GenomeNet

Database: PDB
Entry: 2LGC
LinkDB: 2LGC
Original site: 2LGC 
HEADER    TRANSFERASE                             25-JUL-11   2LGC              
TITLE     JOINT NMR AND X-RAY REFINEMENT REVEALS THE STRUCTURE OF A NOVEL       
TITLE    2 DIBENZO[A,D]CYCLOHEPTENONE INHIBITOR/P38 MAP KINASE COMPLEX IN       
TITLE    3 SOLUTION                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MAP KINASE 14, MAPK 14, CYTOKINE SUPPRESSIVE ANTI-          
COMPND   5 INFLAMMATORY DRUG-BINDING PROTEIN, CSAID-BINDING PROTEIN, CSBP, MAP  
COMPND   6 KINASE MXI2, MAX-INTERACTING PROTEIN 2, MITOGEN-ACTIVATED PROTEIN    
COMPND   7 KINASE P38 ALPHA, MAP KINASE P38 ALPHA, 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_VECTOR: PET                                        
KEYWDS    P38 MAPK KINASE-INHIBITOR COMPLEX, HYBRID NMR/X-RAY STRUCTURE,        
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    SOLUTION NMR                                                          
NUMMDL    10                                                                    
AUTHOR    M.HABECK                                                              
REVDAT   1   25-JUL-12 2LGC    0                                                
JRNL        AUTH   V.S.HONNDORF,N.COUDEVYLLE,S.LAUFER,S.BECKER,C.GRIESINGER,    
JRNL        AUTH 2 M.HABECK                                                     
JRNL        TITL   INFERENTIAL NMR/X-RAY-BASED STRUCTURE DETERMINATION OF A     
JRNL        TITL 2 DIBENZO[A,D]CYCLOHEPTENONE INHIBITOR-P38ALPHA MAP KINASE     
JRNL        TITL 3 COMPLEX IN SOLUTION                                          
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  51  2359 2012              
JRNL        REFN                   ISSN 1433-7851                               
JRNL        PMID   22275118                                                     
JRNL        DOI    10.1002/ANIE.201105241                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : ISD                                                  
REMARK   3   AUTHORS     : HABECK, RIEPING, LAMAZHAPOVA                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: JOINT NMR AND X-RAY REFINEMENT WITH NMR   
REMARK   3  RESTRAINTS AND X-RAY REFLECTIONS FROM PDB ENTRY 3ZYA.               
REMARK   4                                                                      
REMARK   4 2LGC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB102358.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 25                                 
REMARK 210  PH                             : 7.4                                
REMARK 210  IONIC STRENGTH                 : 150                                
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 1 MM [U-13C; U-15N; U-2H] P38,     
REMARK 210                                   90% H2O/10% D2O                    
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D 1H-15N HSQC; 3D HNCO            
REMARK 210  SPECTROMETER FIELD STRENGTH    : 900 MHZ                            
REMARK 210  SPECTROMETER MODEL             : DRX                                
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : PALES, NMRPIPE, SPARKY             
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS, SAMPLING   
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 3000                               
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 10                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : LOWEST R-FREE                      
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
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 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500  1 LYS A  15   CA    LYS A  15   CB     -0.237                       
REMARK 500  1 LYS A  53   CB    LYS A  53   CG     -0.163                       
