HEADER TRANSFERASE/TRANSFERASE INHIBITOR 24-NOV-15 5EYD
TITLE CRYSTAL STRUCTURE OF C-MET IN COMPLEX WITH AMG 337
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATOCYTE GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1048-1351;
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 GENE: MET;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS PHOSPHOTRANSFERASE, INHIBITOR, CANCER, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.WHITTINGTON,A.M.LONG
REVDAT 4 27-SEP-23 5EYD 1 JRNL REMARK
REVDAT 3 06-APR-16 5EYD 1 JRNL
REVDAT 2 17-FEB-16 5EYD 1 JRNL
REVDAT 1 10-FEB-16 5EYD 0
JRNL AUTH A.A.BOEZIO,K.W.COPELAND,K.REX,B.K ALBRECHT,D.BAUER,
JRNL AUTH 2 S.F.BELLON,C.BOEZIO,M.A.BROOME,D.CHOQUETTE,A.COXON,
JRNL AUTH 3 I.DUSSAULT,S.HIRAI,R.LEWIS,M.H.LIN,J.LOHMAN,J.LIU,
JRNL AUTH 4 E.A.PETERSON,M.POTASHMAN,R.SHIMANOVICH,Y.TEFFERA,
JRNL AUTH 5 D.A.WHITTINGTON,K.R.VAIDA,J.C.HARMANGE
JRNL TITL DISCOVERY OF
JRNL TITL 2 (R)-6-(1-(8-FLUORO-6-(1-METHYL-1H-PYRAZOL-4-YL)-[1,2,
JRNL TITL 3 4]TRIAZOLO[4,3-A]PYRIDIN-3-YL)ETHYL)-3-(2-METHOXYETHOXY)-1,
JRNL TITL 4 6-NAPHTHYRIDIN-5(6H)-ONE (AMG 337), A POTENT AND SELECTIVE
JRNL TITL 5 INHIBITOR OF MET WITH HIGH UNBOUND TARGET COVERAGE AND
JRNL TITL 6 ROBUST IN VIVO ANTITUMOR ACTIVITY.
JRNL REF J.MED.CHEM. V. 59 2328 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 26812066
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01716
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.1
REMARK 3 NUMBER OF REFLECTIONS : 20066
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1098
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 665
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 38.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.3810
REMARK 3 BIN FREE R VALUE SET COUNT : 28
REMARK 3 BIN FREE R VALUE : 0.4970
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 : 34
REMARK 3 SOLVENT ATOMS : 247
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.53000
REMARK 3 B22 (A**2) : 1.85000
REMARK 3 B33 (A**2) : -1.32000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.201
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.179
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.115
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.817
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2414 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1647 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3272 ; 1.124 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3995 ; 0.849 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 288 ; 5.477 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 102 ;31.888 ;23.137
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 417 ;12.869 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;12.818 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 361 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2613 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 493 ; 0.001 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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 : MASK
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5EYD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215696.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : VARIMAX HR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21211
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
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 (%) : 83.1
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 44.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.34500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 4XMO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 4000, 3% (V/V) ETHANOL, 6%
REMARK 280 (V/V) ISOPROPANOL, 40 MM BETA-MERCAPTOETHANOL, 100 MM HEPES (PH
REMARK 280 7.8), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 20.92400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.17250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.67200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.17250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.92400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 21.67200
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 GLN A 1048
REMARK 465 ASN A 1049
REMARK 465 THR A 1050
REMARK 465 VAL A 1051
REMARK 465 LEU A 1098
REMARK 465 ASP A 1099
REMARK 465 ASN A 1100
REMARK 465 ASP A 1101
REMARK 465 GLY A 1102
REMARK 465 LYS A 1103
REMARK 465 GLU A 1150
REMARK 465 GLY A 1151
