HEADER TRANSFERASE/TRANSFERASE INHIBITOR 17-MAY-16 5K0K
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE PROTO-ONCOGENE
TITLE 2 TYROSINE-PROTEIN KINASE MER IN COMPLEX WITH INHIBITOR UNC2434
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE MER;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 570-864;
COMPND 5 SYNONYM: PROTO-ONCOGENE C-MER,RECEPTOR TYROSINE KINASE MERTK;
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 GENE: MERTK, MER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MACROCYCLIC, PYRROLOPYRIMIDINES, DRUG DESIGN, FIBRINOLYTIC AGENTS,
KEYWDS 2 PROTEIN KINASE INHIBITORS, PROTO-ONCOGENE PROTEINS, PYRIMIDINES,
KEYWDS 3 RECEPTOR PROTEIN-TYROSINE KINASES, STRUCTURE-ACTIVITY RELATIONSHIP,
KEYWDS 4 THROMBOSIS, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR X.WANG,J.LIU,W.ZHANG,M.A.STASHKO,J.NICHOLS,D.DERYCKERE,M.J.MILEY,
AUTHOR 2 J.NORRIS-DROUIN,Z.CHEN,M.MACHIUS,E.WOOD,D.K.GRAHAM,H.S.EARP,
AUTHOR 3 K.GRAHAM,D.KIREEV,S.V.FRYE
REVDAT 2 27-SEP-23 5K0K 1 COMPND HETNAM
REVDAT 1 11-JAN-17 5K0K 0
JRNL AUTH X.WANG,J.LIU,W.ZHANG,M.A.STASHKO,J.NICHOLS,M.J.MILEY,
JRNL AUTH 2 J.NORRIS-DROUIN,Z.CHEN,M.MACHIUS,D.DERYCKERE,E.WOOD,
JRNL AUTH 3 D.K.GRAHAM,H.S.EARP,D.KIREEV,S.V.FRYE
JRNL TITL DESIGN AND SYNTHESIS OF NOVEL MACROCYCLIC MER TYROSINE
JRNL TITL 2 KINASE INHIBITORS.
JRNL REF ACS MED CHEM LETT V. 7 1044 2016
JRNL REFN ISSN 1948-5875
JRNL PMID 27994735
JRNL DOI 10.1021/ACSMEDCHEMLETT.6B00221
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1261
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.1
REMARK 3 NUMBER OF REFLECTIONS : 17714
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1772
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 34.5498 - 5.9736 1.00 1461 163 0.1925 0.2354
REMARK 3 2 5.9736 - 4.7454 1.00 1434 159 0.1762 0.2076
REMARK 3 3 4.7454 - 4.1466 1.00 1427 158 0.1599 0.1831
REMARK 3 4 4.1466 - 3.7680 1.00 1428 159 0.1684 0.2240
REMARK 3 5 3.7680 - 3.4982 1.00 1438 160 0.1857 0.2256
REMARK 3 6 3.4982 - 3.2921 1.00 1413 157 0.1995 0.2789
REMARK 3 7 3.2921 - 3.1274 1.00 1423 158 0.2323 0.3457
REMARK 3 8 3.1274 - 2.9913 0.98 1380 154 0.2415 0.3189
REMARK 3 9 2.9913 - 2.8762 0.85 1197 133 0.2394 0.3258
REMARK 3 10 2.8762 - 2.7770 0.73 1045 116 0.2365 0.2935
REMARK 3 11 2.7770 - 2.6902 0.65 910 101 0.2399 0.3192
REMARK 3 12 2.6902 - 2.6134 0.54 769 85 0.2458 0.3441
REMARK 3 13 2.6134 - 2.5446 0.44 617 69 0.2387 0.2717
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.60
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 : 0.004 4276
REMARK 3 ANGLE : 0.720 5782
REMARK 3 CHIRALITY : 0.043 640
REMARK 3 PLANARITY : 0.003 722
REMARK 3 DIHEDRAL : 13.799 1650
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 577 THROUGH 612 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.8882 -9.3694 19.0199
REMARK 3 T TENSOR
REMARK 3 T11: 0.3393 T22: 0.4068
REMARK 3 T33: 0.3344 T12: 0.0389
REMARK 3 T13: -0.0479 T23: -0.0477
