HEADER PEPTIDE BINDING PROTEIN 02-FEB-18 6FMQ
TITLE KEAP1 - PEPTIDE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KELCH-LIKE ECH-ASSOCIATED PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CYTOSOLIC INHIBITOR OF NRF2,INRF2,KELCH-LIKE PROTEIN 19;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ACY-SC1-GLU-THR-GLY-GLU-LEU;
COMPND 8 CHAIN: D;
COMPND 9 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 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630
KEYWDS KEAP1, KELCH-DOMAIN, NRF2, NEURODEGENERATIVE, INHIBITOR, PEPTIDE
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.K.TALAPATRA,F.KOZIELSKI,G.WELLS,N.D.GEORGAKOPOULOS
REVDAT 3 17-JAN-24 6FMQ 1 REMARK LINK
REVDAT 2 12-SEP-18 6FMQ 1 JRNL
REVDAT 1 08-AUG-18 6FMQ 0
JRNL AUTH N.D.GEORGAKOPOULOS,S.K.TALAPATRA,J.GATLIFF,F.KOZIELSKI,
JRNL AUTH 2 G.WELLS
JRNL TITL MODIFIED PEPTIDE INHIBITORS OF THE KEAP1-NRF2
JRNL TITL 2 PROTEIN-PROTEIN INTERACTION INCORPORATING UNNATURAL AMINO
JRNL TITL 3 ACIDS.
JRNL REF CHEMBIOCHEM V. 19 1810 2018
JRNL REFN ESSN 1439-7633
JRNL PMID 29927029
JRNL DOI 10.1002/CBIC.201800170
REMARK 2
REMARK 2 RESOLUTION. 2.10 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 71513
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 3639
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 47.8490 - 6.2168 0.99 2797 187 0.1740 0.2232
REMARK 3 2 6.2168 - 4.9361 0.98 2686 133 0.1438 0.1987
REMARK 3 3 4.9361 - 4.3126 0.99 2641 156 0.1109 0.1158
REMARK 3 4 4.3126 - 3.9185 0.99 2640 153 0.1185 0.1451
REMARK 3 5 3.9185 - 3.6377 0.99 2620 142 0.1372 0.1631
REMARK 3 6 3.6377 - 3.4233 0.99 2631 143 0.1490 0.1940
REMARK 3 7 3.4233 - 3.2519 1.00 2619 139 0.1615 0.1774
REMARK 3 8 3.2519 - 3.1104 1.00 2638 142 0.1779 0.2425
REMARK 3 9 3.1104 - 2.9907 1.00 2620 129 0.1881 0.2023
REMARK 3 10 2.9907 - 2.8875 0.99 2628 117 0.1803 0.1891
REMARK 3 11 2.8875 - 2.7972 0.97 2527 148 0.1768 0.2260
REMARK 3 12 2.7972 - 2.7173 0.99 2573 153 0.1952 0.2533
REMARK 3 13 2.7173 - 2.6457 1.00 2590 160 0.2037 0.2508
REMARK 3 14 2.6457 - 2.5812 1.00 2600 142 0.2021 0.2706
REMARK 3 15 2.5812 - 2.5225 1.00 2592 148 0.2122 0.2514
REMARK 3 16 2.5225 - 2.4688 1.00 2589 150 0.2116 0.2492
REMARK 3 17 2.4688 - 2.4195 1.00 2642 102 0.2101 0.2715
REMARK 3 18 2.4195 - 2.3738 1.00 2592 138 0.2030 0.2378
REMARK 3 19 2.3738 - 2.3314 1.00 2612 144 0.2092 0.2773
REMARK 3 20 2.3314 - 2.2919 1.00 2593 108 0.2199 0.2649
REMARK 3 21 2.2919 - 2.2549 1.00 2628 119 0.2245 0.2489
REMARK 3 22 2.2549 - 2.2202 0.98 2553 133 0.2361 0.2872
REMARK 3 23 2.2202 - 2.1876 0.98 2540 135 0.2492 0.2656
REMARK 3 24 2.1876 - 2.1568 0.99 2569 142 0.2480 0.2641
REMARK 3 25 2.1568 - 2.1276 1.00 2618 133 0.2500 0.2928
REMARK 3 26 2.1276 - 2.1000 0.99 2536 143 0.2568 0.3067
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.820
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 : 0.012 4725
REMARK 3 ANGLE : 1.203 6437
REMARK 3 CHIRALITY : 0.086 676
REMARK 3 PLANARITY : 0.007 868
REMARK 3 DIHEDRAL : 8.785 3621
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 6FMQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1200008615.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-17
REMARK 200 TEMPERATURE (KELVIN) : 180
REMARK 200 PH : 4.6
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) : 0.9660
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71681
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
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: PHASER
REMARK 200 STARTING MODEL: 3VNG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4.0 M AMMONIUM ACETATE, 0.1 M SODIUM
REMARK 280 ACETATE TRIHYDRATE PH 4.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 37.82600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 105.56850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.06450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 105.56850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.82600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.06450
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D
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 A 196
REMARK 465 ALA A 197
REMARK 465 MET A 198
REMARK 465 GLY A 199
REMARK 465 SER A 200
REMARK 465 SER A 201
REMARK 465 HIS A 202
REMARK 465 HIS A 203
REMARK 465 HIS A 204
REMARK 465 HIS A 205
REMARK 465 HIS A 206
REMARK 465 HIS A 207
REMARK 465 HIS A 208
REMARK 465 HIS A 209
REMARK 465 SER A 210
REMARK 465 SER A 211
REMARK 465 GLY A 212
REMARK 465 LEU A 213
REMARK 465 VAL A 214
REMARK 465 PRO A 215
REMARK 465 ARG A 216
REMARK 465 GLY A 217
REMARK 465 SER A 218
REMARK 465 HIS A 219
REMARK 465 MET A 220
REMARK 465 ALA A 221
REMARK 465 SER A 222
REMARK 465 MET A 223
REMARK 465 SER A 224
