HEADER TRANSFERASE 21-DEC-18 6NG0
TITLE CRYSTAL STRUCTURE OF HPK1 KINASE DOMAIN T165E,S171E PHOSPHOMIMETIC
TITLE 2 MUTANT IN COMPLEX WITH SUNITINIB IN THE INACTIVE STATE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE KINASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HEMATOPOIETIC PROGENITOR KINASE,MAPK/ERK KINASE KINASE
COMPND 5 KINASE 1,MEKKK 1;
COMPND 6 EC: 2.7.11.1;
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: MAP4K1, HPK1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS KINASE, 3D DOMAIN SWAP, INACTIVE STATE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.JOHNSON,M.MCTIGUE,C.N.CRONIN
REVDAT 5 13-MAR-24 6NG0 1 COMPND HETNAM
REVDAT 4 26-JUN-19 6NG0 1 JRNL
REVDAT 3 19-JUN-19 6NG0 1 JRNL
REVDAT 2 08-MAY-19 6NG0 1 JRNL
REVDAT 1 01-MAY-19 6NG0 0
JRNL AUTH E.JOHNSON,M.MCTIGUE,R.A.GALLEGO,T.W.JOHNSON,S.TIMOFEEVSKI,
JRNL AUTH 2 M.MAESTRE,T.S.FISHER,R.KANIA,S.SAWASDIKOSOL,S.BURAKOFF,
JRNL AUTH 3 C.N.CRONIN
JRNL TITL MULTIPLE CONFORMATIONAL STATES OF THE HPK1 KINASE DOMAIN IN
JRNL TITL 2 COMPLEX WITH SUNITINIB REVEAL THE STRUCTURAL CHANGES
JRNL TITL 3 ACCOMPANYING HPK1 TRANS-REGULATION.
JRNL REF J.BIOL.CHEM. V. 294 9029 2019
JRNL REFN ESSN 1083-351X
JRNL PMID 31018963
JRNL DOI 10.1074/JBC.AC119.007466
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 42208
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 2160
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.06
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.55
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 845
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2200
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 806
REMARK 3 BIN R VALUE (WORKING SET) : 0.2198
REMARK 3 BIN FREE R VALUE : 0.2239
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.62
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 39
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4336
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 320
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.10790
REMARK 3 B22 (A**2) : -0.59080
REMARK 3 B33 (A**2) : 8.69870
REMARK 3 B12 (A**2) : -7.99280
REMARK 3 B13 (A**2) : 6.08210
REMARK 3 B23 (A**2) : -8.13660
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.280
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.185
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.156
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.186
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.158
