HEADER TRANSFERASE 30-OCT-15 5FM3
TITLE CRYSTAL STRUCTURE OF HYPER-PHOSPHORYLATED RET KINASE DOMAIN WITH
TITLE 2 (PROXIMAL) JUXTAMEMBRANE SEGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE RECEPTOR RET;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 659-1013;
COMPND 5 SYNONYM: CADHERIN FAMILY MEMBER 12, PROTO-ONCOGENE C-RET;
COMPND 6 EC: 2.7.10.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF21
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.PLAZA-MENACHO,K.BARNOUIN,R.BARRY,A.BORG,M.ORME,S.MOUILLERON,
AUTHOR 2 R.J.MARTINEZ-TORRES,P.MEIER,N.Q.MCDONALD
REVDAT 3 24-APR-19 5FM3 1 SOURCE LINK
REVDAT 2 01-MAR-17 5FM3 1 JRNL
REVDAT 1 28-DEC-16 5FM3 0
JRNL AUTH I.PLAZA-MENACHO,K.BARNOUIN,R.BARRY,A.BORG,M.ORME,R.CHAUHAN,
JRNL AUTH 2 S.MOUILLERON,R.J.MARTINEZ-TORRES,P.MEIER,N.Q.MCDONALD
JRNL TITL RET FUNCTIONS AS A DUAL-SPECIFICITY KINASE THAT REQUIRES
JRNL TITL 2 ALLOSTERIC INPUTS FROM JUXTAMEMBRANE ELEMENTS.
JRNL REF CELL REP V. 17 3319 2016
JRNL REFN ESSN 2211-1247
JRNL PMID 28009299
JRNL DOI 10.1016/J.CELREP.2016.11.061
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.67
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 9360
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 447
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 34.6674 - 4.2529 1.00 3123 148 0.1825 0.1925
REMARK 3 2 4.2529 - 3.3766 1.00 2905 165 0.2057 0.2538
REMARK 3 3 3.3766 - 2.9500 1.00 2885 134 0.2504 0.2899
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 77.33
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 2196
REMARK 3 ANGLE : 0.665 2992
REMARK 3 CHIRALITY : 0.040 333
REMARK 3 PLANARITY : 0.003 372
REMARK 3 DIHEDRAL : 14.532 1279
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 707 THROUGH 735 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7351 -36.4437 1.2382
REMARK 3 T TENSOR
REMARK 3 T11: 0.3961 T22: 0.3078
REMARK 3 T33: 0.5890 T12: 0.0422
REMARK 3 T13: 0.0126 T23: -0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.0573 L22: 0.0569
REMARK 3 L33: 0.2814 L12: 0.0158
REMARK 3 L13: 0.0278 L23: -0.1511
REMARK 3 S TENSOR
REMARK 3 S11: -0.2547 S12: 0.0371 S13: -0.0704
REMARK 3 S21: 0.1116 S22: 0.2914 S23: -0.8368
REMARK 3 S31: 0.1252 S32: 0.4274 S33: 0.0099
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 736 THROUGH 800 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9601 -35.3626 -3.7082
REMARK 3 T TENSOR
REMARK 3 T11: 0.2930 T22: 0.2527
REMARK 3 T33: 0.4714 T12: 0.0099
REMARK 3 T13: 0.1309 T23: -0.0553
REMARK 3 L TENSOR
REMARK 3 L11: 0.3405 L22: 0.6660
REMARK 3 L33: 0.9298 L12: -0.1047
REMARK 3 L13: -0.1077 L23: -0.2729
REMARK 3 S TENSOR
REMARK 3 S11: -0.0208 S12: -0.0354 S13: -0.2174
REMARK 3 S21: -0.0044 S22: -0.1196 S23: -0.1354
