GenomeNet

Database: PDB
Entry: 4IDV
LinkDB: 4IDV
Original site: 4IDV 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       13-DEC-12   4IDV              
TITLE     CRYSTAL STRUCTURE OF NIK WITH COMPOUND 4-{3-[2-AMINO-5-(2-            
TITLE    2 METHOXYETHOXY)PYRIMIDIN-4-YL]-1H-INDOL-5-YL}-2-METHYLBUT-3-YN-2-OL   
TITLE    3 (13V)                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 14;         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 330-680;                                      
COMPND   5 SYNONYM: NF-KAPPA-BETA-INDUCING KINASE, HSNIK, SERINE/THREONINE-     
COMPND   6 PROTEIN KINASE NIK;                                                  
COMPND   7 EC: 2.7.11.25;                                                       
COMPND   8 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: MAP3K14, NIK                                                   
KEYWDS    NIK, NUCLEAR FACTOR (NF)-KB, P100 PROCESSING, 2-AMINOPYRIMIDINE,      
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LIU,A.SUDOM,Z.WANG                                                  
REVDAT   1   17-APR-13 4IDV    0                                                
JRNL        AUTH   K.LI,L.R.MCGEE,B.FISHER,A.SUDOM,J.LIU,S.M.RUBENSTEIN,        
JRNL        AUTH 2 M.K.ANWER,T.D.CUSHING,Y.SHIN,M.AYRES,F.LEE,J.EKSTEROWICZ,    
JRNL        AUTH 3 P.FAULDER,B.WASZKOWYCZ,O.PLOTNIKOVA,E.FARRELLY,S.H.XIAO,     
JRNL        AUTH 4 G.CHEN,Z.WANG                                                
JRNL        TITL   INHIBITING NF-KB-INDUCING KINASE (NIK): DISCOVERY,           
JRNL        TITL 2 STRUCTURE-BASED DESIGN, SYNTHESIS, STRUCTURE ACTIVITY        
JRNL        TITL 3 RELATIONSHIP, AND CO-CRYSTAL STRUCTURES                      
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  23  1238 2013              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   23374866                                                     
JRNL        DOI    10.1016/J.BMCL.2013.01.012                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 31326                          
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) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1572                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1777                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 65.75                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3700                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 85                           
REMARK   3   BIN FREE R VALUE                    : 0.5210                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10380                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 108                                     
REMARK   3   SOLVENT ATOMS            : 46                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.33                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.05000                                             
REMARK   3    B22 (A**2) : 0.60000                                              
REMARK   3    B33 (A**2) : 0.46000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.508         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.310         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.542        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.915                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.853                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES: REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 4IDV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB076628.                                      
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                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31375                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 127.350                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 81.3                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.14400                            
REMARK 200  R SYM                      (I) : 0.14400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.66600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       22.68900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      127.35050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       73.00700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      127.35050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.68900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       73.00700            
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, 4                                              
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: D                                     
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   325                                                      
REMARK 465     ALA A   326                                                      
REMARK 465     MET A   327                                                      
