HEADER TRANSCRIPTION 16-NOV-15 5FNQ
TITLE STRUCTURE OF THE KEAP1 KELCH DOMAIN IN COMPLEX WITH A SMALL MOLECULE
TITLE 2 INHIBITOR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KELCH-LIKE ECH-ASSOCIATED PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KELCH DOMAIN, RESIDUES 322-624;
COMPND 5 SYNONYM: CYTOSOLIC INHIBITOR OF NRF2, INRF2, KEAP1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSCRIPTION, KEAP1, NRF2, OXIDATIVE STRESS
EXPDTA X-RAY DIFFRACTION
AUTHOR T.G.DAVIES,W.E.WIXTED,J.E.COYLE,C.GRIFFITHS-JONES,K.HEARN,
AUTHOR 2 R.MCMENAMIN,D.NORTON,S.J.RICH,C.RICHARDSON,G.SAXTY,H.M.G.WILLEMS,
AUTHOR 3 A.J.WOOLFORD,J.E.COTTOM,J.KOU,J.G.YONCHUK,H.G.FELDSER,Y.SANCHEZ,
AUTHOR 4 J.P.FOLEY,B.J.BOLOGNESE,G.LOGAN,P.L.PODOLIN,H.YAN,J.F.CALLAHAN,
AUTHOR 5 T.D.HEIGHTMAN,J.K.KERNS
REVDAT 4 10-JAN-24 5FNQ 1 REMARK
REVDAT 3 04-APR-18 5FNQ 1 REMARK ATOM
REVDAT 2 18-MAY-16 5FNQ 1 JRNL
REVDAT 1 13-APR-16 5FNQ 0
JRNL AUTH T.G.DAVIES,W.E.WIXTED,J.E.COYLE,C.GRIFFITHS-JONES,K.HEARN,
JRNL AUTH 2 R.L.MCMENAMIN,D.NORTON,S.J.RICH,C.RICHARDSON,G.SAXTY,
JRNL AUTH 3 H.M.G.WILLEMS,A.J.WOOLFORD,J.E.COTTOM,J.KOU,J.G.YONCHUK,
JRNL AUTH 4 H.G.FELDSER,Y.SANCHEZ,J.P.FOLEY,B.J.BOLOGNESE,G.A.LOGAN,
JRNL AUTH 5 P.L.PODOLIN,H.YAN,J.F.CALLAHAN,T.D.HEIGHTMAN,J.K.KERNS
JRNL TITL MONO-ACIDIC INHIBITORS OF THE KELCH-LIKE ECH-ASSOCIATED
JRNL TITL 2 PROTEIN 1 : NUCLEAR FACTOR ERYTHROID 2-RELATED FACTOR 2
JRNL TITL 3 (KEAP1:NRF2) PROTEIN-PROTEIN INTERACTION WITH HIGH CELL
JRNL TITL 4 POTENCY IDENTIFIED BY FRAGMENT-BASED DISCOVERY.
JRNL REF J.MED.CHEM. V. 59 3991 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 27031670
JRNL DOI 10.1021/ACS.JMEDCHEM.6B00228
REMARK 2
REMARK 2 RESOLUTION. 1.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0107
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) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 24786
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1317
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) : 1.91
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.96
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1630
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2226
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 311
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.26000
REMARK 3 B22 (A**2) : -0.26000
REMARK 3 B33 (A**2) : 0.84000
REMARK 3 B12 (A**2) : -0.13000
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): 0.146
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.135
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.098
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.477
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2302 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8 ; 0.001 ; 0.022
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3136 ; 1.420 ; 1.932
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18 ; 0.050 ; 0.956
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 293 ; 7.302 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 108 ;33.493 ;22.685
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 340 ;13.280 ;15.044
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;18.265 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 333 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1817 ; 0.000 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 4 ; 0.000 ; 0.014
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): 1163 ; 1.028 ; 2.303
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): 1139 ; 1.962 ; 2.745
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 324 A 613
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7977 61.6775 37.8825
REMARK 3 T TENSOR
REMARK 3 T11: 0.0310 T22: 0.0058
REMARK 3 T33: 0.0629 T12: 0.0062
REMARK 3 T13: -0.0208 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 2.5411 L22: 3.5661
REMARK 3 L33: 1.3890 L12: -0.4132
REMARK 3 L13: -0.7548 L23: 0.4014
REMARK 3 S TENSOR
REMARK 3 S11: -0.0380 S12: -0.0259 S13: -0.0846
REMARK 3 S21: 0.1627 S22: 0.0459 S23: 0.2170
REMARK 3 S31: 0.0325 S32: 0.0098 S33: -0.0079
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.
