HEADER LIGASE 04-APR-17 5NLB
TITLE CRYSTAL STRUCTURE OF HUMAN CUL3 N-TERMINAL DOMAIN BOUND TO KEAP1 BTB
TITLE 2 AND 3-BOX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KELCH-LIKE ECH-ASSOCIATED PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 51-204;
COMPND 5 SYNONYM: CYTOSOLIC INHIBITOR OF NRF2,INRF2,KELCH-LIKE PROTEIN 19;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CULLIN-3;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: CUL-3;
COMPND 11 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: KEAP1, INRF2, KIAA0132, KLHL19;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: CUL3, KIAA0617;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS E3 UBIQUITIN LIGASE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.ADAMSON,T.KROJER,D.M.PINKAS,S.G.BARTUAL,N.A.BURGESS-BROWN,
AUTHOR 2 O.BORKOWSKA,R.CHALK,J.A.NEWMAN,J.KOPEC,S.E.DIXON-CLARKE,S.MATHEA,
AUTHOR 3 R.SETHI,S.VELUPILLAI,S.MACKINNON,F.VON DELFT,C.H.ARROWSMITH,
AUTHOR 4 A.M.EDWARDS,C.BOUNTRA,A.BULLOCK
REVDAT 5 17-JAN-24 5NLB 1 REMARK
REVDAT 4 08-NOV-23 5NLB 1 JRNL
REVDAT 3 16-OCT-19 5NLB 1 REMARK
REVDAT 2 02-AUG-17 5NLB 1
REVDAT 1 19-APR-17 5NLB 0
JRNL AUTH R.J.ADAMSON,N.C.PAYNE,S.G.BARTUAL,R.MAZITSCHEK,A.N.BULLOCK
JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION ESTABLISHES A
JRNL TITL 2 DETAILED UNDERSTANDING OF KEAP1-CUL3 COMPLEX ASSEMBLY.
JRNL REF FREE RADIC BIOL MED V. 204 215 2023
JRNL REFN ESSN 1873-4596
JRNL PMID 37156295
JRNL DOI 10.1016/J.FREERADBIOMED.2023.04.021
REMARK 2
REMARK 2 RESOLUTION. 3.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 3.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 10899
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.238
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.770
REMARK 3 FREE R VALUE TEST SET COUNT : 520
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 40.3843 - 5.4731 1.00 2729 134 0.1990 0.2593
REMARK 3 2 5.4731 - 4.3458 1.00 2574 136 0.2746 0.2757
REMARK 3 3 4.3458 - 3.7970 1.00 2555 123 0.2787 0.3502
REMARK 3 4 3.7970 - 3.4500 0.99 2521 127 0.3245 0.3943
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) : 0.480
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.050
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.011 3936
REMARK 3 ANGLE : 1.438 5294
REMARK 3 CHIRALITY : 0.072 597
REMARK 3 PLANARITY : 0.011 688
REMARK 3 DIHEDRAL : 14.589 2412
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -24.2994 30.7683 166.8826
REMARK 3 T TENSOR
REMARK 3 T11: 0.9714 T22: 1.4063
REMARK 3 T33: 1.1361 T12: 0.0341
REMARK 3 T13: 0.1823 T23: -0.2905
REMARK 3 L TENSOR
REMARK 3 L11: 0.7208 L22: 4.9521
REMARK 3 L33: 2.1668 L12: -0.7499
REMARK 3 L13: 0.4155 L23: -1.3646
REMARK 3 S TENSOR
REMARK 3 S11: -0.1615 S12: -0.0386 S13: 0.0103
REMARK 3 S21: 0.4510 S22: 0.2486 S23: -0.3087
REMARK 3 S31: -0.1782 S32: -0.2383 S33: -0.0816
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 5NLB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004281.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-SEP-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