REMARK 465     GLY A   328                                                      
REMARK 465     SER A   329                                                      
REMARK 465     LYS A   330                                                      
REMARK 465     GLY A   364                                                      
REMARK 465     SER A   365                                                      
REMARK 465     ARG A   366                                                      
REMARK 465     SER A   367                                                      
REMARK 465     ARG A   368                                                      
REMARK 465     GLU A   369                                                      
REMARK 465     PRO A   370                                                      
REMARK 465     SER A   371                                                      
REMARK 465     PRO A   372                                                      
REMARK 465     LYS A   373                                                      
REMARK 465     PRO A   676                                                      
REMARK 465     PRO A   677                                                      
REMARK 465     ASN A   678                                                      
REMARK 465     GLN A   679                                                      
REMARK 465     ALA A   680                                                      
REMARK 465     GLY B   325                                                      
REMARK 465     ALA B   326                                                      
REMARK 465     MET B   327                                                      
REMARK 465     GLY B   328                                                      
REMARK 465     SER B   329                                                      
REMARK 465     LYS B   330                                                      
REMARK 465     GLY B   364                                                      
REMARK 465     SER B   365                                                      
REMARK 465     ARG B   366                                                      
REMARK 465     SER B   367                                                      
REMARK 465     ARG B   368                                                      
REMARK 465     GLU B   369                                                      
REMARK 465     PRO B   370                                                      
REMARK 465     SER B   371                                                      
REMARK 465     PRO B   372                                                      
REMARK 465     LYS B   373                                                      
REMARK 465     PRO B   676                                                      
REMARK 465     PRO B   677                                                      
REMARK 465     ASN B   678                                                      
REMARK 465     GLN B   679                                                      
REMARK 465     ALA B   680                                                      
REMARK 465     GLY C   325                                                      
REMARK 465     ALA C   326                                                      
REMARK 465     MET C   327                                                      
REMARK 465     GLY C   328                                                      
REMARK 465     SER C   329                                                      
REMARK 465     LYS C   330                                                      
REMARK 465     GLY C   364                                                      
REMARK 465     SER C   365                                                      
REMARK 465     ARG C   366                                                      
REMARK 465     SER C   367                                                      
REMARK 465     ARG C   368                                                      
REMARK 465     GLU C   369                                                      
REMARK 465     PRO C   370                                                      
REMARK 465     SER C   371                                                      
REMARK 465     PRO C   372                                                      
REMARK 465     LYS C   373                                                      
REMARK 465     PRO C   676                                                      
REMARK 465     PRO C   677                                                      
REMARK 465     ASN C   678                                                      
REMARK 465     GLN C   679                                                      
REMARK 465     ALA C   680                                                      
REMARK 465     GLY D   325                                                      
REMARK 465     ALA D   326                                                      
