  416  HIS GLU GLY ARG THR TRP GLY ASP ALA GLY ALA ALA ALA          
SEQRES   6 B  416  GLY GLY GLY ILE PRO SER LYS GLY VAL ASN PHE ALA GLU          
SEQRES   7 B  416  GLU PRO MET ARG SER ASP SER GLU ASN GLY GLU GLU GLU          
SEQRES   8 B  416  GLU ALA ALA GLU ALA GLY ALA PHE ASN ALA PRO VAL ILE          
SEQRES   9 B  416  ASN ARG PHE THR ARG ARG ALA SER VAL CYS ALA GLU ALA          
SEQRES  10 B  416  TYR ASN PRO ASP GLU GLU GLU ASP ASP ALA GLU SER ARG          
SEQRES  11 B  416  ILE ILE HIS PRO LYS THR ASP ASP GLN ARG ASN ARG LEU          
SEQRES  12 B  416  GLN GLU ALA CYS LYS ASP ILE LEU LEU PHE LYS ASN LEU          
SEQRES  13 B  416  ASP PRO GLU GLN MET SER GLN VAL LEU ASP ALA MET PHE          
SEQRES  14 B  416  GLU LYS LEU VAL LYS GLU GLY GLU HIS VAL ILE ASP GLN          
SEQRES  15 B  416  GLY ASP ASP GLY ASP ASN PHE TYR VAL ILE ASP ARG GLY          
SEQRES  16 B  416  THR PHE ASP ILE TYR VAL LYS CYS ASP GLY VAL GLY ARG          
SEQRES  17 B  416  CYS VAL GLY ASN TYR ASP ASN ARG GLY SER PHE GLY GLU          
SEQRES  18 B  416  LEU ALA LEU MET TYR ASN THR PRO LYS ALA ALA THR ILE          
SEQRES  19 B  416  THR ALA THR SER PRO GLY ALA LEU TRP GLY LEU ASP ARG          
SEQRES  20 B  416  VAL THR PHE ARG ARG ILE ILE VAL LYS ASN ASN ALA LYS          
SEQRES  21 B  416  LYS ARG LYS MET TYR GLU SER PHE ILE GLU SER LEU PRO          
SEQRES  22 B  416  PHE LEU LYS SER LEU GLU VAL SER GLU ARG LEU LYS VAL          
SEQRES  23 B  416  VAL ASP VAL ILE GLY THR LYS VAL TYR ASN ASP GLY GLU          
SEQRES  24 B  416  GLN ILE ILE ALA GLN GLY ASP LEU ALA ASP SER PHE PHE          
SEQRES  25 B  416  ILE VAL GLU SER GLY GLU VAL LYS ILE THR MET LYS ARG          
SEQRES  26 B  416  LYS GLY LYS SER GLU VAL GLU GLU ASN GLY ALA VAL GLU          
SEQRES  27 B  416  ILE ALA ARG CYS PHE ARG GLY GLN TYR PHE GLY GLU LEU          
SEQRES  28 B  416  ALA LEU VAL THR ASN LYS PRO ARG ALA ALA SER ALA HIS          
SEQRES  29 B  416  ALA ILE GLY THR VAL LYS CYS LEU ALA MET ASP VAL GLN          
SEQRES  30 B  416  ALA PHE GLU ARG LEU LEU GLY PRO CYS MET GLU ILE MET          
SEQRES  31 B  416  LYS ARG ASN ILE ALA THR TYR GLU GLU GLN LEU VAL ALA          
SEQRES  32 B  416  LEU PHE GLY THR ASN MET ASP ILE VAL GLU PRO THR ALA          
SEQRES   1 F  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SEP GLU GLN GLU          
SEQRES   2 F  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 F  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 F  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 F  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 F  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 F  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 F  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 F  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 F  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 F  350  HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU PRO HIS ALA          
SEQRES  12 F  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 F  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 F  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 F  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 F  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 F  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 F  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 F  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 F  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 F  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 F  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 F  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 F  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 F  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 F  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 F  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