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 : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10899
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.450
REMARK 200 RESOLUTION RANGE LOW (A) : 40.382
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.420
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
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: PHENIX
REMARK 200 STARTING MODEL: 4AP2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG3350, 10% ETHYLENE GLYCOL, 0.2M
REMARK 280 POTASSIUM CITRATE TRIBASIC, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
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
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 82.35500
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 82.35500
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 20.50000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 116.69000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 20.50000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 116.69000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 82.35500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 20.50000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 116.69000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 82.35500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 20.50000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 116.69000
REMARK 290 SMTRY3 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 50470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 329.42000
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 B 331
REMARK 465 GLU B 332
REMARK 465 GLY B 333
REMARK 465 GLU B 334
REMARK 465 GLY B 335
REMARK 465 LYS B 336
REMARK 465 ASN B 337
REMARK 465 PRO B 338
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 LEU A 70 CD1 CD2
REMARK 470 LEU A 72 CD1 CD2
REMARK 470 GLN A 74 CG CD OE1 NE2
REMARK 470 LEU A 76 CD1 CD2
REMARK 470 GLN A 82 CD OE1 NE2
REMARK 470 VAL A 83 CG1 CG2
REMARK 470 LYS A 84 CG CD CE NZ
REMARK 470 TYR A 85 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A 86 CG CD OE1 NE2
REMARK 470 ASP A 87 CG OD1 OD2
REMARK 470 GLN A 92 CD OE1 NE2
REMARK 470 MET A 94 SD CE
REMARK 470 LYS A 97 CD CE NZ
REMARK 470 VAL A 98 CG2
REMARK 470 SER A 102 OG
REMARK 470 SER A 103 OG
REMARK 470 VAL A 106 CG1
REMARK 470 LYS A 108 CD CE NZ
REMARK 470 THR A 112 CG2
REMARK 470 ASN A 113 CG OD1 ND2
REMARK 470 ARG A 116 CD NE CZ NH1 NH2
REMARK 470 GLN A 118 CD OE1 NE2
REMARK 470 GLU A 121 CG CD OE1 OE2
REMARK 470 VAL A 122 CG2
REMARK 470 ILE A 125 CG2 CD1
REMARK 470 ILE A 128 CG2 CD1
REMARK 470 HIS A 129 ND1 CD2 CE1 NE2
REMARK 470 LYS A 131 CD CE NZ
REMARK 470 MET A 133 SD CE
REMARK 470 ARG A 135 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 136 CD1 CD2
REMARK 470 MET A 147 SD CE
REMARK 470 GLU A 149 CD OE1 OE2
REMARK 470 LYS A 150 CG CD CE NZ
REMARK 470 LEU A 153 CD1 CD2
REMARK 470 HIS A 154 ND1 CD2 CE1 NE2
REMARK 470 VAL A 160 CG1
REMARK 470 GLN A 163 CD OE1 NE2
REMARK 470 ILE A 164 CG2 CD1
REMARK 470 VAL A 167 CG2
REMARK 470 VAL A 168 CG1