REMARK 3 S31: -0.0337 S32: 0.1096 S33: -0.1253
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 801 THROUGH 847 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1722 -21.7310 -13.8269
REMARK 3 T TENSOR
REMARK 3 T11: 0.6291 T22: 0.3427
REMARK 3 T33: 0.6966 T12: -0.1199
REMARK 3 T13: 0.0562 T23: 0.1485
REMARK 3 L TENSOR
REMARK 3 L11: 0.2812 L22: 0.0735
REMARK 3 L33: 0.5648 L12: -0.1323
REMARK 3 L13: 0.1916 L23: -0.1653
REMARK 3 S TENSOR
REMARK 3 S11: -0.1623 S12: 0.1981 S13: 0.1799
REMARK 3 S21: -0.4064 S22: 0.0161 S23: 0.1371
REMARK 3 S31: -0.1321 S32: 0.5379 S33: 0.0809
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 848 THROUGH 890 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6349 -30.6124 -20.8376
REMARK 3 T TENSOR
REMARK 3 T11: 0.5951 T22: 0.5604
REMARK 3 T33: 0.3892 T12: 0.0694
REMARK 3 T13: 0.1117 T23: -0.0947
REMARK 3 L TENSOR
REMARK 3 L11: 0.3192 L22: 0.5603
REMARK 3 L33: 0.2274 L12: -0.1268
REMARK 3 L13: 0.2937 L23: -0.0944
REMARK 3 S TENSOR
REMARK 3 S11: 0.4580 S12: 0.8191 S13: -0.1333
REMARK 3 S21: -0.1304 S22: -0.1502 S23: 0.2626
REMARK 3 S31: -0.1825 S32: 0.0318 S33: 0.0799
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 891 THROUGH 956 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1010 -33.3051 -14.8279
REMARK 3 T TENSOR
REMARK 3 T11: 0.5772 T22: 0.4079
REMARK 3 T33: 0.4340 T12: 0.0762
REMARK 3 T13: -0.0203 T23: -0.1180
REMARK 3 L TENSOR
REMARK 3 L11: 1.5271 L22: 0.6724
REMARK 3 L33: 0.2523 L12: -0.7487
REMARK 3 L13: 0.1678 L23: -0.1707
REMARK 3 S TENSOR
REMARK 3 S11: 0.0836 S12: -0.1090 S13: -0.2839
REMARK 3 S21: 0.0173 S22: -0.0138 S23: 0.7559
REMARK 3 S31: 0.0922 S32: -0.2092 S33: 0.1091
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 957 THROUGH 997 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.6139 -26.5208 -26.5482
REMARK 3 T TENSOR
REMARK 3 T11: 0.8621 T22: 0.9250
REMARK 3 T33: 0.1989 T12: 0.3259
REMARK 3 T13: -0.2946 T23: -0.1068
REMARK 3 L TENSOR
REMARK 3 L11: 0.3516 L22: 0.2973
REMARK 3 L33: 0.1518 L12: 0.1218
REMARK 3 L13: -0.1016 L23: 0.0243
REMARK 3 S TENSOR
REMARK 3 S11: -0.3697 S12: 0.7884 S13: -0.1898
REMARK 3 S21: -0.2053 S22: 0.2248 S23: 0.2991
REMARK 3 S31: -0.1589 S32: -0.0741 S33: -0.1896
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 998 THROUGH 1011 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9419 -30.3057 -33.8916
REMARK 3 T TENSOR
REMARK 3 T11: 0.8844 T22: 1.0606
REMARK 3 T33: 0.5041 T12: 0.0739
REMARK 3 T13: 0.0084 T23: -0.2354
REMARK 3 L TENSOR
REMARK 3 L11: 0.2882 L22: 0.2450
REMARK 3 L33: 0.1333 L12: -0.0371
REMARK 3 L13: -0.1253 L23: -0.1124
REMARK 3 S TENSOR
REMARK 3 S11: 0.5501 S12: 0.2775 S13: 0.1284
REMARK 3 S21: -0.2224 S22: 0.0785 S23: -0.1033