SEQRES   1 E  416  MET SER ILE GLU ILE PRO ALA GLY LEU THR GLU LEU LEU          
SEQRES   2 E  416  GLN GLY PHE THR VAL GLU VAL LEU ARG HIS GLN PRO ALA          
SEQRES   3 E  416  ASP LEU LEU GLU PHE ALA LEU GLN HIS PHE THR ARG LEU          
SEQRES   4 E  416  GLN GLN GLU ASN GLU ARG LYS GLY ALA ALA ARG PHE GLY          
SEQRES   5 E  416  HIS GLU GLY ARG THR TRP GLY ASP ALA GLY ALA ALA ALA          
SEQRES   6 E  416  GLY GLY GLY ILE PRO SER LYS GLY VAL ASN PHE ALA GLU          
SEQRES   7 E  416  GLU PRO MET ARG SER ASP SER GLU ASN GLY GLU GLU GLU          
SEQRES   8 E  416  GLU ALA ALA GLU ALA GLY ALA PHE ASN ALA PRO VAL ILE          
SEQRES   9 E  416  ASN ARG PHE THR ARG ARG ALA SER VAL CYS ALA GLU ALA          
SEQRES  10 E  416  TYR ASN PRO ASP GLU GLU GLU ASP ASP ALA GLU SER ARG          
SEQRES  11 E  416  ILE ILE HIS PRO LYS THR ASP ASP GLN ARG ASN ARG LEU          
SEQRES  12 E  416  GLN GLU ALA CYS LYS ASP ILE LEU LEU PHE LYS ASN LEU          
SEQRES  13 E  416  ASP PRO GLU GLN MET SER GLN VAL LEU ASP ALA MET PHE          
SEQRES  14 E  416  GLU LYS LEU VAL LYS GLU GLY GLU HIS VAL ILE ASP GLN          
SEQRES  15 E  416  GLY ASP ASP GLY ASP ASN PHE TYR VAL ILE ASP ARG GLY          
SEQRES  16 E  416  THR PHE ASP ILE TYR VAL LYS CYS ASP GLY VAL GLY ARG          
SEQRES  17 E  416  CYS VAL GLY ASN TYR ASP ASN ARG GLY SER PHE GLY GLU          
SEQRES  18 E  416  LEU ALA LEU MET TYR ASN THR PRO LYS ALA ALA THR ILE          
SEQRES  19 E  416  THR ALA THR SER PRO GLY ALA LEU TRP GLY LEU ASP ARG          
SEQRES  20 E  416  VAL THR PHE ARG ARG ILE ILE VAL LYS ASN ASN ALA LYS          
SEQRES  21 E  416  LYS ARG LYS MET TYR GLU SER PHE ILE GLU SER LEU PRO          
SEQRES  22 E  416  PHE LEU LYS SER LEU GLU VAL SER GLU ARG LEU LYS VAL          
SEQRES  23 E  416  VAL ASP VAL ILE GLY THR LYS VAL TYR ASN ASP GLY GLU          
SEQRES  24 E  416  GLN ILE ILE ALA GLN GLY ASP LEU ALA ASP SER PHE PHE          
SEQRES  25 E  416  ILE VAL GLU SER GLY GLU VAL LYS ILE THR MET LYS ARG          
SEQRES  26 E  416  LYS GLY LYS SER GLU VAL GLU GLU ASN GLY ALA VAL GLU          
SEQRES  27 E  416  ILE ALA ARG CYS PHE ARG GLY GLN TYR PHE GLY GLU LEU          
SEQRES  28 E  416  ALA LEU VAL THR ASN LYS PRO ARG ALA ALA SER ALA HIS          
SEQRES  29 E  416  ALA ILE GLY THR VAL LYS CYS LEU ALA MET ASP VAL GLN          
SEQRES  30 E  416  ALA PHE GLU ARG LEU LEU GLY PRO CYS MET GLU ILE MET          
SEQRES  31 E  416  LYS ARG ASN ILE ALA THR TYR GLU GLU GLN LEU VAL ALA          
SEQRES  32 E  416  LEU PHE GLY THR ASN MET ASP ILE VAL GLU PRO THR ALA          
MODRES 3TNP SEP C  139  SER  PHOSPHOSERINE                                      
MODRES 3TNP TPO C  197  THR  PHOSPHOTHREONINE                                   
MODRES 3TNP SEP C  338  SER  PHOSPHOSERINE                                      
MODRES 3TNP SEP F  139  SER  PHOSPHOSERINE                                      
MODRES 3TNP TPO F  197  THR  PHOSPHOTHREONINE                                   
MODRES 3TNP SEP F  338  SER  PHOSPHOSERINE                                      
HET    SEP  C 139      10                                                       
HET    TPO  C 197      11                                                       
