HEADER TRANSCRIPTION/INHIBITOR 17-JUL-17 5WHO
TITLE KELCH DOMAIN OF HUMAN KEAP1 BOUND TO SMALL MOLECULE INHIBITOR
TITLE 2 FRAGMENT: 4-OXO-4H-1-BENZOPYRAN-2-CARBOXYLIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KELCH-LIKE ECH-ASSOCIATED PROTEIN 1;
COMPND 3 CHAIN: B, A;
COMPND 4 SYNONYM: CYTOSOLIC INHIBITOR OF NRF2,INRF2,KELCH-LIKE PROTEIN 19;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: HIS-TAGGED VARIANT INCLUDING MUTATIONS FOR ALTERED
COMPND 8 CRYSTALLOGRAPHIC PACKING
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 EXPRESSION_SYSTEM_VECTOR_TYPE: PET15B
KEYWDS SCAFFOLD, INHIBITOR, FRAGMENT, TRANSCRIPTION, TRANSCRIPTION-INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.P.CAROLAN,A.J.LYNCH,K.N.ALLEN
REVDAT 4 04-OCT-23 5WHO 1 REMARK
REVDAT 3 01-APR-20 5WHO 1 JRNL
REVDAT 2 01-JAN-20 5WHO 1 REMARK
REVDAT 1 19-SEP-18 5WHO 0
JRNL AUTH M.ZHONG,A.LYNCH,S.N.MUELLERS,S.JEHLE,L.LUO,D.R.HALL,R.IWASE,
JRNL AUTH 2 J.P.CAROLAN,M.EGBERT,A.WAKEFIELD,K.STREU,C.M.HARVEY,
JRNL AUTH 3 P.C.ORTET,D.KOZAKOV,S.VAJDA,K.N.ALLEN,A.WHITTY
JRNL TITL INTERACTION ENERGETICS AND DRUGGABILITY OF THE
JRNL TITL 2 PROTEIN-PROTEIN INTERACTION BETWEEN KELCH-LIKE
JRNL TITL 3 ECH-ASSOCIATED PROTEIN 1 (KEAP1) AND NUCLEAR FACTOR
JRNL TITL 4 ERYTHROID 2 LIKE 2 (NRF2).
JRNL REF BIOCHEMISTRY V. 59 563 2020
JRNL REFN ISSN 0006-2960
JRNL PMID 31851823
JRNL DOI 10.1021/ACS.BIOCHEM.9B00943
REMARK 2
REMARK 2 RESOLUTION. 2.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 36243
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.340
REMARK 3 FREE R VALUE TEST SET COUNT : 1936
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 51.8617 - 5.3728 1.00 2617 152 0.2053 0.2642
REMARK 3 2 5.3728 - 4.2652 1.00 2542 145 0.1603 0.1912
REMARK 3 3 4.2652 - 3.7262 1.00 2551 142 0.1746 0.2188
REMARK 3 4 3.7262 - 3.3856 1.00 2536 146 0.1884 0.2166
REMARK 3 5 3.3856 - 3.1429 0.99 2508 136 0.1999 0.2129
REMARK 3 6 3.1429 - 2.9577 0.99 2523 147 0.2096 0.2367
REMARK 3 7 2.9577 - 2.8095 0.98 2454 137 0.2003 0.2540
REMARK 3 8 2.8095 - 2.6873 0.98 2476 137 0.2041 0.2691
REMARK 3 9 2.6873 - 2.5838 0.96 2464 137 0.2235 0.2920
REMARK 3 10 2.5838 - 2.4946 0.96 2388 139 0.2278 0.2595
REMARK 3 11 2.4946 - 2.4166 0.93 2355 134 0.2311 0.2892
REMARK 3 12 2.4166 - 2.3476 0.93 2353 129 0.2252 0.2447
REMARK 3 13 2.3476 - 2.2858 0.92 2328 127 0.2244 0.2953
REMARK 3 14 2.2858 - 2.2300 0.88 2212 128 0.2303 0.2824
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.010
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 : 0.007 4494
REMARK 3 ANGLE : 0.961 6124
REMARK 3 CHIRALITY : 0.058 650
REMARK 3 PLANARITY : 0.005 806
REMARK 3 DIHEDRAL : 6.195 2582
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 5WHO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1000229040.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0 - 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTALS MONOCHROMATOR
REMARK 200 OPTICS : 12 V SERVO MOTORS UTILIZING A
REMARK 200 CAMAC-BASED E500 STEPPER
REMARK 200 CONTROLLER