REMARK 3 L TENSOR
REMARK 3 L11: 8.1120 L22: 8.9855
REMARK 3 L33: 9.4433 L12: 0.0587
REMARK 3 L13: 1.7826 L23: 0.5027
REMARK 3 S TENSOR
REMARK 3 S11: 0.1617 S12: -0.6049 S13: -0.4162
REMARK 3 S21: -0.0165 S22: -0.0011 S23: -0.5112
REMARK 3 S31: 0.3193 S32: 0.6197 S33: -0.1983
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 613 THROUGH 628 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4194 -2.0477 25.3059
REMARK 3 T TENSOR
REMARK 3 T11: 0.3393 T22: 0.8161
REMARK 3 T33: 0.5253 T12: 0.0619
REMARK 3 T13: -0.1457 T23: -0.0410
REMARK 3 L TENSOR
REMARK 3 L11: 4.7053 L22: 0.3790
REMARK 3 L33: 3.9801 L12: 0.8658
REMARK 3 L13: 4.1486 L23: 0.4601
REMARK 3 S TENSOR
REMARK 3 S11: -0.6445 S12: -0.3191 S13: 0.3293
REMARK 3 S21: 0.0186 S22: -0.0298 S23: -0.5604
REMARK 3 S31: 0.0784 S32: 0.9512 S33: 0.2963
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 629 THROUGH 651 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6430 -4.3540 33.4314
REMARK 3 T TENSOR
REMARK 3 T11: 0.5409 T22: 0.5161
REMARK 3 T33: 0.4675 T12: 0.0142
REMARK 3 T13: 0.0457 T23: -0.0573
REMARK 3 L TENSOR
REMARK 3 L11: 3.5886 L22: 7.0578
REMARK 3 L33: 8.8664 L12: -4.6811
REMARK 3 L13: 4.4333 L23: -3.9487
REMARK 3 S TENSOR
REMARK 3 S11: 0.3731 S12: 0.6518 S13: 0.0627
REMARK 3 S21: 0.6522 S22: -0.2473 S23: -0.8100
REMARK 3 S31: -0.1660 S32: 1.4965 S33: -0.1297
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 652 THROUGH 763 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4818 4.1131 23.8314
REMARK 3 T TENSOR
REMARK 3 T11: 0.2118 T22: 0.2423
REMARK 3 T33: 0.2538 T12: -0.0362
REMARK 3 T13: -0.0190 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 2.5908 L22: 4.2866
REMARK 3 L33: 2.9471 L12: -1.0789
REMARK 3 L13: -1.2147 L23: -0.2191
REMARK 3 S TENSOR
REMARK 3 S11: 0.0311 S12: -0.1054 S13: -0.2210
REMARK 3 S21: -0.2559 S22: 0.1455 S23: 0.1037
REMARK 3 S31: 0.2046 S32: 0.1161 S33: -0.1978
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 764 THROUGH 814 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4686 19.7738 32.6040
REMARK 3 T TENSOR
REMARK 3 T11: 0.2444 T22: 0.3360
REMARK 3 T33: 0.3794 T12: -0.0726
REMARK 3 T13: -0.0235 T23: -0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 4.5398 L22: 5.5246
REMARK 3 L33: 5.6827 L12: -0.1019
REMARK 3 L13: -0.6500 L23: -0.1334
REMARK 3 S TENSOR
REMARK 3 S11: 0.1998 S12: -0.3504 S13: 0.3940
REMARK 3 S21: 0.4138 S22: -0.0403 S23: -0.6326
REMARK 3 S31: -0.6994 S32: 0.5306 S33: -0.1567
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 815 THROUGH 863 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1189 16.5468 34.6716
REMARK 3 T TENSOR
REMARK 3 T11: 0.2245 T22: 0.3238
REMARK 3 T33: 0.2554 T12: 0.0302
REMARK 3 T13: 0.1101 T23: 0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 4.9423 L22: 5.9934
REMARK 3 L33: 3.9837 L12: 0.9277
REMARK 3 L13: -0.0050 L23: -0.7666
REMARK 3 S TENSOR
REMARK 3 S11: 0.0484 S12: -0.2144 S13: -0.0136