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4486 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6076 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1535 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 787 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4486 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 578 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 5354 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.99
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.76
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.71
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6NG0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1000236783.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-AUG-18
REMARK 200 TEMPERATURE (KELVIN) : 180
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43684
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.026
REMARK 200 RESOLUTION RANGE LOW (A) : 60.176
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.03600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.50100
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 NL PROTEIN (15 MG/ML) PLUS 300 NL
REMARK 280 RESERVOIR SOLUTION (0.1 M TRIS, PH 8.0, 17.5 % 1,6-HEXANEDIOL,
REMARK 280 10 MM MAGNESIUM SULFATE, 24 MM BARIUM ACETATE), VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 286.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: 3700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 VAL A 3
REMARK 465 VAL A 4
REMARK 465 ASP A 5
REMARK 465 GLY A 26
REMARK 465 THR A 27
REMARK 465 TYR A 28
REMARK 465 GLN A 161
REMARK 465 ILE A 162
REMARK 465 GLY A 163
REMARK 465 ALA A 164
REMARK 465 GLU A 165
REMARK 465 ILE A 303
REMARK 465 GLU A 304
REMARK 465 ASP A 305
REMARK 465 GLU A 306
REMARK 465 GLU A 307
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 VAL B 3
REMARK 465 VAL B 4
REMARK 465 ASP B 5
REMARK 465 PRO B 6
REMARK 465 GLY B 26
REMARK 465 THR B 27
REMARK 465 TYR B 28
REMARK 465 GLY B 29
REMARK 465 MET B 50
REMARK 465 GLU B 51
REMARK 465 PRO B 52
REMARK 465 ASP B 53
REMARK 465 PRO B 294
REMARK 465 GLY B 295
REMARK 465 LYS B 296
REMARK 465 GLY B 297
REMARK 465 PRO B 298
REMARK 465 SER B 299
REMARK 465 ILE B 300
REMARK 465 GLY B 301
REMARK 465 ASP B 302
REMARK 465 ILE B 303
REMARK 465 GLU B 304
REMARK 465 ASP B 305
REMARK 465 GLU B 306
REMARK 465 GLU B 307
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 53 CG OD1 OD2
REMARK 470 ILE A 158 CG1 CG2 CD1
REMARK 470 SER A 159 OG
REMARK 470 LEU A 166 CG CD1 CD2
REMARK 470 ARG A 168 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 169 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 170 CG CD1 CD2
REMARK 470 GLU A 171 CG CD OE1 OE2
REMARK 470 PHE A 172 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 222 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 292 CG CD CE NZ