REMARK 465 ASP A 225
REMARK 465 SER A 226
REMARK 465 GLU A 227
REMARK 465 VAL A 228
REMARK 465 ASN A 229
REMARK 465 GLN A 230
REMARK 465 GLU A 231
REMARK 465 ALA A 232
REMARK 465 LYS A 233
REMARK 465 PRO A 234
REMARK 465 GLU A 235
REMARK 465 VAL A 236
REMARK 465 LYS A 237
REMARK 465 PRO A 238
REMARK 465 GLU A 239
REMARK 465 VAL A 240
REMARK 465 LYS A 241
REMARK 465 PRO A 242
REMARK 465 GLU A 243
REMARK 465 THR A 244
REMARK 465 HIS A 245
REMARK 465 ILE A 246
REMARK 465 ASN A 247
REMARK 465 LEU A 248
REMARK 465 LYS A 249
REMARK 465 VAL A 250
REMARK 465 SER A 251
REMARK 465 ASP A 252
REMARK 465 GLY A 253
REMARK 465 SER A 254
REMARK 465 SER A 255
REMARK 465 GLU A 256
REMARK 465 ILE A 257
REMARK 465 PHE A 258
REMARK 465 PHE A 259
REMARK 465 LYS A 260
REMARK 465 ILE A 261
REMARK 465 LYS A 262
REMARK 465 LYS A 263
REMARK 465 THR A 264
REMARK 465 THR A 265
REMARK 465 PRO A 266
REMARK 465 LEU A 267
REMARK 465 ARG A 268
REMARK 465 ARG A 269
REMARK 465 LEU A 270
REMARK 465 MET A 271
REMARK 465 GLU A 272
REMARK 465 ALA A 273
REMARK 465 PHE A 274
REMARK 465 ALA A 275
REMARK 465 LYS A 276
REMARK 465 ARG A 277
REMARK 465 GLN A 278
REMARK 465 GLY A 279
REMARK 465 LYS A 280
REMARK 465 GLU A 281
REMARK 465 MET A 282
REMARK 465 ASP A 283
REMARK 465 SER A 284
REMARK 465 LEU A 285
REMARK 465 ARG A 286
REMARK 465 PHE A 287
REMARK 465 LEU A 288
REMARK 465 TYR A 289
REMARK 465 ASP A 290
REMARK 465 GLY A 291
REMARK 465 ILE A 292
REMARK 465 ARG A 293
REMARK 465 ILE A 294
REMARK 465 GLN A 295
REMARK 465 ALA A 296
REMARK 465 ASP A 297
REMARK 465 GLN A 298
REMARK 465 THR A 299
REMARK 465 PRO A 300
REMARK 465 GLU A 301
REMARK 465 ASP A 302
REMARK 465 LEU A 303
REMARK 465 ASP A 304
REMARK 465 MET A 305
REMARK 465 GLU A 306
REMARK 465 ASP A 307
REMARK 465 ASN A 308
REMARK 465 ASP A 309
REMARK 465 ILE A 310
REMARK 465 ILE A 311
REMARK 465 GLU A 312
REMARK 465 ALA A 313
REMARK 465 HIS A 314
REMARK 465 ARG A 315
REMARK 465 GLU A 316
REMARK 465 GLN A 317
REMARK 465 ILE A 318
REMARK 465 GLY A 319
REMARK 465 GLY A 320
REMARK 465 ALA A 321
REMARK 465 PRO A 322
REMARK 465 LYS A 323
REMARK 465 VAL A 324
REMARK 465 MET B 196
REMARK 465 ALA B 197
REMARK 465 MET B 198
REMARK 465 GLY B 199
REMARK 465 SER B 200
REMARK 465 SER B 201
REMARK 465 HIS B 202
REMARK 465 HIS B 203
REMARK 465 HIS B 204
REMARK 465 HIS B 205
REMARK 465 HIS B 206
REMARK 465 HIS B 207
REMARK 465 HIS B 208
REMARK 465 HIS B 209
REMARK 465 SER B 210
REMARK 465 SER B 211
REMARK 465 GLY B 212
REMARK 465 LEU B 213
REMARK 465 VAL B 214
REMARK 465 PRO B 215
REMARK 465 ARG B 216
REMARK 465 GLY B 217
REMARK 465 SER B 218
REMARK 465 HIS B 219
REMARK 465 MET B 220
REMARK 465 ALA B 221
REMARK 465 SER B 222
REMARK 465 MET B 223
REMARK 465 SER B 224
REMARK 465 ASP B 225
REMARK 465 SER B 226
REMARK 465 GLU B 227
REMARK 465 VAL B 228
REMARK 465 ASN B 229
REMARK 465 GLN B 230
REMARK 465 GLU B 231
REMARK 465 ALA B 232
REMARK 465 LYS B 233
REMARK 465 PRO B 234
REMARK 465 GLU B 235
REMARK 465 VAL B 236
REMARK 465 LYS B 237
REMARK 465 PRO B 238
REMARK 465 GLU B 239
REMARK 465 VAL B 240
REMARK 465 LYS B 241
REMARK 465 PRO B 242
REMARK 465 GLU B 243
REMARK 465 THR B 244
REMARK 465 HIS B 245
REMARK 465 ILE B 246
REMARK 465 ASN B 247
REMARK 465 LEU B 248
REMARK 465 LYS B 249
REMARK 465 VAL B 250
REMARK 465 SER B 251
REMARK 465 ASP B 252
REMARK 465 GLY B 253
REMARK 465 SER B 254
REMARK 465 SER B 255
REMARK 465 GLU B 256
REMARK 465 ILE B 257
REMARK 465 PHE B 258
REMARK 465 PHE B 259
REMARK 465 LYS B 260
REMARK 465 ILE B 261
REMARK 465 LYS B 262
REMARK 465 LYS B 263
REMARK 465 THR B 264
REMARK 465 THR B 265
REMARK 465 PRO B 266
REMARK 465 LEU B 267
REMARK 465 ARG B 268
REMARK 465 ARG B 269
REMARK 465 LEU B 270
REMARK 465 MET B 271
REMARK 465 GLU B 272
REMARK 465 ALA B 273
REMARK 465 PHE B 274
REMARK 465 ALA B 275
REMARK 465 LYS B 276
REMARK 465 ARG B 277
REMARK 465 GLN B 278
REMARK 465 GLY B 279
REMARK 465 LYS B 280
REMARK 465 GLU B 281
REMARK 465 MET B 282
REMARK 465 ASP B 283
REMARK 465 SER B 284
REMARK 465 LEU B 285
REMARK 465 ARG B 286
REMARK 465 PHE B 287
REMARK 465 LEU B 288
REMARK 465 TYR B 289
REMARK 465 ASP B 290
REMARK 465 GLY B 291
REMARK 465 ILE B 292
REMARK 465 ARG B 293
REMARK 465 ILE B 294
REMARK 465 GLN B 295
REMARK 465 ALA B 296
REMARK 465 ASP B 297
REMARK 465 GLN B 298
REMARK 465 THR B 299
REMARK 465 PRO B 300
REMARK 465 GLU B 301
REMARK 465 ASP B 302
REMARK 465 LEU B 303
REMARK 465 ASP B 304
REMARK 465 MET B 305
REMARK 465 GLU B 306
REMARK 465 ASP B 307
REMARK 465 ASN B 308
REMARK 465 ASP B 309
REMARK 465 ILE B 310
REMARK 465 ILE B 311
REMARK 465 GLU B 312
REMARK 465 ALA B 313
REMARK 465 HIS B 314
REMARK 465 ARG B 315
REMARK 465 GLU B 316
REMARK 465 GLN B 317
REMARK 465 ILE B 318
REMARK 465 GLY B 319