REMARK 465     MET D   327                                                      
REMARK 465     GLY D   328                                                      
REMARK 465     SER D   329                                                      
REMARK 465     LYS D   330                                                      
REMARK 465     GLY D   364                                                      
REMARK 465     SER D   365                                                      
REMARK 465     ARG D   366                                                      
REMARK 465     SER D   367                                                      
REMARK 465     ARG D   368                                                      
REMARK 465     GLU D   369                                                      
REMARK 465     PRO D   370                                                      
REMARK 465     SER D   371                                                      
REMARK 465     PRO D   372                                                      
REMARK 465     LYS D   373                                                      
REMARK 465     PRO D   676                                                      
REMARK 465     PRO D   677                                                      
REMARK 465     ASN D   678                                                      
REMARK 465     GLN D   679                                                      
REMARK 465     ALA D   680                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLN A   598     NH1  ARG A   673              2.09            
REMARK 500   OE2  GLU A   483     NH1  ARG A   666              2.14            
REMARK 500   NZ   LYS D   576     O    ARG D   641              2.16            
REMARK 500   OE1  GLN B   598     NH1  ARG B   673              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    THR A   552     OH   TYR D   336     3555     2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 512   CA  -  CB  -  CG  ANGL. DEV. =  18.5 DEGREES          
REMARK 500    PRO C 543   C   -  N   -  CA  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    PRO C 543   C   -  N   -  CD  ANGL. DEV. = -14.2 DEGREES          
REMARK 500    LEU C 546   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    PRO D 543   C   -  N   -  CA  ANGL. DEV. =  15.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 332      116.41    -22.09                                   
REMARK 500    GLU A 375      110.87      2.94                                   
REMARK 500    ASP A 376      162.06    -39.83                                   
REMARK 500    TYR A 393       88.56   -151.06                                   
REMARK 500    GLU A 396      -27.48     74.08                                   
REMARK 500    LEU A 447      124.47    -35.01                                   
REMARK 500    ASP A 515       65.17   -160.12                                   
REMARK 500    LYS A 517      171.02    178.00                                   
REMARK 500    GLN A 542      -98.49   -123.26                                   
REMARK 500    PRO A 543      -90.57    -81.01                                   
REMARK 500    ASP A 544       84.92   -156.65                                   
REMARK 500    LEU A 546       88.94   -165.82                                   
REMARK 500    SER A 549      -72.71    -48.03                                   
REMARK 500    LEU A 551      114.19     91.59                                   
REMARK 500    THR A 552      158.68    138.98                                   
REMARK 500    ASP A 554      -62.78    -24.03                                   
REMARK 500    ASP A 574     -154.71   -150.79                                   
REMARK 500    TRP A 596      -45.17     73.00                                   
REMARK 500    PRO A 614       46.01    -78.19                                   
REMARK 500    SER A 621      -32.06    -38.58                                   
REMARK 500    SER B 332       93.18     -6.37                                   
REMARK 500    VAL B 333      -52.58      9.64                                   
REMARK 500    GLU B 375       75.83     12.48                                   
REMARK 500    ASP B 376      159.94    -19.29                                   
REMARK 500    ASP B 390       58.25     33.71                                   
REMARK 500    TYR B 391       -1.72     83.57                                   
REMARK 500    GLU B 396      -20.05     74.74                                   
REMARK 500    VAL B 397      -62.43    -96.71                                   
REMARK 500    LEU B 447      130.16    -39.01                                   
REMARK 500    PRO B 450        9.51    -67.74                                   
REMARK 500    PRO B 488      154.24    -48.88                                   
REMARK 500    PHE B 535       31.08    -88.41                                   
REMARK 500    GLN B 542     -109.66   -110.38                                   
