HEADER TRANSFERASE 13-NOV-12 3ZBX
TITLE X-RAY STRUCTURE OF C-MET KINASE IN COMPLEX WITH INHIBITOR 6-((6-(4-
TITLE 2 FLUOROPHENYL)-(1,2,4)TRIAZOLO(4,3-B)(1,2,4)TRIAZIN-3-YL)METHYL)
TITLE 3 QUINOLINE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATOCYTE GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TYROSINE KINASE DOMAIN, UNP 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,J.WICKERSHAM,K.RYAN
REVDAT 3 20-DEC-23 3ZBX 1 REMARK
REVDAT 2 08-MAY-19 3ZBX 1 REMARK
REVDAT 1 27-NOV-13 3ZBX 0
JRNL AUTH J.J.CUI,H.SHEN,M.TRAN-DUBE,M.NAMBU,M.MCTIGUE,N.GRODSKY,
JRNL AUTH 2 K.RYAN,S.YAMAZAKI,S.AGUIRRE,M.PARKER,Q.LI,H.ZOU,
JRNL AUTH 3 J.CHRISTENSEN
JRNL TITL LESSONS FROM (S)-6-(1-(6-(1-METHYL-1H-PYRAZOL-4-YL)-[1,2,
JRNL TITL 2 4]TRIAZOLO[4,3-B]PYRIDAZIN-3-YL)ETHYL)QUINOLINE
JRNL TITL 3 (PF-04254644), AN INHIBITOR OF RECEPTOR TYROSINE KINASE
JRNL TITL 4 C-MET WITH HIGH PROTEIN KINASE SELECTIVITY BUT BROAD
JRNL TITL 5 PHOSPHODIESTERASE FAMILY INHIBITION LEADING TO MYOCARDIAL
JRNL TITL 6 DEGENERATION IN RATS.
JRNL REF J.MED.CHEM. V. 56 6651 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23944843
JRNL DOI 10.1021/JM400926X
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 90430.180
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 80.2
REMARK 3 NUMBER OF REFLECTIONS : 14207
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) : 0.179
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 429
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.011
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2064
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE : 0.3600
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 74
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.042
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2256
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 278
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.23000
REMARK 3 B22 (A**2) : -7.89000
REMARK 3 B33 (A**2) : 10.13000
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.23
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) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.38
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 0.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.60
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) : 1.260 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.950 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.230 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.140 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 56.85
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 : 6XE.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 : 6XE.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3ZBX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-NOV-12.
REMARK 100 THE DEPOSITION ID IS D_1290054775.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 96
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : 15108
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.9
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.28000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
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 (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: C-MET COCRYSTALS WERE OBTAINED AT 13
REMARK 280 DEGREES C BY THE HANGING DROP VAPOR DIFFUSION METHOD BY MIXING
REMARK 280 1.2 MICROLITERS OF PROTEIN SOLUTION (CONTAINING 7-13 MG/ML C-MET
REMARK 280 KD (RESIDUES 1051-1348) WITH A 5 FOLD MOLAR EXCESS OF C-MET
REMARK 280 INHIBITOR COMPOUND) WITH 1.2 MICROLITERS OF SOLUTION CONTAINING
REMARK 280 (0.05M CITRATE-PHOSPHATE PH 4.2, 200M NACL, AND 17.4%
REMARK 280 POLYETHYLENE GLYCOL MW=3350), 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 38.42850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.06350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.42850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.06350
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 HIS A 1052
REMARK 465 ILE A 1053
REMARK 465 ASP A 1054
REMARK 465 LEU A 1055
REMARK 465 SER A 1056
REMARK 465 ALA A 1057
REMARK 465 LEU A 1058
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 -11.20 81.84
REMARK 500 ASP A1204 44.97 -149.24
REMARK 500 ALA A1221 -157.04 -133.53
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 A2027 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A2051 DISTANCE = 6.43 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6XE A 2345
DBREF 3ZBX A 1051 1348 UNP P08581 MET_HUMAN 1051 1348
SEQADV 3ZBX MET A 1050 UNP P08581 EXPRESSION TAG
SEQADV 3ZBX HIS A 1349 UNP P08581 EXPRESSION TAG
SEQADV 3ZBX HIS A 1350 UNP P08581 EXPRESSION TAG
SEQADV 3ZBX HIS A 1351 UNP P08581 EXPRESSION TAG
SEQADV 3ZBX HIS A 1352 UNP P08581 EXPRESSION TAG
SEQADV 3ZBX HIS A 1353 UNP P08581 EXPRESSION TAG
SEQADV 3ZBX HIS A 1354 UNP P08581 EXPRESSION TAG
SEQADV 3ZBX 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 6XE A2345 27
HETNAM 6XE 6-[[6-(4-FLUOROPHENYL)-[1,2,4]TRIAZOLO[4,3-B][1,2,
HETNAM 2 6XE 4]TRIAZIN-3-YL]METHYL]QUINOLINE
FORMUL 2 6XE C20 H13 F N6
FORMUL 3 HOH *278(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 ALA A 1251 GLN A 1258 1 8
HELIX 11 11 THR A 1261 THR A 1278 1 18
HELIX 12 12 ASP A 1291 GLN A 1298 1 8
HELIX 13 13 PRO A 1309 TRP A 1320 1 12
HELIX 14 14 LYS A 1323 ARG A 1327 5 5
HELIX 15 15 SER A 1329 THR A 1343 1 15
SHEET 1 AA 5 LEU A1076 ARG A1086 0
SHEET 2 AA 5 CYS A1091 LEU A1097 -1 O VAL A1092 N ILE A1084
SHEET 3 AA 5 ILE A1105 LYS A1110 -1 O ILE A1105 N LEU A1097
SHEET 4 AA 5 LEU A1154 PRO A1158 -1 O VAL A1155 N LYS A1110
SHEET 5 AA 5 GLY A1144 CYS A1146 -1 O GLY A1144 N VAL A1156
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 12 ILE A1084 ALA A1108 PRO A1158 MET A1160
SITE 2 AC1 12 ASP A1164 ASN A1167 ARG A1208 MET A1211
SITE 3 AC1 12 ALA A1221 ASP A1222 ALA A1226 TYR A1230
CRYST1 76.857 94.127 46.418 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 0.013011 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010624 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021543 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