REMARK 465 GLY B 320
REMARK 465 ALA B 321
REMARK 465 PRO B 322
REMARK 465 LYS B 323
REMARK 465 VAL B 324
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 GLU A 446 CG CD OE1 OE2
REMARK 470 LYS B 551 CD CE NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG B 565 CZ
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 NH1 ARG A 336 O HOH A 801 1.70
REMARK 500 O HOH A 928 O HOH A 951 1.95
REMARK 500 O HOH A 901 O HOH A 951 1.98
REMARK 500 NE ARG B 336 O HOH B 801 2.17
REMARK 500 O HOH B 872 O HOH B 947 2.19
REMARK 500 O HOH A 911 O HOH A 962 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 ARG A 380 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 494 NE - CZ - NH2 ANGL. DEV. = -3.6 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 ARG A 336 -18.63 65.75
REMARK 500 ARG A 336 -19.46 68.88
REMARK 500 VAL A 453 -164.87 -115.93
REMARK 500 THR A 481 -34.29 -131.04
REMARK 500 GLN A 528 -68.91 -107.05
REMARK 500 GLN A 528 -62.17 -107.05
REMARK 500 VAL A 547 -167.74 -117.63
REMARK 500 ARG B 336 -34.90 67.79
REMARK 500 ASP B 385 -80.19 -26.64
REMARK 500 VAL B 453 -167.36 -122.54
REMARK 500 THR B 481 -54.16 -127.47
REMARK 500 VAL B 547 -165.89 -115.95
REMARK 500 HIS B 575 -33.17 -137.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 709 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 919 O
REMARK 620 2 HOH A 958 O 99.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 710 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 811 O
REMARK 620 2 HOH A 831 O 145.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 705 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 334 OH
REMARK 620 2 ASN B 382 OD1 117.0
REMARK 620 3 HOH B 889 O 125.1 101.2
REMARK 620 4 HOH B 957 O 138.4 87.5 76.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 707 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 905 O
REMARK 620 2 HOH B 952 O 161.1
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues ACE D 1 and DYW D 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DYW D 2 and GLU D 3
DBREF 6FMQ A 321 609 UNP Q14145 KEAP1_HUMAN 321 609
DBREF 6FMQ B 321 609 UNP Q14145 KEAP1_HUMAN 321 609
DBREF 6FMQ D 1 7 PDB 6FMQ 6FMQ 1 7
SEQADV 6FMQ MET A 196 UNP Q14145 INITIATING METHIONINE
SEQADV 6FMQ ALA A 197 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ MET A 198 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY A 199 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER A 200 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER A 201 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS A 202 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS A 203 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS A 204 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS A 205 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS A 206 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS A 207 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS A 208 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS A 209 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER A 210 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER A 211 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY A 212 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LEU A 213 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ VAL A 214 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PRO A 215 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ARG A 216 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY A 217 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER A 218 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS A 219 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ MET A 220 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ALA A 221 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER A 222 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ MET A 223 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER A 224 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP A 225 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER A 226 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU A 227 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ VAL A 228 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASN A 229 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLN A 230 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU A 231 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ALA A 232 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS A 233 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PRO A 234 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU A 235 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ VAL A 236 