HEADER TRANSFERASE 16-AUG-11 3ZXZ
TITLE X-RAY STRUCTURE OF PF-04217903 BOUND TO THE KINASE DOMAIN OF C-MET
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATOCYTE GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TYROSINE KINASE DOMAIN, RESIDUES 1051-1348;
COMPND 5 SYNONYM: HGF RECEPTOR, HGF/SF RECEPTOR, PROTO-ONCOGENE C-MET, SCATTER
COMPND 6 FACTOR RECEPTOR, SF RECEPTOR, TYROSINE-PROTEIN KINASE MET;
COMPND 7 EC: 2.7.10.1;
COMPND 8 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: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS TRANSFERASE, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MCTIGUE,N.GRODSKY,K.RYAN,J.J.CUI
REVDAT 5 20-DEC-23 3ZXZ 1 REMARK
REVDAT 4 08-MAY-19 3ZXZ 1 REMARK
REVDAT 3 10-OCT-12 3ZXZ 1 JRNL
REVDAT 2 26-SEP-12 3ZXZ 1 AUTHOR JRNL REMARK
REVDAT 1 31-AUG-11 3ZXZ 0
JRNL AUTH J.J.CUI,M.MCTIGUE,M.NAMBU,M.TRAN-DUBE,M.PAIRISH,H.SHEN,
JRNL AUTH 2 L.JIA,H.CHENG,J.HOFFMAN,P.LE,M.JALAIE,G.H.GOETZ,K.RYAN,
JRNL AUTH 3 N.GRODSKY,Y.DENG,M.PARKER,S.TIMOFEEVSKI,B.W.MURRAY,
JRNL AUTH 4 S.YAMAZAKI,S.AGUIRRE,Q.LI,H.ZOU,J.CHRISTENSEN
JRNL TITL DISCOVERY OF A NOVEL CLASS OF EXQUISITELY SELECTIVE
JRNL TITL 2 MESENCHYMAL-EPITHELIAL TRANSITION FACTOR (C-MET) PROTEIN
JRNL TITL 3 KINASE INHIBITORS AND IDENTIFICATION OF THE CLINICAL
JRNL TITL 4 CANDIDATE 2-(4-(1-(QUINOLIN-6-YLMETHYL)-1H-[1,2,
JRNL TITL 5 3]TRIAZOLO[4,5-B]PYRAZIN-6-YL)-1H-PYRAZOL-1-YL)ETHANOL
JRNL TITL 6 (PF-04217903) FOR THE TREATMENT OF CANCER.
JRNL REF J.MED.CHEM. V. 55 8091 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 22924734
JRNL DOI 10.1021/JM300967G
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 2005
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.43
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 88569.580
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 82.9
REMARK 3 NUMBER OF REFLECTIONS : 26320
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 SET) : 0.185
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 782
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 42.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2123
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 75
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2309
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 272
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.23000
REMARK 3 B22 (A**2) : -9.74000
REMARK 3 B33 (A**2) : 12.97000
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) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.12
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.12
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 0.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.590
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.240 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.840 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.160 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.180 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 58.24
REMARK 3
REMARK 3 NCS MODEL : NONE
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : KRW.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : KRW.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3ZXZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1290049356.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 87
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.977