REMARK 500    PRO B 543      -77.68    -89.67                                   
REMARK 500    ASP B 544       65.16   -154.74                                   
REMARK 500    LEU B 546      101.53   -167.16                                   
REMARK 500    SER B 549      -77.17    -48.58                                   
REMARK 500    LEU B 551       79.24    103.53                                   
REMARK 500    TRP B 596      -57.68     64.75                                   
REMARK 500    PRO B 614       40.16    -72.56                                   
REMARK 500    SER B 621       -9.25    -56.28                                   
REMARK 500    SER C 332       99.26      4.34                                   
REMARK 500    GLU C 375       89.10     30.49                                   
REMARK 500    ASP C 376      141.90    -22.94                                   
REMARK 500    ASP C 390       68.31     31.52                                   
REMARK 500    GLU C 396      -21.29     76.98                                   
REMARK 500    HIS C 402       92.12    -66.89                                   
REMARK 500    CYS C 426     -166.84   -169.25                                   
REMARK 500    CYS C 444       14.28   -141.90                                   
REMARK 500    LEU C 447      116.44     -9.17                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      83 RAMACHANDRAN OUTLIERS.                        
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 PRO A  543     ASP A  544                  134.28                    
REMARK 500 ASP A  544     GLY A  545                  143.30                    
REMARK 500 LEU A  551     THR A  552                 -146.20                    
REMARK 500 THR B  374     GLU B  375                 -149.09                    
REMARK 500 GLU B  375     ASP B  376                 -149.22                    
REMARK 500 LEU B  447     THR B  448                 -149.62                    
REMARK 500 THR C  374     GLU C  375                 -149.74                    
REMARK 500 THR D  552     GLY D  553                   38.38                    
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    VAL A 579        24.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13V A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13V B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13V C 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 13V D 701                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4IDT   RELATED DB: PDB                                   
DBREF  4IDV A  330   680  UNP    Q99558   M3K14_HUMAN    330    680             
DBREF  4IDV B  330   680  UNP    Q99558   M3K14_HUMAN    330    680             
DBREF  4IDV C  330   680  UNP    Q99558   M3K14_HUMAN    330    680             
DBREF  4IDV D  330   680  UNP    Q99558   M3K14_HUMAN    330    680             
SEQADV 4IDV GLY A  325  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV ALA A  326  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV MET A  327  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV GLY A  328  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV SER A  329  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV GLY B  325  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV ALA B  326  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV MET B  327  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV GLY B  328  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV SER B  329  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV GLY C  325  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV ALA C  326  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV MET C  327  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV GLY C  328  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV SER C  329  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV GLY D  325  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV ALA D  326  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV MET D  327  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV GLY D  328  UNP  Q99558              EXPRESSION TAG                 
SEQADV 4IDV SER D  329  UNP  Q99558              EXPRESSION TAG                 
SEQRES   1 A  356  GLY ALA MET GLY SER LYS PHE SER VAL GLU GLU TYR LEU          
SEQRES   2 A  356  VAL HIS ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA          
SEQRES   3 A  356  HIS SER LEU THR SER LEU ALA LYS THR TRP ALA ALA ARG          
SEQRES   4 A  356  GLY SER ARG SER ARG GLU PRO SER PRO LYS THR GLU ASP          
SEQRES   5 A  356  ASN GLU GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL          
SEQRES   6 A  356  ASP TYR GLU TYR ARG GLU GLU VAL HIS TRP ALA THR HIS          
SEQRES   7 A  356  GLN LEU ARG LEU GLY ARG GLY SER PHE GLY GLU VAL HIS          
SEQRES   8 A  356  ARG MET GLU ASP LYS GLN THR GLY PHE GLN CYS ALA VAL          
SEQRES   9 A  356  LYS LYS VAL ARG LEU GLU VAL PHE ARG ALA GLU GLU LEU          