REMARK 3 S21: 0.2252 S22: 0.1802 S23: 0.1548
REMARK 3 S31: -0.4129 S32: -0.5894 S33: -0.1961
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 577 THROUGH 643 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7316 51.4224 17.7656
REMARK 3 T TENSOR
REMARK 3 T11: 0.3275 T22: 0.5010
REMARK 3 T33: 0.3098 T12: -0.1135
REMARK 3 T13: -0.0387 T23: -0.0671
REMARK 3 L TENSOR
REMARK 3 L11: 5.6950 L22: 3.9328
REMARK 3 L33: 5.8155 L12: 0.3533
REMARK 3 L13: -2.4181 L23: -1.5327
REMARK 3 S TENSOR
REMARK 3 S11: 0.0953 S12: 0.3173 S13: 0.2254
REMARK 3 S21: -0.3162 S22: 0.1542 S23: -0.0873
REMARK 3 S31: -0.4202 S32: 0.7967 S33: -0.2492
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 644 THROUGH 678 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7642 47.7370 15.2608
REMARK 3 T TENSOR
REMARK 3 T11: 0.3380 T22: 0.5414
REMARK 3 T33: 0.2394 T12: -0.0523
REMARK 3 T13: 0.0029 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 4.5040 L22: 4.5110
REMARK 3 L33: 2.6625 L12: 2.7875
REMARK 3 L13: 2.6588 L23: 1.4333
REMARK 3 S TENSOR
REMARK 3 S11: -0.1736 S12: 0.0143 S13: 0.0607
REMARK 3 S21: 0.0482 S22: 0.1085 S23: -0.0171
REMARK 3 S31: 0.0967 S32: 0.9189 S33: 0.0904
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 679 THROUGH 862 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1040 29.2947 3.7596
REMARK 3 T TENSOR
REMARK 3 T11: 0.1986 T22: 0.2601
REMARK 3 T33: 0.2486 T12: -0.0427
REMARK 3 T13: -0.0093 T23: 0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 2.4004 L22: 5.0714
REMARK 3 L33: 5.2733 L12: -0.2269
REMARK 3 L13: -0.1218 L23: -1.0100
REMARK 3 S TENSOR
REMARK 3 S11: 0.0163 S12: 0.0676 S13: -0.0195
REMARK 3 S21: -0.1005 S22: -0.0100 S23: -0.1426
REMARK 3 S31: 0.1548 S32: 0.1222 S33: 0.0109
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 5K0K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000220286.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20516
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.545
REMARK 200 RESOLUTION RANGE LOW (A) : 34.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.68600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3BRB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 32.5 MG/ML (IN 20 MM TRIS
REMARK 280 PH 8.0, 500 MM NACL, 2MM BME) WAS INCUBATED OVERNIGHT WITH
REMARK 280 INHIBITOR AT 2.5 MM FINAL CONCENTRATION, AND THEN WAS MIXED 1:1
REMARK 280 WITH CRYSTALLIZATION SOLUTION (27-33% (V/V) PEG 400, 200 MM
REMARK 280 MGCL2, 100 MM TRIS PH 8.5)., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 285.2K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 45.65750
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 MET A 552
REMARK 465 GLY A 553
REMARK 465 SER A 554
REMARK 465 SER A 555
REMARK 465 HIS A 556
REMARK 465 HIS A 557
REMARK 465 HIS A 558
REMARK 465 HIS A 559
REMARK 465 HIS A 560
REMARK 465 HIS A 561
REMARK 465 SER A 562
REMARK 465 SER A 563
REMARK 465 GLY A 564
REMARK 465 LEU A 565
REMARK 465 VAL A 566