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37484
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.230
REMARK 200 RESOLUTION RANGE LOW (A) : 51.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.03900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.27900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.850
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: 5WFL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 - 1.5 M AMMONIUM SULFATE, 0.1 M
REMARK 280 BIS-TRIS PH = 6.0 - 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1
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+1/2,Y+1/2,Z+1/2
REMARK 290 4555 -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 37.84291
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.54500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 71.58956
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 37.84291
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.54500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 71.58956
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 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
REMARK 350 BIOMOLECULE: 2
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 MET B 289
REMARK 465 GLY B 290
REMARK 465 SER B 291
REMARK 465 SER B 292
REMARK 465 HIS B 293
REMARK 465 HIS B 294
REMARK 465 HIS B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 SER B 299
REMARK 465 SER B 300
REMARK 465 GLY B 301
REMARK 465 GLY B 302
REMARK 465 GLU B 303
REMARK 465 ASN B 304
REMARK 465 LEU B 305
REMARK 465 TYR B 306
REMARK 465 PHE B 307
REMARK 465 GLN B 308
REMARK 465 GLY B 309
REMARK 465 HIS B 310
REMARK 465 MET B 311
REMARK 465 LYS B 312
REMARK 465 PRO B 313
REMARK 465 THR B 314
REMARK 465 GLN B 315
REMARK 465 VAL B 316
REMARK 465 MET B 317
REMARK 465 PRO B 318
REMARK 465 SER B 319
REMARK 465 ARG B 320
REMARK 465 ALA B 321
REMARK 465 PRO B 322
REMARK 465 LYS B 323
REMARK 465 VAL B 324
REMARK 465 ARG B 614
REMARK 465 LYS B 615
REMARK 465 GLN B 616
REMARK 465 ILE B 617
REMARK 465 ASP B 618
REMARK 465 GLN B 619
REMARK 465 GLN B 620
REMARK 465 ASN B 621
REMARK 465 SER B 622
REMARK 465 THR B 623
REMARK 465 SER B 624
REMARK 465 MET A 289
REMARK 465 GLY A 290
REMARK 465 SER A 291
REMARK 465 SER A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 SER A 299
REMARK 465 SER A 300
REMARK 465 GLY A 301
REMARK 465 GLY A 302
REMARK 465 GLU A 303
REMARK 465 ASN A 304
REMARK 465 LEU A 305
REMARK 465 TYR A 306
REMARK 465 PHE A 307
REMARK 465 GLN A 308
REMARK 465 GLY A 309
REMARK 465 HIS A 310
REMARK 465 MET A 311
REMARK 465 LYS A 312
REMARK 465 PRO A 313
REMARK 465 THR A 314
REMARK 465 GLN A 315
REMARK 465 VAL A 316
REMARK 465 MET A 317
REMARK 465 PRO A 318
REMARK 465 SER A 319
REMARK 465 ARG A 320
REMARK 465 ALA A 321
REMARK 465 PRO A 322
REMARK 465 LYS A 323
REMARK 465 VAL A 324
REMARK 465 GLY A 325
REMARK 465 ARG A 326
REMARK 465 LEU A 327
REMARK 465 ILE A 328
REMARK 465 TYR A 329
REMARK 465 MET A 610
REMARK 465 GLU A 611
REMARK 465 PRO A 612
REMARK 465 SER A 613
