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Database: PDB
Entry: 6NJA
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Original site: 6NJA 
HEADER    TRANSFERASE                             02-JAN-19   6NJA              
TITLE     STRUCTURE OF WT RET PROTEIN TYROSINE KINASE DOMAIN AT 1.92A           
TITLE    2 RESOLUTION.                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE RECEPTOR RET;       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CADHERIN FAMILY MEMBER 12,PROTO-ONCOGENE C-RET;             
COMPND   5 EC: 2.7.10.1;                                                        
COMPND   6 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: RET, CDHF12, CDHR16, PTC, RET51;                               
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PBACPAK6                                  
KEYWDS    TRANSFERASE, ONCOGENE, RET, TYROSINE KINASE, ATP-BINDING, THYROID     
KEYWDS   2 CANCER, NON-SMALL CELL LUNG CANCER                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.S.TERZYAN,T.SHEN,J.WU,B.H.M.MOOERS                                  
REVDAT   3   18-DEC-19 6NJA    1       REMARK                                   
REVDAT   2   17-JUL-19 6NJA    1       JRNL                                     
REVDAT   1   05-JUN-19 6NJA    0                                                
JRNL        AUTH   S.S.TERZYAN,T.SHEN,X.LIU,Q.HUANG,P.TENG,M.ZHOU,F.HILBERG,    
JRNL        AUTH 2 J.CAI,B.H.M.MOOERS,J.WU                                      
JRNL        TITL   STRUCTURAL BASIS OF RESISTANCE OF MUTANT RET                 
JRNL        TITL 2 PROTEIN-TYROSINE KINASE TO ITS INHIBITORS NINTEDANIB AND     
JRNL        TITL 3 VANDETANIB.                                                  
JRNL        REF    J.BIOL.CHEM.                  V. 294 10428 2019              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   31118272                                                     
JRNL        DOI    10.1074/JBC.RA119.007682                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.92 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0238                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.92                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 28780                          
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1441                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.92                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.97                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2025                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.67                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 83                           
REMARK   3   BIN FREE R VALUE                    : 0.3940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2376                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 163                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.71                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.40000                                              
REMARK   3    B22 (A**2) : 0.92000                                              
REMARK   3    B33 (A**2) : -1.44000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.58000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.138         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.144         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.111         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2518 ; 0.007 ; 0.012       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3407 ; 1.490 ; 1.638       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   310 ; 5.617 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   130 ;28.886 ;21.077       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   470 ;15.656 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;23.327 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   304 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1926 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1216 ; 3.090 ; 3.798       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1531 ; 4.483 ; 5.683       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1302 ; 4.322 ; 4.312       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3925 ; 8.888 ;52.255       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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: NULL                                      
REMARK   4                                                                      
REMARK   4 6NJA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000238832.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAY-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : SI (111) DOUBLE CRYSTAL            
REMARK 200  OPTICS                         : FLAT BENT COLLIMATING RH COATED    
REMARK 200                                   MIRROR, TOROIDAL FOCUSSING MIRROR  
