HEADER SIGNALING PROTEIN 21-DEC-18 6NFZ
TITLE CRYSTAL STRUCTURE OF DIPHOSPHORYLATED HPK1 KINASE DOMAIN IN COMPLEX
TITLE 2 WITH SUNITINIB IN THE ACTIVE 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_CELL_LINE: SF21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS KINASE, ACTIVE STATE, DIMER, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.JOHNSON,M.MCTIGUE,C.N.CRONIN
REVDAT 4 26-JUN-19 6NFZ 1 JRNL
REVDAT 3 19-JUN-19 6NFZ 1 JRNL
REVDAT 2 08-MAY-19 6NFZ 1 JRNL
REVDAT 1 01-MAY-19 6NFZ 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. 2.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 14215
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 707
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 37.5200 - 5.0678 1.00 2788 137 0.1838 0.2225
REMARK 3 2 5.0678 - 4.0240 1.00 2699 151 0.1776 0.2048
REMARK 3 3 4.0240 - 3.5158 1.00 2701 132 0.2112 0.2620
REMARK 3 4 3.5158 - 3.1945 1.00 2685 133 0.2533 0.3088
REMARK 3 5 3.1945 - 2.9656 1.00 2635 154 0.2791 0.3449
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) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.410
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 76.61
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.005 4525
REMARK 3 ANGLE : 0.958 6116
REMARK 3 CHIRALITY : 0.035 674
REMARK 3 PLANARITY : 0.003 762
REMARK 3 DIHEDRAL : 18.818 1705
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6NFZ 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_1000236778.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 180
REMARK 200 PH : 7.5
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14226
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.966
REMARK 200 RESOLUTION RANGE LOW (A) : 99.995
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.00
REMARK 200 R MERGE (I) : 0.19600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
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 (%): 49.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM FLUORIDE, 20% PEG 3350,
REMARK 280 100NL WELL + 100NL PROTEIN @ 22MG/ML, PH 7.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 286.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 74.96600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.28164
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 52.25133
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 74.96600
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 43.28164
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 52.25133
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 74.96600
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 43.28164
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 52.25133
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 74.96600
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 43.28164
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 52.25133
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 74.96600
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 43.28164
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 52.25133
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 74.96600
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 43.28164
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 52.25133
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 86.56328
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 104.50267
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 86.56328
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 104.50267
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 86.56328
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 104.50267
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 86.56328
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 104.50267
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 86.56328
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 104.50267
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 86.56328
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 104.50267
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 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 PRO A 6
REMARK 465 GLY A 25
REMARK 465 GLY A 26
REMARK 465 LYS A 49
REMARK 465 MET A 50
REMARK 465 GLU A 51
REMARK 465 PRO A 52
REMARK 465 ASP A 53
REMARK 465 ASP A 54
REMARK 465 ASP A 55
REMARK 465 VAL A 56
REMARK 465 SER A 57
REMARK 465 LEU A 82
REMARK 465 TRP A 83
REMARK 465 LEU A 84
REMARK 465 GLN A 85
REMARK 465 LYS A 86
REMARK 465 ASN A 293
REMARK 465 PRO A 294
REMARK 465 GLY A 295
REMARK 465 LYS A 296
REMARK 465 GLY A 297
REMARK 465 PRO A 298
REMARK 465 SER A 299
REMARK 465 ILE A 300
REMARK 465 GLY A 301
REMARK 465 ASP A 302
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 GLY B 26
REMARK 465 THR B 27
REMARK 465 TYR B 28
REMARK 465 ASP B 54
REMARK 465 ASP B 55
REMARK 465 VAL B 56
REMARK 465 SER B 57
REMARK 465 THR B 58
REMARK 465 ALA B 164
REMARK 465 TPO B 165
REMARK 465 LEU B 166
REMARK 465 ASN B 293