REMARK 4
REMARK 4 5FNQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1290065540.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7
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+
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54187
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26103
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.910
REMARK 200 RESOLUTION RANGE LOW (A) : 44.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.21000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1X2J
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3-0.6 M (NH4)2SO4, 0.4-1.4 M LI2SO4,
REMARK 280 0.1 M NA3CITRATE-HCL PH 5.6, PH 7
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 18.67567
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 37.35133
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 28.01350
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 46.68917
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 9.33783
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 GLY A 321
REMARK 465 PRO A 322
REMARK 465 LYS A 323
REMARK 465 ARG A 614
REMARK 465 LYS A 615
REMARK 465 GLN A 616
REMARK 465 ILE A 617
REMARK 465 ASP A 618
REMARK 465 GLN A 619
REMARK 465 GLN A 620
REMARK 465 ASN A 621
REMARK 465 CYS A 622
REMARK 465 THR A 623
REMARK 465 CYS A 624
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 A 326 -46.74 -159.02
REMARK 500 ARG A 336 -40.62 70.10
REMARK 500 THR A 481 -51.01 -125.52
REMARK 500 HIS A 516 -125.32 53.56
REMARK 500 HIS A 575 -44.44 -146.07
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 A2132 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH A2183 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A2207 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH A2252 DISTANCE = 6.13 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S0W A 1614
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FNR RELATED DB: PDB
REMARK 900 STRUCTURE OF THE KEAP1 KELCH DOMAIN IN COMPLEX WITH A SMALL
REMARK 900 MOLECULE INHIBITOR.
REMARK 900 RELATED ID: 5FNS RELATED DB: PDB
REMARK 900 STRUCTURE OF THE KEAP1 KELCH DOMAIN IN COMPLEX WITH A SMALL
REMARK 900 MOLECULE INHIBITOR.
REMARK 900 RELATED ID: 5FNT RELATED DB: PDB
REMARK 900 STRUCTURE OF THE KEAP1 KELCH DOMAIN IN COMPLEX WITH A SMALL
REMARK 900 MOLECULE INHIBITOR.
REMARK 900 RELATED ID: 5FNU RELATED DB: PDB
REMARK 900 STRUCTURE OF THE KEAP1 KELCH DOMAIN IN COMPLEX WITH A SMALL
REMARK 900 MOLECULE INHIBITOR.
DBREF 5FNQ A 322 624 UNP Q9Z2X8 KEAP1_MOUSE 322 624
SEQADV 5FNQ GLY A 321 UNP Q9Z2X8 EXPRESSION TAG
SEQRES 1 A 304 GLY PRO LYS VAL GLY ARG LEU ILE TYR THR ALA GLY GLY
SEQRES 2 A 304 TYR PHE ARG GLN SER LEU SER TYR LEU GLU ALA TYR ASN
SEQRES 3 A 304 PRO SER ASN GLY SER TRP LEU ARG LEU ALA ASP LEU GLN
SEQRES 4 A 304 VAL PRO ARG SER GLY LEU ALA GLY CYS VAL VAL GLY GLY
SEQRES 5 A 304 LEU LEU TYR ALA VAL GLY GLY ARG ASN ASN SER PRO ASP
SEQRES 6 A 304 GLY ASN THR ASP SER SER ALA LEU ASP CYS TYR ASN PRO
SEQRES 7 A 304 MET THR ASN GLN TRP SER PRO CYS ALA SER MET SER VAL
