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Database: PDB
Entry: 5KMN
LinkDB: 5KMN
Original site: 5KMN 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       27-JUN-16   5KMN              
TITLE     TRKA JM-KINASE WITH 1-(2-METHYL-4-PHENYL-PYRIMIDIN-5-YL)-3-[[2-       
TITLE    2 (TRIFLUOROMETHYL)PHENYL]METHYL]UREA                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HIGH AFFINITY NERVE GROWTH FACTOR RECEPTOR;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN WITH JUXTAMEMBRANE REGION, UNP RESIDUES   
COMPND   5 376-698;                                                             
COMPND   6 SYNONYM: NEUROTROPHIC TYROSINE KINASE RECEPTOR TYPE 1,TRK1-          
COMPND   7 TRANSFORMING TYROSINE KINASE PROTEIN,TROPOMYOSIN-RELATED KINASE A,   
COMPND   8 TYROSINE KINASE RECEPTOR,TYROSINE KINASE RECEPTOR A,TRK-A,GP140TRK,  
COMPND   9 P140-TRKA;                                                           
COMPND  10 EC: 2.7.10.1;                                                        
COMPND  11 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: NTRK1, MTC, TRK, TRKA;                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    KINASE, JUXTAMEMBRANE, INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR   
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.P.SU                                                                
REVDAT   3   01-FEB-17 5KMN    1       JRNL                                     
REVDAT   2   18-JAN-17 5KMN    1       JRNL                                     
REVDAT   1   28-DEC-16 5KMN    0                                                
JRNL        AUTH   H.P.SU,K.RICKERT,C.BURLEIN,K.NARAYAN,M.BUKHTIYAROVA,         
JRNL        AUTH 2 D.M.HURZY,C.A.STUMP,X.ZHANG,J.REID,A.KRASOWSKA-ZOLADEK,      
JRNL        AUTH 3 S.TUMMALA,J.M.SHIPMAN,M.KORNIENKO,P.A.LEMAIRE,D.KROSKY,      
JRNL        AUTH 4 A.HELLER,A.ACHAB,C.CHAMBERLIN,P.SARADJIAN,B.SAUVAGNAT,       
JRNL        AUTH 5 X.YANG,M.R.ZIEBELL,E.NICKBARG,J.M.SANDERS,M.T.BILODEAU,      
JRNL        AUTH 6 S.S.CARROLL,K.J.LUMB,S.M.SOISSON,D.A.HENZE,A.J.COOKE         
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF NONACTIVE SITE,               
JRNL        TITL 2 TRKA-SELECTIVE KINASE INHIBITORS.                            
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 114  E297 2017              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   28039433                                                     
JRNL        DOI    10.1073/PNAS.1611577114                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.14 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT                                           
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 20182                          
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)  : 0.195                          
REMARK   3   R VALUE            (WORKING SET)  : 0.194                          
REMARK   3   FREE R VALUE                      : 0.222                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.100                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1030                           
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               : 10                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.14                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.26                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 100.0                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2934                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2125                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2786                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2104                   
REMARK   3   BIN FREE R VALUE                        : 0.2546                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.04                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 148                      
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            : 2333                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.13                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.58580                                             
REMARK   3    B22 (A**2) : -1.58580                                             
REMARK   3    B33 (A**2) : 3.17160                                              
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) : 0.260               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.202               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.164               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.200               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.165               
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      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2419   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3277   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 820    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 49     ; 8.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 376    ; 8.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2419   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 295    ; 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   : 2768   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.01                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.21                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.19                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5KMN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000222465.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.16                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20356                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.136                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 9.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.14000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.51500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.51500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: BUSTER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES PH 6.5, 150 MM NACL, 5MM        