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27447
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.3
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 37.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.25000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.270
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 2WGJ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE OBTAINED AT 13 DEGREES C
REMARK 280 BY THE HANGING DROP VAPOR DIFFUSION METHOD USING 1.2 MICROLITERS
REMARK 280 OF PROTEIN SOLUTION (CONTAINING 7-13 MG/ML C-MET KD PLUS A 5
REMARK 280 FOLD MOLAR EXCESS OF PF-04217903) AND 1.2 MICROLITERS OF MOTHER
REMARK 280 LIQUOR SOLUTION (0.05 M CITRATE-PHOSHPHATE 4.6, 0-0.275 M NACL,
REMARK 280 AND 21% W/V PEG 3350)., PH 4.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 286K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 38.37000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.06250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.37000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.06250
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 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 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 1050
REMARK 465 VAL A 1051
REMARK 465 ASP A 1099
REMARK 465 ASN A 1100
REMARK 465 ASP A 1101
REMARK 465 GLY A 1102
REMARK 465 GLY A 1346
REMARK 465 GLU A 1347
REMARK 465 HIS A 1348
REMARK 465 HIS A 1349
REMARK 465 HIS A 1350
REMARK 465 HIS A 1351
REMARK 465 HIS A 1352
REMARK 465 HIS A 1353
REMARK 465 HIS A 1354
REMARK 465 HIS A 1355
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 ILE A1345 CA C O CB CG1 CG2 CD1
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 A1203 -11.76 84.76
REMARK 500 ASP A1204 46.13 -145.82
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 A2042 DISTANCE = 6.07 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KRW A 2345
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R1W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THEHEPATOCYTE
REMARK 900 GROWTH FACTOR RECEPTOR C-MET
REMARK 900 RELATED ID: 1UX3 RELATED DB: PDB
REMARK 900 3D STRUCTURE PREDICTION OF AMINO ACIDS 25 TO 656 OF HUMAN
REMARK 900 HEPATOCYTE GROWTH FACTOR/SCATTER FACTOR (MET) RECEPTOR
REMARK 900 RELATED ID: 2WGJ RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF PF-02341066 BOUND TO THE KINASE DOMAIN OF C-MET
REMARK 900 RELATED ID: 1FYR RELATED DB: PDB
REMARK 900 DIMER FORMATION THROUGH DOMAIN SWAPPING IN THE CRYSTALSTRUCTURE OF
REMARK 900 THE GRB2-SH2 AC-PYVNV COMPLEX
REMARK 900 RELATED ID: 2WD1 RELATED DB: PDB
REMARK 900 HUMAN C-MET KINASE IN COMPLEX WITH AZAINDOLE INHIBITOR
REMARK 900 RELATED ID: 2CEW RELATED DB: PDB
REMARK 900 3D STRUCTURE PREDICTION OF THE IG2-IG4 DOMAINS OF THE ECTODOMAIN
REMARK 900 REGION OF THE HUMAN HEPATOCYTE GROWTH FACTOR-SCATTER FACTOR
REMARK 900 RECEPTOR, MET
REMARK 900 RELATED ID: 2WKM RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF PHA-00665752 BOUND TO THE KINASE DOMAIN OF C-MET
REMARK 900 RELATED ID: 2UZX RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HUMAN RECEPTOR TYROSINE KINASE MET IN COMPLEX WITH
REMARK 900 THE LISTERIA MONOCYTOGENES INVASION PROTEIN INLB: CRYSTAL FORM I
REMARK 900 RELATED ID: 1SHY RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF HGF BETA-CHAIN IN COMPLEX WITH THESEMA
REMARK 900 DOMAIN OF THE MET RECEPTOR.