SEQRES 8 A 304 PRO ARG ASN ARG ILE GLY VAL GLY VAL ILE ASP GLY HIS
SEQRES 9 A 304 ILE TYR ALA VAL GLY GLY SER HIS GLY CYS ILE HIS HIS
SEQRES 10 A 304 SER SER VAL GLU ARG TYR GLU PRO GLU ARG ASP GLU TRP
SEQRES 11 A 304 HIS LEU VAL ALA PRO MET LEU THR ARG ARG ILE GLY VAL
SEQRES 12 A 304 GLY VAL ALA VAL LEU ASN ARG LEU LEU TYR ALA VAL GLY
SEQRES 13 A 304 GLY PHE ASP GLY THR ASN ARG LEU ASN SER ALA GLU CYS
SEQRES 14 A 304 TYR TYR PRO GLU ARG ASN GLU TRP ARG MET ILE THR PRO
SEQRES 15 A 304 MET ASN THR ILE ARG SER GLY ALA GLY VAL CYS VAL LEU
SEQRES 16 A 304 HIS ASN CYS ILE TYR ALA ALA GLY GLY TYR ASP GLY GLN
SEQRES 17 A 304 ASP GLN LEU ASN SER VAL GLU ARG TYR ASP VAL GLU THR
SEQRES 18 A 304 GLU THR TRP THR PHE VAL ALA PRO MET ARG HIS HIS ARG
SEQRES 19 A 304 SER ALA LEU GLY ILE THR VAL HIS GLN GLY LYS ILE TYR
SEQRES 20 A 304 VAL LEU GLY GLY TYR ASP GLY HIS THR PHE LEU ASP SER
SEQRES 21 A 304 VAL GLU CYS TYR ASP PRO ASP SER ASP THR TRP SER GLU
SEQRES 22 A 304 VAL THR ARG MET THR SER GLY ARG SER GLY VAL GLY VAL
SEQRES 23 A 304 ALA VAL THR MET GLU PRO CYS ARG LYS GLN ILE ASP GLN
SEQRES 24 A 304 GLN ASN CYS THR CYS
HET S0W A1614 20
HETNAM S0W 3-(4-CHLOROPHENYL)PROPANOIC ACID
FORMUL 2 S0W C9 H9 CL O2
FORMUL 3 HOH *311(H2 O)
SHEET 1 AA 4 TRP A 352 ARG A 354 0
SHEET 2 AA 4 LEU A 342 TYR A 345 -1 O ALA A 344 N LEU A 353
SHEET 3 AA 4 LEU A 327 ALA A 331 -1 O ILE A 328 N TYR A 345
SHEET 4 AA 4 GLY A 605 THR A 609 -1 O GLY A 605 N ALA A 331
SHEET 1 AB 4 ALA A 366 VAL A 370 0
SHEET 2 AB 4 LEU A 373 VAL A 377 -1 O LEU A 373 N VAL A 370
SHEET 3 AB 4 LEU A 393 TYR A 396 -1 O ASP A 394 N ALA A 376
SHEET 4 AB 4 TRP A 403 PRO A 405 -1 O SER A 404 N CYS A 395
SHEET 1 AC 2 ARG A 380 SER A 383 0
SHEET 2 AC 2 GLY A 386 ASP A 389 -1 O GLY A 386 N SER A 383
SHEET 1 AD 4 GLY A 417 ILE A 421 0
SHEET 2 AD 4 HIS A 424 VAL A 428 -1 O HIS A 424 N ILE A 421
SHEET 3 AD 4 VAL A 440 TYR A 443 -1 O GLU A 441 N ALA A 427
SHEET 4 AD 4 TRP A 450 VAL A 453 -1 O HIS A 451 N ARG A 442
SHEET 1 AE 2 SER A 431 HIS A 432 0
SHEET 2 AE 2 ILE A 435 HIS A 436 -1 O ILE A 435 N HIS A 432
SHEET 1 AF 4 GLY A 464 LEU A 468 0
SHEET 2 AF 4 LEU A 471 VAL A 475 -1 O LEU A 471 N LEU A 468
SHEET 3 AF 4 ALA A 487 TYR A 491 -1 O GLU A 488 N ALA A 474
SHEET 4 AF 4 GLU A 496 ILE A 500 -1 O GLU A 496 N TYR A 491
SHEET 1 AG 4 GLY A 511 LEU A 515 0
SHEET 2 AG 4 CYS A 518 ALA A 522 -1 O CYS A 518 N LEU A 515
SHEET 3 AG 4 VAL A 534 ASP A 538 -1 O GLU A 535 N ALA A 521
SHEET 4 AG 4 THR A 543 VAL A 547 -1 O THR A 543 N ASP A 538
SHEET 1 AH 4 GLY A 558 HIS A 562 0
SHEET 2 AH 4 LYS A 565 LEU A 569 -1 O LYS A 565 N HIS A 562
SHEET 3 AH 4 SER A 580 ASP A 585 -1 O GLU A 582 N VAL A 568
SHEET 4 AH 4 THR A 590 ARG A 596 -1 O THR A 590 N ASP A 585
SITE 1 AC1 6 ARG A 415 PHE A 478 ARG A 483 SER A 508
SITE 2 AC1 6 GLY A 509 ALA A 556
CRYST1 103.625 103.625 56.027 90.00 90.00 120.00 P 61 6
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 0.009650 0.005572 0.000000 0.00000
SCALE2 0.000000 0.011143 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017849 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