HET    SEP  C 338      10                                                       
HET    SEP  F 139      10                                                       
HET    TPO  F 197      11                                                       
HET    SEP  F 338      10                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  SEP    4(C3 H8 N O6 P)                                              
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  HOH   *357(H2 O)                                                    
HELIX    1   1 SER C   14  THR C   32  1                                  19    
HELIX    2   2 GLN C   39  ASP C   41  5                                   3    
HELIX    3   3 LYS C   76  LEU C   82  1                                   7    
HELIX    4   4 GLN C   84  GLN C   96  1                                  13    
HELIX    5   5 GLU C  127  GLY C  136  1                                  10    
HELIX    6   6 SEP C  139  SER C  159  1                                  21    
HELIX    7   7 LYS C  168  GLU C  170  5                                   3    
HELIX    8   8 THR C  201  LEU C  205  5                                   5    
HELIX    9   9 ALA C  206  LEU C  211  1                                   6    
HELIX   10  10 LYS C  217  GLY C  234  1                                  18    
HELIX   11  11 GLN C  242  GLY C  253  1                                  12    
HELIX   12  12 SER C  262  LEU C  273  1                                  12    
HELIX   13  13 VAL C  288  ASN C  293  1                                   6    
HELIX   14  14 HIS C  294  ALA C  298  5                                   5    
HELIX   15  15 ASP C  301  GLN C  307  1                                   7    
HELIX   16  16 THR B  136  LYS B  148  1                                  13    
HELIX   17  17 ILE B  150  ASN B  155  1                                   6    
HELIX   18  18 ASP B  157  MET B  168  1                                  12    
HELIX   19  19 GLY B  220  MET B  225  5                                   6    
HELIX   20  20 ARG B  247  ARG B  262  1                                  16    
HELIX   21  21 PHE B  268  LYS B  276  5                                   9    
HELIX   22  22 GLU B  279  ILE B  290  1                                  12    
HELIX   23  23 GLY B  349  VAL B  354  5                                   6    
HELIX   24  24 VAL B  376  GLY B  384  1                                   9    
HELIX   25  25 PRO B  385  LYS B  391  1                                   7    
HELIX   26  26 VAL F   15  THR F   32  1                                  18    
HELIX   27  27 GLN F   39  ASP F   41  5                                   3    
HELIX   28  28 LYS F   76  LEU F   82  1                                   7    
HELIX   29  29 GLN F   84  GLN F   96  1                                  13    
HELIX   30  30 GLU F  127  GLY F  136  1                                  10    
HELIX   31  31 SEP F  139  SER F  159  1                                  21    
HELIX   32  32 LYS F  168  GLU F  170  5                                   3    
HELIX   33  33 THR F  201  LEU F  205  5                                   5    
HELIX   34  34 ALA F  206  LEU F  211  1                                   6    
HELIX   35  35 LYS F  217  GLY F  234  1                                  18    
HELIX   36  36 GLN F  242  GLY F  253  1                                  12    
HELIX   37  37 SER F  262  LEU F  273  1                                  12    
HELIX   38  38 VAL F  288  ASN F  293  1                                   6    
