HEADER TRANSFERASE/TRANSFERASE INHIBITOR 29-JUN-16 5GJF
TITLE CRYSTAL STRUCTURE OF HUMAN TAK1/TAB1 FUSION PROTEIN IN COMPLEX WITH
TITLE 2 LIGAND 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TAK1 KINASE - TAB1 CHIMERA FUSION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 31-303,UNP RESIDUES 468-504;
COMPND 5 EC: 2.7.11.25;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: FUSION OF MITOGEN-ACTIVATED PROTEIN KINASE KINASE
COMPND 8 KINASE 7,TGF-BETA-ACTIVATED KINASE 1 AND MAP3K7-BINDING PROTEIN 1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MAP3K7, TAK1, TAB1, MAP3K7IP1;
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: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX, TAK1-TAB1 KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.IRIE,M.NAKAMURA,T.A.FUKAMI,T.MATSUURA,K.MORISHIMA
REVDAT 3 08-NOV-23 5GJF 1 REMARK
REVDAT 2 26-FEB-20 5GJF 1 JRNL REMARK
REVDAT 1 16-NOV-16 5GJF 0
JRNL AUTH T.MURAOKA,M.IDE,M.IRIE,K.MORIKAMI,T.MIURA,M.NISHIHARA,
JRNL AUTH 2 H.KASHIWAGI
JRNL TITL DEVELOPMENT OF A METHOD FOR CONVERTING A TAK1 TYPE I
JRNL TITL 2 INHIBITOR INTO A TYPE II OR C-HELIX-OUT INHIBITOR BY
JRNL TITL 3 STRUCTURE-BASED DRUG DESIGN (SBDD)
JRNL REF CHEM.PHARM.BULL. V. 64 1622 2016
JRNL REFN ISSN 0009-2363
JRNL PMID 27803473
JRNL DOI 10.1248/CPB.C16-00606
REMARK 2
REMARK 2 RESOLUTION. 2.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 12018
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 615
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) : 2.89
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 848
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.67
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE SET COUNT : 52
REMARK 3 BIN FREE R VALUE : 0.2800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2311
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 13
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.26000
REMARK 3 B22 (A**2) : -0.07000
REMARK 3 B33 (A**2) : 0.34000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.560
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.305
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.233
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.559
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2425 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2266 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3300 ; 1.178 ; 1.939
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5201 ; 0.877 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 295 ; 5.658 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 97 ;35.816 ;23.196
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 371 ;14.766 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;15.707 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 352 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2712 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 565 ; 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): 1189 ; 2.734 ; 6.655
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1188 ; 2.735 ; 6.653
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1481 ; 4.814 ; 9.968
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 : NULL
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 5GJF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1300000881.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12633