SEQRES  10 A  356  MET ALA CYS ALA GLY LEU THR SER PRO ARG ILE VAL PRO          
SEQRES  11 A  356  LEU TYR GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE          
SEQRES  12 A  356  PHE MET GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU          
SEQRES  13 A  356  VAL LYS GLU GLN GLY CYS LEU PRO GLU ASP ARG ALA LEU          
SEQRES  14 A  356  TYR TYR LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU          
SEQRES  15 A  356  HIS SER ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP          
SEQRES  16 A  356  ASN VAL LEU LEU SER SER ASP GLY SER HIS ALA ALA LEU          
SEQRES  17 A  356  CYS ASP PHE GLY HIS ALA VAL CYS LEU GLN PRO ASP GLY          
SEQRES  18 A  356  LEU GLY LYS SER LEU LEU THR GLY ASP TYR ILE PRO GLY          
SEQRES  19 A  356  THR GLU THR HIS MET ALA PRO GLU VAL VAL LEU GLY ARG          
SEQRES  20 A  356  SER CYS ASP ALA LYS VAL ASP VAL TRP SER SER CYS CYS          
SEQRES  21 A  356  MET MET LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR          
SEQRES  22 A  356  GLN PHE PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER          
SEQRES  23 A  356  GLU PRO PRO PRO VAL ARG GLU ILE PRO PRO SER CYS ALA          
SEQRES  24 A  356  PRO LEU THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS          
SEQRES  25 A  356  GLU PRO ILE HIS ARG VAL SER ALA ALA GLU LEU GLY GLY          
SEQRES  26 A  356  LYS VAL ASN ARG ALA LEU GLN GLN VAL GLY GLY LEU LYS          
SEQRES  27 A  356  SER PRO TRP ARG GLY GLU TYR LYS GLU PRO ARG HIS PRO          
SEQRES  28 A  356  PRO PRO ASN GLN ALA                                          
SEQRES   1 B  356  GLY ALA MET GLY SER LYS PHE SER VAL GLU GLU TYR LEU          
SEQRES   2 B  356  VAL HIS ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA          
SEQRES   3 B  356  HIS SER LEU THR SER LEU ALA LYS THR TRP ALA ALA ARG          
SEQRES   4 B  356  GLY SER ARG SER ARG GLU PRO SER PRO LYS THR GLU ASP          
SEQRES   5 B  356  ASN GLU GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL          
SEQRES   6 B  356  ASP TYR GLU TYR ARG GLU GLU VAL HIS TRP ALA THR HIS          
SEQRES   7 B  356  GLN LEU ARG LEU GLY ARG GLY SER PHE GLY GLU VAL HIS          
SEQRES   8 B  356  ARG MET GLU ASP LYS GLN THR GLY PHE GLN CYS ALA VAL          
SEQRES   9 B  356  LYS LYS VAL ARG LEU GLU VAL PHE ARG ALA GLU GLU LEU          
SEQRES  10 B  356  MET ALA CYS ALA GLY LEU THR SER PRO ARG ILE VAL PRO          
SEQRES  11 B  356  LEU TYR GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE          
SEQRES  12 B  356  PHE MET GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU          
SEQRES  13 B  356  VAL LYS GLU GLN GLY CYS LEU PRO GLU ASP ARG ALA LEU          
SEQRES  14 B  356  TYR TYR LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU          
SEQRES  15 B  356  HIS SER ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP          
SEQRES  16 B  356  ASN VAL LEU LEU SER SER ASP GLY SER HIS ALA ALA LEU          
SEQRES  17 B  356  CYS ASP PHE GLY HIS ALA VAL CYS LEU GLN PRO ASP GLY          
SEQRES  18 B  356  LEU GLY LYS SER LEU LEU THR GLY ASP TYR ILE PRO GLY          
SEQRES  19 B  356  THR GLU THR HIS MET ALA PRO GLU VAL VAL LEU GLY ARG          
SEQRES  20 B  356  SER CYS ASP ALA LYS VAL ASP VAL TRP SER SER CYS CYS          
SEQRES  21 B  356  MET MET LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR          
SEQRES  22 B  356  GLN PHE PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER          
SEQRES  23 B  356  GLU PRO PRO PRO VAL ARG GLU ILE PRO PRO SER CYS ALA          
SEQRES  24 B  356  PRO LEU THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS          
SEQRES  25 B  356  GLU PRO ILE HIS ARG VAL SER ALA ALA GLU LEU GLY GLY          
SEQRES  26 B  356  LYS VAL ASN ARG ALA LEU GLN GLN VAL GLY GLY LEU LYS          
SEQRES  27 B  356  SER PRO TRP ARG GLY GLU TYR LYS GLU PRO ARG HIS PRO          
SEQRES  28 B  356  PRO PRO ASN GLN ALA                                          
SEQRES   1 C  356  GLY ALA MET GLY SER LYS PHE SER VAL GLU GLU TYR LEU          
SEQRES   2 C  356  VAL HIS ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA          
SEQRES   3 C  356  HIS SER LEU THR SER LEU ALA LYS THR TRP ALA ALA ARG          
SEQRES   4 C  356  GLY SER ARG SER ARG GLU PRO SER PRO LYS THR GLU ASP          
SEQRES   5 C  356  ASN GLU GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL          
SEQRES   6 C  356  ASP TYR GLU TYR ARG GLU GLU VAL HIS TRP ALA THR HIS          
SEQRES   7 C  356  GLN LEU ARG LEU GLY ARG GLY SER PHE GLY GLU VAL HIS          
SEQRES   8 C  356  ARG MET GLU ASP LYS GLN THR GLY PHE GLN CYS ALA VAL          
SEQRES   9 C  356  LYS LYS VAL ARG LEU GLU VAL PHE ARG ALA GLU GLU LEU          
SEQRES  10 C  356  MET ALA CYS ALA GLY LEU THR SER PRO ARG ILE VAL PRO          
SEQRES  11 C  356  LEU TYR GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE          
SEQRES  12 C  356  PHE MET GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU          