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 SER A 622
REMARK 465 THR A 623
REMARK 465 SER 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 B 336 -35.90 72.68
REMARK 500 LEU B 515 -79.21 -103.11
REMARK 500 HIS B 516 -84.51 -96.71
REMARK 500 GLN B 528 -41.44 -131.14
REMARK 500 VAL B 547 -165.17 -118.15
REMARK 500 HIS B 575 -30.99 -132.51
REMARK 500 ARG A 336 -29.55 67.25
REMARK 500 TYR A 341 155.09 -47.51
REMARK 500 ASP A 349 -141.52 66.53
REMARK 500 LEU A 355 -167.55 -104.90
REMARK 500 ASN A 387 66.33 -155.17
REMARK 500 ASP A 422 73.35 49.19
REMARK 500 THR A 481 -35.82 -134.31
REMARK 500 LEU A 515 -73.10 -97.85
REMARK 500 HIS A 516 -74.34 -114.25
REMARK 500 THR A 595 -179.34 -171.00
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 SO4 B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AO7 A 702
DBREF 5WHO B 312 624 UNP Q14145 KEAP1_HUMAN 312 624
DBREF 5WHO A 312 624 UNP Q14145 KEAP1_HUMAN 312 624
SEQADV 5WHO MET B 289 UNP Q14145 INITIATING METHIONINE
SEQADV 5WHO GLY B 290 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO SER B 291 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO SER B 292 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO HIS B 293 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO HIS B 294 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO HIS B 295 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO HIS B 296 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO HIS B 297 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO HIS B 298 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO SER B 299 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO SER B 300 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO GLY B 301 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO GLY B 302 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO GLU B 303 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO ASN B 304 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO LEU B 305 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO TYR B 306 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO PHE B 307 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO GLN B 308 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO GLY B 309 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO HIS B 310 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO MET B 311 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO SER B 319 UNP Q14145 CYS 319 ENGINEERED MUTATION
SEQADV 5WHO ALA B 540 UNP Q14145 GLU 540 ENGINEERED MUTATION
SEQADV 5WHO ALA B 542 UNP Q14145 GLU 542 ENGINEERED MUTATION
SEQADV 5WHO SER B 613 UNP Q14145 CYS 613 ENGINEERED MUTATION
SEQADV 5WHO SER B 622 UNP Q14145 CYS 622 ENGINEERED MUTATION
SEQADV 5WHO SER B 624 UNP Q14145 CYS 624 ENGINEERED MUTATION
SEQADV 5WHO MET A 289 UNP Q14145 INITIATING METHIONINE