REMARK 465 PRO A 567
REMARK 465 ARG A 568
REMARK 465 GLY A 569
REMARK 465 SER A 570
REMARK 465 GLU A 571
REMARK 465 GLU A 572
REMARK 465 LEU A 573
REMARK 465 GLN A 574
REMARK 465 ASN A 575
REMARK 465 LYS A 576
REMARK 465 GLY A 596
REMARK 465 GLU A 597
REMARK 465 PHE A 598
REMARK 465 MET A 659
REMARK 465 SER A 660
REMARK 465 SER A 661
REMARK 465 GLN A 662
REMARK 465 GLY A 663
REMARK 465 ILE A 664
REMARK 465 SER A 745
REMARK 465 LYS A 746
REMARK 465 LYS A 747
REMARK 465 ILE A 748
REMARK 465 TYR A 749
REMARK 465 SER A 750
REMARK 465 GLY A 751
REMARK 465 ASP A 752
REMARK 465 TYR A 753
REMARK 465 TYR A 754
REMARK 465 ARG A 755
REMARK 465 GLN A 756
REMARK 465 GLY A 757
REMARK 465 ARG A 758
REMARK 465 ILE A 759
REMARK 465 ALA A 760
REMARK 465 LYS A 761
REMARK 465 MET A 762
REMARK 465 VAL A 864
REMARK 465 MET B 552
REMARK 465 GLY B 553
REMARK 465 SER B 554
REMARK 465 SER B 555
REMARK 465 HIS B 556
REMARK 465 HIS B 557
REMARK 465 HIS B 558
REMARK 465 HIS B 559
REMARK 465 HIS B 560
REMARK 465 HIS B 561
REMARK 465 SER B 562
REMARK 465 SER B 563
REMARK 465 GLY B 564
REMARK 465 LEU B 565
REMARK 465 VAL B 566
REMARK 465 PRO B 567
REMARK 465 ARG B 568
REMARK 465 GLY B 569
REMARK 465 SER B 570
REMARK 465 GLU B 571
REMARK 465 GLU B 572
REMARK 465 LEU B 573
REMARK 465 GLN B 574
REMARK 465 ASN B 575
REMARK 465 LYS B 576
REMARK 465 GLU B 597
REMARK 465 PHE B 598
REMARK 465 MET B 621
REMARK 465 LYS B 622
REMARK 465 LEU B 623
REMARK 465 ASP B 624
REMARK 465 ASN B 625
REMARK 465 SER B 626
REMARK 465 SER B 627
REMARK 465 GLN B 628
REMARK 465 ARG B 629
REMARK 465 GLU B 630
REMARK 465 ILE B 631
REMARK 465 GLU B 632
REMARK 465 GLU B 633
REMARK 465 PHE B 634
REMARK 465 LEU B 635
REMARK 465 SER B 636
REMARK 465 GLY B 743
REMARK 465 LEU B 744
REMARK 465 SER B 745
REMARK 465 LYS B 746
REMARK 465 LYS B 747
REMARK 465 ILE B 748
REMARK 465 TYR B 749
REMARK 465 SER B 750
REMARK 465 GLY B 751
REMARK 465 ASP B 752
REMARK 465 TYR B 753
REMARK 465 TYR B 754
REMARK 465 ARG B 755
REMARK 465 GLN B 756
REMARK 465 GLY B 757
REMARK 465 ARG B 758
REMARK 465 ILE B 759
REMARK 465 ALA B 760
REMARK 465 LYS B 761
REMARK 465 MET B 762
REMARK 465 ASP B 863
REMARK 465 VAL B 864
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 O GLU A 689 HG1 THR A 690 1.59
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 THR A 690 -51.89 70.42
REMARK 500 PRO A 692 152.21 -46.03
REMARK 500 ASP A 723 43.54 -163.93
REMARK 500 THR B 690 -56.31 70.85
REMARK 500 ARG B 722 -7.68 74.51
REMARK 500 ASP B 723 55.16 -155.02
REMARK 500 ASN B 728 41.67 -106.19
REMARK 500 ALA B 773 -68.58 -96.91
REMARK 500 ASP B 824 67.03 -104.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 903 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 728 OD1
REMARK 620 2 ASP B 741 OD1 85.5
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6Q1 A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6Q1 B 904
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5K0X RELATED DB: PDB