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS A 237 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PRO A 238 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU A 239 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ VAL A 240 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS A 241 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PRO A 242 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU A 243 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ THR A 244 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS A 245 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE A 246 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASN A 247 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LEU A 248 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS A 249 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ VAL A 250 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER A 251 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP A 252 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY A 253 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER A 254 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER A 255 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU A 256 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE A 257 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PHE A 258 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PHE A 259 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS A 260 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE A 261 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS A 262 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS A 263 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ THR A 264 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ THR A 265 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PRO A 266 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LEU A 267 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ARG A 268 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ARG A 269 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LEU A 270 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ MET A 271 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU A 272 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ALA A 273 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PHE A 274 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ALA A 275 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS A 276 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ARG A 277 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLN A 278 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY A 279 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS A 280 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU A 281 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ MET A 282 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP A 283 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER A 284 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LEU A 285 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ARG A 286 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PHE A 287 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LEU A 288 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ TYR A 289 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP A 290 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY A 291 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE A 292 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ARG A 293 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE A 294 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLN A 295 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ALA A 296 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP A 297 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLN A 298 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ THR A 299 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PRO A 300 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU A 301 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP A 302 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LEU A 303 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP A 304 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ MET A 305 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU A 306 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP A 307 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASN A 308 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP A 309 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE A 310 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE A 311 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU A 312 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ALA A 313 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS A 314 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ARG A 315 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU A 316 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLN A 317 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE A 318 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY A 319 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY A 320 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ MET B 196 UNP Q14145 INITIATING METHIONINE