HELIX   39  39 HIS F  294  ALA F  298  5                                   5    
HELIX   40  40 ASP F  301  GLN F  307  1                                   7    
HELIX   41  41 THR E  136  LYS E  148  1                                  13    
HELIX   42  42 ILE E  150  ASN E  155  1                                   6    
HELIX   43  43 ASP E  157  MET E  168  1                                  12    
HELIX   44  44 GLY E  220  MET E  225  5                                   6    
HELIX   45  45 ARG E  247  ARG E  262  1                                  16    
HELIX   46  46 PHE E  268  LYS E  276  5                                   9    
HELIX   47  47 GLU E  279  ILE E  290  1                                  12    
HELIX   48  48 GLY E  349  VAL E  354  5                                   6    
HELIX   49  49 VAL E  376  GLY E  384  1                                   9    
HELIX   50  50 PRO E  385  LYS E  391  1                                   7    
SHEET    1   A 5 PHE C  43  THR C  51  0                                        
SHEET    2   A 5 ARG C  56  HIS C  62 -1  O  LEU C  59   N  LYS C  47           
SHEET    3   A 5 HIS C  68  ASP C  75 -1  O  MET C  71   N  MET C  58           
SHEET    4   A 5 ASN C 115  GLU C 121 -1  O  MET C 118   N  LYS C  72           
SHEET    5   A 5 LEU C 106  LYS C 111 -1  N  GLU C 107   O  VAL C 119           
SHEET    1   B 2 LEU C 162  ILE C 163  0                                        
SHEET    2   B 2 LYS C 189  ARG C 190 -1  O  LYS C 189   N  ILE C 163           
SHEET    1   C 2 LEU C 172  ILE C 174  0                                        
SHEET    2   C 2 ILE C 180  VAL C 182 -1  O  GLN C 181   N  LEU C 173           
SHEET    1   D 2 CYS C 199  GLY C 200  0                                        
SHEET    2   D 2 VAL B 113  CYS B 114 -1  O  VAL B 113   N  GLY C 200           
SHEET    1   E 5 ASP C 329  TYR C 330  0                                        
SHEET    2   E 5 VAL E 206  ASP E 214 -1  O  GLY E 207   N  ASP C 329           
SHEET    3   E 5 THR E 196  LYS E 202 -1  N  ILE E 199   O  GLY E 211           
SHEET    4   E 5 THR E 233  ALA E 236 -1  O  THR E 233   N  TYR E 200           
SHEET    5   E 5 HIS E 178  ILE E 180 -1  N  VAL E 179   O  ILE E 234           
SHEET    1   F 4 PHE B 169  VAL B 173  0                                        
SHEET    2   F 4 GLY B 240  ASP B 246 -1  O  LEU B 242   N  LYS B 171           
SHEET    3   F 4 ASN B 188  ARG B 194 -1  N  VAL B 191   O  TRP B 243           
SHEET    4   F 4 SER B 218  PHE B 219 -1  O  PHE B 219   N  TYR B 190           
SHEET    1   G 4 HIS B 178  ILE B 180  0                                        
SHEET    2   G 4 THR B 233  ALA B 236 -1  O  ILE B 234   N  VAL B 179           
SHEET    3   G 4 THR B 196  LYS B 202 -1  N  TYR B 200   O  THR B 233           
SHEET    4   G 4 GLY B 207  ASP B 214 -1  O  GLY B 211   N  ILE B 199           
SHEET    1   H 4 GLY B 291  TYR B 295  0                                        
SHEET    2   H 4 SER B 362  ASP B 375 -1  O  CYS B 371   N  LYS B 293           
SHEET    3   H 4 SER B 310  THR B 322 -1  N  GLU B 318   O  ILE B 366           
SHEET    4   H 4 GLU B 338  CYS B 342 -1  O  CYS B 342   N  VAL B 319           
SHEET    1   I 4 GLN B 300  ILE B 302  0                                        
SHEET    2   I 4 SER B 362  ASP B 375 -1  O  ALA B 363   N  ILE B 302           
SHEET    3   I 4 SER B 310  THR B 322 -1  N  GLU B 318   O  ILE B 366           
SHEET    4   I 4 TYR B 347  PHE B 348 -1  O  PHE B 348   N  PHE B 312           