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.890
REMARK 200 RESOLUTION RANGE LOW (A) : 48.441
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.14200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 1.22200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2EVA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.94M SODIUM POTASSIUM PHOSPHATE,
REMARK 280 20%(V/V) GLYCEROL AS CRYOPROTECTANT, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 29.03500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 66.48000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 70.73000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.03500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.48000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.73000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.03500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 66.48000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.73000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.03500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 66.48000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 70.73000
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 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 GLU A 66
REMARK 465 SER A 67
REMARK 465 GLU A 68
REMARK 465 SER A 69
REMARK 465 GLU A 70
REMARK 465 PRO A 472
REMARK 465 GLY A 473
REMARK 465 GLU A 474
REMARK 465 ASP A 475
REMARK 465 GLU A 497
REMARK 465 GLN A 498
REMARK 465 SER A 499
REMARK 465 VAL A 500
REMARK 465 VAL A 501
REMARK 465 THR A 502
REMARK 465 ALA A 503
REMARK 465 PRO A 504
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 32 CG OD1 OD2
REMARK 470 LYS A 34 CG CD CE NZ
REMARK 470 GLU A 35 CG CD OE1 OE2
REMARK 470 GLU A 37 CG CD OE1 OE2
REMARK 470 GLU A 39 CG CD OE1 OE2
REMARK 470 GLU A 40 CG CD OE1 OE2
REMARK 470 ARG A 44 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 71 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 72 CG CD CE NZ
REMARK 470 LYS A 150 CG CD CE NZ
REMARK 470 THR A 184 OG1 CG2
REMARK 470 HIS A 185 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 190 CD CE NZ
REMARK 470 LYS A 282 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 ALA A 46 -103.00 65.95
REMARK 500 TRP A 55 111.70 -164.64
REMARK 500 ALA A 57 -52.28 84.58
REMARK 500 LYS A 72 -74.16 -73.04
REMARK 500 ARG A 155 16.61 57.64
REMARK 500 ASP A 156 46.23 -162.49
REMARK 500 ASP A 175 87.52 -157.19
REMARK 500 CYS A 180 -58.31 -163.12
REMARK 500 GLN A 183 -80.11 -58.50
REMARK 500 THR A 184 49.87 -96.08
REMARK 500 HIS A 185 -81.89 -169.01
REMARK 500 SER A 192 35.69 -147.33
REMARK 500 ILE A 232 -73.39 -73.04
REMARK 500 HIS A 495 47.96 -100.99
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 6V4 A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5GJD RELATED DB: PDB
REMARK 900 RELATED ID: 5GJG RELATED DB: PDB
DBREF 5GJF A 31 303 UNP O43318 M3K7_HUMAN 31 303
DBREF 5GJF A 468 504 UNP Q15750 TAB1_HUMAN 468 504
SEQADV 5GJF GLY A 26 UNP O43318 EXPRESSION TAG
SEQADV 5GJF PRO A 27 UNP O43318 EXPRESSION TAG
SEQADV 5GJF LEU A 28 UNP O43318 EXPRESSION TAG
SEQADV 5GJF HIS A 29 UNP O43318 EXPRESSION TAG
SEQADV 5GJF MET A 30 UNP O43318 EXPRESSION TAG
SEQRES 1 A 315 GLY PRO LEU HIS MET ILE ASP TYR LYS GLU ILE GLU VAL
SEQRES 2 A 315 GLU GLU VAL VAL GLY ARG GLY ALA PHE GLY VAL VAL CYS
SEQRES 3 A 315 LYS ALA LYS TRP ARG ALA LYS ASP VAL ALA ILE LYS GLN
