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Database: PDB
Entry: 5HD7
LinkDB: 5HD7
Original site: 5HD7 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       04-JAN-16   5HD7              
TITLE     DISSECTING THERAPEUTIC RESISTANCE TO ERK INHIBITION RAT MUTANT        
TITLE    2 SCH772984 IN COMPLEX WITH (3R)-1-(2-OXO-2-{4-[4-(PYRIMIDIN-2-YL)     
TITLE    3 PHENYL]PIPERAZIN-1-YL}ETHYL)-N-[3-(PYRIDIN-4-YL)-2H-INDAZOL-5-       
TITLE    4 YL]PYRROLIDINE-3-CARBOXAMIDE                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MAPK 1,ERT1,EXTRACELLULAR SIGNAL-REGULATED KINASE 2,ERK-2,  
COMPND   5 MAP KINASE ISOFORM P42,P42-MAPK,MITOGEN-ACTIVATED PROTEIN KINASE 2,  
COMPND   6 MAPK 2;                                                              
COMPND   7 EC: 2.7.11.24;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: MAPK1, ERK2, MAPK, PRKM1;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, MAP KINASE,             
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.JHA,E.J.MORRIS,A.HRUZA,M.S.MANSUETO,G.SCHROEDER,J.ARBANAS,          
AUTHOR   2 D.MCMASTERS,C.R.RESTAINO,R.DAYANANTH,S.BLACK,N.L.ELSEN,A.MANNARINO,  
AUTHOR   3 A.COOPER,S.FAWELL,L.ZAWEL,L.JAYARAMAN,A.A.SAMATAR                    
REVDAT   3   22-NOV-17 5HD7    1       REMARK                                   
REVDAT   2   01-JUN-16 5HD7    1       JRNL                                     
REVDAT   1   24-FEB-16 5HD7    0                                                
JRNL        AUTH   S.JHA,E.J.MORRIS,A.HRUZA,M.S.MANSUETO,G.K.SCHROEDER,         
JRNL        AUTH 2 J.ARBANAS,D.MCMASTERS,C.R.RESTAINO,P.DAYANANTH,S.BLACK,      
JRNL        AUTH 3 N.L.ELSEN,A.MANNARINO,A.COOPER,S.FAWELL,L.ZAWEL,L.JAYARAMAN, 
JRNL        AUTH 4 A.A.SAMATAR                                                  
JRNL        TITL   DISSECTING THERAPEUTIC RESISTANCE TO ERK INHIBITION.         
JRNL        REF    MOL.CANCER THER.              V.  15   548 2016              
JRNL        REFN                   ESSN 1538-8514                               
JRNL        PMID   26832798                                                     
JRNL        DOI    10.1158/1535-7163.MCT-15-0172                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.4                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 17.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 44384                          
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)  : 0.182                          
REMARK   3   R VALUE            (WORKING SET)  : 0.181                          
REMARK   3   FREE R VALUE                      : 0.207                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.990                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2214                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.69                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.73                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 95.38                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3099                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1971                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2971                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1955                   
REMARK   3   BIN FREE R VALUE                        : 0.2354                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.13                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 128                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2839                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 274                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.27                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.06990                                             
REMARK   3    B22 (A**2) : -1.14600                                             
REMARK   3    B33 (A**2) : 3.21590                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.203               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.101               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.096               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.126               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.096               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5992   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 10844  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1335   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 79     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 915    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5992   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : 5      ; 0.000  ; HARMONIC            
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 385    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 6763   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.02                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.58                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 15.13                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   52.7730   19.1907   18.9692           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0240 T22:   -0.0869                                    
REMARK   3     T33:   -0.0270 T12:    0.0073                                    
REMARK   3     T13:    0.0045 T23:    0.0035                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9415 L22:    0.5940                                    