REMARK 900 RELATED ID: 2UZY RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HUMAN RECEPTOR TYROSINE KINASE MET IN COMPLEX WITH
REMARK 900 THE LISTERIA MONOCYTOGENES INVASION PROTEIN INLB: LOW RESOLUTION,
REMARK 900 CRYSTAL FORM II
REMARK 900 RELATED ID: 1R0P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THEHEPATOCYTE
REMARK 900 GROWTH FACTOR RECEPTOR C-MET IN COMPLEX WITHTHE MICROBIAL ALKALOID
REMARK 900 K-252A
REMARK 900 RELATED ID: 2G15 RELATED DB: PDB
REMARK 900 STRUCTURAL CHARACTERIZATION OF AUTOINHIBITED C-MET KINASE
REMARK 900 RELATED ID: 1SSL RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE PSI DOMAIN FROM THE MET RECEPTOR
REMARK 900 RELATED ID: 3ZZE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF C-MET KINASE DOMAIN IN COMPLEX WITH N'-((3Z)-4-
REMARK 900 CHLORO-7-METHYL-2-OXO-1,2- DIHYDRO-3H-INDOL-3-YLIDENE)-2-(4-
REMARK 900 HYDROXYPHENYL) PROPANOHYDRAZIDE
REMARK 900 RELATED ID: 4AOI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF C-MET KINASE DOMAIN IN COMPLEX WITH 4-(3-((1H-
REMARK 900 PYRROLO(2,3-B)PYRIDIN-3-YL)METHYL )-(1,2,4)TRIAZOLO(4,3-B)(1,2,4)
REMARK 900 TRIAZIN-6-YL) BENZONITRILE
REMARK 900 RELATED ID: 4AP7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF C-MET KINASE DOMAIN IN COMPLEX WITH 4-((6-(4-
REMARK 900 FLUOROPHENYL)-(1,2,4)TRIAZOLO(4,3- B)(1,2,4)TRIAZIN-3-YL)METHYL)
REMARK 900 PHENOL
DBREF 3ZXZ A 1051 1348 UNP P08581 MET_HUMAN 1051 1348
SEQADV 3ZXZ MET A 1050 UNP P08581 EXPRESSION TAG
SEQADV 3ZXZ HIS A 1349 UNP P08581 EXPRESSION TAG
SEQADV 3ZXZ HIS A 1350 UNP P08581 EXPRESSION TAG
SEQADV 3ZXZ HIS A 1351 UNP P08581 EXPRESSION TAG
SEQADV 3ZXZ HIS A 1352 UNP P08581 EXPRESSION TAG
SEQADV 3ZXZ HIS A 1353 UNP P08581 EXPRESSION TAG
SEQADV 3ZXZ HIS A 1354 UNP P08581 EXPRESSION TAG
SEQADV 3ZXZ HIS A 1355 UNP P08581 EXPRESSION TAG
SEQRES 1 A 306 MET VAL HIS ILE ASP LEU SER ALA LEU ASN PRO GLU LEU
SEQRES 2 A 306 VAL GLN ALA VAL GLN HIS VAL VAL ILE GLY PRO SER SER
SEQRES 3 A 306 LEU ILE VAL HIS PHE ASN GLU VAL ILE GLY ARG GLY HIS
SEQRES 4 A 306 PHE GLY CYS VAL TYR HIS GLY THR LEU LEU ASP ASN ASP
SEQRES 5 A 306 GLY LYS LYS ILE HIS CYS ALA VAL LYS SER LEU ASN ARG
SEQRES 6 A 306 ILE THR ASP ILE GLY GLU VAL SER GLN PHE LEU THR GLU
SEQRES 7 A 306 GLY ILE ILE MET LYS ASP PHE SER HIS PRO ASN VAL LEU
SEQRES 8 A 306 SER LEU LEU GLY ILE CYS LEU ARG SER GLU GLY SER PRO
SEQRES 9 A 306 LEU VAL VAL LEU PRO TYR MET LYS HIS GLY ASP LEU ARG
SEQRES 10 A 306 ASN PHE ILE ARG ASN GLU THR HIS ASN PRO THR VAL LYS
SEQRES 11 A 306 ASP LEU ILE GLY PHE GLY LEU GLN VAL ALA LYS GLY MET