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 ARG A 22 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 28 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 37 CG CD CE NZ
REMARK 470 LYS A 46 CG CD CE NZ
REMARK 470 MET A 47 CG SD CE
REMARK 470 THR A 58 OG1 CG2
REMARK 470 LYS A 61 CG CD CE NZ
REMARK 470 LEU A 87 CG CD1 CD2
REMARK 470 ASP B 53 CG OD1 OD2
REMARK 470 LEU B 59 CG CD1 CD2
REMARK 470 GLN B 60 CG CD OE1 NE2
REMARK 470 LYS B 61 CG CD CE NZ
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 HB3 ASP A 101 H21 B49 A 401 1.31
REMARK 500 HA3 GLY A 29 O MET A 47 1.43
REMARK 500 H LEU B 20 O LYS B 33 1.47
REMARK 500 O ASP A 137 HD22 ASN A 142 1.55
REMARK 500 OD1 ASP B 18 HZ3 LYS B 37 1.55
REMARK 500 HD21 ASN B 146 OE1 GLU B 150 1.58
REMARK 500 O PHE B 156 HG SER B 159 1.58
REMARK 500 O HIS A 271 HG SER A 275 1.59
REMARK 500 CA GLY A 29 O MET A 47 2.13
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 TYR A 17 -159.29 -131.06
REMARK 500 TYR A 28 -124.11 63.11
REMARK 500 ARG A 136 -9.45 72.34
REMARK 500 ASP A 155 80.12 58.53
REMARK 500 PHE A 156 31.70 -96.32
REMARK 500 LEU A 211 -3.86 66.35
REMARK 500 LEU A 255 51.10 -101.00
REMARK 500 ARG B 70 72.38 -160.05
REMARK 500 ASP B 137 35.62 -144.70
REMARK 500 ASN B 193 -159.87 -143.26
REMARK 500 LEU B 211 -5.29 67.46
REMARK 500 LYS B 238 -73.15 -71.29
REMARK 500 LEU B 291 21.35 -79.77
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B49 B 9001
DBREF 6NFZ A 1 307 UNP Q92918 M4K1_HUMAN 1 307
DBREF 6NFZ B 1 307 UNP Q92918 M4K1_HUMAN 1 307
SEQADV 6NFZ GLY A -1 UNP Q92918 EXPRESSION TAG
SEQADV 6NFZ SER A 0 UNP Q92918 EXPRESSION TAG
SEQADV 6NFZ GLY B -1 UNP Q92918 EXPRESSION TAG
SEQADV 6NFZ SER B 0 UNP Q92918 EXPRESSION TAG
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 TPO LEU ALA
SEQRES 14 A 309 ARG ARG LEU SEP 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 TPO LEU ALA
SEQRES 14 B 309 ARG ARG LEU SEP 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
MODRES 6NFZ TPO A 165 THR MODIFIED RESIDUE
MODRES 6NFZ SEP A 171 SER MODIFIED RESIDUE
MODRES 6NFZ SEP B 171 SER MODIFIED RESIDUE
HET TPO A 165 16
HET SEP A 171 14
HET SEP B 171 13
HET B49 A 401 56
HET B49 B9001 56
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
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-CARBOXAMIDE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
HETSYN B49 SUNITINIB
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 3 B49 2(C22 H27 F N4 O2)
HELIX 1 AA1 ASP A 12 HIS A 16 5 5
HELIX 2 AA2 LYS A 61 LYS A 67 1 7
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 THR A 175 MET A 179 5 5
HELIX 7 AA7 ALA A 180 ALA A 185 1 6
HELIX 8 AA8 GLU A 194 LEU A 211 1 18
HELIX 9 AA9 HIS A 219 MET A 227 1 9
HELIX 10 AB1 SER A 244 LEU A 255 1 12
HELIX 11 AB2 SER A 258 ARG A 262 5 5
HELIX 12 AB3 SER A 264 LEU A 269 1 6
HELIX 13 AB4 ARG A 281 LYS A 292 1 12
HELIX 14 AB5 ASP B 12 ASP B 15 5 4
HELIX 15 AB6 GLN B 60 THR B 68 1 9
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 THR B 175 MET B 179 5 5
HELIX 20 AC2 ALA B 180 ALA B 185 1 6
HELIX 21 AC3 ALA B 185 GLY B 190 1 6
HELIX 22 AC4 LEU B 195 LEU B 211 1 17
HELIX 23 AC5 HIS B 219 LYS B 229 1 11
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 LYS B 290 1 10
SHEET 1 AA1 5 GLN A 21 LEU A 23 0
SHEET 2 AA1 5 VAL A 31 ARG A 35 -1 O VAL A 31 N LEU A 23
SHEET 3 AA1 5 LEU A 42 MET A 47 -1 O VAL A 43 N ALA A 34
SHEET 4 AA1 5 TRP A 88 GLU A 92 -1 O MET A 91 N ALA A 44
SHEET 5 AA1 5 TYR A 77 SER A 80 -1 N GLY A 79 O CYS A 90
SHEET 1 AA2 2 LYS A 133 ILE A 134 0
SHEET 2 AA2 2 ALA A 160 GLN A 161 -1 O ALA A 160 N ILE A 134
SHEET 1 AA3 2 ILE A 143 ILE A 145 0
SHEET 2 AA3 2 VAL A 151 LEU A 153 -1 O ARG A 152 N LEU A 144
SHEET 1 AA4 5 TYR B 17 ARG B 22 0
SHEET 2 AA4 5 GLU B 30 ASP B 36 -1 O LYS B 33 N LEU B 20
SHEET 3 AA4 5 LEU B 42 LYS B 49 -1 O MET B 47 N GLU B 30
SHEET 4 AA4 5 LYS B 86 MET B 91 -1 O MET B 91 N ALA B 44
SHEET 5 AA4 5 TYR B 77 TRP B 83 -1 N TYR B 81 O TRP B 88
SHEET 1 AA5 2 LYS B 133 ILE B 134 0
SHEET 2 AA5 2 ALA B 160 GLN B 161 -1 O ALA B 160 N ILE B 134
SHEET 1 AA6 2 ILE B 143 ILE B 145 0
SHEET 2 AA6 2 VAL B 151 LEU B 153 -1 O ARG B 152 N LEU B 144
LINK C ALA A 164 N TPO A 165 1555 1555 1.33
LINK C TPO A 165 N LEU A 166 1555 1555 1.33
LINK C LEU A 170 N SEP A 171 1555 1555 1.33
LINK C SEP A 171 N PHE A 172 1555 1555 1.33
LINK C LEU B 170 N SEP B 171 1555 1555 1.33
LINK C SEP B 171 N PHE B 172 1555 1555 1.33
SITE 1 AC1 10 LEU A 23 GLY A 24 VAL A 31 MET A 91
SITE 2 AC1 10 GLU A 92 CYS A 94 GLY A 95 GLY A 97
SITE 3 AC1 10 ASP A 101 LEU A 144
SITE 1 AC2 11 LEU B 23 ALA B 44 LYS B 46 VAL B 75
SITE 2 AC2 11 MET B 91 GLU B 92 PHE B 93 CYS B 94
SITE 3 AC2 11 GLY B 95 ASP B 101 LEU B 144
CRYST1 149.932 149.932 156.754 90.00 90.00 120.00 H 3 2 36
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 0.006670 0.003851 0.000000 0.00000
SCALE2 0.000000 0.007701 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006379 0.00000
(ATOM LINES ARE NOT SHOWN.)
END