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HEADER HYDROLASE 07-AUG-17 5Y57
TITLE CRYSTAL STRUCTURE OF A NOVEL PYRETHROID HYDROLASE FROM SPHINGOBIUM
TITLE 2 FANIAE JZ-2
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 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.Q.XU,T.T.RAN,J.HE,W.W.WANG
REVDAT 1 08-AUG-18 5Y57 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. 1.96 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) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 125199
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.258
REMARK 3 R VALUE (WORKING SET) : 0.255
REMARK 3 FREE R VALUE : 0.309
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 6268
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 19.8534 - 6.0372 1.00 4313 221 0.1806 0.2021
REMARK 3 2 6.0372 - 4.8144 1.00 4156 206 0.1966 0.2108
REMARK 3 3 4.8144 - 4.2125 1.00 4041 266 0.1875 0.2526
REMARK 3 4 4.2125 - 3.8303 1.00 4094 197 0.2018 0.2664
REMARK 3 5 3.8303 - 3.5575 1.00 4061 207 0.2266 0.2874
REMARK 3 6 3.5575 - 3.3488 1.00 4052 205 0.2378 0.3119
REMARK 3 7 3.3488 - 3.1818 1.00 4013 211 0.2467 0.2852
REMARK 3 8 3.1818 - 3.0438 1.00 4028 221 0.2569 0.3300
REMARK 3 9 3.0438 - 2.9270 1.00 4001 231 0.2794 0.3639
REMARK 3 10 2.9270 - 2.8263 1.00 3982 218 0.2862 0.3478
REMARK 3 11 2.8263 - 2.7381 1.00 3985 223 0.2913 0.3384
REMARK 3 12 2.7381 - 2.6601 1.00 4000 223 0.2948 0.3718
REMARK 3 13 2.6601 - 2.5902 1.00 4003 198 0.3019 0.3387
REMARK 3 14 2.5902 - 2.5271 1.00 4008 193 0.2931 0.3531
REMARK 3 15 2.5271 - 2.4698 1.00 3989 219 0.2940 0.3655
REMARK 3 16 2.4698 - 2.4173 1.00 3968 218 0.2985 0.3575
REMARK 3 17 2.4173 - 2.3690 1.00 3980 220 0.3196 0.3950
REMARK 3 18 2.3690 - 2.3244 1.00 3984 217 0.3158 0.3847
REMARK 3 19 2.3244 - 2.2829 1.00 3982 204 0.3106 0.3572
REMARK 3 20 2.2829 - 2.2443 1.00 3969 200 0.3188 0.4050
REMARK 3 21 2.2443 - 2.2081 1.00 3966 223 0.3179 0.3443
REMARK 3 22 2.2081 - 2.1742 1.00 3994 194 0.3217 0.3951
REMARK 3 23 2.1742 - 2.1423 1.00 3965 206 0.3276 0.3587
REMARK 3 24 2.1423 - 2.1121 1.00 3967 203 0.3458 0.4023
REMARK 3 25 2.1121 - 2.0836 1.00 3974 224 0.3365 0.3869
REMARK 3 26 2.0836 - 2.0566 1.00 3953 202 0.3469 0.3714
REMARK 3 27 2.0566 - 2.0309 1.00 3949 204 0.3529 0.4003
REMARK 3 28 2.0309 - 2.0065 0.99 3989 163 0.3576 0.4090
REMARK 3 29 2.0065 - 1.9832 0.99 3870 220 0.3790 0.4039
REMARK 3 30 1.9832 - 1.9609 0.68 2695 131 0.4222 0.5048
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) : 36.470
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 : 0.009 11935
REMARK 3 ANGLE : 1.127 16357
REMARK 3 CHIRALITY : 0.058 1815
REMARK 3 PLANARITY : 0.008 2184
REMARK 3 DIHEDRAL : 18.094 7105
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 5Y57 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1300004681.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 0.9792
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 : 125394
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.200
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 11.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.9
REMARK 200 DATA REDUNDANCY IN SHELL : 8.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 7.5, 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 84.22650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 84.22650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 61.79650
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 84.22650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 84.22650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 61.79650