SEQRES 12 A 306 LYS TYR LEU ALA SER LYS LYS PHE VAL HIS ARG ASP LEU
SEQRES 13 A 306 ALA ALA ARG ASN CYS MET LEU ASP GLU LYS PHE THR VAL
SEQRES 14 A 306 LYS VAL ALA ASP PHE GLY LEU ALA ARG ASP MET TYR ASP
SEQRES 15 A 306 LYS GLU TYR TYR SER VAL HIS ASN LYS THR GLY ALA LYS
SEQRES 16 A 306 LEU PRO VAL LYS TRP MET ALA LEU GLU SER LEU GLN THR
SEQRES 17 A 306 GLN LYS PHE THR THR LYS SER ASP VAL TRP SER PHE GLY
SEQRES 18 A 306 VAL LEU LEU TRP GLU LEU MET THR ARG GLY ALA PRO PRO
SEQRES 19 A 306 TYR PRO ASP VAL ASN THR PHE ASP ILE THR VAL TYR LEU
SEQRES 20 A 306 LEU GLN GLY ARG ARG LEU LEU GLN PRO GLU TYR CYS PRO
SEQRES 21 A 306 ASP PRO LEU TYR GLU VAL MET LEU LYS CYS TRP HIS PRO
SEQRES 22 A 306 LYS ALA GLU MET ARG PRO SER PHE SER GLU LEU VAL SER
SEQRES 23 A 306 ARG ILE SER ALA ILE PHE SER THR PHE ILE GLY GLU HIS
SEQRES 24 A 306 HIS HIS HIS HIS HIS HIS HIS
HET KRW A2345 28
HETNAM KRW 2-{4-[1-(QUINOLIN-6-YLMETHYL)-1H-[1,2,3]TRIAZOLO[4,5-
HETNAM 2 KRW B]PYRAZIN-6-YL]-1H-PYRAZOL-1-YL}ETHANOL
FORMUL 2 KRW C19 H16 N8 O
FORMUL 3 HOH *272(H2 O)
HELIX 1 1 ASN A 1059 HIS A 1068 1 10
HELIX 2 2 GLY A 1072 SER A 1074 5 3
HELIX 3 3 ASP A 1117 ILE A 1129 1 13
HELIX 4 4 ILE A 1130 PHE A 1134 5 5
HELIX 5 5 ASP A 1164 ASN A 1171 1 8
HELIX 6 6 THR A 1177 LYS A 1198 1 22
HELIX 7 7 ALA A 1206 ARG A 1208 5 3
HELIX 8 8 PHE A 1223 ARG A 1227 5 5
HELIX 9 9 ASP A 1231 TYR A 1235 5 5
HELIX 10 10 PRO A 1246 MET A 1250 5 5
HELIX 11 11 ALA A 1251 GLN A 1258 1 8
HELIX 12 12 THR A 1261 THR A 1278 1 18
HELIX 13 13 ASP A 1291 GLN A 1298 1 8
HELIX 14 14 PRO A 1309 TRP A 1320 1 12
HELIX 15 15 LYS A 1323 ARG A 1327 5 5
HELIX 16 16 SER A 1329 THR A 1343 1 15
SHEET 1 AA 6 VAL A1070 ILE A1071 0
SHEET 2 AA 6 GLY A1144 CYS A1146 1 O ILE A1145 N ILE A1071
SHEET 3 AA 6 LEU A1154 PRO A1158 -1 O LEU A1154 N CYS A1146
SHEET 4 AA 6 ILE A1105 LYS A1110 -1 O ALA A1108 N LEU A1157
SHEET 5 AA 6 CYS A1091 LEU A1097 -1 O TYR A1093 N VAL A1109
SHEET 6 AA 6 LEU A1076 ARG A1086 -1 O ILE A1077 N THR A1096
SHEET 1 AB 2 CYS A1210 LEU A1212 0
SHEET 2 AB 2 VAL A1218 VAL A1220 -1 O LYS A1219 N MET A1211
SITE 1 AC1 16 ILE A1084 ALA A1108 PRO A1158 TYR A1159
SITE 2 AC1 16 MET A1160 ASP A1164 ARG A1208 MET A1211
SITE 3 AC1 16 ALA A1221 ASP A1222 ALA A1226 TYR A1230
SITE 4 AC1 16 ASP A1231 HOH A2067 HOH A2117 HOH A2126
CRYST1 76.740 94.125 46.138 90.00 90.00 90.00 P 21 21 2 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 0.013031 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010624 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021674 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