REMARK   3     L33:    0.9191 L12:   -0.3751                                    
REMARK   3     L13:   -0.4885 L23:    0.1697                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0388 S12:    0.1609 S13:   -0.0534                     
REMARK   3     S21:   -0.0062 S22:   -0.0648 S23:    0.0688                     
REMARK   3     S31:   -0.0473 S32:   -0.0793 S33:    0.0259                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5HD7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000216854.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : AUTOPROC 1.1.2                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44558                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.030                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 9.700                              
REMARK 200  R MERGE                    (I) : 0.05100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.60400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, PH 6.4, 2.0M AMMONIUM          
REMARK 280  SULFATE, 5% PEG 400, 0.5% DMSO, 1% GLYEROL, 0.0005M OLOMOUCINE,     
REMARK 280  10 DAY SOAK WITH 500 MICROMOLAR OF NEW COMPOUND, VAPOR DIFFUSION,   
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       35.49300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.71100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.49300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.71100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 TOTAL BURIED SURFACE AREA: 930 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 16550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 KCAL/MOL                        
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 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     ALA A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     TYR A   356                                                      
REMARK 465     ARG A   357                                                      
REMARK 465     SER A   358                                                      
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    ILE A  29      -65.25   -109.06                                   
REMARK 500    ASP A 147       42.20   -152.36                                   
REMARK 500    ASP A 165       85.26     68.56                                   
REMARK 500    ASN A 199       12.12   -162.37                                   
REMARK 500    ILE A 254      -62.51     75.84                                   
REMARK 500    LEU A 292       43.75    -95.83                                   
REMARK 500    LEU A 292       43.75    -98.54                                   
REMARK 500    ALA A 325       76.38   -116.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ASN A 274         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 774        DISTANCE =  5.95 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 38Z A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 406                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5HD4   RELATED DB: PDB                                   
DBREF  5HD7 A    1   358  UNP    P63086   MK01_RAT         1    358             
SEQADV 5HD7 ALA A   -6  UNP  P63086              EXPRESSION TAG                 
SEQADV 5HD7 HIS A   -5  UNP  P63086              EXPRESSION TAG                 
SEQADV 5HD7 HIS A   -4  UNP  P63086              EXPRESSION TAG                 
SEQADV 5HD7 HIS A   -3  UNP  P63086              EXPRESSION TAG                 
SEQADV 5HD7 HIS A   -2  UNP  P63086              EXPRESSION TAG                 
SEQADV 5HD7 HIS A   -1  UNP  P63086              EXPRESSION TAG                 
SEQADV 5HD7 HIS A    0  UNP  P63086              EXPRESSION TAG                 
SEQADV 5HD7 ASP A  167  UNP  P63086    GLY   167 ENGINEERED MUTATION            
SEQRES   1 A  365  ALA HIS HIS HIS HIS HIS HIS MET ALA ALA ALA ALA ALA          
SEQRES   2 A  365  ALA GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL          
SEQRES   3 A  365  GLY PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY          
SEQRES   4 A  365  ALA TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN          
SEQRES   5 A  365  LYS VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU          
SEQRES   6 A  365  HIS GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS          
SEQRES   7 A  365  ILE LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE          
SEQRES   8 A  365  ASN ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS          
SEQRES   9 A  365  ASP VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU          
SEQRES  10 A  365  TYR LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS          
SEQRES  11 A  365  ILE CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS          
SEQRES  12 A  365  TYR ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS          
SEQRES  13 A  365  PRO SER ASN LEU LEU LEU ASN THR THR CYS ASP LEU LYS          
SEQRES  14 A  365  ILE CYS ASP PHE ASP LEU ALA ARG VAL ALA ASP PRO ASP          
SEQRES  15 A  365  HIS ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR          
SEQRES  16 A  365  ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS          
SEQRES  17 A  365  GLY TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS          
SEQRES  18 A  365  ILE LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO          