DBREF 5K0K A 570 864 UNP Q12866 MERTK_HUMAN 570 864
DBREF 5K0K B 570 864 UNP Q12866 MERTK_HUMAN 570 864
SEQADV 5K0K MET A 552 UNP Q12866 INITIATING METHIONINE
SEQADV 5K0K GLY A 553 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K SER A 554 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K SER A 555 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K HIS A 556 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K HIS A 557 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K HIS A 558 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K HIS A 559 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K HIS A 560 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K HIS A 561 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K SER A 562 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K SER A 563 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K GLY A 564 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K LEU A 565 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K VAL A 566 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K PRO A 567 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K ARG A 568 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K GLY A 569 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K MET B 552 UNP Q12866 INITIATING METHIONINE
SEQADV 5K0K GLY B 553 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K SER B 554 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K SER B 555 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K HIS B 556 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K HIS B 557 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K HIS B 558 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K HIS B 559 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K HIS B 560 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K HIS B 561 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K SER B 562 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K SER B 563 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K GLY B 564 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K LEU B 565 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K VAL B 566 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K PRO B 567 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K ARG B 568 UNP Q12866 EXPRESSION TAG
SEQADV 5K0K GLY B 569 UNP Q12866 EXPRESSION TAG
SEQRES 1 A 313 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 313 LEU VAL PRO ARG GLY SER GLU GLU LEU GLN ASN LYS LEU
SEQRES 3 A 313 GLU ASP VAL VAL ILE ASP ARG ASN LEU LEU ILE LEU GLY
SEQRES 4 A 313 LYS ILE LEU GLY GLU GLY GLU PHE GLY SER VAL MET GLU
SEQRES 5 A 313 GLY ASN LEU LYS GLN GLU ASP GLY THR SER LEU LYS VAL
SEQRES 6 A 313 ALA VAL LYS THR MET LYS LEU ASP ASN SER SER GLN ARG
SEQRES 7 A 313 GLU ILE GLU GLU PHE LEU SER GLU ALA ALA CYS MET LYS
SEQRES 8 A 313 ASP PHE SER HIS PRO ASN VAL ILE ARG LEU LEU GLY VAL