REMARK 500  1 SER A 339   CA    SER A 339   CB      0.117                       
REMARK 500  2 LYS A  15   CA    LYS A  15   CB     -0.238                       
REMARK 500  2 LYS A  53   CB    LYS A  53   CG     -0.163                       
REMARK 500  2 SER A 339   CA    SER A 339   CB      0.118                       
REMARK 500  3 LYS A  15   CA    LYS A  15   CB     -0.237                       
REMARK 500  3 LYS A  53   CB    LYS A  53   CG     -0.163                       
REMARK 500  3 SER A 339   CA    SER A 339   CB      0.118                       
REMARK 500  4 LYS A  15   CA    LYS A  15   CB     -0.239                       
REMARK 500  4 LYS A  53   CB    LYS A  53   CG     -0.163                       
REMARK 500  4 SER A 339   CA    SER A 339   CB      0.118                       
REMARK 500  5 LYS A  15   CA    LYS A  15   CB     -0.237                       
REMARK 500  5 LYS A  53   CB    LYS A  53   CG     -0.163                       
REMARK 500  5 SER A 339   CA    SER A 339   CB      0.117                       
REMARK 500  6 LYS A  15   CA    LYS A  15   CB     -0.238                       
REMARK 500  6 LYS A  53   CB    LYS A  53   CG     -0.163                       
REMARK 500  6 SER A 339   CA    SER A 339   CB      0.118                       
REMARK 500  7 LYS A  15   CA    LYS A  15   CB     -0.238                       
REMARK 500  7 LYS A  53   CB    LYS A  53   CG     -0.163                       
REMARK 500  7 SER A 339   CA    SER A 339   CB      0.117                       
REMARK 500  8 LYS A  15   CA    LYS A  15   CB     -0.238                       
REMARK 500  8 LYS A  53   CB    LYS A  53   CG     -0.163                       
REMARK 500  8 SER A 339   CA    SER A 339   CB      0.118                       
REMARK 500  9 LYS A  15   CA    LYS A  15   CB     -0.237                       
REMARK 500  9 LYS A  53   CB    LYS A  53   CG     -0.162                       
REMARK 500  9 SER A 339   CA    SER A 339   CB      0.117                       
REMARK 500 10 LYS A  15   CA    LYS A  15   CB     -0.237                       
REMARK 500 10 LYS A  53   CB    LYS A  53   CG     -0.164                       
REMARK 500 10 SER A 339   CA    SER A 339   CB      0.118                       
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  1 ARG A  10   CG  -  CD  -  NE  ANGL. DEV. = -13.2 DEGREES          
REMARK 500  1 ARG A  10   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500  1 ARG A  10   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500  1 LYS A  15   N   -  CA  -  CB  ANGL. DEV. =  14.2 DEGREES          
REMARK 500  1 LYS A  15   CA  -  CB  -  CG  ANGL. DEV. = -15.0 DEGREES          
REMARK 500  1 LEU A  74   CB  -  CG  -  CD2 ANGL. DEV. = -12.4 DEGREES          
REMARK 500  1 LEU A 138   CB  -  CG  -  CD1 ANGL. DEV. =  10.6 DEGREES          
REMARK 500  1 ASP A 150   CB  -  CA  -  C   ANGL. DEV. =  12.5 DEGREES          
REMARK 500  1 ASP A 150   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500  1 LEU A 167   CB  -  CG  -  CD2 ANGL. DEV. = -11.5 DEGREES          
REMARK 500  1 LEU A 289   CB  -  CG  -  CD1 ANGL. DEV. =  11.8 DEGREES          
REMARK 500  1 SER A 339   N   -  CA  -  CB  ANGL. DEV. =  12.2 DEGREES          
REMARK 500  2 ARG A  10   CG  -  CD  -  NE  ANGL. DEV. = -13.3 DEGREES          
REMARK 500  2 ARG A  10   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500  2 ARG A  10   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500  2 LYS A  15   N   -  CA  -  CB  ANGL. DEV. =  14.2 DEGREES          
REMARK 500  2 LYS A  15   CA  -  CB  -  CG  ANGL. DEV. = -15.0 DEGREES          
REMARK 500  2 LEU A  74   CB  -  CG  -  CD2 ANGL. DEV. = -12.4 DEGREES          
REMARK 500  2 LEU A 138   CB  -  CG  -  CD1 ANGL. DEV. =  10.6 DEGREES          