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28781                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.920                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.04100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.3200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: FFT                                                   
REMARK 200 STARTING MODEL: 2IVT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: TRANSPARANT SMALL RECTANGLE PRIZMS                           
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2-2.6M NA FORMATE, 0.1M NA CITRATE     
REMARK 280  PH5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       35.85150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.40800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       35.85150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       35.40800            
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 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   823                                                      
REMARK 465     PRO A   824                                                      
REMARK 465     GLY A   825                                                      
REMARK 465     TYR A   826                                                      
REMARK 465     LEU A   827                                                      
REMARK 465     GLY A   828                                                      
REMARK 465     SER A   829                                                      
REMARK 465     GLY A   830                                                      
REMARK 465     GLY A   831                                                      
REMARK 465     SER A   832                                                      
REMARK 465     ARG A   833                                                      
REMARK 465     ASN A   834                                                      
REMARK 465     SER A   835                                                      
REMARK 465     SER A   836                                                      
REMARK 465     SER A   837                                                      
REMARK 465     LEU A   838                                                      
REMARK 465     ASP A   839                                                      
REMARK 465     HIS A   840                                                      
REMARK 465     PRO A   841                                                      
REMARK 465     ASP A   842                                                      
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 843    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NZ   LYS A   710     O    HOH A  1201              1.94            
REMARK 500   NH2  ARG A   770     O    HOH A  1202              2.07            
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    ARG A 873      -25.42     82.54                                   
REMARK 500    ASP A 892       76.10     65.42                                   
REMARK 500    ASP A 892       76.10     57.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1363        DISTANCE =  6.15 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADE A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1103                
DBREF  6NJA A  705  1013  UNP    P07949   RET_HUMAN      705   1013             
SEQADV 6NJA GLY A  700  UNP  P07949              EXPRESSION TAG                 
SEQADV 6NJA PRO A  701  UNP  P07949              EXPRESSION TAG                 
SEQADV 6NJA LEU A  702  UNP  P07949              EXPRESSION TAG                 
SEQADV 6NJA SER A  703  UNP  P07949              EXPRESSION TAG                 
SEQADV 6NJA LEU A  704  UNP  P07949              EXPRESSION TAG                 
SEQRES   1 A  314  GLY PRO LEU SER LEU SER VAL ASP ALA PHE LYS ILE LEU          
SEQRES   2 A  314  GLU ASP PRO LYS TRP GLU PHE PRO ARG LYS ASN LEU VAL          
SEQRES   3 A  314  LEU GLY LYS THR LEU GLY GLU GLY GLU PHE GLY LYS VAL          
SEQRES   4 A  314  VAL LYS ALA THR ALA PHE HIS LEU LYS GLY ARG ALA GLY          
SEQRES   5 A  314  TYR THR THR VAL ALA VAL LYS MET LEU LYS GLU ASN ALA          
SEQRES   6 A  314  SER PRO SER GLU LEU ARG ASP LEU LEU SER GLU PHE ASN          
SEQRES   7 A  314  VAL LEU LYS GLN VAL ASN HIS PRO HIS VAL ILE LYS LEU          
SEQRES   8 A  314  TYR GLY ALA CYS SER GLN ASP GLY PRO LEU LEU LEU ILE          
SEQRES   9 A  314  VAL GLU TYR ALA LYS TYR GLY SER LEU ARG GLY PHE LEU          
SEQRES  10 A  314  ARG GLU SER ARG LYS VAL GLY PRO GLY TYR LEU GLY SER          
SEQRES  11 A  314  GLY GLY SER ARG ASN SER SER SER LEU ASP HIS PRO ASP          
SEQRES  12 A  314  GLU ARG ALA LEU THR MET GLY ASP LEU ILE SER PHE ALA          
SEQRES  13 A  314  TRP GLN ILE SER GLN GLY MET GLN TYR LEU ALA GLU MET          
SEQRES  14 A  314  LYS LEU VAL HIS ARG ASP LEU ALA ALA ARG ASN ILE LEU          
SEQRES  15 A  314  VAL ALA GLU GLY ARG LYS MET LYS ILE SER ASP PHE GLY          
SEQRES  16 A  314  LEU SER ARG ASP VAL PTR GLU GLU ASP SER PTR VAL LYS          
SEQRES  17 A  314  ARG SER GLN GLY ARG ILE PRO VAL LYS TRP MET ALA ILE          
