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HEADER HYDROLASE 09-AUG-17 5Y5R
TITLE CRYSTAL STRUCTURE OF A NOVEL PYRETHROID HYDROLASE PYTH WITH BIF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRETHROID HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: UNP RESIDUES 2-280;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOBIUM FANIAE;
SOURCE 3 ORGANISM_TAXID: 570446;
SOURCE 4 GENE: PYTH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PYTH, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.Q.XU,T.T.RAN,W.W.WANG
REVDAT 1 15-AUG-18 5Y5R 0
JRNL AUTH D.Q.XU,T.T.RAN,J.HE,W.W.WANG
JRNL TITL STRUCTURE AND CATALYTIC MECHANISM OF A NOVEL PYRETHROID
JRNL TITL 2 HYDROLASE FROM SPHINGOBIUM FANIAE JZ-2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2247: ???)
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 139583
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.276
REMARK 3 R VALUE (WORKING SET) : 0.273
REMARK 3 FREE R VALUE : 0.322
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 7012
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 19.9144 - 5.8513 1.00 4766 250 0.1992 0.2296
REMARK 3 2 5.8513 - 4.6640 1.00 4600 221 0.2109 0.2362
REMARK 3 3 4.6640 - 4.0802 1.00 4535 249 0.2049 0.2705
REMARK 3 4 4.0802 - 3.7098 1.00 4508 231 0.2319 0.2777
REMARK 3 5 3.7098 - 3.4453 1.00 4453 247 0.2349 0.2997
REMARK 3 6 3.4453 - 3.2431 1.00 4461 264 0.2609 0.2998
REMARK 3 7 3.2431 - 3.0813 1.00 4457 239 0.2737 0.3367
REMARK 3 8 3.0813 - 2.9476 1.00 4439 251 0.2907 0.3545
REMARK 3 9 2.9476 - 2.8345 1.00 4467 213 0.2981 0.3422
REMARK 3 10 2.8345 - 2.7369 1.00 4459 239 0.2897 0.3298
REMARK 3 11 2.7369 - 2.6516 1.00 4405 237 0.2747 0.3213
REMARK 3 12 2.6516 - 2.5759 1.00 4455 243 0.2933 0.3407
REMARK 3 13 2.5759 - 2.5082 1.00 4424 235 0.3044 0.3788
REMARK 3 14 2.5082 - 2.4472 1.00 4354 270 0.3130 0.3631
REMARK 3 15 2.4472 - 2.3916 1.00 4430 229 0.3177 0.3642
REMARK 3 16 2.3916 - 2.3408 1.00 4404 233 0.3148 0.3870
REMARK 3 17 2.3408 - 2.2941 1.00 4434 212 0.3244 0.3930
REMARK 3 18 2.2941 - 2.2508 1.00 4400 241 0.3436 0.3697
REMARK 3 19 2.2508 - 2.2107 1.00 4441 211 0.3390 0.4096
REMARK 3 20 2.2107 - 2.1732 1.00 4416 225 0.3313 0.3613
REMARK 3 21 2.1732 - 2.1382 1.00 4394 225 0.3312 0.3904
REMARK 3 22 2.1382 - 2.1054 1.00 4414 245 0.3533 0.4244
REMARK 3 23 2.1054 - 2.0744 1.00 4401 225 0.3601 0.4136
REMARK 3 24 2.0744 - 2.0453 1.00 4406 237 0.3679 0.4270
REMARK 3 25 2.0453 - 2.0176 1.00 4390 236 0.3580 0.3925
REMARK 3 26 2.0176 - 1.9915 1.00 4382 217 0.3475 0.3756
REMARK 3 27 1.9915 - 1.9666 1.00 4410 219 0.3583 0.3773
REMARK 3 28 1.9666 - 1.9429 1.00 4377 247 0.3567 0.4010
REMARK 3 29 1.9429 - 1.9203 1.00 4410 216 0.3987 0.4588
REMARK 3 30 1.9203 - 1.8988 0.84 3679 205 0.3729 0.3697
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) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.020
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 11917
REMARK 3 ANGLE : 1.461 16353
REMARK 3 CHIRALITY : 0.075 1819
REMARK 3 PLANARITY : 0.010 2178
REMARK 3 DIHEDRAL : 16.896 7053
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 5Y5R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1300004682.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 139606
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.899
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 14.90
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.9100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 14.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.180
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 7.7, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 84.42850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 84.42850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 61.93200
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 84.42850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 84.42850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 61.93200
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 84.42850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 84.42850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 61.93200
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 84.42850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 84.42850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 61.93200
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 MSE A 1
REMARK 465 GLU A 162
REMARK 465 ARG A 255
REMARK 465 GLN A 256
REMARK 465 THR A 257
REMARK 465 ALA A 258
REMARK 465 THR A 259
REMARK 465 LYS A 260
REMARK 465 ALA A 261
REMARK 465 GLY A 262
REMARK 465 PRO A 263
REMARK 465 ASP A 264
REMARK 465 ARG A 265
REMARK 465 PRO A 266
REMARK 465 ALA A 267
REMARK 465 GLY A 268
REMARK 465 ALA A 269
REMARK 465 ASP A 270
REMARK 465 GLY A 271
REMARK 465 GLY A 272
REMARK 465 ARG A 273
REMARK 465 ALA A 274
REMARK 465 ASP A 275
REMARK 465 ARG A 276
REMARK 465 ALA A 277
REMARK 465 ASP A 278
REMARK 465 LEU A 279
REMARK 465 PRO A 280
REMARK 465 LEU A 281
REMARK 465 GLU A 282
REMARK 465 HIS A 283
REMARK 465 HIS A 284
REMARK 465 HIS A 285