SEQRES 9 A 313 CYS ILE GLU MET SER SER GLN GLY ILE PRO LYS PRO MET
SEQRES 10 A 313 VAL ILE LEU PRO PHE MET LYS TYR GLY ASP LEU HIS THR
SEQRES 11 A 313 TYR LEU LEU TYR SER ARG LEU GLU THR GLY PRO LYS HIS
SEQRES 12 A 313 ILE PRO LEU GLN THR LEU LEU LYS PHE MET VAL ASP ILE
SEQRES 13 A 313 ALA LEU GLY MET GLU TYR LEU SER ASN ARG ASN PHE LEU
SEQRES 14 A 313 HIS ARG ASP LEU ALA ALA ARG ASN CYS MET LEU ARG ASP
SEQRES 15 A 313 ASP MET THR VAL CYS VAL ALA ASP PHE GLY LEU SER LYS
SEQRES 16 A 313 LYS ILE TYR SER GLY ASP TYR TYR ARG GLN GLY ARG ILE
SEQRES 17 A 313 ALA LYS MET PRO VAL LYS TRP ILE ALA ILE GLU SER LEU
SEQRES 18 A 313 ALA ASP ARG VAL TYR THR SER LYS SER ASP VAL TRP ALA
SEQRES 19 A 313 PHE GLY VAL THR MET TRP GLU ILE ALA THR ARG GLY MET
SEQRES 20 A 313 THR PRO TYR PRO GLY VAL GLN ASN HIS GLU MET TYR ASP
SEQRES 21 A 313 TYR LEU LEU HIS GLY HIS ARG LEU LYS GLN PRO GLU ASP
SEQRES 22 A 313 CYS LEU ASP GLU LEU TYR GLU ILE MET TYR SER CYS TRP
SEQRES 23 A 313 ARG THR ASP PRO LEU ASP ARG PRO THR PHE SER VAL LEU
SEQRES 24 A 313 ARG LEU GLN LEU GLU LYS LEU LEU GLU SER LEU PRO ASP
SEQRES 25 A 313 VAL
SEQRES 1 B 313 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 313 LEU VAL PRO ARG GLY SER GLU GLU LEU GLN ASN LYS LEU
SEQRES 3 B 313 GLU ASP VAL VAL ILE ASP ARG ASN LEU LEU ILE LEU GLY
SEQRES 4 B 313 LYS ILE LEU GLY GLU GLY GLU PHE GLY SER VAL MET GLU
SEQRES 5 B 313 GLY ASN LEU LYS GLN GLU ASP GLY THR SER LEU LYS VAL
SEQRES 6 B 313 ALA VAL LYS THR MET LYS LEU ASP ASN SER SER GLN ARG
SEQRES 7 B 313 GLU ILE GLU GLU PHE LEU SER GLU ALA ALA CYS MET LYS
SEQRES 8 B 313 ASP PHE SER HIS PRO ASN VAL ILE ARG LEU LEU GLY VAL
SEQRES 9 B 313 CYS ILE GLU MET SER SER GLN GLY ILE PRO LYS PRO MET
SEQRES 10 B 313 VAL ILE LEU PRO PHE MET LYS TYR GLY ASP LEU HIS THR
SEQRES 11 B 313 TYR LEU LEU TYR SER ARG LEU GLU THR GLY PRO LYS HIS
SEQRES 12 B 313 ILE PRO LEU GLN THR LEU LEU LYS PHE MET VAL ASP ILE
SEQRES 13 B 313 ALA LEU GLY MET GLU TYR LEU SER ASN ARG ASN PHE LEU
SEQRES 14 B 313 HIS ARG ASP LEU ALA ALA ARG ASN CYS MET LEU ARG ASP
SEQRES 15 B 313 ASP MET THR VAL CYS VAL ALA ASP PHE GLY LEU SER LYS
SEQRES 16 B 313 LYS ILE TYR SER GLY ASP TYR TYR ARG GLN GLY ARG ILE
SEQRES 17 B 313 ALA LYS MET PRO VAL LYS TRP ILE ALA ILE GLU SER LEU
SEQRES 18 B 313 ALA ASP ARG VAL TYR THR SER LYS SER ASP VAL TRP ALA
SEQRES 19 B 313 PHE GLY VAL THR MET TRP GLU ILE ALA THR ARG GLY MET
SEQRES 20 B 313 THR PRO TYR PRO GLY VAL GLN ASN HIS GLU MET TYR ASP
SEQRES 21 B 313 TYR LEU LEU HIS GLY HIS ARG LEU LYS GLN PRO GLU ASP
SEQRES 22 B 313 CYS LEU ASP GLU LEU TYR GLU ILE MET TYR SER CYS TRP
SEQRES 23 B 313 ARG THR ASP PRO LEU ASP ARG PRO THR PHE SER VAL LEU
SEQRES 24 B 313 ARG LEU GLN LEU GLU LYS LEU LEU GLU SER LEU PRO ASP
SEQRES 25 B 313 VAL
HET CL A 901 1
HET CL A 902 1
HET CL A 903 1
HET 6Q1 A 904 69
HET CL A 905 1
HET CL B 901 1
HET CL B 902 1
HET MG B 903 1
HET 6Q1 B 904 69
HETNAM CL CHLORIDE ION