SEQADV 6FMQ ALA B 197 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ MET B 198 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY B 199 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER B 200 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER B 201 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS B 202 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS B 203 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS B 204 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS B 205 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS B 206 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS B 207 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS B 208 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS B 209 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER B 210 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER B 211 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY B 212 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LEU B 213 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ VAL B 214 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PRO B 215 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ARG B 216 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY B 217 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER B 218 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS B 219 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ MET B 220 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ALA B 221 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER B 222 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ MET B 223 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER B 224 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP B 225 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER B 226 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU B 227 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ VAL B 228 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASN B 229 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLN B 230 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU B 231 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ALA B 232 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS B 233 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PRO B 234 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU B 235 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ VAL B 236 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS B 237 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PRO B 238 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU B 239 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ VAL B 240 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS B 241 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PRO B 242 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU B 243 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ THR B 244 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS B 245 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE B 246 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASN B 247 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LEU B 248 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS B 249 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ VAL B 250 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER B 251 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP B 252 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY B 253 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER B 254 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER B 255 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU B 256 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE B 257 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PHE B 258 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PHE B 259 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS B 260 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE B 261 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS B 262 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS B 263 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ THR B 264 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ THR B 265 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PRO B 266 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LEU B 267 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ARG B 268 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ARG B 269 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LEU B 270 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ MET B 271 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU B 272 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ALA B 273 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PHE B 274 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ALA B 275 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS B 276 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ARG B 277 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLN B 278 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY B 279 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LYS B 280 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU B 281 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ MET B 282 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP B 283 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ SER B 284 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LEU B 285 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ARG B 286 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PHE B 287 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LEU B 288 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ TYR B 289 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP B 290 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY B 291 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE B 292 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ARG B 293 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE B 294 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLN B 295 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ALA B 296 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP B 297 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLN B 298 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ THR B 299 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ PRO B 300 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU B 301 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP B 302 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ LEU B 303 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP B 304 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ MET B 305 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU B 306 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP B 307 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASN B 308 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ASP B 309 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE B 310 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE B 311 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU B 312 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ALA B 313 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ HIS B 314 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ARG B 315 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLU B 316 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLN B 317 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ ILE B 318 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY B 319 UNP Q14145 EXPRESSION TAG
SEQADV 6FMQ GLY B 320 UNP Q14145 EXPRESSION TAG
SEQRES 1 A 414 MET ALA MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS
SEQRES 2 A 414 HIS SER SER GLY LEU VAL PRO ARG GLY SER HIS MET ALA
SEQRES 3 A 414 SER MET SER ASP SER GLU VAL ASN GLN GLU ALA LYS PRO
SEQRES 4 A 414 GLU VAL LYS PRO GLU VAL LYS PRO GLU THR HIS ILE ASN
SEQRES 5 A 414 LEU LYS VAL SER ASP GLY SER SER GLU ILE PHE PHE LYS
SEQRES 6 A 414 ILE LYS LYS THR THR PRO LEU ARG ARG LEU MET GLU ALA
SEQRES 7 A 414 PHE ALA LYS ARG GLN GLY LYS GLU MET ASP SER LEU ARG
SEQRES 8 A 414 PHE LEU TYR ASP GLY ILE ARG ILE GLN ALA ASP GLN THR
SEQRES 9 A 414 PRO GLU ASP LEU ASP MET GLU ASP ASN ASP ILE ILE GLU
SEQRES 10 A 414 ALA HIS ARG GLU GLN ILE GLY GLY ALA PRO LYS VAL GLY
SEQRES 11 A 414 ARG LEU ILE TYR THR ALA GLY GLY TYR PHE ARG GLN SER
SEQRES 12 A 414 LEU SER TYR LEU GLU ALA TYR ASN PRO SER ASP GLY THR
SEQRES 13 A 414 TRP LEU ARG LEU ALA ASP LEU GLN VAL PRO ARG SER GLY
SEQRES 14 A 414 LEU ALA GLY CYS VAL VAL GLY GLY LEU LEU TYR ALA VAL
SEQRES 15 A 414 GLY GLY ARG ASN ASN SER PRO ASP GLY ASN THR ASP SER
SEQRES 16 A 414 SER ALA LEU ASP CYS TYR ASN PRO MET THR ASN GLN TRP