SEQADV 5WHO GLY A 290 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO SER A 291 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO SER A 292 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO HIS A 293 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO HIS A 294 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO HIS A 295 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO HIS A 296 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO HIS A 297 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO HIS A 298 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO SER A 299 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO SER A 300 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO GLY A 301 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO GLY A 302 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO GLU A 303 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO ASN A 304 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO LEU A 305 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO TYR A 306 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO PHE A 307 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO GLN A 308 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO GLY A 309 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO HIS A 310 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO MET A 311 UNP Q14145 EXPRESSION TAG
SEQADV 5WHO SER A 319 UNP Q14145 CYS 319 ENGINEERED MUTATION
SEQADV 5WHO ALA A 540 UNP Q14145 GLU 540 ENGINEERED MUTATION
SEQADV 5WHO ALA A 542 UNP Q14145 GLU 542 ENGINEERED MUTATION
SEQADV 5WHO SER A 613 UNP Q14145 CYS 613 ENGINEERED MUTATION
SEQADV 5WHO SER A 622 UNP Q14145 CYS 622 ENGINEERED MUTATION
SEQADV 5WHO SER A 624 UNP Q14145 CYS 624 ENGINEERED MUTATION
SEQRES 1 B 336 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 336 GLY GLU ASN LEU TYR PHE GLN GLY HIS MET LYS PRO THR
SEQRES 3 B 336 GLN VAL MET PRO SER ARG ALA PRO LYS VAL GLY ARG LEU
SEQRES 4 B 336 ILE TYR THR ALA GLY GLY TYR PHE ARG GLN SER LEU SER
SEQRES 5 B 336 TYR LEU GLU ALA TYR ASN PRO SER ASP GLY THR TRP LEU
SEQRES 6 B 336 ARG LEU ALA ASP LEU GLN VAL PRO ARG SER GLY LEU ALA
SEQRES 7 B 336 GLY CYS VAL VAL GLY GLY LEU LEU TYR ALA VAL GLY GLY
SEQRES 8 B 336 ARG ASN ASN SER PRO ASP GLY ASN THR ASP SER SER ALA
SEQRES 9 B 336 LEU ASP CYS TYR ASN PRO MET THR ASN GLN TRP SER PRO
SEQRES 10 B 336 CYS ALA PRO MET SER VAL PRO ARG ASN ARG ILE GLY VAL
SEQRES 11 B 336 GLY VAL ILE ASP GLY HIS ILE TYR ALA VAL GLY GLY SER
SEQRES 12 B 336 HIS GLY CYS ILE HIS HIS ASN SER VAL GLU ARG TYR GLU
SEQRES 13 B 336 PRO GLU ARG ASP GLU TRP HIS LEU VAL ALA PRO MET LEU
SEQRES 14 B 336 THR ARG ARG ILE GLY VAL GLY VAL ALA VAL LEU ASN ARG
SEQRES 15 B 336 LEU LEU TYR ALA VAL GLY GLY PHE ASP GLY THR ASN ARG
SEQRES 16 B 336 LEU ASN SER ALA GLU CYS TYR TYR PRO GLU ARG ASN GLU
SEQRES 17 B 336 TRP ARG MET ILE THR ALA MET ASN THR ILE ARG SER GLY
SEQRES 18 B 336 ALA GLY VAL CYS VAL LEU HIS ASN CYS ILE TYR ALA ALA
SEQRES 19 B 336 GLY GLY TYR ASP GLY GLN ASP GLN LEU ASN SER VAL GLU
SEQRES 20 B 336 ARG TYR ASP VAL ALA THR ALA THR TRP THR PHE VAL ALA
SEQRES 21 B 336 PRO MET LYS HIS ARG ARG SER ALA LEU GLY ILE THR VAL
