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Database: PDB
Entry: 3HV6
LinkDB: 3HV6
Original site: 3HV6 
HEADER    TRANSFERASE                             15-JUN-09   3HV6              
TITLE     HUMAN P38 MAP KINASE IN COMPLEX WITH RL39                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MITOGEN-ACTIVATED PROTEIN KINASE P38 ALPHA, MAP             
COMPND   5 KINASE P38 ALPHA, CYTOKINE SUPPRESSIVE ANTI-INFLAMMATORY             
COMPND   6 DRUG-BINDING PROTEIN, CSAID-BINDING PROTEIN, CSBP, MAX-              
COMPND   7 INTERACTING PROTEIN 2, MAP KINASE MXI2, SAPK2A;                      
COMPND   8 EC: 2.7.11.24;                                                       
COMPND   9 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: MAPK14, CSBP, CSBP1, CSBP2, CSPB1, MXI2;                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX 6P-1                                 
KEYWDS    DFG-OUT, TYPE II, RL39, ALTERNATIVE SPLICING, ATP-BINDING,            
KEYWDS   2 CYTOPLASM, KINASE, NUCLEOTIDE-BINDING, NUCLEUS,                      
KEYWDS   3 PHOSPHOPROTEIN, POLYMORPHISM, SERINE/THREONINE-PROTEIN               
KEYWDS   4 KINASE, TRANSFERASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.GRUETTER,J.R.SIMARD,M.GETLIK,D.RAUH                                 
REVDAT   2   16-FEB-10 3HV6    1       JRNL                                     
REVDAT   1   17-NOV-09 3HV6    0                                                
JRNL        AUTH   S.KLUTER,C.GRUTTER,T.NAQVI,M.RABILLER,J.R.SIMARD,            
JRNL        AUTH 2 V.PAWAR,M.GETLIK,D.RAUH                                      
JRNL        TITL   DISPLACEMENT ASSAY FOR THE DETECTION OF STABILIZERS          
JRNL        TITL 2 OF INACTIVE KINASE CONFORMATIONS.                            
JRNL        REF    J.MED.CHEM.                   V.  53   357 2010              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   19928858                                                     
JRNL        DOI    10.1021/JM901297E                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 28963                          
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) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 869                             
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2046                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2550                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 63                           
REMARK   3   BIN FREE R VALUE                    : 0.3300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2668                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 177                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.44                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.58000                                             
REMARK   3    B33 (A**2) : 0.59000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.173         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.161         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.115         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.912         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2801 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3802 ; 1.503 ; 1.995       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   327 ; 5.718 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   128 ;37.973 ;23.906       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   472 ;16.359 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;20.886 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   432 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2079 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1307 ; 0.213 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1909 ; 0.311 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   203 ; 0.171 ; 0.200       
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):    26 ; 0.210 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.194 ; 0.200       
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):  1713 ; 1.110 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2686 ; 1.736 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1247 ; 2.487 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1116 ; 3.791 ; 4.500       
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3HV6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053621.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUL-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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 MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54170                            
REMARK 200  MONOCHROMATOR                  : MULTILAYER OPTIK                   
REMARK 200  OPTICS                         : OSMIC                              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28964                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.660                              
REMARK 200  R MERGE                    (I) : 0.03300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.3900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.57                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1ZYJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 20-30% PEG4000, 50 MM N      