REMARK 470 ASN A 293 CG OD1 ND2
REMARK 470 LYS A 296 CG CD CE NZ
REMARK 470 ASP B 7 CG OD1 OD2
REMARK 470 ILE B 8 CG1 CG2 CD1
REMARK 470 ASN B 10 CG OD1 ND2
REMARK 470 ARG B 11 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 22 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 30 CG CD OE1 OE2
REMARK 470 LYS B 49 CG CD CE NZ
REMARK 470 ASP B 54 CG OD1 OD2
REMARK 470 ASP B 55 CG OD1 OD2
REMARK 470 VAL B 56 CG1 CG2
REMARK 470 SER B 57 OG
REMARK 470 LEU B 59 CG CD1 CD2
REMARK 470 GLN B 60 CG CD OE1 NE2
REMARK 470 LEU B 82 CG CD1 CD2
REMARK 470 TRP B 83 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 83 CZ3 CH2
REMARK 470 LEU B 84 CG CD1 CD2
REMARK 470 GLN B 85 CG CD OE1 NE2
REMARK 470 GLU B 165 CG CD OE1 OE2
REMARK 470 ARG B 168 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 169 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 171 CG CD OE1 OE2
REMARK 470 PHE B 172 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE B 173 CG1 CG2 CD1
REMARK 470 LYS B 292 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 SER A 108 141.39 -39.84
REMARK 500 ARG A 136 -8.02 77.74
REMARK 500 LYS A 240 -74.47 -106.43
REMARK 500 LEU A 255 38.73 -92.55
REMARK 500 ASP B 12 129.22 -39.20
REMARK 500 LEU B 20 -165.85 -122.51
REMARK 500 GLN B 85 -0.29 66.81
REMARK 500 ARG B 136 -7.21 68.34
REMARK 500 ASP B 137 44.79 -141.90
REMARK 500 LYS B 189 23.99 -146.59
REMARK 500 LEU B 255 44.11 -91.96
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 B49 A 9000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B49 B 9000
DBREF 6NG0 A 1 307 UNP Q92918 M4K1_HUMAN 1 307
DBREF 6NG0 B 1 307 UNP Q92918 M4K1_HUMAN 1 307
SEQADV 6NG0 GLY A -1 UNP Q92918 EXPRESSION TAG
SEQADV 6NG0 SER A 0 UNP Q92918 EXPRESSION TAG
SEQADV 6NG0 GLU A 165 UNP Q92918 THR 165 ENGINEERED MUTATION
SEQADV 6NG0 GLU A 171 UNP Q92918 SER 171 ENGINEERED MUTATION
SEQADV 6NG0 GLY B -1 UNP Q92918 EXPRESSION TAG
SEQADV 6NG0 SER B 0 UNP Q92918 EXPRESSION TAG
SEQADV 6NG0 GLU B 165 UNP Q92918 THR 165 ENGINEERED MUTATION
SEQADV 6NG0 GLU B 171 UNP Q92918 SER 171 ENGINEERED MUTATION
SEQRES 1 A 309 GLY SER MET ASP VAL VAL ASP PRO ASP ILE PHE ASN ARG
SEQRES 2 A 309 ASP PRO ARG ASP HIS TYR ASP LEU LEU GLN ARG LEU GLY
SEQRES 3 A 309 GLY GLY THR TYR GLY GLU VAL PHE LYS ALA ARG ASP LYS
SEQRES 4 A 309 VAL SER GLY ASP LEU VAL ALA LEU LYS MET VAL LYS MET
SEQRES 5 A 309 GLU PRO ASP ASP ASP VAL SER THR LEU GLN LYS GLU ILE
SEQRES 6 A 309 LEU ILE LEU LYS THR CYS ARG HIS ALA ASN ILE VAL ALA
SEQRES 7 A 309 TYR HIS GLY SER TYR LEU TRP LEU GLN LYS LEU TRP ILE
SEQRES 8 A 309 CYS MET GLU PHE CYS GLY ALA GLY SER LEU GLN ASP ILE
SEQRES 9 A 309 TYR GLN VAL THR GLY SER LEU SER GLU LEU GLN ILE SER