HETNAM 6Q1 15-{4-[(4-METHYLPIPERAZIN-1-YL)METHYL]PHENYL}-4,5,6,7,
HETNAM 2 6Q1 9,10,11,12-OCTAHYDRO-2,16-(AZENOMETHENO)PYRROLO[2,1-
HETNAM 3 6Q1 D][1,3,5,9]TE TRAAZACYCLOTETRADECIN-8(3H)-ONE
HETNAM MG MAGNESIUM ION
HETSYN 6Q1 UNC2434
FORMUL 3 CL 6(CL 1-)
FORMUL 6 6Q1 2(C26 H35 N7 O)
FORMUL 10 MG MG 2+
FORMUL 12 HOH *28(H2 O)
HELIX 1 AA1 ASP A 583 ASN A 585 5 3
HELIX 2 AA2 GLN A 628 LYS A 642 1 15
HELIX 3 AA3 ASP A 678 ARG A 687 1 10
HELIX 4 AA4 PRO A 696 ARG A 717 1 22
HELIX 5 AA5 ALA A 725 ARG A 727 5 3
HELIX 6 AA6 PRO A 763 ILE A 767 5 5
HELIX 7 AA7 ALA A 768 ASP A 774 1 7
HELIX 8 AA8 THR A 778 THR A 795 1 18
HELIX 9 AA9 GLN A 805 HIS A 807 5 3
HELIX 10 AB1 GLU A 808 HIS A 815 1 8
HELIX 11 AB2 LEU A 826 CYS A 836 1 11
HELIX 12 AB3 THR A 846 SER A 860 1 15
HELIX 13 AB4 ASP B 583 ASN B 585 5 3
HELIX 14 AB5 ALA B 638 PHE B 644 1 7
HELIX 15 AB6 ASP B 678 SER B 686 1 9
HELIX 16 AB7 PRO B 696 ARG B 717 1 22
HELIX 17 AB8 ALA B 725 ARG B 727 5 3
HELIX 18 AB9 PRO B 763 ILE B 767 5 5
HELIX 19 AC1 ALA B 768 ASP B 774 1 7
HELIX 20 AC2 THR B 778 THR B 795 1 18
HELIX 21 AC3 GLN B 805 HIS B 807 5 3
HELIX 22 AC4 GLU B 808 HIS B 815 1 8
HELIX 23 AC5 LEU B 826 SER B 835 1 10
HELIX 24 AC6 CYS B 836 ARG B 838 5 3
HELIX 25 AC7 ASP B 840 ARG B 844 5 5
HELIX 26 AC8 THR B 846 LEU B 861 1 16
SHEET 1 AA1 5 LEU A 587 GLY A 594 0
SHEET 2 AA1 5 VAL A 601 LYS A 607 -1 O VAL A 601 N GLY A 594
SHEET 3 AA1 5 SER A 613 THR A 620 -1 O LEU A 614 N LEU A 606
SHEET 4 AA1 5 PRO A 667 PRO A 672 -1 O LEU A 671 N ALA A 617
SHEET 5 AA1 5 GLY A 654 ILE A 657 -1 N GLY A 654 O ILE A 670
SHEET 1 AA2 2 CYS A 729 LEU A 731 0
SHEET 2 AA2 2 VAL A 737 VAL A 739 -1 O CYS A 738 N MET A 730
SHEET 1 AA3 5 LEU B 587 GLY B 594 0
SHEET 2 AA3 5 VAL B 601 LYS B 607 -1 O VAL B 601 N GLY B 594
SHEET 3 AA3 5 SER B 613 LYS B 619 -1 O LEU B 614 N LEU B 606
SHEET 4 AA3 5 PRO B 665 PRO B 672 -1 O LEU B 671 N ALA B 617
SHEET 5 AA3 5 GLY B 654 MET B 659 -1 N GLU B 658 O LYS B 666
SHEET 1 AA4 2 CYS B 729 LEU B 731 0
SHEET 2 AA4 2 VAL B 737 VAL B 739 -1 O CYS B 738 N MET B 730
LINK OD1AASN B 728 MG MG B 903 1555 1555 2.17
LINK OD1 ASP B 741 MG MG B 903 1555 1555 2.26
SITE 1 AC1 2 ARG A 651 ARG A 732
SITE 1 AC2 2 PRO A 802 LYS A 820
SITE 1 AC3 3 ARG A 584 ILE A 588 LEU A 589
SITE 1 AC4 10 ALA A 617 ILE A 650 LEU A 671 PRO A 672
SITE 2 AC4 10 PHE A 673 MET A 674 LYS A 675 ARG A 727
SITE 3 AC4 10 MET A 730 ALA A 740
SITE 1 AC5 3 ARG A 687 HOH A1010 ARG B 687
SITE 1 AC6 3 ARG B 584 ILE B 588 LEU B 589
SITE 1 AC7 2 LEU B 819 LYS B 820
SITE 1 AC8 2 ASN B 728 ASP B 741
SITE 1 AC9 9 LYS B 591 VAL B 601 ALA B 617 PRO B 672
SITE 2 AC9 9 PHE B 673 MET B 674 LYS B 675 MET B 730
SITE 3 AC9 9 ASP B 741
CRYST1 51.072 91.315 69.203 90.00 100.42 90.00 P 1 21 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 0.019580 0.000000 0.003599 0.00000
SCALE2 0.000000 0.010951 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014692 0.00000
(ATOM LINES ARE NOT SHOWN.)
END