REMARK 465 HIS A 286
REMARK 465 HIS A 287
REMARK 465 HIS A 288
REMARK 465 MSE B 1
REMARK 465 GLU B 162
REMARK 465 ARG B 255
REMARK 465 GLN B 256
REMARK 465 THR B 257
REMARK 465 ALA B 258
REMARK 465 THR B 259
REMARK 465 LYS B 260
REMARK 465 ALA B 261
REMARK 465 GLY B 262
REMARK 465 PRO B 263
REMARK 465 ASP B 264
REMARK 465 ARG B 265
REMARK 465 PRO B 266
REMARK 465 ALA B 267
REMARK 465 GLY B 268
REMARK 465 ALA B 269
REMARK 465 ASP B 270
REMARK 465 GLY B 271
REMARK 465 GLY B 272
REMARK 465 ARG B 273
REMARK 465 ALA B 274
REMARK 465 ASP B 275
REMARK 465 ARG B 276
REMARK 465 ALA B 277
REMARK 465 ASP B 278
REMARK 465 LEU B 279
REMARK 465 PRO B 280
REMARK 465 LEU B 281
REMARK 465 GLU B 282
REMARK 465 HIS B 283
REMARK 465 HIS B 284
REMARK 465 HIS B 285
REMARK 465 HIS B 286
REMARK 465 HIS B 287
REMARK 465 HIS B 288
REMARK 465 MSE C 1
REMARK 465 GLU C 162
REMARK 465 ARG C 255
REMARK 465 GLN C 256
REMARK 465 THR C 257
REMARK 465 ALA C 258
REMARK 465 THR C 259
REMARK 465 LYS C 260
REMARK 465 ALA C 261
REMARK 465 GLY C 262
REMARK 465 PRO C 263
REMARK 465 ASP C 264
REMARK 465 ARG C 265
REMARK 465 PRO C 266
REMARK 465 ALA C 267
REMARK 465 GLY C 268
REMARK 465 ALA C 269
REMARK 465 ASP C 270
REMARK 465 GLY C 271
REMARK 465 GLY C 272
REMARK 465 ARG C 273
REMARK 465 ALA C 274
REMARK 465 ASP C 275
REMARK 465 ARG C 276
REMARK 465 ALA C 277
REMARK 465 ASP C 278
REMARK 465 LEU C 279
REMARK 465 PRO C 280
REMARK 465 LEU C 281
REMARK 465 GLU C 282
REMARK 465 HIS C 283
REMARK 465 HIS C 284
REMARK 465 HIS C 285
REMARK 465 HIS C 286
REMARK 465 HIS C 287
REMARK 465 HIS C 288
REMARK 465 MSE D 1
REMARK 465 ARG D 255
REMARK 465 GLN D 256
REMARK 465 THR D 257
REMARK 465 ALA D 258
REMARK 465 THR D 259
REMARK 465 LYS D 260
REMARK 465 ALA D 261
REMARK 465 GLY D 262
REMARK 465 PRO D 263
REMARK 465 ASP D 264
REMARK 465 ARG D 265
REMARK 465 PRO D 266
REMARK 465 ALA D 267
REMARK 465 GLY D 268
REMARK 465 ALA D 269
REMARK 465 ASP D 270
REMARK 465 GLY D 271
REMARK 465 GLY D 272
REMARK 465 ARG D 273
REMARK 465 ALA D 274
REMARK 465 ASP D 275
REMARK 465 ARG D 276
REMARK 465 ALA D 277
REMARK 465 ASP D 278
REMARK 465 LEU D 279
REMARK 465 PRO D 280
REMARK 465 LEU D 281
REMARK 465 GLU D 282
REMARK 465 HIS D 283
REMARK 465 HIS D 284
REMARK 465 HIS D 285
REMARK 465 HIS D 286
REMARK 465 HIS D 287
REMARK 465 HIS D 288
REMARK 465 MSE E 1
REMARK 465 GLU E 162
REMARK 465 GLY E 163
REMARK 465 ARG E 255
REMARK 465 GLN E 256
REMARK 465 THR E 257
REMARK 465 ALA E 258
REMARK 465 THR E 259
REMARK 465 LYS E 260
REMARK 465 ALA E 261
REMARK 465 GLY E 262
REMARK 465 PRO E 263
REMARK 465 ASP E 264
REMARK 465 ARG E 265
REMARK 465 PRO E 266
REMARK 465 ALA E 267
REMARK 465 GLY E 268
REMARK 465 ALA E 269
REMARK 465 ASP E 270
REMARK 465 GLY E 271
REMARK 465 GLY E 272
REMARK 465 ARG E 273
REMARK 465 ALA E 274
REMARK 465 ASP E 275
REMARK 465 ARG E 276
REMARK 465 ALA E 277
REMARK 465 ASP E 278
REMARK 465 LEU E 279
REMARK 465 PRO E 280
REMARK 465 LEU E 281
REMARK 465 GLU E 282
REMARK 465 HIS E 283
REMARK 465 HIS E 284
REMARK 465 HIS E 285
REMARK 465 HIS E 286
REMARK 465 HIS E 287
REMARK 465 HIS E 288
REMARK 465 MSE F 1
REMARK 465 GLY F 161
REMARK 465 TYR F 254
REMARK 465 ARG F 255
REMARK 465 GLN F 256
REMARK 465 THR F 257
REMARK 465 ALA F 258
REMARK 465 THR F 259
REMARK 465 LYS F 260
REMARK 465 ALA F 261
REMARK 465 GLY F 262
REMARK 465 PRO F 263
REMARK 465 ASP F 264
REMARK 465 ARG F 265
REMARK 465 PRO F 266
REMARK 465 ALA F 267
REMARK 465 GLY F 268
REMARK 465 ALA F 269
REMARK 465 ASP F 270
REMARK 465 GLY F 271
REMARK 465 GLY F 272
REMARK 465 ARG F 273
REMARK 465 ALA F 274
REMARK 465 ASP F 275
REMARK 465 ARG F 276
REMARK 465 ALA F 277
REMARK 465 ASP F 278
REMARK 465 LEU F 279
REMARK 465 PRO F 280
REMARK 465 LEU F 281
REMARK 465 GLU F 282
REMARK 465 HIS F 283
REMARK 465 HIS F 284
REMARK 465 HIS F 285
REMARK 465 HIS F 286
REMARK 465 HIS F 287
REMARK 465 HIS F 288
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 ARG C 32 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 188 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 74 CG CD1 CD2
REMARK 470 ASP E 93 CG OD1 OD2
REMARK 470 LYS E 94 CG CD CE NZ
REMARK 470 ILE E 132 CG1 CG2 CD1
REMARK 470 GLU E 137 CG CD OE1 OE2
REMARK 470 ARG E 139 CG CD NE CZ NH1 NH2
REMARK 470 THR F 4 OG1 CG2
REMARK 470 ILE F 9 CG1 CG2 CD1
REMARK 470 ARG F 32 CG CD NE CZ NH1 NH2
REMARK 470 VAL F 52 CG1 CG2
REMARK 470 ASP F 53 CG OD1 OD2
REMARK 470 GLU F 55 CG CD OE1 OE2
REMARK 470 VAL F 61 CG1 CG2
REMARK 470 ARG F 67 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 69 CG CD OE1 OE2
REMARK 470 LEU F 74 CG CD1 CD2
REMARK 470 LEU F 75 CG CD1 CD2
REMARK 470 LEU F 79 CG CD1 CD2
REMARK 470 LEU F 87 CG CD1 CD2
REMARK 470 ASP F 93 CG OD1 OD2
REMARK 470 LYS F 94 CG CD CE NZ
REMARK 470 LEU F 98 CG CD1 CD2
REMARK 470 THR F 181 OG1 CG2
REMARK 470 GLU F 186 CG CD OE1 OE2
REMARK 470 ARG F 188 CG CD NE CZ NH1 NH2
REMARK 470 LEU F 190 CG CD1 CD2
REMARK 470 GLU F 191 CG CD OE1 OE2
REMARK 470 ILE F 192 CG1 CG2 CD1
REMARK 470 GLU F 253 CG CD OE1 OE2
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 O MSE F 54 OG1 THR F 58 1.85