REMARK 280  TCEP, 0.1% BETA-OCTYLGLUCOSIDE, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 1 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -Y,-X,-Z+2/3                                            
REMARK 290       5555   -X+Y,Y,-Z+1/3                                           
REMARK 290       6555   X,X-Y,-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       76.17667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      152.35333            
REMARK 290   SMTRY1   4  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000      152.35333            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       76.17667            
REMARK 290   SMTRY1   6  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  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: 200 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 14360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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     GLU A   480                                                      
REMARK 465     GLY A   481                                                      
REMARK 465     LYS A   482                                                      
REMARK 465     GLY A   483                                                      
REMARK 465     SER A   484                                                      
REMARK 465     GLY A   485                                                      
REMARK 465     LEU A   486                                                      
REMARK 465     GLN A   487                                                      
REMARK 465     GLY A   488                                                      
REMARK 465     HIS A   489                                                      
REMARK 465     ILE A   490                                                      
REMARK 465     ILE A   491                                                      
REMARK 465     GLU A   492                                                      
REMARK 465     ASN A   493                                                      
REMARK 465     PRO A   494                                                      
REMARK 465     GLN A   495                                                      
REMARK 465     TYR A   496                                                      
REMARK 465     PHE A   497                                                      
REMARK 465     SER A   498                                                      
REMARK 465     GLU A   535                                                      
REMARK 465     GLN A   536                                                      
REMARK 465     ALA A   549                                                      
REMARK 465     LYS A   609                                                      
REMARK 465     LEU A   610                                                      
REMARK 465     LEU A   611                                                      
REMARK 465     ALA A   612                                                      
REMARK 465     GLY A   613                                                      
REMARK 465     HIS A   797                                                      
REMARK 465     HIS A   798                                                      
REMARK 465     HIS A   799                                                      
REMARK 465     HIS A   800                                                      
REMARK 465     HIS A   801                                                      
REMARK 465     HIS A   802                                                      
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     ASP A 499    CG   OD1  OD2                                       
REMARK 470     GLU A 548    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 559    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 568    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 686    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 761    CG   CD   NE   CZ   NH1  NH2                        
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    ASP A 650       48.40   -142.64                                   
REMARK 500    VAL A 683     -167.54   -129.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6UK A 901                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5KMI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KMJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KMK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KML   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KMM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KMO   RELATED DB: PDB                                   
DBREF  5KMN A  474   796  UNP    P04629   NTRK1_HUMAN    376    698             
SEQADV 5KMN ACE A    0  UNP  P04629              ACETYLATION                    
SEQADV 5KMN HIS A  797  UNP  P04629              EXPRESSION TAG                 
SEQADV 5KMN HIS A  798  UNP  P04629              EXPRESSION TAG                 
SEQADV 5KMN HIS A  799  UNP  P04629              EXPRESSION TAG                 
SEQADV 5KMN HIS A  800  UNP  P04629              EXPRESSION TAG                 
SEQADV 5KMN HIS A  801  UNP  P04629              EXPRESSION TAG                 
SEQADV 5KMN HIS A  802  UNP  P04629              EXPRESSION TAG                 