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 84.22650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 84.22650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 61.79650
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 84.22650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 84.22650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 61.79650
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 GLY A 163
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 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 GLU D 162
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 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 E 59 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 69 CG CD OE1 OE2
REMARK 470 ASP E 93 CG OD1 OD2
REMARK 470 LYS E 215 CG CD CE NZ
REMARK 470 ARG F 32 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 94 CG CD CE NZ
REMARK 470 VAL F 135 CG1 CG2
REMARK 470 GLU F 137 CG CD OE1 OE2
REMARK 470 ARG F 139 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 162 CG CD OE1 OE2
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 ARG F 194 CG CD NE CZ NH1 NH2
REMARK 470 TYR F 254 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLY F 138 OG1 THR F 176 1.65
REMARK 500 O HOH A 445 O HOH A 495 2.04
REMARK 500 O HOH D 437 O HOH D 497 2.07
REMARK 500 ND1 HIS C 48 O HOH C 401 2.15
REMARK 500 O ASP C 37 O HOH C 402 2.15
REMARK 500 O HOH A 496 O HOH A 504 2.17
REMARK 500 O LEU E 8 O HOH E 401 2.17
REMARK 500 OH TYR C 31 OD1 ASP C 249 2.18
REMARK 500 N ARG D 150 O HOH D 401 2.19
REMARK 500 N GLY D 163 O HOH D 402 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 O HOH A 449 O HOH C 479 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 ARG A 29 4.77 -68.13
REMARK 500 SER A 78 -121.54 55.24
REMARK 500 SER A 78 -125.87 56.49
REMARK 500 THR A 102 59.76 25.53
REMARK 500 PRO A 227 49.34 -79.88
REMARK 500 SER A 229 -144.36 -98.01
REMARK 500 ALA A 250 75.78 -166.87
REMARK 500 GLU A 253 -72.23 -70.29
REMARK 500 LEU B 13 9.12 58.39
REMARK 500 SER B 78 -118.53 54.56
REMARK 500 SER B 78 -108.53 37.02
REMARK 500 THR B 102 57.59 29.16
REMARK 500 THR B 125 69.85 -113.24
REMARK 500 SER B 229 -149.70 -87.78
REMARK 500 ALA B 250 82.80 -166.67
REMARK 500 LEU C 13 14.41 57.75
REMARK 500 SER C 78 -121.62 52.46
REMARK 500 SER C 78 -128.58 57.46
REMARK 500 ASP C 93 0.32 -64.64
REMARK 500 THR C 102 53.09 30.36
REMARK 500 THR C 125 66.36 -110.62
REMARK 500 GLU C 186 139.38 -170.24
REMARK 500 SER C 229 -145.97 -82.96
REMARK 500 ALA C 250 92.51 -164.25
REMARK 500 SER D 78 -120.48 45.85
REMARK 500 SER D 78 -127.14 56.22
REMARK 500 THR D 102 60.61 29.78
REMARK 500 THR D 125 74.33 -118.12
REMARK 500 GLU D 186 141.70 -173.21
REMARK 500 SER D 229 -151.32 -92.52
REMARK 500 MSE D 236 69.09 -153.30
REMARK 500 ALA D 250 82.59 -162.47
REMARK 500 LEU E 13 -0.02 66.21
REMARK 500 ASP E 53 -167.40 -164.59
REMARK 500 PRO E 60 -19.23 -44.55
REMARK 500 SER E 78 -115.74 49.12
REMARK 500 SER E 78 -127.20 59.52
REMARK 500 THR E 102 62.55 30.20
REMARK 500 PRO E 227 50.47 -69.37
REMARK 500 SER E 229 -151.09 -82.11
REMARK 500 ALA E 231 74.40 -118.45
REMARK 500 ASP E 249 -70.16 -56.05
REMARK 500 THR F 4 -33.10 -134.58
REMARK 500 LEU F 13 -1.42 76.05
REMARK 500 CYS F 18 5.51 -64.25
REMARK 500 VAL F 52 -87.08 -118.25
REMARK 500 SER F 78 -126.67 61.78
REMARK 500 SER F 78 -129.64 56.46
REMARK 500 THR F 102 56.07 27.49
REMARK 500 ASN F 122 73.80 59.83
REMARK 500
REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS.