SEQRES 17 A 414 SER PRO CYS ALA PRO MET SER VAL PRO ARG ASN ARG ILE
SEQRES 18 A 414 GLY VAL GLY VAL ILE ASP GLY HIS ILE TYR ALA VAL GLY
SEQRES 19 A 414 GLY SER HIS GLY CYS ILE HIS HIS ASN SER VAL GLU ARG
SEQRES 20 A 414 TYR GLU PRO GLU ARG ASP GLU TRP HIS LEU VAL ALA PRO
SEQRES 21 A 414 MET LEU THR ARG ARG ILE GLY VAL GLY VAL ALA VAL LEU
SEQRES 22 A 414 ASN ARG LEU LEU TYR ALA VAL GLY GLY PHE ASP GLY THR
SEQRES 23 A 414 ASN ARG LEU ASN SER ALA GLU CYS TYR TYR PRO GLU ARG
SEQRES 24 A 414 ASN GLU TRP ARG MET ILE THR ALA MET ASN THR ILE ARG
SEQRES 25 A 414 SER GLY ALA GLY VAL CYS VAL LEU HIS ASN CYS ILE TYR
SEQRES 26 A 414 ALA ALA GLY GLY TYR ASP GLY GLN ASP GLN LEU ASN SER
SEQRES 27 A 414 VAL GLU ARG TYR ASP VAL GLU THR GLU THR TRP THR PHE
SEQRES 28 A 414 VAL ALA PRO MET LYS HIS ARG ARG SER ALA LEU GLY ILE
SEQRES 29 A 414 THR VAL HIS GLN GLY ARG ILE TYR VAL LEU GLY GLY TYR
SEQRES 30 A 414 ASP GLY HIS THR PHE LEU ASP SER VAL GLU CYS TYR ASP
SEQRES 31 A 414 PRO ASP THR ASP THR TRP SER GLU VAL THR ARG MET THR
SEQRES 32 A 414 SER GLY ARG SER GLY VAL GLY VAL ALA VAL THR
SEQRES 1 B 414 MET ALA MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS
SEQRES 2 B 414 HIS SER SER GLY LEU VAL PRO ARG GLY SER HIS MET ALA
SEQRES 3 B 414 SER MET SER ASP SER GLU VAL ASN GLN GLU ALA LYS PRO
SEQRES 4 B 414 GLU VAL LYS PRO GLU VAL LYS PRO GLU THR HIS ILE ASN
SEQRES 5 B 414 LEU LYS VAL SER ASP GLY SER SER GLU ILE PHE PHE LYS
SEQRES 6 B 414 ILE LYS LYS THR THR PRO LEU ARG ARG LEU MET GLU ALA
SEQRES 7 B 414 PHE ALA LYS ARG GLN GLY LYS GLU MET ASP SER LEU ARG
SEQRES 8 B 414 PHE LEU TYR ASP GLY ILE ARG ILE GLN ALA ASP GLN THR
SEQRES 9 B 414 PRO GLU ASP LEU ASP MET GLU ASP ASN ASP ILE ILE GLU
SEQRES 10 B 414 ALA HIS ARG GLU GLN ILE GLY GLY ALA PRO LYS VAL GLY
SEQRES 11 B 414 ARG LEU ILE TYR THR ALA GLY GLY TYR PHE ARG GLN SER
SEQRES 12 B 414 LEU SER TYR LEU GLU ALA TYR ASN PRO SER ASP GLY THR
SEQRES 13 B 414 TRP LEU ARG LEU ALA ASP LEU GLN VAL PRO ARG SER GLY
SEQRES 14 B 414 LEU ALA GLY CYS VAL VAL GLY GLY LEU LEU TYR ALA VAL
SEQRES 15 B 414 GLY GLY ARG ASN ASN SER PRO ASP GLY ASN THR ASP SER
SEQRES 16 B 414 SER ALA LEU ASP CYS TYR ASN PRO MET THR ASN GLN TRP
SEQRES 17 B 414 SER PRO CYS ALA PRO MET SER VAL PRO ARG ASN ARG ILE
SEQRES 18 B 414 GLY VAL GLY VAL ILE ASP GLY HIS ILE TYR ALA VAL GLY
SEQRES 19 B 414 GLY SER HIS GLY CYS ILE HIS HIS ASN SER VAL GLU ARG
SEQRES 20 B 414 TYR GLU PRO GLU ARG ASP GLU TRP HIS LEU VAL ALA PRO
SEQRES 21 B 414 MET LEU THR ARG ARG ILE GLY VAL GLY VAL ALA VAL LEU
SEQRES 22 B 414 ASN ARG LEU LEU TYR ALA VAL GLY GLY PHE ASP GLY THR
SEQRES 23 B 414 ASN ARG LEU ASN SER ALA GLU CYS TYR TYR PRO GLU ARG
SEQRES 24 B 414 ASN GLU TRP ARG MET ILE THR ALA MET ASN THR ILE ARG
SEQRES 25 B 414 SER GLY ALA GLY VAL CYS VAL LEU HIS ASN CYS ILE TYR
SEQRES 26 B 414 ALA ALA GLY GLY TYR ASP GLY GLN ASP GLN LEU ASN SER
SEQRES 27 B 414 VAL GLU ARG TYR ASP VAL GLU THR GLU THR TRP THR PHE
SEQRES 28 B 414 VAL ALA PRO MET LYS HIS ARG ARG SER ALA LEU GLY ILE
SEQRES 29 B 414 THR VAL HIS GLN GLY ARG ILE TYR VAL LEU GLY GLY TYR
SEQRES 30 B 414 ASP GLY HIS THR PHE LEU ASP SER VAL GLU CYS TYR ASP
SEQRES 31 B 414 PRO ASP THR ASP THR TRP SER GLU VAL THR ARG MET THR
SEQRES 32 B 414 SER GLY ARG SER GLY VAL GLY VAL ALA VAL THR
SEQRES 1 D 7 ACE DYW GLU THR GLY GLU LEU
HET ACE D 1 3
HET DYW D 2 15
HET EDO A 701 4
HET EDO A 702 4
HET ACT A 703 4
HET ACT A 704 4
HET ACT A 705 4
HET ACT A 706 4
HET ACT A 707 4
HET NA A 708 1
HET NA A 709 1
HET NA A 710 1
HET EDO B 701 4
HET EDO B 702 4
HET ACT B 703 4
HET ACT B 704 4
HET NA B 705 1
HET NA B 706 1
HET NA B 707 1
HET NA B 708 1
HETNAM ACE ACETYL GROUP
HETNAM DYW (2~{S})-1-[(2~{S})-2-AZANYL-4-OXIDANYL-4-OXIDANYLIDENE-
HETNAM 2 DYW BUTANOYL]PYRROLIDINE-2-CARBOXYLIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ACT ACETATE ION
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 ACE C2 H4 O
FORMUL 3 DYW C9 H14 N2 O5
FORMUL 4 EDO 4(C2 H6 O2)
FORMUL 6 ACT 7(C2 H3 O2 1-)
FORMUL 11 NA 7(NA 1+)
FORMUL 22 HOH *356(H2 O)
SHEET 1 AA1 4 TRP A 352 ARG A 354 0
SHEET 2 AA1 4 LEU A 342 TYR A 345 -1 N ALA A 344 O LEU A 353
SHEET 3 AA1 4 LEU A 327 ALA A 331 -1 N THR A 330 O GLU A 343
SHEET 4 AA1 4 GLY A 605 THR A 609 -1 O THR A 609 N LEU A 327
SHEET 1 AA2 4 ALA A 366 VAL A 370 0
SHEET 2 AA2 4 LEU A 373 VAL A 377 -1 O TYR A 375 N CYS A 368
SHEET 3 AA2 4 LEU A 393 ASN A 397 -1 O TYR A 396 N LEU A 374
SHEET 4 AA2 4 GLN A 402 PRO A 405 -1 O SER A 404 N CYS A 395
SHEET 1 AA3 2 ARG A 380 SER A 383 0
SHEET 2 AA3 2 GLY A 386 ASP A 389 -1 O THR A 388 N ASN A 381
SHEET 1 AA4 4 GLY A 417 ILE A 421 0
SHEET 2 AA4 4 HIS A 424 VAL A 428 -1 O TYR A 426 N GLY A 419
SHEET 3 AA4 4 VAL A 440 GLU A 444 -1 O GLU A 441 N ALA A 427