REMARK 280  -BOG, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K       
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       33.20500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.17500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.33000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.17500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.20500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.33000            
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 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     GLY A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     TYR A    35                                                      
REMARK 465     GLY A    36                                                      
REMARK 465     CYS A   119                                                      
REMARK 465     GLN A   120                                                      
REMARK 465     LEU A   171                                                      
REMARK 465     ALA A   172                                                      
REMARK 465     ARG A   173                                                      
REMARK 465     HIS A   174                                                      
REMARK 465     THR A   175                                                      
REMARK 465     ASP A   176                                                      
REMARK 465     ASP A   177                                                      
REMARK 465     GLU A   178                                                      
REMARK 465     MET A   179                                                      
REMARK 465     THR A   180                                                      
REMARK 465     GLY A   181                                                      
REMARK 465     TYR A   182                                                      
REMARK 465     LEU A   353                                                      
REMARK 465     ASP A   354                                                      
REMARK 465     GLN A   355                                                      
REMARK 465     GLU A   356                                                      
REMARK 465     GLU A   357                                                      
REMARK 465     MET A   358                                                      
REMARK 465     GLU A   359                                                      
REMARK 465     SER A   360                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A   4    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 118    CG   CD   CE   NZ                                   
REMARK 470     LYS A 121    CG   CD   CE   NZ                                   
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    LYS A  15       -8.03     79.90                                   
REMARK 500    ARG A  23      -39.11    -33.80                                   
REMARK 500    VAL A  30      -54.64   -126.27                                   
REMARK 500    ARG A 149      -16.11     84.50                                   
REMARK 500    PHE A 274       52.74   -109.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     BOG A  362                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE R39 A 361                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 362                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3GCP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3GCQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3GCS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3GCU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3GCV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HV4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HV3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HV5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HV7   RELATED DB: PDB                                   
DBREF  3HV6 A    2   360  UNP    Q16539   MK14_HUMAN       2    360             
SEQADV 3HV6 GLY A    1  UNP  Q16539              EXPRESSION TAG                 
SEQRES   1 A  360  GLY SER GLN GLU ARG PRO THR PHE TYR ARG GLN GLU LEU          
SEQRES   2 A  360  ASN LYS THR ILE TRP GLU VAL PRO GLU ARG TYR GLN ASN          
SEQRES   3 A  360  LEU SER PRO VAL GLY SER GLY ALA TYR GLY SER VAL CYS          
SEQRES   4 A  360  ALA ALA PHE ASP THR LYS THR GLY LEU ARG VAL ALA VAL          
SEQRES   5 A  360  LYS LYS LEU SER ARG PRO PHE GLN SER ILE ILE HIS ALA          
SEQRES   6 A  360  LYS ARG THR TYR ARG GLU LEU ARG LEU LEU LYS HIS MET          
SEQRES   7 A  360  LYS HIS GLU ASN VAL ILE GLY LEU LEU ASP VAL PHE THR          
SEQRES   8 A  360  PRO ALA ARG SER LEU GLU GLU PHE ASN ASP VAL TYR LEU          
SEQRES   9 A  360  VAL THR HIS LEU MET GLY ALA ASP LEU ASN ASN ILE VAL          
SEQRES  10 A  360  LYS CYS GLN LYS LEU THR ASP ASP HIS VAL GLN PHE LEU          
SEQRES  11 A  360  ILE TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE HIS SER          
SEQRES  12 A  360  ALA ASP ILE ILE HIS ARG ASP LEU LYS PRO SER ASN LEU          
SEQRES  13 A  360  ALA VAL ASN GLU ASP CYS GLU LEU LYS ILE LEU ASP PHE          
SEQRES  14 A  360  GLY LEU ALA ARG HIS THR ASP ASP GLU MET THR GLY TYR          
SEQRES  15 A  360  VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET LEU          