SHEET    1   J 5 PHE F  43  THR F  51  0                                        
SHEET    2   J 5 ARG F  56  HIS F  62 -1  O  LEU F  59   N  LYS F  47           
SHEET    3   J 5 HIS F  68  ASP F  75 -1  O  MET F  71   N  MET F  58           
SHEET    4   J 5 ASN F 115  GLU F 121 -1  O  MET F 118   N  LYS F  72           
SHEET    5   J 5 LEU F 106  LYS F 111 -1  N  GLU F 107   O  VAL F 119           
SHEET    1   K 2 LEU F 162  ILE F 163  0                                        
SHEET    2   K 2 LYS F 189  ARG F 190 -1  O  LYS F 189   N  ILE F 163           
SHEET    1   L 2 LEU F 172  ILE F 174  0                                        
SHEET    2   L 2 ILE F 180  VAL F 182 -1  O  GLN F 181   N  LEU F 173           
SHEET    1   M 2 CYS F 199  GLY F 200  0                                        
SHEET    2   M 2 VAL E 113  CYS E 114 -1  O  VAL E 113   N  GLY F 200           
SHEET    1   N 4 PHE E 169  VAL E 173  0                                        
SHEET    2   N 4 GLY E 240  ASP E 246 -1  O  LEU E 242   N  LYS E 171           
SHEET    3   N 4 ASN E 188  ARG E 194 -1  N  VAL E 191   O  TRP E 243           
SHEET    4   N 4 SER E 218  PHE E 219 -1  O  PHE E 219   N  TYR E 190           
SHEET    1   O 4 GLY E 291  TYR E 295  0                                        
SHEET    2   O 4 SER E 362  ASP E 375 -1  O  CYS E 371   N  LYS E 293           
SHEET    3   O 4 SER E 310  THR E 322 -1  N  GLU E 318   O  ILE E 366           
SHEET    4   O 4 GLU E 338  CYS E 342 -1  O  CYS E 342   N  VAL E 319           
SHEET    1   P 4 GLN E 300  ILE E 302  0                                        
SHEET    2   P 4 SER E 362  ASP E 375 -1  O  ALA E 363   N  ILE E 302           
SHEET    3   P 4 SER E 310  THR E 322 -1  N  GLU E 318   O  ILE E 366           
SHEET    4   P 4 TYR E 347  PHE E 348 -1  O  PHE E 348   N  PHE E 312           
LINK         C   PHE C 138                 N   SEP C 139     1555   1555  1.33  
LINK         C   SEP C 139                 N   GLU C 140     1555   1555  1.33  
LINK         C   TRP C 196                 N   TPO C 197     1555   1555  1.33  
LINK         C   TPO C 197                 N   LEU C 198     1555   1555  1.33  
LINK         C   VAL C 337                 N   SEP C 338     1555   1555  1.33  
LINK         C   SEP C 338                 N   ILE C 339     1555   1555  1.33  
LINK         C   PHE F 138                 N   SEP F 139     1555   1555  1.33  
LINK         C   SEP F 139                 N   GLU F 140     1555   1555  1.33  
LINK         C   TRP F 196                 N   TPO F 197     1555   1555  1.33  
LINK         C   TPO F 197                 N   LEU F 198     1555   1555  1.33  
LINK         C   VAL F 337                 N   SEP F 338     1555   1555  1.33  
LINK         C   SEP F 338                 N   ILE F 339     1555   1555  1.33  
CISPEP   1 ASP B  204    GLY B  205          0        -7.53                     
CISPEP   2 LYS B  263    MET B  264          0        11.67                     
CISPEP   3 ASP E  204    GLY E  205          0        -7.55                     
CISPEP   4 LYS E  263    MET E  264          0        11.67                     
CRYST1  151.962  213.277   61.625  90.00  90.41  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006581  0.000000  0.000047        0.00000                         
SCALE2      0.000000  0.004689  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016228        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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