SEQRES 4 A 315 ILE GLU SER GLU SER GLU ARG LYS ALA PHE ILE VAL GLU
SEQRES 5 A 315 LEU ARG GLN LEU SER ARG VAL ASN HIS PRO ASN ILE VAL
SEQRES 6 A 315 LYS LEU TYR GLY ALA CYS LEU ASN PRO VAL CYS LEU VAL
SEQRES 7 A 315 MET GLU TYR ALA GLU GLY GLY SER LEU TYR ASN VAL LEU
SEQRES 8 A 315 HIS GLY ALA GLU PRO LEU PRO TYR TYR THR ALA ALA HIS
SEQRES 9 A 315 ALA MET SER TRP CYS LEU GLN CYS SER GLN GLY VAL ALA
SEQRES 10 A 315 TYR LEU HIS SER MET GLN PRO LYS ALA LEU ILE HIS ARG
SEQRES 11 A 315 ASP LEU LYS PRO PRO ASN LEU LEU LEU VAL ALA GLY GLY
SEQRES 12 A 315 THR VAL LEU LYS ILE CYS ASP PHE GLY THR ALA CYS ASP
SEQRES 13 A 315 ILE GLN THR HIS MET THR ASN ASN LYS GLY SER ALA ALA
SEQRES 14 A 315 TRP MET ALA PRO GLU VAL PHE GLU GLY SER ASN TYR SER
SEQRES 15 A 315 GLU LYS CYS ASP VAL PHE SER TRP GLY ILE ILE LEU TRP
SEQRES 16 A 315 GLU VAL ILE THR ARG ARG LYS PRO PHE ASP GLU ILE GLY
SEQRES 17 A 315 GLY PRO ALA PHE ARG ILE MET TRP ALA VAL HIS ASN GLY
SEQRES 18 A 315 THR ARG PRO PRO LEU ILE LYS ASN LEU PRO LYS PRO ILE
SEQRES 19 A 315 GLU SER LEU MET THR ARG CYS TRP SER LYS ASP PRO SER
SEQRES 20 A 315 GLN ARG PRO SER MET GLU GLU ILE VAL LYS ILE MET THR
SEQRES 21 A 315 HIS LEU MET ARG TYR PHE PRO GLY ALA ASP GLU PRO LEU
SEQRES 22 A 315 GLN TYR PRO CYS GLN HIS SER LEU PRO PRO GLY GLU ASP
SEQRES 23 A 315 GLY ARG VAL GLU PRO TYR VAL ASP PHE ALA GLU PHE TYR
SEQRES 24 A 315 ARG LEU TRP SER VAL ASP HIS GLY GLU GLN SER VAL VAL
SEQRES 25 A 315 THR ALA PRO
HET 6V4 A 601 43
HETNAM 6V4 N-(2-ISOPROPOXY-4-(4-METHYLPIPERAZINE-1-CARBONYL)
HETNAM 2 6V4 PHENYL)-2-(3-(3-PHENYLUREIDO)PHENYL)THIAZOLE-4-
HETNAM 3 6V4 CARBOXAMIDE
FORMUL 2 6V4 C32 H34 N6 O4 S
FORMUL 3 HOH *13(H2 O)
HELIX 1 AA1 ASP A 32 ILE A 36 5 5
HELIX 2 AA2 ALA A 73 VAL A 84 1 12
HELIX 3 AA3 LEU A 112 GLY A 118 1 7
HELIX 4 AA4 THR A 126 SER A 146 1 21
HELIX 5 AA5 LYS A 158 PRO A 160 5 3
HELIX 6 AA6 ALA A 197 GLY A 203 1 7
HELIX 7 AA7 GLU A 208 ARG A 225 1 18
HELIX 8 AA8 PRO A 235 GLY A 246 1 12
HELIX 9 AA9 PRO A 256 TRP A 267 1 12
HELIX 10 AB1 ASP A 270 ARG A 274 5 5
HELIX 11 AB2 SER A 276 MET A 288 1 13
HELIX 12 AB3 ARG A 289 PHE A 291 5 3
HELIX 13 AB4 PHE A 484 HIS A 495 1 12
SHEET 1 AA1 6 HIS A 29 MET A 30 0
SHEET 2 AA1 6 LEU A 92 CYS A 96 1 O TYR A 93 N HIS A 29
SHEET 3 AA1 6 CYS A 101 GLU A 105 -1 O VAL A 103 N GLY A 94
SHEET 4 AA1 6 LYS A 58 GLN A 64 -1 N ALA A 61 O MET A 104
SHEET 5 AA1 6 VAL A 49 TRP A 55 -1 N CYS A 51 O ILE A 62
SHEET 6 AA1 6 GLU A 37 VAL A 41 -1 N GLU A 40 O LYS A 52
SHEET 1 AA2 3 GLY A 110 SER A 111 0
SHEET 2 AA2 3 LEU A 162 VAL A 165 -1 O LEU A 164 N GLY A 110
SHEET 3 AA2 3 VAL A 170 ILE A 173 -1 O LYS A 172 N LEU A 163
SHEET 1 AA3 2 LEU A 122 PRO A 123 0
SHEET 2 AA3 2 PRO A 301 CYS A 302 -1 O CYS A 302 N LEU A 122
SSBOND 1 CYS A 180 CYS A 180 1555 2545 2.90
CISPEP 1 ASN A 98 PRO A 99 0 -2.56
CISPEP 2 GLU A 120 PRO A 121 0 -9.32
CISPEP 3 GLN A 148 PRO A 149 0 6.40
SITE 1 AC1 14 VAL A 42 VAL A 50 ALA A 61 GLU A 77
SITE 2 AC1 14 GLN A 80 LEU A 81 VAL A 90 MET A 104
SITE 3 AC1 14 GLU A 105 TYR A 106 ALA A 107 LEU A 163
SITE 4 AC1 14 CYS A 174 ASP A 175
CRYST1 58.070 132.960 141.460 90.00 90.00 90.00 I 2 2 2 8
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 0.017221 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007521 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007069 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