REMARK 3 S31: 0.0488 S32: -0.1137 S33: 0.1588
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5FM3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1290065400.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9361
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.900
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 73.15050
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 73.15050
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 73.15050
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 73.15050
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 73.15050
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 73.15050
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.9 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 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 CYS A 659
REMARK 465 TYR A 660
REMARK 465 HIS A 661
REMARK 465 LYS A 662
REMARK 465 PHE A 663
REMARK 465 ALA A 664
REMARK 465 HIS A 665
REMARK 465 LYS A 666
REMARK 465 PRO A 667
REMARK 465 PRO A 668
REMARK 465 ILE A 669
REMARK 465 SER A 670
REMARK 465 SER A 671
REMARK 465 ALA A 672
REMARK 465 GLU A 673
REMARK 465 MET A 674
REMARK 465 THR A 675
REMARK 465 PHE A 676
REMARK 465 ARG A 677
REMARK 465 ARG A 678
REMARK 465 PRO A 679
REMARK 465 ALA A 680
REMARK 465 GLN A 681
REMARK 465 ALA A 682
REMARK 465 PHE A 683
REMARK 465 PRO A 684
REMARK 465 VAL A 685
REMARK 465 SER A 686
REMARK 465 TYR A 687
REMARK 465 SER A 688
REMARK 465 SER A 689
REMARK 465 SER A 690
REMARK 465 GLY A 691
REMARK 465 ALA A 692
REMARK 465 ARG A 693
REMARK 465 ARG A 694
REMARK 465 PRO A 695
REMARK 465 SER A 696
REMARK 465 LEU A 697
REMARK 465 ASP A 698
REMARK 465 SER A 699
REMARK 465 MET A 700
REMARK 465 GLU A 701
REMARK 465 ASN A 702
REMARK 465 GLN A 703
REMARK 465 VAL A 704
REMARK 465 SER A 705
REMARK 465 VAL A 706
REMARK 465 ARG A 820
REMARK 465 LYS A 821
REMARK 465 VAL A 822
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 465 GLU A 843
REMARK 465 ARG A 844
REMARK 465 ARG A 1012
REMARK 465 ARG A 1013
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 707 CG OD1 OD2
REMARK 470 LYS A 710 CG CD CE NZ
REMARK 470 LEU A 712 CG CD1 CD2
REMARK 470 GLU A 713 CG CD OE1 OE2
REMARK 470 LYS A 728 CG CD CE NZ
REMARK 470 GLU A 734 CG CD OE1 OE2
REMARK 470 PHE A 744 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 747 CG CD CE NZ
REMARK 470 ARG A 749 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 762 CG CD OE1 OE2
REMARK 470 LYS A 789 CD CE NZ
REMARK 470 ASP A 797 CG OD1 OD2
REMARK 470 LYS A 869 CG CD CE NZ
REMARK 470 ASP A 874 CG OD1 OD2
REMARK 470 TYR A 900 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 901 CG CD OE1 OE2
REMARK 470 GLU A 902 CG CD OE1 OE2
REMARK 470 VAL A 906 CG1 CG2
REMARK 470 LYS A 907 NZ