REMARK 470 ARG A 169 CD NE CZ NH1 NH2
REMARK 470 SER A 172 OG
REMARK 470 ASP A 173 OD1 OD2
REMARK 470 VAL A 176 CG2
REMARK 470 GLN A 177 CD OE1 NE2
REMARK 470 GLN A 178 CD OE1 NE2
REMARK 470 ASP A 180 OD1 OD2
REMARK 470 PRO A 181 CD
REMARK 470 ASN A 183 CG OD1 ND2
REMARK 470 ILE A 185 CD1
REMARK 470 ASN A 189 OD1 ND2
REMARK 470 PHE A 190 CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 192 CD OE1 OE2
REMARK 470 GLN A 193 CD OE1 NE2
REMARK 470 ILE A 194 CG2 CD1
REMARK 470 CYS A 196 SG
REMARK 470 VAL A 197 CG1 CG2
REMARK 470 HIS A 200 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 201 CG CD OE1 NE2
REMARK 470 TYR B 320 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP B 340 CG OD1 OD2
REMARK 470 TYR B 341 CG CD1 CD2 CE1 CE2 CZ OH
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 OH TYR B 74 O GLU B 137 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS B 236 OE1 GLU B 375 1655 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS B 187 CA - CB - SG ANGL. DEV. = 8.9 DEGREES
REMARK 500 LEU B 225 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
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 SER A 53 120.70 -179.05
REMARK 500 GLN A 74 47.33 33.49
REMARK 500 LEU A 76 14.99 57.39
REMARK 500 THR A 112 -179.92 -62.60
REMARK 500 ASN A 113 -22.79 -36.33
REMARK 500 LEU A 115 -145.95 -96.04
REMARK 500 GLU A 117 34.60 -81.89
REMARK 500 GLU A 121 -23.12 72.04
REMARK 500 GLN A 163 91.10 61.96
REMARK 500 GLN A 178 39.78 -94.53
REMARK 500 ILE A 194 -53.84 -27.99
REMARK 500 ASN B 48 44.71 -104.95
REMARK 500 LEU B 123 32.57 -97.16
REMARK 500 VAL B 151 -75.84 -118.90
REMARK 500 GLU B 227 -69.53 -124.74
REMARK 500 ILE B 269 -70.34 -109.01
REMARK 500 SER B 282 -18.84 -156.97
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5NLB A 51 204 UNP Q14145 KEAP1_HUMAN 51 204
DBREF 5NLB B 26 381 UNP Q13618 CUL3_HUMAN 26 381
SEQADV 5NLB ARG B 342 UNP Q13618 ILE 342 ENGINEERED MUTATION
SEQADV 5NLB ASP B 346 UNP Q13618 LEU 346 ENGINEERED MUTATION
SEQRES 1 A 154 THR PHE SER TYR THR LEU GLU ASP HIS THR LYS GLN ALA
SEQRES 2 A 154 PHE GLY ILE MET ASN GLU LEU ARG LEU SER GLN GLN LEU
SEQRES 3 A 154 CYS ASP VAL THR LEU GLN VAL LYS TYR GLN ASP ALA PRO
SEQRES 4 A 154 ALA ALA GLN PHE MET ALA HIS LYS VAL VAL LEU ALA SER
SEQRES 5 A 154 SER SER PRO VAL PHE LYS ALA MET PHE THR ASN GLY LEU
SEQRES 6 A 154 ARG GLU GLN GLY MET GLU VAL VAL SER ILE GLU GLY ILE
SEQRES 7 A 154 HIS PRO LYS VAL MET GLU ARG LEU ILE GLU PHE ALA TYR
SEQRES 8 A 154 THR ALA SER ILE SER MET GLY GLU LYS CYS VAL LEU HIS
SEQRES 9 A 154 VAL MET ASN GLY ALA VAL MET TYR GLN ILE ASP SER VAL
SEQRES 10 A 154 VAL ARG ALA CYS SER ASP PHE LEU VAL GLN GLN LEU ASP
SEQRES 11 A 154 PRO SER ASN ALA ILE GLY ILE ALA ASN PHE ALA GLU GLN
SEQRES 12 A 154 ILE GLY CYS VAL GLU LEU HIS GLN ARG ALA ARG
SEQRES 1 B 356 ASP GLU LYS TYR VAL ASN SER ILE TRP ASP LEU LEU LYS
SEQRES 2 B 356 ASN ALA ILE GLN GLU ILE GLN ARG LYS ASN ASN SER GLY
SEQRES 3 B 356 LEU SER PHE GLU GLU LEU TYR ARG ASN ALA TYR THR MET
SEQRES 4 B 356 VAL LEU HIS LYS HIS GLY GLU LYS LEU TYR THR GLY LEU