SEQRES  19 A  365  GLY LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY          
SEQRES  20 A  365  ILE LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE          
SEQRES  21 A  365  ILE ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO          
SEQRES  22 A  365  HIS LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN          
SEQRES  23 A  365  ALA ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU          
SEQRES  24 A  365  THR PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA          
SEQRES  25 A  365  LEU ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER          
SEQRES  26 A  365  ASP GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET          
SEQRES  27 A  365  GLU LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU          
SEQRES  28 A  365  ILE PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG          
SEQRES  29 A  365  SER                                                          
HET    38Z  A 401      78                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    SO4  A 405       5                                                       
HET    SO4  A 406       5                                                       
HETNAM     38Z (3R)-1-(2-OXO-2-{4-[4-(PYRIMIDIN-2-YL)PHENYL]PIPERAZIN-          
HETNAM   2 38Z  1-YL}ETHYL)-N-[3-(PYRIDIN-4-YL)-2H-INDAZOL-5-                   
HETNAM   3 38Z  YL]PYRROLIDINE-3-CARBOXAMIDE                                    
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  38Z    C33 H33 N9 O2                                                
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   8  HOH   *274(H2 O)                                                    
HELIX    1 AA1 HIS A   59  PHE A   76  1                                  18    
HELIX    2 AA2 LEU A  110  GLN A  117  1                                   8    
HELIX    3 AA3 SER A  120  ALA A  141  1                                  22    
HELIX    4 AA4 LYS A  149  SER A  151  5                                   3    
HELIX    5 AA5 ASP A  173  ASP A  177  5                                   5    
HELIX    6 AA6 THR A  188  ARG A  192  5                                   5    
HELIX    7 AA7 ALA A  193  MET A  197  5                                   5    
HELIX    8 AA8 LYS A  205  ASN A  222  1                                  18    
HELIX    9 AA9 HIS A  230  GLY A  243  1                                  14    
HELIX   10 AB1 SER A  246  CYS A  252  1                                   7    
HELIX   11 AB2 ASN A  255  LEU A  265  1                                  11    
HELIX   12 AB3 PRO A  272  PHE A  277  1                                   6    
HELIX   13 AB4 ASP A  281  LEU A  292  1                                  12    
HELIX   14 AB5 GLU A  301  ALA A  307  1                                   7    
HELIX   15 AB6 HIS A  308  GLU A  312  5                                   5    
HELIX   16 AB7 ASP A  316  GLU A  320  5                                   5    
HELIX   17 AB8 PRO A  337  ALA A  350  1                                  14    
HELIX   18 AB9 ARG A  351  GLN A  353  5                                   3    
SHEET    1 AA1 5 TYR A  23  GLY A  32  0                                        
SHEET    2 AA1 5 GLY A  35  ASP A  42 -1  O  TYR A  41   N  THR A  24           
SHEET    3 AA1 5 VAL A  47  ILE A  54 -1  O  VAL A  49   N  ALA A  40           
SHEET    4 AA1 5 VAL A  99  ASP A 104 -1  O  GLN A 103   N  ALA A  50           
SHEET    5 AA1 5 ASP A  86  ILE A  88 -1  N  ILE A  88   O  TYR A 100           
SHEET    1 AA2 3 THR A 108  ASP A 109  0                                        
SHEET    2 AA2 3 LEU A 153  LEU A 155 -1  O  LEU A 155   N  THR A 108           
SHEET    3 AA2 3 LEU A 161  ILE A 163 -1  O  LYS A 162   N  LEU A 154           
SHEET    1 AA3 2 VAL A 143  LEU A 144  0                                        
SHEET    2 AA3 2 ARG A 170  VAL A 171 -1  O  ARG A 170   N  LEU A 144           
SITE     1 AC1 19 ALA A  33  TYR A  34  ALA A  50  LYS A  52                    
SITE     2 AC1 19 ILE A  54  TYR A  62  THR A  66  GLN A 103                    
SITE     3 AC1 19 ASP A 104  MET A 106  GLU A 107  THR A 108                    
SITE     4 AC1 19 LYS A 112  LEU A 154  ASP A 165  ASP A 167                    
SITE     5 AC1 19 HOH A 509  HOH A 537  HOH A 640                               
SITE     1 AC2  7 ARG A  68  ARG A 170  VAL A 171  ASP A 330                    
SITE     2 AC2  7 MET A 331  GLU A 332  HOH A 522                               
SITE     1 AC3  5 ARG A  75  PRO A 326  PHE A 327  LYS A 328                    
SITE     2 AC3  5 PHE A 329                                                     
SITE     1 AC4  5 ARG A 146  ARG A 170  VAL A 186  HOH A 507                    
SITE     2 AC4  5 HOH A 551                                                     
SITE     1 AC5  6 TYR A 185  ARG A 189  ARG A 192  TYR A 231                    
SITE     2 AC5  6 HOH A 563  HOH A 662                                          
SITE     1 AC6  7 ASN A 121  GLY A 180  LYS A 257  HOH A 573                    
SITE     2 AC6  7 HOH A 636  HOH A 657  HOH A 693                               
CRYST1   70.986   91.422   62.972  90.00  90.00  90.00 P 21 21 2     4          
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      0.014087  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010938  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015880        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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