SEQRES 22 B 336 HIS GLN GLY ARG ILE TYR VAL LEU GLY GLY TYR ASP GLY
SEQRES 23 B 336 HIS THR PHE LEU ASP SER VAL GLU CYS TYR ASP PRO ASP
SEQRES 24 B 336 THR ASP THR TRP SER GLU VAL THR ARG MET THR SER GLY
SEQRES 25 B 336 ARG SER GLY VAL GLY VAL ALA VAL THR MET GLU PRO SER
SEQRES 26 B 336 ARG LYS GLN ILE ASP GLN GLN ASN SER THR SER
SEQRES 1 A 336 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 336 GLY GLU ASN LEU TYR PHE GLN GLY HIS MET LYS PRO THR
SEQRES 3 A 336 GLN VAL MET PRO SER ARG ALA PRO LYS VAL GLY ARG LEU
SEQRES 4 A 336 ILE TYR THR ALA GLY GLY TYR PHE ARG GLN SER LEU SER
SEQRES 5 A 336 TYR LEU GLU ALA TYR ASN PRO SER ASP GLY THR TRP LEU
SEQRES 6 A 336 ARG LEU ALA ASP LEU GLN VAL PRO ARG SER GLY LEU ALA
SEQRES 7 A 336 GLY CYS VAL VAL GLY GLY LEU LEU TYR ALA VAL GLY GLY
SEQRES 8 A 336 ARG ASN ASN SER PRO ASP GLY ASN THR ASP SER SER ALA
SEQRES 9 A 336 LEU ASP CYS TYR ASN PRO MET THR ASN GLN TRP SER PRO
SEQRES 10 A 336 CYS ALA PRO MET SER VAL PRO ARG ASN ARG ILE GLY VAL
SEQRES 11 A 336 GLY VAL ILE ASP GLY HIS ILE TYR ALA VAL GLY GLY SER
SEQRES 12 A 336 HIS GLY CYS ILE HIS HIS ASN SER VAL GLU ARG TYR GLU
SEQRES 13 A 336 PRO GLU ARG ASP GLU TRP HIS LEU VAL ALA PRO MET LEU
SEQRES 14 A 336 THR ARG ARG ILE GLY VAL GLY VAL ALA VAL LEU ASN ARG
SEQRES 15 A 336 LEU LEU TYR ALA VAL GLY GLY PHE ASP GLY THR ASN ARG
SEQRES 16 A 336 LEU ASN SER ALA GLU CYS TYR TYR PRO GLU ARG ASN GLU
SEQRES 17 A 336 TRP ARG MET ILE THR ALA MET ASN THR ILE ARG SER GLY
SEQRES 18 A 336 ALA GLY VAL CYS VAL LEU HIS ASN CYS ILE TYR ALA ALA
SEQRES 19 A 336 GLY GLY TYR ASP GLY GLN ASP GLN LEU ASN SER VAL GLU
SEQRES 20 A 336 ARG TYR ASP VAL ALA THR ALA THR TRP THR PHE VAL ALA
SEQRES 21 A 336 PRO MET LYS HIS ARG ARG SER ALA LEU GLY ILE THR VAL
SEQRES 22 A 336 HIS GLN GLY ARG ILE TYR VAL LEU GLY GLY TYR ASP GLY
SEQRES 23 A 336 HIS THR PHE LEU ASP SER VAL GLU CYS TYR ASP PRO ASP
SEQRES 24 A 336 THR ASP THR TRP SER GLU VAL THR ARG MET THR SER GLY
SEQRES 25 A 336 ARG SER GLY VAL GLY VAL ALA VAL THR MET GLU PRO SER
SEQRES 26 A 336 ARG LYS GLN ILE ASP GLN GLN ASN SER THR SER
HET SO4 B 701 5
HET SO4 B 702 5
HET SO4 B 703 5
HET SO4 A 701 5
HET AO7 A 702 14
HETNAM SO4 SULFATE ION
HETNAM AO7 4-OXO-4H-1-BENZOPYRAN-2-CARBOXYLIC ACID
HETSYN AO7 9,10-SECOCHOLESTA-5,7,10(19)-TRIENE-1,3,25-TRIOL,2-(3-
HETSYN 2 AO7 HYDROXYPROPOXY)-,(1A,2A,3B,5Z,7E)
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 AO7 C10 H6 O4
FORMUL 8 HOH *155(H2 O)
SHEET 1 AA1 4 TRP B 352 ARG B 354 0
SHEET 2 AA1 4 LEU B 342 TYR B 345 -1 N ALA B 344 O LEU B 353
SHEET 3 AA1 4 ARG B 326 ALA B 331 -1 N THR B 330 O GLU B 343
SHEET 4 AA1 4 GLY B 605 MET B 610 -1 O ALA B 607 N TYR B 329
SHEET 1 AA2 4 ALA B 366 VAL B 370 0
SHEET 2 AA2 4 LEU B 373 VAL B 377 -1 O TYR B 375 N CYS B 368
SHEET 3 AA2 4 LEU B 393 TYR B 396 -1 O TYR B 396 N LEU B 374
SHEET 4 AA2 4 TRP B 403 PRO B 405 -1 O SER B 404 N CYS B 395
SHEET 1 AA3 2 ARG B 380 ASN B 382 0
SHEET 2 AA3 2 ASN B 387 ASP B 389 -1 O THR B 388 N ASN B 381
SHEET 1 AA4 4 GLY B 417 ILE B 421 0