SEQRES  16 A  360  ASN TRP MET HIS TYR ASN GLN THR VAL ASP ILE TRP SER          
SEQRES  17 A  360  VAL GLY CYS ILE MET ALA GLU LEU LEU THR GLY ARG THR          
SEQRES  18 A  360  LEU PHE PRO GLY THR ASP HIS ILE ASP GLN LEU LYS LEU          
SEQRES  19 A  360  ILE LEU ARG LEU VAL GLY THR PRO GLY ALA GLU LEU LEU          
SEQRES  20 A  360  LYS LYS ILE SER SER GLU SER ALA ARG ASN TYR ILE GLN          
SEQRES  21 A  360  SER LEU THR GLN MET PRO LYS MET ASN PHE ALA ASN VAL          
SEQRES  22 A  360  PHE ILE GLY ALA ASN PRO LEU ALA VAL ASP LEU LEU GLU          
SEQRES  23 A  360  LYS MET LEU VAL LEU ASP SER ASP LYS ARG ILE THR ALA          
SEQRES  24 A  360  ALA GLN ALA LEU ALA HIS ALA TYR PHE ALA GLN TYR HIS          
SEQRES  25 A  360  ASP PRO ASP ASP GLU PRO VAL ALA ASP PRO TYR ASP GLN          
SEQRES  26 A  360  SER PHE GLU SER ARG ASP LEU LEU ILE ASP GLU TRP LYS          
SEQRES  27 A  360  SER LEU THR TYR ASP GLU VAL ILE SER PHE VAL PRO PRO          
SEQRES  28 A  360  PRO LEU ASP GLN GLU GLU MET GLU SER                          
HET    BOG  A1000      20                                                       
HET    R39  A 361      35                                                       
HET    BOG  A 362      15                                                       
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     R39 1-[3-TERT-BUTYL-1-(4-METHYLPHENYL)-1H-PYRAZOL-5-YL]-3-           
HETNAM   2 R39  [4-(2-MORPHOLIN-4-YLETHOXY)PHENYL]UREA                          
HETSYN     R39 1-(3-TERT-BUTYL-1-P-TOLYL-1H-PYRAZOL-5-YL)-3-(4-(2-              
HETSYN   2 R39  MORPHOLINOETHOXY)PHENYL)UREA                                    
FORMUL   2  BOG    2(C14 H28 O6)                                                
FORMUL   3  R39    C27 H35 N5 O3                                                
FORMUL   5  HOH   *177(H2 O)                                                    
HELIX    1   1 SER A   61  MET A   78  1                                  18    
HELIX    2   2 SER A   95  PHE A   99  5                                   5    
HELIX    3   3 ASN A  114  ILE A  116  5                                   3    
HELIX    4   4 THR A  123  ALA A  144  1                                  22    
HELIX    5   5 LYS A  152  SER A  154  5                                   3    
HELIX    6   6 ALA A  184  ARG A  189  5                                   6    
HELIX    7   7 ALA A  190  LEU A  195  1                                   6    
HELIX    8   8 THR A  203  GLY A  219  1                                  17    
HELIX    9   9 ASP A  227  GLY A  240  1                                  14    
HELIX   10  10 GLY A  243  LYS A  248  1                                   6    
HELIX   11  11 SER A  252  SER A  261  1                                  10    
HELIX   12  12 ASN A  269  PHE A  274  1                                   6    
HELIX   13  13 ASN A  278  LEU A  289  1                                  12    
HELIX   14  14 ASP A  292  ARG A  296  5                                   5    
HELIX   15  15 THR A  298  ALA A  304  1                                   7    
HELIX   16  16 HIS A  305  ALA A  309  5                                   5    
HELIX   17  17 ASP A  313  GLU A  317  5                                   5    
HELIX   18  18 GLN A  325  ARG A  330  5                                   6    
HELIX   19  19 LEU A  333  SER A  347  1                                  15    
SHEET    1   A 2 PHE A   8  LEU A  13  0                                        
SHEET    2   A 2 THR A  16  PRO A  21 -1  O  THR A  16   N  LEU A  13           
SHEET    1   B 5 TYR A  24  GLY A  31  0                                        
SHEET    2   B 5 VAL A  38  ASP A  43 -1  O  PHE A  42   N  GLN A  25           
SHEET    3   B 5 ARG A  49  LYS A  54 -1  O  VAL A  52   N  CYS A  39           
SHEET    4   B 5 TYR A 103  HIS A 107 -1  O  THR A 106   N  ALA A  51           
SHEET    5   B 5 ASP A  88  PHE A  90 -1  N  ASP A  88   O  VAL A 105           
SHEET    1   C 3 ALA A 111  ASP A 112  0                                        
SHEET    2   C 3 LEU A 156  VAL A 158 -1  O  VAL A 158   N  ALA A 111           
SHEET    3   C 3 LEU A 164  ILE A 166 -1  O  LYS A 165   N  ALA A 157           
SITE     1 AC1 14 GLU A 192  TRP A 197  HIS A 199  TYR A 200                    
SITE     2 AC1 14 ASN A 201  LEU A 246  LYS A 249  LEU A 291                    
SITE     3 AC1 14 ASP A 292  SER A 293  ASP A 294  HOH A 415                    
SITE     4 AC1 14 HOH A 437  HOH A 454                                          
SITE     1 AC2 11 ARG A  67  GLU A  71  LEU A  74  MET A  78                    
SITE     2 AC2 11 ILE A  84  HIS A 107  MET A 109  LEU A 167                    
SITE     3 AC2 11 ASP A 168  PHE A 169  HOH A 413                               
SITE     1 AC3  7 LEU A 195  ASN A 196  TRP A 197  MET A 198                    
SITE     2 AC3  7 SER A 251  SER A 252  HOH A 457                               
CRYST1   66.410   74.660   78.350  90.00  90.00  90.00 P 21 21 21    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      0.015058  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013394  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012763        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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