SEQRES   1 A  330  ACE SER SER LEU SER PRO THR GLU GLY LYS GLY SER GLY          
SEQRES   2 A  330  LEU GLN GLY HIS ILE ILE GLU ASN PRO GLN TYR PHE SER          
SEQRES   3 A  330  ASP ALA CYS VAL HIS HIS ILE LYS ARG ARG ASP ILE VAL          
SEQRES   4 A  330  LEU LYS TRP GLU LEU GLY GLU GLY ALA PHE GLY LYS VAL          
SEQRES   5 A  330  PHE LEU ALA GLU CYS HIS ASN LEU LEU PRO GLU GLN ASP          
SEQRES   6 A  330  LYS MET LEU VAL ALA VAL LYS ALA LEU LYS GLU ALA SER          
SEQRES   7 A  330  GLU SER ALA ARG GLN ASP PHE GLN ARG GLU ALA GLU LEU          
SEQRES   8 A  330  LEU THR MET LEU GLN HIS GLN HIS ILE VAL ARG PHE PHE          
SEQRES   9 A  330  GLY VAL CYS THR GLU GLY ARG PRO LEU LEU MET VAL PHE          
SEQRES  10 A  330  GLU TYR MET ARG HIS GLY ASP LEU ASN ARG PHE LEU ARG          
SEQRES  11 A  330  SER HIS GLY PRO ASP ALA LYS LEU LEU ALA GLY GLY GLU          
SEQRES  12 A  330  ASP VAL ALA PRO GLY PRO LEU GLY LEU GLY GLN LEU LEU          
SEQRES  13 A  330  ALA VAL ALA SER GLN VAL ALA ALA GLY MET VAL TYR LEU          
SEQRES  14 A  330  ALA GLY LEU HIS PHE VAL HIS ARG ASP LEU ALA THR ARG          
SEQRES  15 A  330  ASN CYS LEU VAL GLY GLN GLY LEU VAL VAL LYS ILE GLY          
SEQRES  16 A  330  ASP PHE GLY MET SER ARG ASP ILE TYR SER THR ASP TYR          
SEQRES  17 A  330  TYR ARG VAL GLY GLY ARG THR MET LEU PRO ILE ARG TRP          
SEQRES  18 A  330  MET PRO PRO GLU SER ILE LEU TYR ARG LYS PHE THR THR          
SEQRES  19 A  330  GLU SER ASP VAL TRP SER PHE GLY VAL VAL LEU TRP GLU          
SEQRES  20 A  330  ILE PHE THR TYR GLY LYS GLN PRO TRP TYR GLN LEU SER          
SEQRES  21 A  330  ASN THR GLU ALA ILE ASP CYS ILE THR GLN GLY ARG GLU          
SEQRES  22 A  330  LEU GLU ARG PRO ARG ALA CYS PRO PRO GLU VAL TYR ALA          
SEQRES  23 A  330  ILE MET ARG GLY CYS TRP GLN ARG GLU PRO GLN GLN ARG          
SEQRES  24 A  330  HIS SER ILE LYS ASP VAL HIS ALA ARG LEU GLN ALA LEU          
SEQRES  25 A  330  ALA GLN ALA PRO PRO VAL TYR LEU ASP VAL LEU GLY HIS          
SEQRES  26 A  330  HIS HIS HIS HIS HIS                                          
HET    ACE  A   0       3                                                       
HET    6UK  A 901      28                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     6UK 1-(2-METHYL-4-PHENYL-PYRIMIDIN-5-YL)-3-[[2-                      
HETNAM   2 6UK  (TRIFLUOROMETHYL)PHENYL]METHYL]UREA                             
FORMUL   1  ACE    C2 H4 O                                                      
FORMUL   2  6UK    C20 H17 F3 N4 O                                              
FORMUL   3  HOH   *88(H2 O)                                                     
HELIX    1 AA1 LYS A  506  ARG A  508  5                                   3    
HELIX    2 AA2 GLU A  551  LEU A  567  1                                  17    
HELIX    3 AA3 ASP A  596  HIS A  604  1                                   9    
HELIX    4 AA4 GLY A  623  LEU A  644  1                                  22    
HELIX    5 AA5 ALA A  652  ARG A  654  5                                   3    
HELIX    6 AA6 MET A  671  TYR A  676  1                                   6    
HELIX    7 AA7 SER A  677  TYR A  680  5                                   4    
HELIX    8 AA8 PRO A  690  MET A  694  5                                   5    
HELIX    9 AA9 PRO A  695  ARG A  702  1                                   8    
HELIX   10 AB1 THR A  705  THR A  722  1                                  18    
HELIX   11 AB2 SER A  732  GLY A  743  1                                  12    
HELIX   12 AB3 PRO A  753  TRP A  764  1                                  12    
HELIX   13 AB4 GLU A  767  ARG A  771  5                                   5    
HELIX   14 AB5 SER A  773  GLN A  786  1                                  14    
HELIX   15 AB6 PRO A  788  VAL A  794  1                                   7    
SHEET    1 AA1 2 LEU A 476  PRO A 478  0                                        
SHEET    2 AA1 2 PHE A 646  HIS A 648 -1  O  VAL A 647   N  SER A 477           
SHEET    1 AA2 5 ILE A 510  GLU A 518  0                                        
SHEET    2 AA2 5 GLY A 522  HIS A 530 -1  O  LEU A 526   N  LYS A 513           
SHEET    3 AA2 5 LYS A 538  LEU A 546 -1  O  ALA A 545   N  LYS A 523           
SHEET    4 AA2 5 LEU A 586  GLU A 590 -1  O  PHE A 589   N  ALA A 542           
SHEET    5 AA2 5 PHE A 575  CYS A 579 -1  N  GLY A 577   O  VAL A 588           
SHEET    1 AA3 2 CYS A 656  GLY A 659  0                                        
SHEET    2 AA3 2 VAL A 663  ILE A 666 -1  O  LYS A 665   N  LEU A 657           
SHEET    1 AA4 2 TYR A 681  ARG A 682  0                                        
SHEET    2 AA4 2 MET A 688  LEU A 689 -1  O  LEU A 689   N  TYR A 681           
LINK         C   ACE A   0                 N   SER A 474     1555   1555  1.33  
CISPEP   1 ARG A  583    PRO A  584          0        -3.01                     
SITE     1 AC1 12 ACE A   0  SER A 474  SER A 475  LEU A 476                    
SITE     2 AC1 12 LYS A 544  GLU A 560  LEU A 567  ILE A 572                    
SITE     3 AC1 12 HIS A 648  ILE A 666  ASP A 668  GLY A 670                    
CRYST1   52.150   52.150  228.530  90.00  90.00 120.00 P 31 1 2      6          
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      0.019175  0.011071  0.000000        0.00000                         
SCALE2      0.000000  0.022142  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004376        0.00000                         
HETATM    1  C   ACE A   0     -18.712  -4.237 -27.849  1.00 32.51           C  
HETATM    2  O   ACE A   0     -18.658  -4.900 -28.883  1.00 33.59           O  
HETATM    3  CH3 ACE A   0     -19.490  -4.757 -26.638  1.00 33.13           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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