SEQRES  13 C  356  VAL LYS GLU GLN GLY CYS LEU PRO GLU ASP ARG ALA LEU          
SEQRES  14 C  356  TYR TYR LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU          
SEQRES  15 C  356  HIS SER ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP          
SEQRES  16 C  356  ASN VAL LEU LEU SER SER ASP GLY SER HIS ALA ALA LEU          
SEQRES  17 C  356  CYS ASP PHE GLY HIS ALA VAL CYS LEU GLN PRO ASP GLY          
SEQRES  18 C  356  LEU GLY LYS SER LEU LEU THR GLY ASP TYR ILE PRO GLY          
SEQRES  19 C  356  THR GLU THR HIS MET ALA PRO GLU VAL VAL LEU GLY ARG          
SEQRES  20 C  356  SER CYS ASP ALA LYS VAL ASP VAL TRP SER SER CYS CYS          
SEQRES  21 C  356  MET MET LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR          
SEQRES  22 C  356  GLN PHE PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER          
SEQRES  23 C  356  GLU PRO PRO PRO VAL ARG GLU ILE PRO PRO SER CYS ALA          
SEQRES  24 C  356  PRO LEU THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS          
SEQRES  25 C  356  GLU PRO ILE HIS ARG VAL SER ALA ALA GLU LEU GLY GLY          
SEQRES  26 C  356  LYS VAL ASN ARG ALA LEU GLN GLN VAL GLY GLY LEU LYS          
SEQRES  27 C  356  SER PRO TRP ARG GLY GLU TYR LYS GLU PRO ARG HIS PRO          
SEQRES  28 C  356  PRO PRO ASN GLN ALA                                          
SEQRES   1 D  356  GLY ALA MET GLY SER LYS PHE SER VAL GLU GLU TYR LEU          
SEQRES   2 D  356  VAL HIS ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA          
SEQRES   3 D  356  HIS SER LEU THR SER LEU ALA LYS THR TRP ALA ALA ARG          
SEQRES   4 D  356  GLY SER ARG SER ARG GLU PRO SER PRO LYS THR GLU ASP          
SEQRES   5 D  356  ASN GLU GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL          
SEQRES   6 D  356  ASP TYR GLU TYR ARG GLU GLU VAL HIS TRP ALA THR HIS          
SEQRES   7 D  356  GLN LEU ARG LEU GLY ARG GLY SER PHE GLY GLU VAL HIS          
SEQRES   8 D  356  ARG MET GLU ASP LYS GLN THR GLY PHE GLN CYS ALA VAL          
SEQRES   9 D  356  LYS LYS VAL ARG LEU GLU VAL PHE ARG ALA GLU GLU LEU          
SEQRES  10 D  356  MET ALA CYS ALA GLY LEU THR SER PRO ARG ILE VAL PRO          
SEQRES  11 D  356  LEU TYR GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE          
SEQRES  12 D  356  PHE MET GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU          
SEQRES  13 D  356  VAL LYS GLU GLN GLY CYS LEU PRO GLU ASP ARG ALA LEU          
SEQRES  14 D  356  TYR TYR LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU          
SEQRES  15 D  356  HIS SER ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP          
SEQRES  16 D  356  ASN VAL LEU LEU SER SER ASP GLY SER HIS ALA ALA LEU          
SEQRES  17 D  356  CYS ASP PHE GLY HIS ALA VAL CYS LEU GLN PRO ASP GLY          
SEQRES  18 D  356  LEU GLY LYS SER LEU LEU THR GLY ASP TYR ILE PRO GLY          
SEQRES  19 D  356  THR GLU THR HIS MET ALA PRO GLU VAL VAL LEU GLY ARG          
SEQRES  20 D  356  SER CYS ASP ALA LYS VAL ASP VAL TRP SER SER CYS CYS          
SEQRES  21 D  356  MET MET LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR          
SEQRES  22 D  356  GLN PHE PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER          
SEQRES  23 D  356  GLU PRO PRO PRO VAL ARG GLU ILE PRO PRO SER CYS ALA          
SEQRES  24 D  356  PRO LEU THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS          
SEQRES  25 D  356  GLU PRO ILE HIS ARG VAL SER ALA ALA GLU LEU GLY GLY          
SEQRES  26 D  356  LYS VAL ASN ARG ALA LEU GLN GLN VAL GLY GLY LEU LYS          
SEQRES  27 D  356  SER PRO TRP ARG GLY GLU TYR LYS GLU PRO ARG HIS PRO          
SEQRES  28 D  356  PRO PRO ASN GLN ALA                                          
HET    13V  A 701      27                                                       
HET    13V  B 701      27                                                       
HET    13V  C 701      27                                                       
HET    13V  D 701      27                                                       
HETNAM     13V 4-{3-[2-AMINO-5-(2-METHOXYETHOXY)PYRIMIDIN-4-YL]-1H-             
HETNAM   2 13V  INDOL-5-YL}-2-METHYLBUT-3-YN-2-OL                               
FORMUL   5  13V    4(C20 H22 N4 O3)                                             
FORMUL   9  HOH   *46(H2 O)                                                     
HELIX    1   1 SER A  332  ALA A  340  1                                   9    
HELIX    2   2 GLN A  349  ARG A  363  1                                  15    
HELIX    3   3 GLU A  434  ARG A  437  5                                   4    
HELIX    4   4 ALA A  438  ALA A  443  1                                   6    
HELIX    5   5 LEU A  477  GLY A  485  1                                   9    
HELIX    6   6 PRO A  488  ARG A  509  1                                  22    
HELIX    7   7 LYS A  517  ASP A  519  5                                   3    
HELIX    8   8 ASP A  534  ALA A  538  5                                   5    