SEQRES 10 A 309 TYR VAL CYS ARG GLU VAL LEU GLN GLY LEU ALA TYR LEU
SEQRES 11 A 309 HIS SER GLN LYS LYS ILE HIS ARG ASP ILE LYS GLY ALA
SEQRES 12 A 309 ASN ILE LEU ILE ASN ASP ALA GLY GLU VAL ARG LEU ALA
SEQRES 13 A 309 ASP PHE GLY ILE SER ALA GLN ILE GLY ALA GLU LEU ALA
SEQRES 14 A 309 ARG ARG LEU GLU PHE ILE GLY THR PRO TYR TRP MET ALA
SEQRES 15 A 309 PRO GLU VAL ALA ALA VAL ALA LEU LYS GLY GLY TYR ASN
SEQRES 16 A 309 GLU LEU CYS ASP ILE TRP SER LEU GLY ILE THR ALA ILE
SEQRES 17 A 309 GLU LEU ALA GLU LEU GLN PRO PRO LEU PHE ASP VAL HIS
SEQRES 18 A 309 PRO LEU ARG VAL LEU PHE LEU MET THR LYS SER GLY TYR
SEQRES 19 A 309 GLN PRO PRO ARG LEU LYS GLU LYS GLY LYS TRP SER ALA
SEQRES 20 A 309 ALA PHE HIS ASN PHE ILE LYS VAL THR LEU THR LYS SER
SEQRES 21 A 309 PRO LYS LYS ARG PRO SER ALA THR LYS MET LEU SER HIS
SEQRES 22 A 309 GLN LEU VAL SER GLN PRO GLY LEU ASN ARG GLY LEU ILE
SEQRES 23 A 309 LEU ASP LEU LEU ASP LYS LEU LYS ASN PRO GLY LYS GLY
SEQRES 24 A 309 PRO SER ILE GLY ASP ILE GLU ASP GLU GLU
SEQRES 1 B 309 GLY SER MET ASP VAL VAL ASP PRO ASP ILE PHE ASN ARG
SEQRES 2 B 309 ASP PRO ARG ASP HIS TYR ASP LEU LEU GLN ARG LEU GLY
SEQRES 3 B 309 GLY GLY THR TYR GLY GLU VAL PHE LYS ALA ARG ASP LYS
SEQRES 4 B 309 VAL SER GLY ASP LEU VAL ALA LEU LYS MET VAL LYS MET
SEQRES 5 B 309 GLU PRO ASP ASP ASP VAL SER THR LEU GLN LYS GLU ILE
SEQRES 6 B 309 LEU ILE LEU LYS THR CYS ARG HIS ALA ASN ILE VAL ALA
SEQRES 7 B 309 TYR HIS GLY SER TYR LEU TRP LEU GLN LYS LEU TRP ILE
SEQRES 8 B 309 CYS MET GLU PHE CYS GLY ALA GLY SER LEU GLN ASP ILE
SEQRES 9 B 309 TYR GLN VAL THR GLY SER LEU SER GLU LEU GLN ILE SER
SEQRES 10 B 309 TYR VAL CYS ARG GLU VAL LEU GLN GLY LEU ALA TYR LEU
SEQRES 11 B 309 HIS SER GLN LYS LYS ILE HIS ARG ASP ILE LYS GLY ALA
SEQRES 12 B 309 ASN ILE LEU ILE ASN ASP ALA GLY GLU VAL ARG LEU ALA
SEQRES 13 B 309 ASP PHE GLY ILE SER ALA GLN ILE GLY ALA GLU LEU ALA
SEQRES 14 B 309 ARG ARG LEU GLU PHE ILE GLY THR PRO TYR TRP MET ALA
SEQRES 15 B 309 PRO GLU VAL ALA ALA VAL ALA LEU LYS GLY GLY TYR ASN
SEQRES 16 B 309 GLU LEU CYS ASP ILE TRP SER LEU GLY ILE THR ALA ILE
SEQRES 17 B 309 GLU LEU ALA GLU LEU GLN PRO PRO LEU PHE ASP VAL HIS
SEQRES 18 B 309 PRO LEU ARG VAL LEU PHE LEU MET THR LYS SER GLY TYR
SEQRES 19 B 309 GLN PRO PRO ARG LEU LYS GLU LYS GLY LYS TRP SER ALA
SEQRES 20 B 309 ALA PHE HIS ASN PHE ILE LYS VAL THR LEU THR LYS SER
SEQRES 21 B 309 PRO LYS LYS ARG PRO SER ALA THR LYS MET LEU SER HIS
SEQRES 22 B 309 GLN LEU VAL SER GLN PRO GLY LEU ASN ARG GLY LEU ILE
SEQRES 23 B 309 LEU ASP LEU LEU ASP LYS LEU LYS ASN PRO GLY LYS GLY
SEQRES 24 B 309 PRO SER ILE GLY ASP ILE GLU ASP GLU GLU
HET B49 A9000 29
HET B49 B9000 29