REMARK 500  2 ASP A 150   CB  -  CA  -  C   ANGL. DEV. =  12.5 DEGREES          
REMARK 500  2 ASP A 150   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500  2 LEU A 167   CB  -  CG  -  CD2 ANGL. DEV. = -11.5 DEGREES          
REMARK 500  2 LEU A 289   CB  -  CG  -  CD1 ANGL. DEV. =  11.8 DEGREES          
REMARK 500  2 SER A 339   N   -  CA  -  CB  ANGL. DEV. =  12.3 DEGREES          
REMARK 500  3 ARG A  10   CG  -  CD  -  NE  ANGL. DEV. = -13.3 DEGREES          
REMARK 500  3 ARG A  10   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500  3 ARG A  10   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500  3 LYS A  15   N   -  CA  -  CB  ANGL. DEV. =  14.2 DEGREES          
REMARK 500  3 LYS A  15   CA  -  CB  -  CG  ANGL. DEV. = -15.0 DEGREES          
REMARK 500  3 LEU A  74   CB  -  CG  -  CD2 ANGL. DEV. = -12.3 DEGREES          
REMARK 500  3 LEU A 138   CB  -  CG  -  CD1 ANGL. DEV. =  10.6 DEGREES          
REMARK 500  3 ASP A 150   CB  -  CA  -  C   ANGL. DEV. =  12.5 DEGREES          
REMARK 500  3 ASP A 150   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500  3 LEU A 167   CB  -  CG  -  CD2 ANGL. DEV. = -11.5 DEGREES          
REMARK 500  3 LEU A 289   CB  -  CG  -  CD1 ANGL. DEV. =  11.8 DEGREES          
REMARK 500  3 SER A 339   N   -  CA  -  CB  ANGL. DEV. =  12.3 DEGREES          
REMARK 500  4 ARG A  10   CG  -  CD  -  NE  ANGL. DEV. = -13.2 DEGREES          
REMARK 500  4 ARG A  10   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500  4 ARG A  10   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500  4 LYS A  15   N   -  CA  -  CB  ANGL. DEV. =  14.2 DEGREES          
REMARK 500  4 LYS A  15   CA  -  CB  -  CG  ANGL. DEV. = -15.0 DEGREES          
REMARK 500  4 LEU A  74   CB  -  CG  -  CD2 ANGL. DEV. = -12.3 DEGREES          
REMARK 500  4 LEU A 138   CB  -  CG  -  CD1 ANGL. DEV. =  10.6 DEGREES          
REMARK 500  4 ASP A 150   CB  -  CA  -  C   ANGL. DEV. =  12.5 DEGREES          
REMARK 500  4 ASP A 150   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500  4 LEU A 167   CB  -  CG  -  CD2 ANGL. DEV. = -11.5 DEGREES          
REMARK 500  4 LEU A 289   CB  -  CG  -  CD1 ANGL. DEV. =  11.8 DEGREES          
REMARK 500  4 SER A 339   N   -  CA  -  CB  ANGL. DEV. =  12.3 DEGREES          
REMARK 500  5 ARG A  10   CG  -  CD  -  NE  ANGL. DEV. = -13.2 DEGREES          
REMARK 500  5 ARG A  10   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     120 ANGLE DEVIATIONS.                             
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  1 GLU A  22        1.96    -68.36                                   
REMARK 500  1 ASN A  26       54.16     71.12                                   
REMARK 500  1 TYR A  35     -130.44    -95.11                                   
REMARK 500  1 ARG A  57       30.48   -143.24                                   
REMARK 500  1 ASN A 100      -61.13   -141.55                                   
REMARK 500  1 ARG A 149      -21.43     83.93                                   
REMARK 500  1 ASP A 150      -89.74   -107.76                                   
REMARK 500  1 LEU A 151      106.83     62.77                                   
REMARK 500  1 ASP A 168       71.25     60.42                                   
REMARK 500  1 ARG A 173       54.40   -143.17                                   
REMARK 500  1 HIS A 174     -164.25     77.16                                   
REMARK 500  1 ASP A 176     -109.42   -144.59                                   
REMARK 500  1 ASP A 177     -118.21     65.27                                   
REMARK 500  1 VAL A 183     -176.74     50.30                                   
REMARK 500  1 ASN A 196       74.64     31.82                                   
REMARK 500  1 MET A 198     -140.80   -110.11                                   