HELIX    9   9 THR A  559  MET A  563  5                                   5    
HELIX   10  10 ALA A  564  LEU A  569  1                                   6    
HELIX   11  11 ALA A  575  GLY A  592  1                                  18    
HELIX   12  12 PRO A  603  GLU A  611  1                                   9    
HELIX   13  13 PRO A  613  ILE A  618  5                                   6    
HELIX   14  14 ALA A  623  LEU A  634  1                                  12    
HELIX   15  15 SER A  643  VAL A  658  1                                  16    
HELIX   16  16 VAL B  333  GLN B  342  1                                  10    
HELIX   17  17 GLN B  349  ARG B  363  1                                  15    
HELIX   18  18 GLU B  434  ARG B  437  5                                   4    
HELIX   19  19 ALA B  438  ALA B  443  1                                   6    
HELIX   20  20 SER B  476  GLY B  485  1                                  10    
HELIX   21  21 PRO B  488  ARG B  509  1                                  22    
HELIX   22  22 LYS B  517  ASP B  519  5                                   3    
HELIX   23  23 THR B  559  MET B  563  5                                   5    
HELIX   24  24 ALA B  564  GLY B  570  1                                   7    
HELIX   25  25 ALA B  575  GLY B  592  1                                  18    
HELIX   26  26 LEU B  604  GLU B  611  1                                   8    
HELIX   27  27 ALA B  623  GLY B  633  1                                  11    
HELIX   28  28 SER B  643  VAL B  658  1                                  16    
HELIX   29  29 SER C  332  GLN C  342  1                                  11    
HELIX   30  30 GLN C  349  ARG C  363  1                                  15    
HELIX   31  31 GLU C  434  ARG C  437  5                                   4    
HELIX   32  32 ALA C  438  ALA C  443  1                                   6    
HELIX   33  33 SER C  476  GLY C  485  1                                  10    
HELIX   34  34 PRO C  488  ARG C  509  1                                  22    
HELIX   35  35 LYS C  517  ASP C  519  5                                   3    
HELIX   36  36 THR C  559  MET C  563  5                                   5    
HELIX   37  37 ALA C  564  LEU C  569  1                                   6    
HELIX   38  38 ALA C  575  GLY C  592  1                                  18    
HELIX   39  39 LEU C  604  GLU C  611  1                                   8    
HELIX   40  40 PRO C  614  ILE C  618  5                                   5    
HELIX   41  41 ALA C  623  LEU C  634  1                                  12    
HELIX   42  42 SER C  643  VAL C  658  1                                  16    
HELIX   43  43 VAL D  333  GLN D  342  1                                  10    
HELIX   44  44 GLN D  349  ARG D  363  1                                  15    
HELIX   45  45 GLU D  434  ARG D  437  5                                   4    
HELIX   46  46 ALA D  438  ALA D  443  1                                   6    
HELIX   47  47 LEU D  477  GLY D  485  1                                   9    
HELIX   48  48 PRO D  488  ARG D  509  1                                  22    
HELIX   49  49 LYS D  517  ASP D  519  5                                   3    
HELIX   50  50 THR D  559  MET D  563  5                                   5    
HELIX   51  51 ALA D  564  LEU D  569  1                                   6    
HELIX   52  52 ALA D  575  GLY D  592  1                                  18    
HELIX   53  53 PRO D  603  GLU D  611  1                                   9    
HELIX   54  54 PRO D  613  ILE D  618  5                                   6    
HELIX   55  55 ALA D  623  LEU D  634  1                                  12    
HELIX   56  56 SER D  643  VAL D  658  1                                  16    
SHEET    1   A 7 VAL A 345  SER A 347  0                                        
SHEET    2   A 7 ASN A 377  LEU A 381  1  O  LEU A 381   N  SER A 346           
SHEET    3   A 7 LEU A 455  GLU A 461 -1  O  ARG A 460   N  GLU A 378           
SHEET    4   A 7 TRP A 464  MET A 469 -1  O  ASN A 466   N  VAL A 459           
SHEET    5   A 7 GLN A 425  ARG A 432 -1  N  ALA A 427   O  MET A 469           
SHEET    6   A 7 VAL A 414  ASP A 419 -1  N  MET A 417   O  CYS A 426           
SHEET    7   A 7 TRP A 399  THR A 401 -1  N  ALA A 400   O  GLU A 418           
SHEET    1   B 3 GLY A 475  SER A 476  0                                        
SHEET    2   B 3 VAL A 521  LEU A 523 -1  O  LEU A 523   N  GLY A 475           
SHEET    3   B 3 ALA A 530  LEU A 532 -1  O  ALA A 531   N  LEU A 522           
SHEET    1   C 2 ILE A 511  LEU A 512  0                                        
SHEET    2   C 2 VAL A 539  CYS A 540 -1  O  VAL A 539   N  LEU A 512           
SHEET    1   D 7 VAL B 345  SER B 347  0                                        
SHEET    2   D 7 ASN B 377  LEU B 381  1  O  LEU B 381   N  SER B 346           