SEQRES 5 B 356 ARG GLU VAL VAL THR GLU HIS LEU ILE ASN LYS VAL ARG
SEQRES 6 B 356 GLU ASP VAL LEU ASN SER LEU ASN ASN ASN PHE LEU GLN
SEQRES 7 B 356 THR LEU ASN GLN ALA TRP ASN ASP HIS GLN THR ALA MET
SEQRES 8 B 356 VAL MET ILE ARG ASP ILE LEU MET TYR MET ASP ARG VAL
SEQRES 9 B 356 TYR VAL GLN GLN ASN ASN VAL GLU ASN VAL TYR ASN LEU
SEQRES 10 B 356 GLY LEU ILE ILE PHE ARG ASP GLN VAL VAL ARG TYR GLY
SEQRES 11 B 356 CYS ILE ARG ASP HIS LEU ARG GLN THR LEU LEU ASP MET
SEQRES 12 B 356 ILE ALA ARG GLU ARG LYS GLY GLU VAL VAL ASP ARG GLY
SEQRES 13 B 356 ALA ILE ARG ASN ALA CYS GLN MET LEU MET ILE LEU GLY
SEQRES 14 B 356 LEU GLU GLY ARG SER VAL TYR GLU GLU ASP PHE GLU ALA
SEQRES 15 B 356 PRO PHE LEU GLU MET SER ALA GLU PHE PHE GLN MET GLU
SEQRES 16 B 356 SER GLN LYS PHE LEU ALA GLU ASN SER ALA SER VAL TYR
SEQRES 17 B 356 ILE LYS LYS VAL GLU ALA ARG ILE ASN GLU GLU ILE GLU
SEQRES 18 B 356 ARG VAL MET HIS CYS LEU ASP LYS SER THR GLU GLU PRO
SEQRES 19 B 356 ILE VAL LYS VAL VAL GLU ARG GLU LEU ILE SER LYS HIS
SEQRES 20 B 356 MET LYS THR ILE VAL GLU MET GLU ASN SER GLY LEU VAL
SEQRES 21 B 356 HIS MET LEU LYS ASN GLY LYS THR GLU ASP LEU GLY CYS
SEQRES 22 B 356 MET TYR LYS LEU PHE SER ARG VAL PRO ASN GLY LEU LYS
SEQRES 23 B 356 THR MET CYS GLU CYS MET SER SER TYR LEU ARG GLU GLN
SEQRES 24 B 356 GLY LYS ALA LEU VAL SER GLU GLU GLY GLU GLY LYS ASN
SEQRES 25 B 356 PRO VAL ASP TYR ARG GLN GLY LEU ASP ASP LEU LYS SER
SEQRES 26 B 356 ARG PHE ASP ARG PHE LEU LEU GLU SER PHE ASN ASN ASP
SEQRES 27 B 356 ARG LEU PHE LYS GLN THR ILE ALA GLY ASP PHE GLU TYR
SEQRES 28 B 356 PHE LEU ASN LEU ASN
HELIX 1 AA1 GLU A 57 SER A 73 1 17
HELIX 2 AA2 HIS A 96 SER A 104 1 9
HELIX 3 AA3 SER A 104 PHE A 111 1 8
HELIX 4 AA4 HIS A 129 ALA A 143 1 15
HELIX 5 AA5 CYS A 151 GLN A 163 1 13
HELIX 6 AA6 ILE A 164 ASP A 173 1 10
HELIX 7 AA7 ASN A 183 GLY A 195 1 13
HELIX 8 AA8 GLU A 198 ALA A 203 1 6
HELIX 9 AA9 GLU B 27 ARG B 46 1 20
HELIX 10 AB1 SER B 53 HIS B 67 1 15
HELIX 11 AB2 HIS B 69 LYS B 88 1 20
HELIX 12 AB3 LYS B 88 ASN B 95 1 8
HELIX 13 AB4 ASN B 100 LEU B 123 1 24
HELIX 14 AB5 LEU B 123 ASN B 134 1 12
HELIX 15 AB6 ASN B 138 VAL B 151 1 14
HELIX 16 AB7 GLY B 155 LYS B 174 1 20
HELIX 17 AB8 ASP B 179 LEU B 193 1 15
HELIX 18 AB9 ARG B 198 PHE B 205 1 8
HELIX 19 AC1 PHE B 205 GLU B 227 1 23
HELIX 20 AC2 SER B 229 CYS B 251 1 23
HELIX 21 AC3 ASP B 253 SER B 255 5 3
HELIX 22 AC4 THR B 256 ILE B 269 1 14
HELIX 23 AC5 HIS B 272 GLU B 278 1 7
HELIX 24 AC6 GLY B 283 ASN B 290 1 8
HELIX 25 AC7 LYS B 292 SER B 304 1 13
HELIX 26 AC8 ASN B 308 SER B 330 1 23
HELIX 27 AC9 ASP B 340 SER B 359 1 20
HELIX 28 AD1 ASP B 363 ASN B 381 1 19
SHEET 1 AA1 3 ALA A 91 ALA A 95 0
SHEET 2 AA1 3 VAL A 79 VAL A 83 -1 N VAL A 79 O ALA A 95
SHEET 3 AA1 3 VAL A 123 ILE A 125 1 O VAL A 123 N THR A 80
CRYST1 41.000 233.380 164.710 90.00 90.00 90.00 C 2 2 21 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 0.024390 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004285 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006071 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