SHEET 2 AA4 4 HIS B 424 VAL B 428 -1 O VAL B 428 N GLY B 417
SHEET 3 AA4 4 VAL B 440 TYR B 443 -1 O GLU B 441 N ALA B 427
SHEET 4 AA4 4 TRP B 450 VAL B 453 -1 O HIS B 451 N ARG B 442
SHEET 1 AA5 2 SER B 431 HIS B 432 0
SHEET 2 AA5 2 ILE B 435 HIS B 436 -1 O ILE B 435 N HIS B 432
SHEET 1 AA6 4 GLY B 464 LEU B 468 0
SHEET 2 AA6 4 LEU B 471 PHE B 478 -1 O VAL B 475 N GLY B 464
SHEET 3 AA6 4 ARG B 483 TYR B 491 -1 O TYR B 490 N LEU B 472
SHEET 4 AA6 4 GLU B 496 MET B 499 -1 O ARG B 498 N CYS B 489
SHEET 1 AA7 4 GLY B 511 VAL B 514 0
SHEET 2 AA7 4 ILE B 519 ALA B 522 -1 O ALA B 522 N GLY B 511
SHEET 3 AA7 4 VAL B 534 ASP B 538 -1 O TYR B 537 N ILE B 519
SHEET 4 AA7 4 THR B 543 VAL B 547 -1 O VAL B 547 N VAL B 534
SHEET 1 AA8 4 GLY B 558 HIS B 562 0
SHEET 2 AA8 4 ARG B 565 LEU B 569 -1 O LEU B 569 N GLY B 558
SHEET 3 AA8 4 SER B 580 ASP B 585 -1 O TYR B 584 N ILE B 566
SHEET 4 AA8 4 THR B 590 ARG B 596 -1 O THR B 590 N ASP B 585
SHEET 1 AA9 2 GLU A 343 TYR A 345 0
SHEET 2 AA9 2 TRP A 352 ARG A 354 -1 O LEU A 353 N ALA A 344
SHEET 1 AB1 4 ALA A 366 VAL A 370 0
SHEET 2 AB1 4 LEU A 373 VAL A 377 -1 O TYR A 375 N CYS A 368
SHEET 3 AB1 4 LEU A 393 TYR A 396 -1 O ASP A 394 N ALA A 376
SHEET 4 AB1 4 SER A 404 CYS A 406 -1 O SER A 404 N CYS A 395
SHEET 1 AB2 2 ARG A 380 SER A 383 0
SHEET 2 AB2 2 GLY A 386 ASP A 389 -1 O THR A 388 N ASN A 381
SHEET 1 AB3 4 GLY A 417 ILE A 421 0
SHEET 2 AB3 4 HIS A 424 VAL A 428 -1 O VAL A 428 N GLY A 417
SHEET 3 AB3 4 VAL A 440 TYR A 443 -1 O GLU A 441 N ALA A 427
SHEET 4 AB3 4 TRP A 450 VAL A 453 -1 O VAL A 453 N VAL A 440
SHEET 1 AB4 2 SER A 431 HIS A 432 0
SHEET 2 AB4 2 ILE A 435 HIS A 436 -1 O ILE A 435 N HIS A 432
SHEET 1 AB5 4 GLY A 464 LEU A 468 0
SHEET 2 AB5 4 LEU A 471 PHE A 478 -1 O TYR A 473 N ALA A 466
SHEET 3 AB5 4 ARG A 483 TYR A 490 -1 O TYR A 490 N LEU A 472
SHEET 4 AB5 4 TRP A 497 MET A 499 -1 O ARG A 498 N CYS A 489
SHEET 1 AB6 4 GLY A 511 VAL A 514 0
SHEET 2 AB6 4 CYS A 518 ALA A 522 -1 O TYR A 520 N CYS A 513
SHEET 3 AB6 4 VAL A 534 ASP A 538 -1 O TYR A 537 N ILE A 519
SHEET 4 AB6 4 THR A 543 PHE A 546 -1 O THR A 545 N ARG A 536
SHEET 1 AB7 4 GLY A 558 HIS A 562 0
SHEET 2 AB7 4 ARG A 565 LEU A 569 -1 O TYR A 567 N THR A 560
SHEET 3 AB7 4 SER A 580 ASP A 585 -1 O TYR A 584 N ILE A 566
SHEET 4 AB7 4 THR A 590 ARG A 596 -1 O VAL A 594 N VAL A 581
SITE 1 AC1 7 GLN A 337 PRO A 384 ARG B 380 ASN B 382
SITE 2 AC1 7 ASN B 414 ARG B 415 HOH B 817
SITE 1 AC2 5 ILE B 435 HIS B 437 ASN B 438 SER B 439
SITE 2 AC2 5 HOH B 851
SITE 1 AC3 4 TYR B 341 THR B 598 SER B 599 HOH B 858
SITE 1 AC4 5 ILE A 435 HIS A 437 ASN A 438 SER A 439
SITE 2 AC4 5 ARG A 459
SITE 1 AC5 7 ARG A 415 PHE A 478 ARG A 483 SER A 508
SITE 2 AC5 7 TYR A 525 GLN A 530 SER A 555
CRYST1 78.460 69.090 143.206 90.00 91.11 90.00 I 1 2 1 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 0.012745 0.000000 0.000247 0.00000
SCALE2 0.000000 0.014474 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006984 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