SHEET    3   D 7 LEU B 455  GLU B 461 -1  O  ARG B 460   N  GLU B 378           
SHEET    4   D 7 TRP B 464  MET B 469 -1  O  ASN B 466   N  VAL B 459           
SHEET    5   D 7 GLN B 425  ARG B 432 -1  N  LYS B 429   O  ILE B 467           
SHEET    6   D 7 VAL B 414  ASP B 419 -1  N  MET B 417   O  CYS B 426           
SHEET    7   D 7 TRP B 399  THR B 401 -1  N  ALA B 400   O  GLU B 418           
SHEET    1   E 2 ILE B 511  LEU B 512  0                                        
SHEET    2   E 2 VAL B 539  CYS B 540 -1  O  VAL B 539   N  LEU B 512           
SHEET    1   F 2 VAL B 521  LEU B 523  0                                        
SHEET    2   F 2 ALA B 530  LEU B 532 -1  O  ALA B 531   N  LEU B 522           
SHEET    1   G 7 VAL C 345  SER C 347  0                                        
SHEET    2   G 7 GLU C 378  LEU C 381  1  O  LEU C 381   N  SER C 346           
SHEET    3   G 7 LEU C 455  GLU C 461 -1  O  ARG C 460   N  GLU C 378           
SHEET    4   G 7 TRP C 464  MET C 469 -1  O  ASN C 466   N  VAL C 459           
SHEET    5   G 7 GLN C 425  ARG C 432 -1  N  ALA C 427   O  MET C 469           
SHEET    6   G 7 VAL C 414  ASP C 419 -1  N  MET C 417   O  CYS C 426           
SHEET    7   G 7 TRP C 399  THR C 401 -1  N  ALA C 400   O  GLU C 418           
SHEET    1   H 2 ILE C 511  LEU C 512  0                                        
SHEET    2   H 2 VAL C 539  CYS C 540 -1  O  VAL C 539   N  LEU C 512           
SHEET    1   I 2 VAL C 521  LEU C 523  0                                        
SHEET    2   I 2 ALA C 530  LEU C 532 -1  O  ALA C 531   N  LEU C 522           
SHEET    1   J 7 VAL D 345  SER D 347  0                                        
SHEET    2   J 7 GLU D 378  LEU D 381  1  O  LEU D 381   N  SER D 346           
SHEET    3   J 7 LEU D 455  GLU D 461 -1  O  ARG D 460   N  GLU D 378           
SHEET    4   J 7 TRP D 464  MET D 469 -1  O  ASN D 466   N  VAL D 459           
SHEET    5   J 7 GLN D 425  ARG D 432 -1  N  VAL D 431   O  VAL D 465           
SHEET    6   J 7 VAL D 414  ASP D 419 -1  N  HIS D 415   O  VAL D 428           
SHEET    7   J 7 TRP D 399  THR D 401 -1  N  ALA D 400   O  GLU D 418           
SHEET    1   K 3 GLY D 475  SER D 476  0                                        
SHEET    2   K 3 VAL D 521  LEU D 523 -1  O  LEU D 523   N  GLY D 475           
SHEET    3   K 3 ALA D 530  LEU D 532 -1  O  ALA D 531   N  LEU D 522           
SHEET    1   L 2 ILE D 511  LEU D 512  0                                        
SHEET    2   L 2 VAL D 539  CYS D 540 -1  O  VAL D 539   N  LEU D 512           
CISPEP   1 GLN A  403    LEU A  404          0       -15.16                     
CISPEP   2 GLY A  602    PRO A  603          0       -11.80                     
CISPEP   3 GLN B  403    LEU B  404          0         4.94                     
CISPEP   4 THR B  552    GLY B  553          0        29.26                     
CISPEP   5 GLY B  602    PRO B  603          0        -2.78                     
CISPEP   6 GLN C  403    LEU C  404          0       -14.72                     
CISPEP   7 GLN C  542    PRO C  543          0        21.76                     
CISPEP   8 GLY C  602    PRO C  603          0        -6.82                     
CISPEP   9 GLN D  403    LEU D  404          0        -4.12                     
CISPEP  10 GLN D  542    PRO D  543          0        15.24                     
CISPEP  11 GLY D  602    PRO D  603          0        -4.05                     
SITE     1 AC1 14 ARG A 408  GLY A 409  VAL A 414  GLU A 440                    
SITE     2 AC1 14 ILE A 467  MET A 469  GLU A 470  LEU A 472                    
SITE     3 AC1 14 GLY A 475  SER A 476  GLN A 479  LEU A 522                    
SITE     4 AC1 14 ASP A 534  PHE A 535                                          
SITE     1 AC2 16 ARG B 408  GLY B 409  VAL B 414  ALA B 427                    
SITE     2 AC2 16 GLU B 440  VAL B 453  ILE B 467  MET B 469                    
SITE     3 AC2 16 GLU B 470  LEU B 471  LEU B 472  SER B 476                    
SITE     4 AC2 16 GLN B 479  LEU B 522  ASP B 534  PHE B 535                    
SITE     1 AC3 13 ARG C 408  GLY C 409  GLU C 440  ILE C 467                    
SITE     2 AC3 13 MET C 469  GLU C 470  LEU C 471  LEU C 472                    
SITE     3 AC3 13 SER C 476  GLN C 479  LEU C 522  ASP C 534                    
SITE     4 AC3 13 PHE C 535                                                     
SITE     1 AC4 15 ARG D 408  GLY D 409  VAL D 414  GLU D 440                    
SITE     2 AC4 15 ILE D 467  MET D 469  GLU D 470  LEU D 471                    
SITE     3 AC4 15 LEU D 472  SER D 476  GLN D 479  LEU D 522                    
SITE     4 AC4 15 CYS D 533  ASP D 534  PHE D 535                               
CRYST1   45.378  146.014  254.701  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022037  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006849  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003926        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system