HETNAM B49 N-[2-(DIETHYLAMINO)ETHYL]-5-[(Z)-(5-FLUORO-2-OXO-1,2-
HETNAM 2 B49 DIHYDRO-3H-INDOL-3-YLIDENE)METHYL]-2,4-DIMETHYL-1H-
HETNAM 3 B49 PYRROLE-3-CARBO XAMIDE
HETSYN B49 SUNITINIB
FORMUL 3 B49 2(C22 H27 F N4 O2)
FORMUL 5 HOH *320(H2 O)
HELIX 1 AA1 ASP A 12 ASP A 15 5 4
HELIX 2 AA2 ASP A 55 THR A 68 1 14
HELIX 3 AA3 SER A 98 GLY A 107 1 10
HELIX 4 AA4 SER A 110 GLN A 131 1 22
HELIX 5 AA5 LYS A 139 ALA A 141 5 3
HELIX 6 AA6 ARG A 168 ILE A 173 1 6
HELIX 7 AA7 ALA A 180 GLY A 190 1 11
HELIX 8 AA8 LEU A 195 LEU A 211 1 17
HELIX 9 AA9 HIS A 219 LYS A 229 1 11
HELIX 10 AB1 SER A 244 LEU A 255 1 12
HELIX 11 AB2 SER A 264 LEU A 269 1 6
HELIX 12 AB3 HIS A 271 GLN A 276 1 6
HELIX 13 AB4 ARG A 281 ASN A 293 1 13
HELIX 14 AB5 ASP B 12 ASP B 15 5 4
HELIX 15 AB6 ASP B 55 THR B 68 1 14
HELIX 16 AB7 SER B 98 GLY B 107 1 10
HELIX 17 AB8 SER B 110 GLN B 131 1 22
HELIX 18 AB9 LYS B 139 ALA B 141 5 3
HELIX 19 AC1 ILE B 158 PHE B 172 1 15
HELIX 20 AC2 ALA B 180 GLY B 190 1 11
HELIX 21 AC3 LEU B 195 LEU B 211 1 17
HELIX 22 AC4 HIS B 219 THR B 228 1 10
HELIX 23 AC5 GLU B 239 TRP B 243 5 5
HELIX 24 AC6 SER B 244 LEU B 255 1 12
HELIX 25 AC7 SER B 264 LEU B 269 1 6
HELIX 26 AC8 HIS B 271 GLN B 276 1 6
HELIX 27 AC9 ARG B 281 ASN B 293 1 13
SHEET 1 AA1 6 ILE A 8 PHE A 9 0
SHEET 2 AA1 6 TYR A 77 LEU A 82 1 O SER A 80 N PHE A 9
SHEET 3 AA1 6 LYS A 86 GLU A 92 -1 O CYS A 90 N GLY A 79
SHEET 4 AA1 6 LEU A 42 LYS A 49 -1 N LYS A 46 O ILE A 89
SHEET 5 AA1 6 GLU A 30 ASP A 36 -1 N GLU A 30 O MET A 47
SHEET 6 AA1 6 TYR A 17 GLY A 24 -1 N GLY A 24 O VAL A 31
SHEET 1 AA2 2 ILE A 143 ILE A 145 0
SHEET 2 AA2 2 VAL A 151 LEU A 153 -1 O ARG A 152 N LEU A 144
SHEET 1 AA3 6 ILE B 8 PHE B 9 0
SHEET 2 AA3 6 TYR B 77 TRP B 83 1 O LEU B 82 N PHE B 9
SHEET 3 AA3 6 LYS B 86 GLU B 92 -1 O CYS B 90 N GLY B 79
SHEET 4 AA3 6 LEU B 42 VAL B 48 -1 N VAL B 48 O LEU B 87
SHEET 5 AA3 6 VAL B 31 ASP B 36 -1 N PHE B 32 O LEU B 45
SHEET 6 AA3 6 TYR B 17 GLY B 24 -1 N LEU B 23 O VAL B 31
SHEET 1 AA4 2 ILE B 143 ILE B 145 0
SHEET 2 AA4 2 VAL B 151 LEU B 153 -1 O ARG B 152 N LEU B 144
SITE 1 AC1 12 LEU A 23 ALA A 44 MET A 91 GLU A 92
SITE 2 AC1 12 PHE A 93 CYS A 94 GLY A 95 GLY A 97
SITE 3 AC1 12 ASP A 101 LEU A 144 ALA A 154 ASP A 155
SITE 1 AC2 13 LEU B 23 ALA B 44 MET B 91 GLU B 92
SITE 2 AC2 13 PHE B 93 CYS B 94 GLY B 95 GLY B 97
SITE 3 AC2 13 ASP B 101 LEU B 144 ASP B 155 PHE B 156
SITE 4 AC2 13 HOH B9139
CRYST1 55.810 58.920 60.930 82.44 82.31 64.34 P 1 2
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 0.017918 -0.008608 -0.001716 0.00000
SCALE2 0.000000 0.018829 -0.001557 0.00000
SCALE3 0.000000 0.000000 0.016618 0.00000
(ATOM LINES ARE NOT SHOWN.)
END