REMARK 465 TYR A 1349
REMARK 465 VAL 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 465 HIS A 1356
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 -19.82 78.63
REMARK 500 ASP A1204 41.20 -141.47
REMARK 500 ALA A1221 -156.55 -123.82
REMARK 500 GLN A1258 19.12 56.48
REMARK 500 THR A1289 -112.51 39.42
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 A1747 DISTANCE = 6.47 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5T1 A 1401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5EYC RELATED DB: PDB
DBREF 5EYD A 1048 1351 UNP P08581 MET_HUMAN 1048 1351
SEQADV 5EYD HIS A 1352 UNP P08581 EXPRESSION TAG
SEQADV 5EYD HIS A 1353 UNP P08581 EXPRESSION TAG
SEQADV 5EYD HIS A 1354 UNP P08581 EXPRESSION TAG
SEQADV 5EYD HIS A 1355 UNP P08581 EXPRESSION TAG
SEQADV 5EYD HIS A 1356 UNP P08581 EXPRESSION TAG
SEQRES 1 A 309 GLN ASN THR VAL HIS ILE ASP LEU SER ALA LEU ASN PRO
SEQRES 2 A 309 GLU LEU VAL GLN ALA VAL GLN HIS VAL VAL ILE GLY PRO
SEQRES 3 A 309 SER SER LEU ILE VAL HIS PHE ASN GLU VAL ILE GLY ARG
SEQRES 4 A 309 GLY HIS PHE GLY CYS VAL TYR HIS GLY THR LEU LEU ASP
SEQRES 5 A 309 ASN ASP GLY LYS LYS ILE HIS CYS ALA VAL LYS SER LEU
SEQRES 6 A 309 ASN ARG ILE THR ASP ILE GLY GLU VAL SER GLN PHE LEU
SEQRES 7 A 309 THR GLU GLY ILE ILE MET LYS ASP PHE SER HIS PRO ASN
SEQRES 8 A 309 VAL LEU SER LEU LEU GLY ILE CYS LEU ARG SER GLU GLY
SEQRES 9 A 309 SER PRO LEU VAL VAL LEU PRO TYR MET LYS HIS GLY ASP
SEQRES 10 A 309 LEU ARG ASN PHE ILE ARG ASN GLU THR HIS ASN PRO THR
SEQRES 11 A 309 VAL LYS ASP LEU ILE GLY PHE GLY LEU GLN VAL ALA LYS
SEQRES 12 A 309 GLY MET LYS TYR LEU ALA SER LYS LYS PHE VAL HIS ARG
SEQRES 13 A 309 ASP LEU ALA ALA ARG ASN CYS MET LEU ASP GLU LYS PHE
SEQRES 14 A 309 THR VAL LYS VAL ALA ASP PHE GLY LEU ALA ARG ASP MET
SEQRES 15 A 309 TYR ASP LYS GLU TYR TYR SER VAL HIS ASN LYS THR GLY
SEQRES 16 A 309 ALA LYS LEU PRO VAL LYS TRP MET ALA LEU GLU SER LEU
SEQRES 17 A 309 GLN THR GLN LYS PHE THR THR LYS SER ASP VAL TRP SER
SEQRES 18 A 309 PHE GLY VAL LEU LEU TRP GLU LEU MET THR ARG GLY ALA
SEQRES 19 A 309 PRO PRO TYR PRO ASP VAL ASN THR PHE ASP ILE THR VAL
SEQRES 20 A 309 TYR LEU LEU GLN GLY ARG ARG LEU LEU GLN PRO GLU TYR
SEQRES 21 A 309 CYS PRO ASP PRO LEU TYR GLU VAL MET LEU LYS CYS TRP
SEQRES 22 A 309 HIS PRO LYS ALA GLU MET ARG PRO SER PHE SER GLU LEU
SEQRES 23 A 309 VAL SER ARG ILE SER ALA ILE PHE SER THR PHE ILE GLY
SEQRES 24 A 309 GLU HIS TYR VAL HIS HIS HIS HIS HIS HIS
HET 5T1 A1401 34
HETNAM 5T1 6-[(1~{R})-1-[8-FLUORANYL-6-(1-METHYLPYRAZOL-4-YL)-[1,
HETNAM 2 5T1 2,4]TRIAZOLO[4,3-A]PYRIDIN-3-YL]ETHYL]-3-(2-
HETNAM 3 5T1 METHOXYETHOXY)-1,6-NAPHTHYRIDIN-5-ONE
FORMUL 2 5T1 C23 H22 F N7 O3
FORMUL 3 HOH *247(H2 O)
HELIX 1 AA1 ASP A 1054 LEU A 1058 5 5
HELIX 2 AA2 ASN A 1059 GLN A 1064 5 6
HELIX 3 AA3 ALA A 1065 VAL A 1069 1 5
HELIX 4 AA4 GLY A 1072 LEU A 1076 5 5
HELIX 5 AA5 GLU A 1120 PHE A 1134 1 15
HELIX 6 AA6 ASP A 1164 ASN A 1171 1 8
HELIX 7 AA7 THR A 1177 LYS A 1198 1 22
HELIX 8 AA8 ALA A 1206 ARG A 1208 5 3
HELIX 9 AA9 PHE A 1223 ARG A 1227 5 5
HELIX 10 AB1 ASP A 1231 TYR A 1235 5 5
HELIX 11 AB2 PRO A 1246 MET A 1250 5 5
HELIX 12 AB3 ALA A 1251 GLN A 1258 1 8
HELIX 13 AB4 THR A 1261 THR A 1278 1 18
HELIX 14 AB5 ASN A 1288 PHE A 1290 5 3
HELIX 15 AB6 ASP A 1291 GLN A 1298 1 8
HELIX 16 AB7 PRO A 1309 TRP A 1320 1 12
HELIX 17 AB8 LYS A 1323 ARG A 1327 5 5
HELIX 18 AB9 SER A 1329 THR A 1343 1 15
SHEET 1 AA1 6 VAL A1070 ILE A1071 0
SHEET 2 AA1 6 GLY A1144 CYS A1146 1 O ILE A1145 N ILE A1071
SHEET 3 AA1 6 LEU A1154 PRO A1158 -1 O LEU A1154 N CYS A1146
SHEET 4 AA1 6 HIS A1106 LYS A1110 -1 N ALA A1108 O LEU A1157
SHEET 5 AA1 6 CYS A1091 THR A1096 -1 N TYR A1093 O VAL A1109
SHEET 6 AA1 6 ILE A1077 ARG A1086 -1 N ILE A1084 O VAL A1092
SHEET 1 AA2 2 CYS A1210 LEU A1212 0
SHEET 2 AA2 2 VAL A1218 VAL A1220 -1 O LYS A1219 N MET A1211
SHEET 1 AA3 2 SER A1236 VAL A1237 0
SHEET 2 AA3 2 LYS A1244 LEU A1245 -1 O LEU A1245 N SER A1236
SITE 1 AC1 17 ILE A1084 VAL A1092 ALA A1108 LEU A1157
SITE 2 AC1 17 PRO A1158 MET A1160 GLY A1163 ASP A1164
SITE 3 AC1 17 ASN A1167 ARG A1208 ASN A1209 MET A1211
SITE 4 AC1 17 ALA A1221 ASP A1222 TYR A1230 HOH A1639
SITE 5 AC1 17 HOH A1644
CRYST1 41.848 43.344 158.345 90.00 90.00 90.00 P 21 21 21 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 0.023896 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023071 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006315 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