REMARK 470 ARG A 908 NE CZ NH1 NH2
REMARK 470 GLN A 910 CG CD OE1 NE2
REMARK 470 ASP A 925 CG OD1 OD2
REMARK 470 GLU A 958 CG CD OE1 OE2
REMARK 470 ARG A 959 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 962 CG OD1 ND2
REMARK 470 LYS A 965 CG CD CE NZ
REMARK 470 GLU A 971 CG CD OE1 OE2
REMARK 470 ASN A 975 CG OD1 ND2
REMARK 470 GLU A 978 CG CD OE1 OE2
REMARK 470 GLU A 979 CG CD OE1 OE2
REMARK 470 ARG A 982 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 989 CD CE NZ
REMARK 470 GLU A 991 CG CD OE1 OE2
REMARK 470 ASP A 993 CG OD1 OD2
REMARK 470 LYS A 994 CG CD CE NZ
REMARK 470 LYS A1003 CG CD CE NZ
REMARK 470 LYS A1007 CG CD CE NZ
REMARK 470 LYS A1011 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 708 -19.29 67.10
REMARK 500 ARG A 749 -142.04 -168.42
REMARK 500 ALA A 750 78.43 64.19
REMARK 500 ASN A 783 102.59 -161.81
REMARK 500 VAL A 804 -162.66 -125.75
REMARK 500 GLU A 805 -172.73 -67.43
REMARK 500 ARG A 873 -52.48 68.93
REMARK 500 ASP A 874 53.41 -95.47
REMARK 500 ASP A 892 73.86 58.01
REMARK 500 TYR A 952 70.39 51.14
REMARK 500 ASP A 974 -75.35 -66.91
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 PP1 A 2012
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FM2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHORYLATED RET TYROSINE KINASE JM-KD
DBREF 5FM3 A 659 1013 UNP P07949 RET_HUMAN 659 1013
SEQRES 1 A 355 CYS TYR HIS LYS PHE ALA HIS LYS PRO PRO ILE SER SER
SEQRES 2 A 355 ALA GLU MET THR PHE ARG ARG PRO ALA GLN ALA PHE PRO
SEQRES 3 A 355 VAL SER TYR SER SER SER GLY ALA ARG ARG PRO SER LEU
SEQRES 4 A 355 ASP SER MET GLU ASN GLN VAL SER VAL ASP ALA PHE LYS
SEQRES 5 A 355 ILE LEU GLU ASP PRO LYS TRP GLU PHE PRO ARG LYS ASN
SEQRES 6 A 355 LEU VAL LEU GLY LYS THR LEU GLY GLU GLY GLU PHE GLY
SEQRES 7 A 355 LYS VAL VAL LYS ALA THR ALA PHE HIS LEU LYS GLY ARG
SEQRES 8 A 355 ALA GLY TYR THR THR VAL ALA VAL LYS MET LEU LYS GLU
SEQRES 9 A 355 ASN ALA SER PRO SER GLU LEU ARG ASP LEU LEU SER GLU
SEQRES 10 A 355 PHE ASN VAL LEU LYS GLN VAL ASN HIS PRO HIS VAL ILE
SEQRES 11 A 355 LYS LEU TYR GLY ALA CYS SER GLN ASP GLY PRO LEU LEU
SEQRES 12 A 355 LEU ILE VAL GLU TYR ALA LYS PTR GLY SER LEU ARG GLY
SEQRES 13 A 355 PHE LEU ARG GLU SER ARG LYS VAL GLY PRO GLY TYR LEU
SEQRES 14 A 355 GLY SER GLY GLY SER ARG ASN SER SER SER LEU ASP HIS
SEQRES 15 A 355 PRO ASP GLU ARG ALA LEU THR MET GLY ASP LEU ILE SER
SEQRES 16 A 355 PHE ALA TRP GLN ILE SER GLN GLY MET GLN TYR LEU ALA
SEQRES 17 A 355 GLU MET LYS LEU VAL HIS ARG ASP LEU ALA ALA ARG ASN
SEQRES 18 A 355 ILE LEU VAL ALA GLU GLY ARG LYS MET LYS ILE SER ASP
SEQRES 19 A 355 PHE GLY LEU SER ARG ASP VAL TYR GLU GLU ASP SER PTR
SEQRES 20 A 355 VAL LYS ARG SEP GLN GLY ARG ILE PRO VAL LYS TRP MET