REMARK 500 OG SER F 78 C17 8NL F 301 2.00
REMARK 500 OG SER F 78 C19 8NL F 301 2.01
REMARK 500 O HOH B 504 O HOH B 506 2.04
REMARK 500 O HOH D 454 O HOH D 475 2.04
REMARK 500 O HOH E 432 O HOH E 441 2.08
REMARK 500 O GLY A 30 O HOH A 401 2.09
REMARK 500 O HOH C 462 O HOH C 470 2.10
REMARK 500 O MSE F 185 O HOH F 401 2.11
REMARK 500 O TYR E 254 O HOH E 401 2.11
REMARK 500 O HOH A 488 O HOH A 498 2.11
REMARK 500 O HOH B 436 O HOH B 483 2.11
REMARK 500 OG1 THR E 106 O HOH E 402 2.12
REMARK 500 O HOH B 502 O HOH B 505 2.14
REMARK 500 O HOH D 420 O HOH D 464 2.15
REMARK 500 OE2 GLU E 198 OG SER E 225 2.15
REMARK 500 OD1 ASP F 45 O HOH F 402 2.15
REMARK 500 O GLU D 55 O HOH D 401 2.16
REMARK 500 O GLU F 137 O HOH F 403 2.17
REMARK 500 O ARG C 123 O HOH C 401 2.18
REMARK 500 NE2 GLN A 172 O HOH A 402 2.18
REMARK 500 O HOH A 486 O HOH D 473 2.18
REMARK 500 OE1 GLU B 55 NH2 ARG B 59 2.18
REMARK 500 O HOH F 439 O HOH F 440 2.19
REMARK 500 O HOH C 410 O HOH C 454 2.19
REMARK 500 OD1 ASP A 136 O HOH A 403 2.19
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 N MSE E 164 OE1 GLU F 149 8554 1.95
REMARK 500 O HOH B 415 O HOH F 404 3555 2.17
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 78 -116.31 49.48
REMARK 500 THR A 102 57.69 31.41
REMARK 500 SER A 229 -147.06 -90.20
REMARK 500 ALA A 250 79.78 -164.05
REMARK 500 SER B 78 -115.48 51.78
REMARK 500 THR B 102 56.02 31.25
REMARK 500 THR B 125 68.13 -119.57
REMARK 500 MSE B 164 -176.54 -65.41
REMARK 500 SER B 229 -147.91 -93.29
REMARK 500 ALA B 250 81.70 -162.67
REMARK 500 GLU C 69 -71.11 -62.00
REMARK 500 SER C 78 -121.99 53.65
REMARK 500 THR C 102 55.28 31.00
REMARK 500 THR C 125 68.67 -120.00
REMARK 500 SER C 229 -146.23 -90.66
REMARK 500 MSE C 236 69.41 -153.11
REMARK 500 ALA C 250 82.43 -161.64
REMARK 500 LEU D 13 10.52 59.93
REMARK 500 SER D 78 -118.91 49.31
REMARK 500 THR D 102 54.05 29.70
REMARK 500 SER D 229 -150.25 -89.55
REMARK 500 MSE D 236 59.26 -147.64
REMARK 500 ALA D 250 81.20 -164.10
REMARK 500 ASP E 53 -168.12 -163.81
REMARK 500 SER E 78 -109.56 53.61
REMARK 500 THR E 102 59.02 34.65
REMARK 500 PRO E 160 99.40 -59.34
REMARK 500 SER E 229 -155.57 -88.93
REMARK 500 MSE E 236 66.13 -152.03
REMARK 500 ALA E 250 82.34 -165.05
REMARK 500 GLU E 253 41.33 -147.27
REMARK 500 SER F 78 -115.39 58.87
REMARK 500 THR F 102 57.35 32.40
REMARK 500 GLU F 137 60.82 61.44
REMARK 500 PRO F 184 -17.14 -49.97
REMARK 500 SER F 229 -149.49 -90.12
REMARK 500 ALA F 250 77.88 -163.84
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 B 507 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH B 508 DISTANCE = 7.83 ANGSTROMS
REMARK 525 HOH D 481 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH D 482 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH F 442 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 8NL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NL C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NL D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NL E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NL F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 302
DBREF 5Y5R A 2 280 UNP D0VUS3 D0VUS3_9SPHN 2 280
DBREF 5Y5R B 2 280 UNP D0VUS3 D0VUS3_9SPHN 2 280
DBREF 5Y5R C 2 280 UNP D0VUS3 D0VUS3_9SPHN 2 280
DBREF 5Y5R D 2 280 UNP D0VUS3 D0VUS3_9SPHN 2 280
DBREF 5Y5R E 2 280 UNP D0VUS3 D0VUS3_9SPHN 2 280
DBREF 5Y5R F 2 280 UNP D0VUS3 D0VUS3_9SPHN 2 280
SEQADV 5Y5R MSE A 1 UNP D0VUS3 INITIATING METHIONINE
SEQADV 5Y5R LEU A 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R GLU A 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS A 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS A 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS A 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS A 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS A 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS A 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R MSE B 1 UNP D0VUS3 INITIATING METHIONINE
SEQADV 5Y5R LEU B 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R GLU B 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS B 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS B 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS B 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS B 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS B 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS B 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R MSE C 1 UNP D0VUS3 INITIATING METHIONINE
SEQADV 5Y5R LEU C 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R GLU C 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS C 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS C 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS C 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS C 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS C 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS C 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R MSE D 1 UNP D0VUS3 INITIATING METHIONINE