REMARK 500  1 TYR A 200      177.58     47.75                                   
REMARK 500  1 ASP A 313      101.10   -161.88                                   
REMARK 500  1 ASP A 316       58.96   -119.05                                   
REMARK 500  1 GLU A 317       71.57   -153.88                                   
REMARK 500  1 ILE A 334      -72.36    -56.85                                   
REMARK 500  1 ASP A 335        3.23    -55.39                                   
REMARK 500  2 GLU A  22        4.14    -68.94                                   
REMARK 500  2 ASN A  26       52.23     71.93                                   
REMARK 500  2 TYR A  35     -128.93    -99.40                                   
REMARK 500  2 ARG A  57       27.81   -147.32                                   
REMARK 500  2 ASN A 100      -62.41   -140.13                                   
REMARK 500  2 ARG A 149      -18.24     77.54                                   
REMARK 500  2 ASP A 150      -90.18   -113.07                                   
REMARK 500  2 LEU A 151      110.43     65.17                                   
REMARK 500  2 ASP A 168       77.21     54.51                                   
REMARK 500  2 HIS A 174     -177.86     55.41                                   
REMARK 500  2 ASP A 176     -126.89   -168.25                                   
REMARK 500  2 ASP A 177     -100.96     76.76                                   
REMARK 500  2 VAL A 183      179.59     63.76                                   
REMARK 500  2 ASN A 196       67.97     32.63                                   
REMARK 500  2 MET A 198     -144.71   -110.90                                   
REMARK 500  2 TYR A 200      170.55     50.72                                   
REMARK 500  2 ASN A 201     -163.36   -128.15                                   
REMARK 500  2 ASP A 227     -178.02   -172.77                                   
REMARK 500  2 PHE A 274       75.28   -100.58                                   
REMARK 500  2 GLU A 317       70.24   -150.54                                   
REMARK 500  2 ILE A 334      -71.59    -47.28                                   
REMARK 500  2 ASP A 335        3.81    -56.71                                   
REMARK 500  3 SER A   2      175.05    168.59                                   
REMARK 500  3 GLU A  22        2.83    -69.66                                   
REMARK 500  3 ASN A  26       48.52     76.77                                   
REMARK 500  3 TYR A  35     -125.02    -85.84                                   
REMARK 500  3 ARG A  57       28.72   -141.52                                   
REMARK 500  3 ASN A 100      -61.49   -142.93                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     234 RAMACHANDRAN OUTLIERS.                        
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  1 LYS A  15        23.1      L          L   OUTSIDE RANGE           
REMARK 500  2 LYS A  15        23.1      L          L   OUTSIDE RANGE           
REMARK 500  3 LYS A  15        23.0      L          L   OUTSIDE RANGE           
REMARK 500  4 LYS A  15        23.1      L          L   OUTSIDE RANGE           
REMARK 500  5 LYS A  15        23.1      L          L   OUTSIDE RANGE           
REMARK 500  6 LYS A  15        23.1      L          L   OUTSIDE RANGE           
REMARK 500  7 LYS A  15        23.0      L          L   OUTSIDE RANGE           
REMARK 500  8 LYS A  15        23.1      L          L   OUTSIDE RANGE           
REMARK 500  9 LYS A  15        23.1      L          L   OUTSIDE RANGE           
REMARK 500 10 LYS A  15        23.1      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6468   RELATED DB: BMRB                                  
DBREF  2LGC A    2   354  UNP    Q16539   MK14_HUMAN       2    354             