SEQRES 21 A 355 ALA ILE GLU SER LEU PHE ASP HIS ILE PTR THR THR GLN
SEQRES 22 A 355 SER ASP VAL TRP SER PHE GLY VAL LEU LEU TRP GLU ILE
SEQRES 23 A 355 VAL THR LEU GLY GLY ASN PRO TYR PRO GLY ILE PRO PRO
SEQRES 24 A 355 GLU ARG LEU PHE ASN LEU LEU LYS THR GLY HIS ARG MET
SEQRES 25 A 355 GLU ARG PRO ASP ASN CYS SER GLU GLU MET TYR ARG LEU
SEQRES 26 A 355 MET LEU GLN CYS TRP LYS GLN GLU PRO ASP LYS ARG PRO
SEQRES 27 A 355 VAL PHE ALA ASP ILE SER LYS ASP LEU GLU LYS MET MET
SEQRES 28 A 355 VAL LYS ARG ARG
MODRES 5FM3 PTR A 809 TYR O-PHOSPHOTYROSINE
MODRES 5FM3 PTR A 905 TYR O-PHOSPHOTYROSINE
MODRES 5FM3 SEP A 909 SER PHOSPHOSERINE
MODRES 5FM3 PTR A 928 TYR O-PHOSPHOTYROSINE
HET PTR A 809 16
HET PTR A 905 16
HET SEP A 909 10
HET PTR A 928 16
HET PP1 A2012 21
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM SEP PHOSPHOSERINE
HETNAM PP1 1-TER-BUTYL-3-P-TOLYL-1H-PYRAZOLO[3,4-D]PYRIMIDIN-4-
HETNAM 2 PP1 YLAMINE
HETSYN PTR PHOSPHONOTYROSINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 PTR 3(C9 H12 N O6 P)
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 PP1 C16 H19 N5
FORMUL 3 HOH *5(H2 O)
HELIX 1 1 SER A 765 VAL A 782 1 18
HELIX 2 2 SER A 811 GLU A 818 1 8
HELIX 3 3 THR A 847 MET A 868 1 22
HELIX 4 4 ALA A 876 ARG A 878 5 3
HELIX 5 5 PRO A 914 MET A 918 5 5
HELIX 6 6 ALA A 919 HIS A 926 1 8
HELIX 7 7 THR A 929 THR A 946 1 18
HELIX 8 8 PRO A 956 THR A 966 1 11
HELIX 9 9 SER A 977 TRP A 988 1 12
HELIX 10 10 GLU A 991 ARG A 995 5 5
HELIX 11 11 VAL A 997 LYS A 1011 1 15
SHEET 1 AA 5 LEU A 724 GLY A 733 0
SHEET 2 AA 5 GLY A 736 PHE A 744 -1 O GLY A 736 N GLY A 733
SHEET 3 AA 5 TYR A 752 MET A 759 -1 O THR A 753 N ALA A 743
SHEET 4 AA 5 LEU A 801 VAL A 804 -1 O LEU A 802 N LYS A 758
SHEET 5 AA 5 LEU A 790 CYS A 794 -1 N TYR A 791 O ILE A 803
SHEET 1 AB 2 LEU A 870 VAL A 871 0
SHEET 2 AB 2 ARG A 897 ASP A 898 -1 O ARG A 897 N VAL A 871
SHEET 1 AC 2 ILE A 880 ALA A 883 0
SHEET 2 AC 2 LYS A 887 ILE A 890 -1 O LYS A 887 N ALA A 883
LINK C LYS A 808 N PTR A 809 1555 1555 1.33
LINK C PTR A 809 N GLY A 810 1555 1555 1.33
LINK C SER A 904 N PTR A 905 1555 1555 1.33
LINK C PTR A 905 N VAL A 906 1555 1555 1.33
LINK C ARG A 908 N SEP A 909 1555 1555 1.33
LINK C SEP A 909 N GLN A 910 1555 1555 1.33
LINK C ILE A 927 N PTR A 928 1555 1555 1.33
LINK C PTR A 928 N THR A 929 1555 1555 1.33
SITE 1 AC1 10 LEU A 730 PHE A 735 VAL A 738 ALA A 756
SITE 2 AC1 10 LYS A 758 GLU A 775 VAL A 804 GLU A 805
SITE 3 AC1 10 ALA A 807 SER A 891
CRYST1 98.569 98.569 146.301 90.00 90.00 120.00 P 63 2 2 12
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 0.010145 0.005857 0.000000 0.00000
SCALE2 0.000000 0.011715 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006835 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