SEQADV 5Y5R LEU D 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R GLU D 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS D 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS D 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS D 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS D 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS D 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS D 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R MSE E 1 UNP D0VUS3 INITIATING METHIONINE
SEQADV 5Y5R LEU E 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R GLU E 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS E 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS E 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS E 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS E 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS E 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS E 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R MSE F 1 UNP D0VUS3 INITIATING METHIONINE
SEQADV 5Y5R LEU F 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R GLU F 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS F 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS F 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS F 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS F 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS F 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y5R HIS F 288 UNP D0VUS3 EXPRESSION TAG
SEQRES 1 A 288 MSE THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU
SEQRES 2 A 288 ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU
SEQRES 3 A 288 GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR
SEQRES 4 A 288 GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL
SEQRES 5 A 288 ASP MSE GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU
SEQRES 6 A 288 ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS SER
SEQRES 7 A 288 LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS
SEQRES 8 A 288 PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL
SEQRES 9 A 288 LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU
SEQRES 10 A 288 PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP
SEQRES 11 A 288 LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA
SEQRES 12 A 288 ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MSE
SEQRES 13 A 288 GLY ASP TYR PRO GLY GLU GLY MSE PRO PRO ALA GLU HIS
SEQRES 14 A 288 PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO
SEQRES 15 A 288 ASN PRO MSE GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU
SEQRES 16 A 288 TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA
SEQRES 17 A 288 VAL GLN ARG GLN MSE GLN LYS GLU PHE PRO GLY PRO VAL
SEQRES 18 A 288 ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR
SEQRES 19 A 288 SER MSE PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE
SEQRES 20 A 288 ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS
SEQRES 21 A 288 ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG
SEQRES 22 A 288 ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS
SEQRES 23 A 288 HIS HIS
SEQRES 1 B 288 MSE THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU
SEQRES 2 B 288 ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU
SEQRES 3 B 288 GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR
SEQRES 4 B 288 GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL
SEQRES 5 B 288 ASP MSE GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU
SEQRES 6 B 288 ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS SER
SEQRES 7 B 288 LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS
SEQRES 8 B 288 PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL
SEQRES 9 B 288 LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU
SEQRES 10 B 288 PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP
SEQRES 11 B 288 LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA
SEQRES 12 B 288 ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MSE
SEQRES 13 B 288 GLY ASP TYR PRO GLY GLU GLY MSE PRO PRO ALA GLU HIS
SEQRES 14 B 288 PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO
SEQRES 15 B 288 ASN PRO MSE GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU
SEQRES 16 B 288 TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA
SEQRES 17 B 288 VAL GLN ARG GLN MSE GLN LYS GLU PHE PRO GLY PRO VAL
SEQRES 18 B 288 ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR
SEQRES 19 B 288 SER MSE PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE
SEQRES 20 B 288 ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS
SEQRES 21 B 288 ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG
SEQRES 22 B 288 ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS
SEQRES 23 B 288 HIS HIS
SEQRES 1 C 288 MSE THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU
SEQRES 2 C 288 ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU
SEQRES 3 C 288 GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR
SEQRES 4 C 288 GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL
SEQRES 5 C 288 ASP MSE GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU
SEQRES 6 C 288 ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS SER
SEQRES 7 C 288 LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS
SEQRES 8 C 288 PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL
SEQRES 9 C 288 LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU
SEQRES 10 C 288 PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP
SEQRES 11 C 288 LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA
SEQRES 12 C 288 ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MSE
SEQRES 13 C 288 GLY ASP TYR PRO GLY GLU GLY MSE PRO PRO ALA GLU HIS
SEQRES 14 C 288 PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO
SEQRES 15 C 288 ASN PRO MSE GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU
SEQRES 16 C 288 TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA
SEQRES 17 C 288 VAL GLN ARG GLN MSE GLN LYS GLU PHE PRO GLY PRO VAL
SEQRES 18 C 288 ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR
SEQRES 19 C 288 SER MSE PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE
SEQRES 20 C 288 ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS
SEQRES 21 C 288 ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG
SEQRES 22 C 288 ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS
SEQRES 23 C 288 HIS HIS
SEQRES 1 D 288 MSE THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU
SEQRES 2 D 288 ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU
SEQRES 3 D 288 GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR
SEQRES 4 D 288 GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL
SEQRES 5 D 288 ASP MSE GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU
SEQRES 6 D 288 ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS SER
SEQRES 7 D 288 LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS
SEQRES 8 D 288 PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL
SEQRES 9 D 288 LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU
SEQRES 10 D 288 PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP
SEQRES 11 D 288 LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA
SEQRES 12 D 288 ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MSE
SEQRES 13 D 288 GLY ASP TYR PRO GLY GLU GLY MSE PRO PRO ALA GLU HIS
SEQRES 14 D 288 PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO
SEQRES 15 D 288 ASN PRO MSE GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU
SEQRES 16 D 288 TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA
SEQRES 17 D 288 VAL GLN ARG GLN MSE GLN LYS GLU PHE PRO GLY PRO VAL
SEQRES 18 D 288 ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR
SEQRES 19 D 288 SER MSE PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE
SEQRES 20 D 288 ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS
SEQRES 21 D 288 ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG
SEQRES 22 D 288 ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS
SEQRES 23 D 288 HIS HIS
SEQRES 1 E 288 MSE THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU
SEQRES 2 E 288 ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU
SEQRES 3 E 288 GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR
SEQRES 4 E 288 GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL
SEQRES 5 E 288 ASP MSE GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU
SEQRES 6 E 288 ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS SER
SEQRES 7 E 288 LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS
SEQRES 8 E 288 PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL
SEQRES 9 E 288 LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU
SEQRES 10 E 288 PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP
SEQRES 11 E 288 LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA
SEQRES 12 E 288 ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MSE
SEQRES 13 E 288 GLY ASP TYR PRO GLY GLU GLY MSE PRO PRO ALA GLU HIS
SEQRES 14 E 288 PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO
SEQRES 15 E 288 ASN PRO MSE GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU
SEQRES 16 E 288 TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA
SEQRES 17 E 288 VAL GLN ARG GLN MSE GLN LYS GLU PHE PRO GLY PRO VAL
SEQRES 18 E 288 ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR
SEQRES 19 E 288 SER MSE PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE
SEQRES 20 E 288 ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS
SEQRES 21 E 288 ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG
SEQRES 22 E 288 ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS
SEQRES 23 E 288 HIS HIS
SEQRES 1 F 288 MSE THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU
SEQRES 2 F 288 ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU
SEQRES 3 F 288 GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR
SEQRES 4 F 288 GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL
SEQRES 5 F 288 ASP MSE GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU
SEQRES 6 F 288 ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS SER
SEQRES 7 F 288 LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS
SEQRES 8 F 288 PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL
SEQRES 9 F 288 LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU
SEQRES 10 F 288 PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP
SEQRES 11 F 288 LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA
SEQRES 12 F 288 ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MSE
SEQRES 13 F 288 GLY ASP TYR PRO GLY GLU GLY MSE PRO PRO ALA GLU HIS
SEQRES 14 F 288 PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO
SEQRES 15 F 288 ASN PRO MSE GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU
SEQRES 16 F 288 TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA
SEQRES 17 F 288 VAL GLN ARG GLN MSE GLN LYS GLU PHE PRO GLY PRO VAL
SEQRES 18 F 288 ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR
SEQRES 19 F 288 SER MSE PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE
SEQRES 20 F 288 ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS
SEQRES 21 F 288 ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG
SEQRES 22 F 288 ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS
SEQRES 23 F 288 HIS HIS
MODRES 5Y5R MSE A 54 MET MODIFIED RESIDUE
MODRES 5Y5R MSE A 156 MET MODIFIED RESIDUE
MODRES 5Y5R MSE A 164 MET MODIFIED RESIDUE
MODRES 5Y5R MSE A 185 MET MODIFIED RESIDUE
MODRES 5Y5R MSE A 213 MET MODIFIED RESIDUE
MODRES 5Y5R MSE A 236 MET MODIFIED RESIDUE
MODRES 5Y5R MSE B 54 MET MODIFIED RESIDUE
MODRES 5Y5R MSE B 156 MET MODIFIED RESIDUE
MODRES 5Y5R MSE B 164 MET MODIFIED RESIDUE
MODRES 5Y5R MSE B 185 MET MODIFIED RESIDUE
MODRES 5Y5R MSE B 213 MET MODIFIED RESIDUE
MODRES 5Y5R MSE B 236 MET MODIFIED RESIDUE
MODRES 5Y5R MSE C 54 MET MODIFIED RESIDUE
MODRES 5Y5R MSE C 156 MET MODIFIED RESIDUE
MODRES 5Y5R MSE C 164 MET MODIFIED RESIDUE
MODRES 5Y5R MSE C 185 MET MODIFIED RESIDUE
MODRES 5Y5R MSE C 213 MET MODIFIED RESIDUE
MODRES 5Y5R MSE C 236 MET MODIFIED RESIDUE
MODRES 5Y5R MSE D 54 MET MODIFIED RESIDUE
MODRES 5Y5R MSE D 156 MET MODIFIED RESIDUE
MODRES 5Y5R MSE D 164 MET MODIFIED RESIDUE
MODRES 5Y5R MSE D 185 MET MODIFIED RESIDUE
MODRES 5Y5R MSE D 213 MET MODIFIED RESIDUE
MODRES 5Y5R MSE D 236 MET MODIFIED RESIDUE
MODRES 5Y5R MSE E 54 MET MODIFIED RESIDUE
MODRES 5Y5R MSE E 156 MET MODIFIED RESIDUE
MODRES 5Y5R MSE E 164 MET MODIFIED RESIDUE
MODRES 5Y5R MSE E 185 MET MODIFIED RESIDUE
MODRES 5Y5R MSE E 213 MET MODIFIED RESIDUE
MODRES 5Y5R MSE E 236 MET MODIFIED RESIDUE
MODRES 5Y5R MSE F 54 MET MODIFIED RESIDUE
MODRES 5Y5R MSE F 156 MET MODIFIED RESIDUE
MODRES 5Y5R MSE F 164 MET MODIFIED RESIDUE
MODRES 5Y5R MSE F 185 MET MODIFIED RESIDUE
MODRES 5Y5R MSE F 213 MET MODIFIED RESIDUE
MODRES 5Y5R MSE F 236 MET MODIFIED RESIDUE
HET MSE A 54 8
HET MSE A 156 8
HET MSE A 164 8
HET MSE A 185 8
HET MSE A 213 8
HET MSE A 236 8
HET MSE B 54 8
HET MSE B 156 8
HET MSE B 164 8
HET MSE B 185 8
HET MSE B 213 8
HET MSE B 236 8
HET MSE C 54 8
HET MSE C 156 8
HET MSE C 164 8
HET MSE C 185 8
HET MSE C 213 8
HET MSE C 236 8
HET MSE D 54 8
HET MSE D 156 8
HET MSE D 164 8
HET MSE D 185 8
HET MSE D 213 8
HET MSE D 236 8
HET MSE E 54 8
HET MSE E 156 8
HET MSE E 164 8
HET MSE E 185 8
HET MSE E 213 8
HET MSE E 236 8
HET MSE F 54 8
HET MSE F 156 8
HET MSE F 164 8
HET MSE F 185 8
HET MSE F 213 8
HET MSE F 236 8
HET 8NL A 301 29
HET SO4 A 302 5
HET 8NL B 301 29
HET SO4 B 302 5
HET 8NL C 301 29
HET SO4 C 302 5
HET 8NL D 301 29
HET SO4 D 302 5
HET 8NL E 301 29
HET SO4 E 302 5
HET 8NL F 301 29
HET SO4 F 302 5
HETNAM MSE SELENOMETHIONINE
HETNAM 8NL (2-METHYL-3-PHENYL-PHENYL)METHYL (1~{S})-3-[(~{E})-2-
HETNAM 2 8NL CHLORANYL-3,3,3-TRIS(FLUORANYL)PROP-1-ENYL]-2,2-
HETNAM 3 8NL DIMETHYL-CYCLOPROPANE-1-CARBOXYLATE
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 36(C5 H11 N O2 SE)
FORMUL 7 8NL 6(C23 H22 CL F3 O2)
FORMUL 8 SO4 6(O4 S 2-)
FORMUL 19 HOH *471(H2 O)
HELIX 1 AA1 ARG A 15 ASP A 20 5 6
HELIX 2 AA2 VAL A 22 ARG A 29 1 8
HELIX 3 AA3 GLY A 47 VAL A 51 5 5
HELIX 4 AA4 ASP A 53 THR A 58 1 6
HELIX 5 AA5 THR A 58 ALA A 68 1 11
HELIX 6 AA6 LEU A 79 HIS A 91 1 13
HELIX 7 AA7 PRO A 112 LEU A 117 1 6
HELIX 8 AA8 THR A 125 LEU A 131 1 7
HELIX 9 AA9 ARG A 147 MSE A 156 1 10
HELIX 10 AB1 PRO A 166 PHE A 170 5 5
HELIX 11 AB2 VAL A 177 THR A 181 5 5
HELIX 12 AB3 GLU A 186 ILE A 192 5 7
HELIX 13 AB4 PRO A 206 PHE A 217 1 12
HELIX 14 AB5 ALA A 231 MSE A 236 1 6
HELIX 15 AB6 MSE A 236 ALA A 250 1 15
HELIX 16 AB7 ARG B 15 ASP B 20 5 6
HELIX 17 AB8 VAL B 22 ALA B 28 1 7
HELIX 18 AB9 GLY B 47 VAL B 51 5 5
HELIX 19 AC1 ASP B 53 THR B 58 1 6
HELIX 20 AC2 THR B 58 ARG B 67 1 10
HELIX 21 AC3 LEU B 79 HIS B 91 1 13
HELIX 22 AC4 PRO B 112 LEU B 117 1 6
HELIX 23 AC5 THR B 125 LEU B 131 1 7
HELIX 24 AC6 ARG B 147 MSE B 156 1 10
HELIX 25 AC7 PRO B 166 PHE B 170 5 5
HELIX 26 AC8 THR B 176 THR B 181 1 6
HELIX 27 AC9 GLU B 186 ILE B 192 5 7
HELIX 28 AD1 PRO B 206 GLU B 216 1 11
HELIX 29 AD2 ALA B 231 MSE B 236 1 6
HELIX 30 AD3 MSE B 236 ALA B 250 1 15
HELIX 31 AD4 ARG C 15 ASP C 20 5 6
HELIX 32 AD5 VAL C 22 ARG C 29 1 8
HELIX 33 AD6 GLY C 47 VAL C 51 5 5
HELIX 34 AD7 ASP C 53 THR C 58 1 6
HELIX 35 AD8 THR C 58 ALA C 68 1 11
HELIX 36 AD9 LEU C 79 HIS C 91 1 13
HELIX 37 AE1 PRO C 112 LEU C 117 1 6
HELIX 38 AE2 THR C 125 LEU C 131 1 7