SEQADV 2LGC SER A   -4  UNP  Q16539              EXPRESSION TAG                 
SEQADV 2LGC HIS A   -3  UNP  Q16539              EXPRESSION TAG                 
SEQADV 2LGC MET A   -2  UNP  Q16539              EXPRESSION TAG                 
SEQADV 2LGC LEU A   -1  UNP  Q16539              EXPRESSION TAG                 
SEQADV 2LGC GLU A    0  UNP  Q16539              EXPRESSION TAG                 
SEQADV 2LGC MET A    1  UNP  Q16539              EXPRESSION TAG                 
SEQRES   1 A  359  SER HIS MET LEU GLU MET SER GLN GLU ARG PRO THR PHE          
SEQRES   2 A  359  TYR ARG GLN GLU LEU ASN LYS THR ILE TRP GLU VAL PRO          
SEQRES   3 A  359  GLU ARG TYR GLN ASN LEU SER PRO VAL GLY SER GLY ALA          
SEQRES   4 A  359  TYR GLY SER VAL CYS ALA ALA PHE ASP THR LYS THR GLY          
SEQRES   5 A  359  LEU ARG VAL ALA VAL LYS LYS LEU SER ARG PRO PHE GLN          
SEQRES   6 A  359  SER ILE ILE HIS ALA LYS ARG THR TYR ARG GLU LEU ARG          
SEQRES   7 A  359  LEU LEU LYS HIS MET LYS HIS GLU ASN VAL ILE GLY LEU          
SEQRES   8 A  359  LEU ASP VAL PHE THR PRO ALA ARG SER LEU GLU GLU PHE          
SEQRES   9 A  359  ASN ASP VAL TYR LEU VAL THR HIS LEU MET GLY ALA ASP          
SEQRES  10 A  359  LEU ASN ASN ILE VAL LYS CYS GLN LYS LEU THR ASP ASP          
SEQRES  11 A  359  HIS VAL GLN PHE LEU ILE TYR GLN ILE LEU ARG GLY LEU          
SEQRES  12 A  359  LYS TYR ILE HIS SER ALA ASP ILE ILE HIS ARG ASP LEU          
SEQRES  13 A  359  LYS PRO SER ASN LEU ALA VAL ASN GLU ASP CYS GLU LEU          
SEQRES  14 A  359  LYS ILE LEU ASP PHE GLY LEU ALA ARG HIS THR ASP ASP          
SEQRES  15 A  359  GLU MET THR GLY TYR VAL ALA THR ARG TRP TYR ARG ALA          
SEQRES  16 A  359  PRO GLU ILE MET LEU ASN TRP MET HIS TYR ASN GLN THR          
SEQRES  17 A  359  VAL ASP ILE TRP SER VAL GLY CYS ILE MET ALA GLU LEU          
SEQRES  18 A  359  LEU THR GLY ARG THR LEU PHE PRO GLY THR ASP HIS ILE          
SEQRES  19 A  359  ASP GLN LEU LYS LEU ILE LEU ARG LEU VAL GLY THR PRO          
SEQRES  20 A  359  GLY ALA GLU LEU LEU LYS LYS ILE SER SER GLU SER ALA          
SEQRES  21 A  359  ARG ASN TYR ILE GLN SER LEU THR GLN MET PRO LYS MET          
SEQRES  22 A  359  ASN PHE ALA ASN VAL PHE ILE GLY ALA ASN PRO LEU ALA          
SEQRES  23 A  359  VAL ASP LEU LEU GLU LYS MET LEU VAL LEU ASP SER ASP          
SEQRES  24 A  359  LYS ARG ILE THR ALA ALA GLN ALA LEU ALA HIS ALA TYR          
SEQRES  25 A  359  PHE ALA GLN TYR HIS ASP PRO ASP ASP GLU PRO VAL ALA          
SEQRES  26 A  359  ASP PRO TYR ASP GLN SER PHE GLU SER ARG ASP LEU LEU          
SEQRES  27 A  359  ILE ASP GLU TRP LYS SER LEU THR TYR ASP GLU VAL ILE          
SEQRES  28 A  359  SER PHE VAL PRO PRO PRO LEU ASP                              
HELIX    1   1 GLY A   31  ALA A   34  5                                   4    
HELIX    2   2 SER A   61  MET A   78  1                                  18    
HELIX    3   3 SER A   95  PHE A   99  5                                   5    
HELIX    4   4 LEU A  113  CYS A  119  1                                   7    
HELIX    5   5 THR A  123  ALA A  144  1                                  22    
HELIX    6   6 LYS A  152  SER A  154  5                                   3    
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  249  1                                   7    
HELIX   11  11 GLU A  253  LEU A  262  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  VAL A  20   N  TYR A   9           
SHEET    1   B 5 TYR A  24  PRO A  29  0                                        
SHEET    2   B 5 SER A  37  ASP A  43 -1  O  ALA A  40   N  SER A  28           
SHEET    3   B 5 LEU A  48  LEU A  55 -1  O  VAL A  52   N  CYS A  39           
SHEET    4   B 5 VAL A 102  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           
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system