SHEET 4 AA4 4 GLU A 449 LEU A 452 -1 O HIS A 451 N ARG A 442
SHEET 1 AA5 2 SER A 431 HIS A 432 0
SHEET 2 AA5 2 ILE A 435 HIS A 436 -1 O ILE A 435 N HIS A 432
SHEET 1 AA6 4 GLY A 464 LEU A 468 0
SHEET 2 AA6 4 LEU A 471 PHE A 478 -1 O TYR A 473 N ALA A 466
SHEET 3 AA6 4 ARG A 483 TYR A 491 -1 O TYR A 490 N LEU A 472
SHEET 4 AA6 4 GLU A 496 ILE A 500 -1 O ARG A 498 N CYS A 489
SHEET 1 AA7 4 GLY A 511 LEU A 515 0
SHEET 2 AA7 4 CYS A 518 ALA A 522 -1 O ALA A 522 N GLY A 511
SHEET 3 AA7 4 VAL A 534 ASP A 538 -1 O TYR A 537 N ILE A 519
SHEET 4 AA7 4 THR A 543 VAL A 547 -1 O VAL A 547 N VAL A 534
SHEET 1 AA8 4 GLY A 558 HIS A 562 0
SHEET 2 AA8 4 ARG A 565 LEU A 569 -1 O TYR A 567 N THR A 560
SHEET 3 AA8 4 SER A 580 ASP A 585 -1 O TYR A 584 N ILE A 566
SHEET 4 AA8 4 THR A 590 ARG A 596 -1 O SER A 592 N CYS A 583
SHEET 1 AA9 4 TRP B 352 ARG B 354 0
SHEET 2 AA9 4 LEU B 342 TYR B 345 -1 N ALA B 344 O LEU B 353
SHEET 3 AA9 4 LEU B 327 ALA B 331 -1 N THR B 330 O GLU B 343
SHEET 4 AA9 4 GLY B 605 THR B 609 -1 O ALA B 607 N TYR B 329
SHEET 1 AB1 4 ALA B 366 VAL B 370 0
SHEET 2 AB1 4 LEU B 373 VAL B 377 -1 O TYR B 375 N CYS B 368
SHEET 3 AB1 4 LEU B 393 ASN B 397 -1 O TYR B 396 N LEU B 374
SHEET 4 AB1 4 GLN B 402 CYS B 406 -1 O SER B 404 N CYS B 395
SHEET 1 AB2 2 ARG B 380 SER B 383 0
SHEET 2 AB2 2 GLY B 386 ASP B 389 -1 O THR B 388 N ASN B 381
SHEET 1 AB3 4 GLY B 417 ILE B 421 0
SHEET 2 AB3 4 HIS B 424 VAL B 428 -1 O TYR B 426 N GLY B 419
SHEET 3 AB3 4 VAL B 440 TYR B 443 -1 O TYR B 443 N ILE B 425
SHEET 4 AB3 4 TRP B 450 LEU B 452 -1 O HIS B 451 N ARG B 442
SHEET 1 AB4 2 SER B 431 HIS B 432 0
SHEET 2 AB4 2 ILE B 435 HIS B 436 -1 O ILE B 435 N HIS B 432
SHEET 1 AB5 4 GLY B 464 LEU B 468 0
SHEET 2 AB5 4 LEU B 471 PHE B 478 -1 O VAL B 475 N GLY B 464
SHEET 3 AB5 4 ARG B 483 TYR B 491 -1 O TYR B 490 N LEU B 472
SHEET 4 AB5 4 GLU B 496 ILE B 500 -1 O ARG B 498 N CYS B 489
SHEET 1 AB6 4 GLY B 511 LEU B 515 0
SHEET 2 AB6 4 CYS B 518 ALA B 522 -1 O TYR B 520 N CYS B 513
SHEET 3 AB6 4 VAL B 534 ASP B 538 -1 O TYR B 537 N ILE B 519
SHEET 4 AB6 4 THR B 543 VAL B 547 -1 O VAL B 547 N VAL B 534
SHEET 1 AB7 4 GLY B 558 HIS B 562 0
SHEET 2 AB7 4 ARG B 565 LEU B 569 -1 O TYR B 567 N THR B 560
SHEET 3 AB7 4 SER B 580 ASP B 585 -1 O TYR B 584 N ILE B 566
SHEET 4 AB7 4 THR B 590 ARG B 596 -1 O THR B 590 N ASP B 585
LINK C ACE D 1 N53 DYW D 2 1555 1555 1.52
LINK C08 DYW D 2 N GLU D 3 1555 1555 1.47
LINK NA NA A 708 O AASP B 385 1555 1555 3.08
LINK NA NA A 709 O HOH A 919 1555 1555 2.98
LINK NA NA A 709 O HOH A 958 1555 1555 2.12
LINK NA NA A 710 O HOH A 811 1555 1555 2.06
LINK NA NA A 710 O HOH A 831 1555 1555 2.53
LINK OH TYR B 334 NA NA B 705 1555 1555 2.85
LINK OD1 ASN B 382 NA NA B 705 1555 1555 2.72
LINK NA NA B 705 O HOH B 889 1555 1555 2.31
LINK NA NA B 705 O HOH B 957 1555 1555 2.60
LINK NA NA B 706 O HOH B 943 1555 1555 2.15
LINK NA NA B 707 O HOH B 905 1555 1555 2.16
LINK NA NA B 707 O HOH B 952 1555 1555 2.72
LINK NA NA B 708 O HOH B 896 1555 1555 3.17
SITE 1 AC1 5 ARG A 380 THR A 388 ASP A 389 GLY A 433
SITE 2 AC1 5 HOH A 817
SITE 1 AC2 3 ALA A 356 ASP A 357 ARG A 470
SITE 1 AC3 2 HIS A 432 HIS A 437
SITE 1 AC4 6 LEU A 471 TYR A 491 PRO A 492 GLU A 493
SITE 2 AC4 6 ARG A 494 HOH A 842
SITE 1 AC5 5 TYR A 334 ARG A 415 SER A 602 HOH A 803
SITE 2 AC5 5 HOH A 854
SITE 1 AC6 7 ARG A 415 PHE A 478 ARG A 483 SER A 508
SITE 2 AC6 7 HOH A 805 ASP B 385 GLY B 386
SITE 1 AC7 4 GLN A 337 ASN A 382 SER A 383 HOH A 809
SITE 1 AC8 3 ARG A 415 SER A 508 ASP B 385
SITE 1 AC9 4 SER A 390 SER A 391 HOH A 919 HOH A 958
SITE 1 AD1 4 MET A 399 TYR A 491 HOH A 811 HOH A 831
SITE 1 AD2 5 PHE A 478 GLY A 480 ASN B 387 THR B 388
SITE 2 AD2 5 ASP B 389
SITE 1 AD3 7 GLY B 364 ARG B 415 GLY B 509 ALA B 556
SITE 2 AD3 7 HOH B 808 HOH B 852 HOH B 903
SITE 1 AD4 6 LEU B 355 TYR B 491 PRO B 492 GLU B 493
SITE 2 AD4 6 ARG B 494 HOH B 822
SITE 1 AD5 3 LEU B 355 ASP B 357 ARG B 470
SITE 1 AD6 5 TYR B 334 ARG B 336 ASN B 382 HOH B 889
SITE 2 AD6 5 HOH B 957
SITE 1 AD7 2 HIS B 432 HOH B 943
SITE 1 AD8 3 HIS B 436 HOH B 905 HOH B 952
SITE 1 AD9 1 ARG B 380
SITE 1 AE1 11 GLY A 386 ASN A 387 TYR B 525 GLN B 530
SITE 2 AE1 11 SER B 555 TYR B 572 GLU D 3 THR D 4
SITE 3 AE1 11 GLY D 5 GLU D 6 HOH D 103
SITE 1 AE2 15 GLY A 386 ASN A 387 ARG B 415 ARG B 483
SITE 2 AE2 15 SER B 508 TYR B 525 GLN B 530 SER B 555
SITE 3 AE2 15 ALA B 556 TYR B 572 ACE D 1 THR D 4
SITE 4 AE2 15 GLY D 5 GLU D 6 HOH D 103
CRYST1 75.652 76.129 211.137 90.00 90.00 90.00 P 21 21 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 0.013218 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013136 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004736 0.00000
(ATOM LINES ARE NOT SHOWN.)
END