HELIX 39 AE3 ARG C 147 MSE C 156 1 10
HELIX 40 AE4 PRO C 166 PHE C 170 5 5
HELIX 41 AE5 THR C 176 THR C 181 1 6
HELIX 42 AE6 GLU C 186 ILE C 192 5 7
HELIX 43 AE7 PRO C 206 PHE C 217 1 12
HELIX 44 AE8 ALA C 231 MSE C 236 1 6
HELIX 45 AE9 MSE C 236 ALA C 250 1 15
HELIX 46 AF1 PRO C 251 TYR C 254 5 4
HELIX 47 AF2 ARG D 15 ASP D 20 5 6
HELIX 48 AF3 VAL D 22 ARG D 29 1 8
HELIX 49 AF4 GLY D 47 VAL D 51 5 5
HELIX 50 AF5 ASP D 53 THR D 58 1 6
HELIX 51 AF6 THR D 58 ARG D 67 1 10
HELIX 52 AF7 LEU D 79 HIS D 91 1 13
HELIX 53 AF8 PRO D 112 LEU D 117 1 6
HELIX 54 AF9 THR D 125 LEU D 131 1 7
HELIX 55 AG1 ARG D 147 MSE D 156 1 10
HELIX 56 AG2 PRO D 166 PHE D 170 5 5
HELIX 57 AG3 THR D 176 THR D 181 1 6
HELIX 58 AG4 GLU D 186 ILE D 192 5 7
HELIX 59 AG5 PRO D 206 PHE D 217 1 12
HELIX 60 AG6 ALA D 231 MSE D 236 1 6
HELIX 61 AG7 MSE D 236 ALA D 250 1 15
HELIX 62 AG8 ARG E 15 ASP E 20 5 6
HELIX 63 AG9 VAL E 22 ARG E 29 1 8
HELIX 64 AH1 GLY E 47 VAL E 51 5 5
HELIX 65 AH2 ASP E 53 THR E 58 1 6
HELIX 66 AH3 THR E 58 ALA E 68 1 11
HELIX 67 AH4 LEU E 79 HIS E 91 1 13
HELIX 68 AH5 PRO E 112 LEU E 117 1 6
HELIX 69 AH6 THR E 125 LEU E 131 1 7
HELIX 70 AH7 ARG E 147 MSE E 156 1 10
HELIX 71 AH8 PRO E 166 PHE E 170 5 5
HELIX 72 AH9 THR E 176 THR E 181 1 6
HELIX 73 AI1 GLU E 186 ILE E 192 5 7
HELIX 74 AI2 PRO E 206 PHE E 217 1 12
HELIX 75 AI3 ALA E 231 MSE E 236 1 6
HELIX 76 AI4 MSE E 236 ALA E 250 1 15
HELIX 77 AI5 PRO E 251 TYR E 254 5 4
HELIX 78 AI6 ARG F 15 ASP F 20 5 6
HELIX 79 AI7 VAL F 22 ALA F 28 1 7
HELIX 80 AI8 GLY F 47 VAL F 51 5 5
HELIX 81 AI9 ASP F 53 THR F 58 1 6
HELIX 82 AJ1 THR F 58 ARG F 67 1 10
HELIX 83 AJ2 LEU F 79 HIS F 91 1 13
HELIX 84 AJ3 PRO F 112 LEU F 117 1 6
HELIX 85 AJ4 THR F 125 LEU F 131 1 7
HELIX 86 AJ5 ARG F 147 MSE F 156 1 10
HELIX 87 AJ6 PRO F 166 PHE F 170 5 5
HELIX 88 AJ7 THR F 176 THR F 181 1 6
HELIX 89 AJ8 GLU F 186 ILE F 192 5 7
HELIX 90 AJ9 PRO F 206 GLU F 216 1 11
HELIX 91 AK1 ALA F 231 MSE F 236 1 6
HELIX 92 AK2 MSE F 236 ALA F 250 1 15
SHEET 1 AA1 6 ARG A 32 HIS A 34 0
SHEET 2 AA1 6 VAL A 3 ILE A 9 1 N LEU A 8 O HIS A 34
SHEET 3 AA1 6 GLN A 71 HIS A 77 1 O ILE A 73 N ILE A 7
SHEET 4 AA1 6 VAL A 95 LEU A 101 1 O ILE A 99 N LEU A 74
SHEET 5 AA1 6 ARG A 194 ALA A 199 1 O LEU A 195 N TYR A 100
SHEET 6 AA1 6 ALA A 222 LEU A 226 1 O ALA A 222 N TYR A 196
SHEET 1 AA2 3 ILE A 132 VAL A 135 0
SHEET 2 AA2 3 GLY A 140 ALA A 143 -1 O GLN A 142 N GLN A 133
SHEET 3 AA2 3 GLN A 174 SER A 175 -1 O GLN A 174 N LEU A 141
SHEET 1 AA3 6 ARG B 32 HIS B 34 0
SHEET 2 AA3 6 VAL B 3 ILE B 9 1 N LEU B 8 O HIS B 34
SHEET 3 AA3 6 GLN B 71 HIS B 77 1 O LEU B 75 N ILE B 7
SHEET 4 AA3 6 VAL B 95 LEU B 101 1 O LEU B 101 N GLY B 76
SHEET 5 AA3 6 ARG B 194 ALA B 199 1 O LEU B 195 N TYR B 100
SHEET 6 AA3 6 ALA B 222 LEU B 226 1 O VAL B 224 N GLU B 198
SHEET 1 AA4 3 ILE B 132 VAL B 135 0
SHEET 2 AA4 3 GLY B 140 ALA B 143 -1 O GLN B 142 N GLN B 133
SHEET 3 AA4 3 GLN B 174 SER B 175 -1 O GLN B 174 N LEU B 141
SHEET 1 AA5 6 ARG C 32 HIS C 34 0
SHEET 2 AA5 6 VAL C 3 ILE C 9 1 N LEU C 8 O HIS C 34
SHEET 3 AA5 6 GLN C 71 HIS C 77 1 O LEU C 75 N ILE C 9
SHEET 4 AA5 6 VAL C 95 LEU C 101 1 O ILE C 99 N LEU C 74
SHEET 5 AA5 6 ARG C 194 ALA C 199 1 O LEU C 195 N TYR C 100
SHEET 6 AA5 6 ALA C 222 LEU C 226 1 O ALA C 222 N ARG C 194
SHEET 1 AA6 3 ILE C 132 VAL C 135 0
SHEET 2 AA6 3 GLY C 140 ALA C 143 -1 O GLY C 140 N VAL C 135
SHEET 3 AA6 3 GLN C 174 SER C 175 -1 O GLN C 174 N LEU C 141
SHEET 1 AA7 6 ARG D 32 HIS D 34 0
SHEET 2 AA7 6 VAL D 3 ILE D 9 1 N ILE D 6 O ARG D 32
SHEET 3 AA7 6 GLN D 71 HIS D 77 1 O ILE D 73 N ILE D 7
SHEET 4 AA7 6 VAL D 95 LEU D 101 1 O ALA D 96 N SER D 72
SHEET 5 AA7 6 ARG D 194 ALA D 199 1 O LEU D 195 N TYR D 100
SHEET 6 AA7 6 ALA D 222 LEU D 226 1 O ALA D 222 N TYR D 196
SHEET 1 AA8 3 ILE D 132 VAL D 135 0
SHEET 2 AA8 3 GLY D 140 ALA D 143 -1 O GLY D 140 N VAL D 135
SHEET 3 AA8 3 GLN D 174 SER D 175 -1 O GLN D 174 N LEU D 141
SHEET 1 AA9 6 ARG E 32 HIS E 34 0
SHEET 2 AA9 6 VAL E 3 ILE E 9 1 N LEU E 8 O HIS E 34
SHEET 3 AA9 6 GLN E 71 HIS E 77 1 O LEU E 75 N ILE E 9
SHEET 4 AA9 6 VAL E 95 LEU E 101 1 O LEU E 101 N GLY E 76
SHEET 5 AA9 6 ARG E 194 ALA E 199 1 O ILE E 197 N TYR E 100
SHEET 6 AA9 6 ALA E 222 LEU E 226 1 O LEU E 226 N GLU E 198
SHEET 1 AB1 3 ILE E 132 VAL E 135 0
SHEET 2 AB1 3 GLY E 140 ALA E 143 -1 O GLN E 142 N GLN E 133
SHEET 3 AB1 3 THR E 173 SER E 175 -1 O GLN E 174 N LEU E 141
SHEET 1 AB2 6 ARG F 32 HIS F 34 0
SHEET 2 AB2 6 VAL F 3 ILE F 9 1 N ILE F 6 O ARG F 32
SHEET 3 AB2 6 GLN F 71 HIS F 77 1 O ILE F 73 N ILE F 7
SHEET 4 AB2 6 VAL F 95 LEU F 101 1 O ILE F 99 N GLY F 76
SHEET 5 AB2 6 ARG F 194 ALA F 199 1 O LEU F 195 N TYR F 100
SHEET 6 AB2 6 ALA F 222 LEU F 226 1 O ALA F 222 N TYR F 196
SHEET 1 AB3 3 ILE F 132 VAL F 135 0
SHEET 2 AB3 3 GLY F 140 ALA F 143 -1 O GLY F 140 N VAL F 135
SHEET 3 AB3 3 GLN F 174 SER F 175 -1 O GLN F 174 N LEU F 141
LINK C ASP A 53 N MSE A 54 1555 1555 1.33
LINK C MSE A 54 N GLU A 55 1555 1555 1.33
LINK C PHE A 155 N MSE A 156 1555 1555 1.34
LINK C MSE A 156 N GLY A 157 1555 1555 1.33
LINK C GLY A 163 N MSE A 164 1555 1555 1.32