SEQRES  18 A  314  GLU SER LEU PHE ASP HIS ILE TYR THR THR GLN SER ASP          
SEQRES  19 A  314  VAL TRP SER PHE GLY VAL LEU LEU TRP GLU ILE VAL THR          
SEQRES  20 A  314  LEU GLY GLY ASN PRO TYR PRO GLY ILE PRO PRO GLU ARG          
SEQRES  21 A  314  LEU PHE ASN LEU LEU LYS THR GLY HIS ARG MET GLU ARG          
SEQRES  22 A  314  PRO ASP ASN CYS SER GLU GLU MET TYR ARG LEU MET LEU          
SEQRES  23 A  314  GLN CYS TRP LYS GLN GLU PRO ASP LYS ARG PRO VAL PHE          
SEQRES  24 A  314  ALA ASP ILE SER LYS ASP LEU GLU LYS MET MET VAL LYS          
SEQRES  25 A  314  ARG ARG                                                      
MODRES 6NJA PTR A  900  TYR  MODIFIED RESIDUE                                   
MODRES 6NJA PTR A  905  TYR  MODIFIED RESIDUE                                   
HET    PTR  A 900      16                                                       
HET    PTR  A 905      16                                                       
HET    ADE  A1101      10                                                       
HET    FMT  A1102       3                                                       
HET    FMT  A1103       3                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     ADE ADENINE                                                          
HETNAM     FMT FORMIC ACID                                                      
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  PTR    2(C9 H12 N O6 P)                                             
FORMUL   2  ADE    C5 H5 N5                                                     
FORMUL   3  FMT    2(C H2 O2)                                                   
FORMUL   5  HOH   *163(H2 O)                                                    
HELIX    1 AA1 GLY A  700  LEU A  712  1                                  13    
HELIX    2 AA2 PRO A  720  LYS A  722  5                                   3    
HELIX    3 AA3 SER A  765  LYS A  780  1                                  16    
HELIX    4 AA4 SER A  811  GLU A  818  1                                   8    
HELIX    5 AA5 THR A  847  MET A  868  1                                  22    
HELIX    6 AA6 ALA A  876  ARG A  878  5                                   3    
HELIX    7 AA7 PRO A  914  MET A  918  5                                   5    
HELIX    8 AA8 ALA A  919  HIS A  926  1                                   8    
HELIX    9 AA9 THR A  929  THR A  946  1                                  18    
HELIX   10 AB1 PRO A  956  GLU A  958  5                                   3    
HELIX   11 AB2 ARG A  959  THR A  966  1                                   8    
HELIX   12 AB3 SER A  977  TRP A  988  1                                  12    
HELIX   13 AB4 GLU A  991  ARG A  995  5                                   5    
HELIX   14 AB5 VAL A  997  ARG A 1013  1                                  17    
SHEET    1 AA1 5 LEU A 724  GLU A 732  0                                        
SHEET    2 AA1 5 GLY A 736  LEU A 746 -1  O  VAL A 738   N  LEU A 730           
SHEET    3 AA1 5 ARG A 749  LEU A 760 -1  O  THR A 753   N  ALA A 743           
SHEET    4 AA1 5 LEU A 801  VAL A 804 -1  O  VAL A 804   N  ALA A 756           
SHEET    5 AA1 5 LEU A 790  CYS A 794 -1  N  GLY A 792   O  ILE A 803           
SHEET    1 AA2 2 SER A 819  LYS A 821  0                                        
SHEET    2 AA2 2 ARG A 844  LEU A 846  1  O  LEU A 846   N  ARG A 820           
SHEET    1 AA3 2 LEU A 870  VAL A 871  0                                        
SHEET    2 AA3 2 ARG A 897  ASP A 898 -1  O  ARG A 897   N  VAL A 871           
SHEET    1 AA4 2 ILE A 880  ALA A 883  0                                        
SHEET    2 AA4 2 LYS A 887  ILE A 890 -1  O  LYS A 889   N  LEU A 881           
SHEET    1 AA5 2 PTR A 905  VAL A 906  0                                        
SHEET    2 AA5 2 ILE A 927  TYR A 928 -1  O  TYR A 928   N  PTR A 905           
LINK         C   VAL A 899                 N   PTR A 900     1555   1555  1.32  
LINK         C   PTR A 900                 N   GLU A 901     1555   1555  1.33  
LINK         C   SER A 904                 N   PTR A 905     1555   1555  1.32  
LINK         C   PTR A 905                 N   VAL A 906     1555   1555  1.32  
SITE     1 AC1  7 LEU A 730  VAL A 738  ALA A 756  GLU A 805                    
SITE     2 AC1  7 TYR A 806  ALA A 807  LEU A 881                               
SITE     1 AC2  8 GLY A 700  PRO A 701  LEU A 702  SER A 703                    
SITE     2 AC2  8 GLN A 910  LEU A 923  PHE A 924  HIS A 926                    
SITE     1 AC3  4 ARG A 873  LEU A 895  GLY A 911  ARG A 912                    
CRYST1   71.703   70.816   78.869  90.00 102.05  90.00 C 1 2 1       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      0.013946  0.000000  0.002978        0.00000                         
SCALE2      0.000000  0.014121  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012965        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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