LINK C MSE A 164 N PRO A 165 1555 1555 1.33
LINK C PRO A 184 N MSE A 185 1555 1555 1.33
LINK C MSE A 185 N GLU A 186 1555 1555 1.33
LINK C GLN A 212 N MSE A 213 1555 1555 1.33
LINK C MSE A 213 N GLN A 214 1555 1555 1.33
LINK C SER A 235 N MSE A 236 1555 1555 1.34
LINK C MSE A 236 N PRO A 237 1555 1555 1.33
LINK C ASP B 53 N MSE B 54 1555 1555 1.33
LINK C MSE B 54 N GLU B 55 1555 1555 1.35
LINK C PHE B 155 N MSE B 156 1555 1555 1.34
LINK C MSE B 156 N GLY B 157 1555 1555 1.33
LINK C GLY B 163 N MSE B 164 1555 1555 1.31
LINK C MSE B 164 N PRO B 165 1555 1555 1.33
LINK C PRO B 184 N MSE B 185 1555 1555 1.34
LINK C MSE B 185 N GLU B 186 1555 1555 1.33
LINK C GLN B 212 N MSE B 213 1555 1555 1.33
LINK C MSE B 213 N GLN B 214 1555 1555 1.34
LINK C SER B 235 N MSE B 236 1555 1555 1.33
LINK C MSE B 236 N PRO B 237 1555 1555 1.33
LINK C ASP C 53 N MSE C 54 1555 1555 1.32
LINK C MSE C 54 N GLU C 55 1555 1555 1.33
LINK C PHE C 155 N MSE C 156 1555 1555 1.33
LINK C MSE C 156 N GLY C 157 1555 1555 1.33
LINK C GLY C 163 N MSE C 164 1555 1555 1.33
LINK C MSE C 164 N PRO C 165 1555 1555 1.33
LINK C PRO C 184 N MSE C 185 1555 1555 1.33
LINK C MSE C 185 N GLU C 186 1555 1555 1.33
LINK C GLN C 212 N MSE C 213 1555 1555 1.32
LINK C MSE C 213 N GLN C 214 1555 1555 1.35
LINK C SER C 235 N MSE C 236 1555 1555 1.33
LINK C MSE C 236 N PRO C 237 1555 1555 1.33
LINK C ASP D 53 N MSE D 54 1555 1555 1.32
LINK C MSE D 54 N GLU D 55 1555 1555 1.34
LINK C PHE D 155 N MSE D 156 1555 1555 1.32
LINK C MSE D 156 N GLY D 157 1555 1555 1.33
LINK C GLY D 163 N MSE D 164 1555 1555 1.32
LINK C MSE D 164 N PRO D 165 1555 1555 1.33
LINK C PRO D 184 N MSE D 185 1555 1555 1.33
LINK C MSE D 185 N GLU D 186 1555 1555 1.33
LINK C GLN D 212 N MSE D 213 1555 1555 1.33
LINK C MSE D 213 N GLN D 214 1555 1555 1.33
LINK C SER D 235 N MSE D 236 1555 1555 1.33
LINK C MSE D 236 N PRO D 237 1555 1555 1.34
LINK C ASP E 53 N MSE E 54 1555 1555 1.34
LINK C MSE E 54 N GLU E 55 1555 1555 1.33
LINK C PHE E 155 N MSE E 156 1555 1555 1.33
LINK C MSE E 156 N GLY E 157 1555 1555 1.33
LINK C MSE E 164 N PRO E 165 1555 1555 1.38
LINK C PRO E 184 N MSE E 185 1555 1555 1.33
LINK C MSE E 185 N GLU E 186 1555 1555 1.33
LINK C GLN E 212 N MSE E 213 1555 1555 1.32
LINK C MSE E 213 N GLN E 214 1555 1555 1.34
LINK C SER E 235 N MSE E 236 1555 1555 1.32
LINK C MSE E 236 N PRO E 237 1555 1555 1.34
LINK C ASP F 53 N MSE F 54 1555 1555 1.32
LINK C MSE F 54 N GLU F 55 1555 1555 1.31
LINK C PHE F 155 N MSE F 156 1555 1555 1.32
LINK C MSE F 156 N GLY F 157 1555 1555 1.33
LINK C GLY F 163 N MSE F 164 1555 1555 1.32
LINK C MSE F 164 N PRO F 165 1555 1555 1.33
LINK C PRO F 184 N MSE F 185 1555 1555 1.31
LINK C MSE F 185 N GLU F 186 1555 1555 1.34
LINK C GLN F 212 N MSE F 213 1555 1555 1.34
LINK C MSE F 213 N GLN F 214 1555 1555 1.33
LINK C SER F 235 N MSE F 236 1555 1555 1.33
LINK C MSE F 236 N PRO F 237 1555 1555 1.34
LINK CE MSE E 164 SE MSE F 164 1555 8554 1.81
CISPEP 1 GLU A 120 PRO A 121 0 -3.79
CISPEP 2 GLU B 120 PRO B 121 0 -2.19
CISPEP 3 GLU C 120 PRO C 121 0 -2.35
CISPEP 4 GLU D 120 PRO D 121 0 0.09
CISPEP 5 GLU E 120 PRO E 121 0 -2.45
CISPEP 6 GLU F 120 PRO F 121 0 -5.53
SITE 1 AC1 12 ALA A 12 ASN A 14 SER A 78 LEU A 79
SITE 2 AC1 12 VAL A 116 THR A 125 ALA A 128 ALA A 143
SITE 3 AC1 12 PHE A 155 PHE A 179 VAL A 204 HIS A 230
SITE 1 AC2 5 SER A 235 MSE A 236 PRO A 237 GLU A 238
SITE 2 AC2 5 ARG A 239
SITE 1 AC3 10 ALA B 12 ASN B 14 SER B 78 LEU B 79
SITE 2 AC3 10 ALA B 128 ILE B 132 PHE B 155 PHE B 170
SITE 3 AC3 10 PHE B 179 HIS B 230
SITE 1 AC4 5 SER B 235 MSE B 236 PRO B 237 GLU B 238
SITE 2 AC4 5 ARG B 239
SITE 1 AC5 11 ALA C 12 ASN C 14 SER C 78 LEU C 79
SITE 2 AC5 11 ALA C 128 ILE C 132 PHE C 155 PHE C 170
SITE 3 AC5 11 PHE C 179 VAL C 204 HIS C 230
SITE 1 AC6 5 SER C 235 MSE C 236 PRO C 237 GLU C 238
SITE 2 AC6 5 ARG C 239
SITE 1 AC7 13 ALA D 12 LEU D 13 ASN D 14 SER D 78
SITE 2 AC7 13 LEU D 79 VAL D 116 THR D 125 ALA D 128
SITE 3 AC7 13 ILE D 132 ALA D 143 PHE D 155 PHE D 179
SITE 4 AC7 13 HIS D 230
SITE 1 AC8 5 SER D 235 MSE D 236 PRO D 237 GLU D 238
SITE 2 AC8 5 ARG D 239
SITE 1 AC9 17 ALA E 12 LEU E 13 ASN E 14 SER E 78
SITE 2 AC9 17 LEU E 79 VAL E 116 THR E 125 ALA E 128
SITE 3 AC9 17 LEU E 129 ILE E 132 LEU E 141 ALA E 143
SITE 4 AC9 17 LEU E 151 PHE E 155 MSE E 156 PHE E 179
SITE 5 AC9 17 HIS E 230
SITE 1 AD1 6 SER E 235 MSE E 236 PRO E 237 GLU E 238
SITE 2 AD1 6 ARG E 239 HOH E 425
SITE 1 AD2 14 GLY F 11 ALA F 12 ASN F 14 SER F 78
SITE 2 AD2 14 LEU F 79 VAL F 116 THR F 125 ALA F 128
SITE 3 AD2 14 ALA F 143 PHE F 155 MSE F 156 PHE F 170
SITE 4 AD2 14 PHE F 179 HIS F 230
SITE 1 AD3 4 MSE F 236 PRO F 237 GLU F 238 ARG F 239
CRYST1 168.857 168.857 123.864 90.00 90.00 90.00 P 42 21 2 48
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 0.005922 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005922 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008073 0.00000
TER 1915 TYR A 254
TER 3830 TYR B 254
TER 5739 TYR C 254
TER 7657 TYR D 254
TER 9545 TYR E 254
TER 11373 GLU F 253
MASTER 703 0 48 92 54 0 33 612042 6 563 138
END |