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 A 505 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH C 485 DISTANCE = 6.88 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PMS 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 SO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PMS B 301 and SER B
REMARK 800 78
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PMS C 301 and SER C
REMARK 800 78
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PMS C 301 and SER C
REMARK 800 78
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PMS D 301 and SER D
REMARK 800 78
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PMS D 301 and SER D
REMARK 800 78
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PMS E 301 and SER E
REMARK 800 78
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PMS F 301 and SER F
REMARK 800 78
DBREF 5Y57 A 2 280 UNP D0VUS3 D0VUS3_9SPHN 2 280
DBREF 5Y57 B 2 280 UNP D0VUS3 D0VUS3_9SPHN 2 280
DBREF 5Y57 C 2 280 UNP D0VUS3 D0VUS3_9SPHN 2 280
DBREF 5Y57 D 2 280 UNP D0VUS3 D0VUS3_9SPHN 2 280
DBREF 5Y57 E 2 280 UNP D0VUS3 D0VUS3_9SPHN 2 280
DBREF 5Y57 F 2 280 UNP D0VUS3 D0VUS3_9SPHN 2 280
SEQADV 5Y57 MSE A 1 UNP D0VUS3 INITIATING METHIONINE
SEQADV 5Y57 LEU A 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 GLU A 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS A 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS A 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS A 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS A 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS A 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS A 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 MSE B 1 UNP D0VUS3 INITIATING METHIONINE
SEQADV 5Y57 LEU B 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 GLU B 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS B 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS B 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS B 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS B 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS B 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS B 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 MSE C 1 UNP D0VUS3 INITIATING METHIONINE
SEQADV 5Y57 LEU C 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 GLU C 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS C 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS C 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS C 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS C 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS C 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS C 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 MSE D 1 UNP D0VUS3 INITIATING METHIONINE
SEQADV 5Y57 LEU D 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 GLU D 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS D 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS D 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS D 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS D 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS D 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS D 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 MSE E 1 UNP D0VUS3 INITIATING METHIONINE
SEQADV 5Y57 LEU E 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 GLU E 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS E 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS E 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS E 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS E 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS E 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS E 288 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 MSE F 1 UNP D0VUS3 INITIATING METHIONINE
SEQADV 5Y57 LEU F 281 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 GLU F 282 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS F 283 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS F 284 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS F 285 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS F 286 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 HIS F 287 UNP D0VUS3 EXPRESSION TAG
SEQADV 5Y57 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 5Y57 MSE A 54 MET MODIFIED RESIDUE
MODRES 5Y57 MSE A 156 MET MODIFIED RESIDUE
MODRES 5Y57 MSE A 164 MET MODIFIED RESIDUE
MODRES 5Y57 MSE A 185 MET MODIFIED RESIDUE
MODRES 5Y57 MSE A 213 MET MODIFIED RESIDUE
MODRES 5Y57 MSE A 236 MET MODIFIED RESIDUE
MODRES 5Y57 MSE B 54 MET MODIFIED RESIDUE
MODRES 5Y57 MSE B 156 MET MODIFIED RESIDUE
MODRES 5Y57 MSE B 164 MET MODIFIED RESIDUE
MODRES 5Y57 MSE B 185 MET MODIFIED RESIDUE
MODRES 5Y57 MSE B 213 MET MODIFIED RESIDUE
MODRES 5Y57 MSE B 236 MET MODIFIED RESIDUE
MODRES 5Y57 MSE C 54 MET MODIFIED RESIDUE
MODRES 5Y57 MSE C 156 MET MODIFIED RESIDUE
MODRES 5Y57 MSE C 164 MET MODIFIED RESIDUE
MODRES 5Y57 MSE C 185 MET MODIFIED RESIDUE
MODRES 5Y57 MSE C 213 MET MODIFIED RESIDUE
MODRES 5Y57 MSE C 236 MET MODIFIED RESIDUE
MODRES 5Y57 MSE D 54 MET MODIFIED RESIDUE
MODRES 5Y57 MSE D 156 MET MODIFIED RESIDUE
MODRES 5Y57 MSE D 164 MET MODIFIED RESIDUE
MODRES 5Y57 MSE D 185 MET MODIFIED RESIDUE
MODRES 5Y57 MSE D 213 MET MODIFIED RESIDUE
MODRES 5Y57 MSE D 236 MET MODIFIED RESIDUE
MODRES 5Y57 MSE E 54 MET MODIFIED RESIDUE
MODRES 5Y57 MSE E 156 MET MODIFIED RESIDUE
MODRES 5Y57 MSE E 164 MET MODIFIED RESIDUE
MODRES 5Y57 MSE E 185 MET MODIFIED RESIDUE
MODRES 5Y57 MSE E 213 MET MODIFIED RESIDUE
MODRES 5Y57 MSE E 236 MET MODIFIED RESIDUE
MODRES 5Y57 MSE F 54 MET MODIFIED RESIDUE
MODRES 5Y57 MSE F 156 MET MODIFIED RESIDUE
MODRES 5Y57 MSE F 164 MET MODIFIED RESIDUE
MODRES 5Y57 MSE F 185 MET MODIFIED RESIDUE
MODRES 5Y57 MSE F 213 MET MODIFIED RESIDUE
MODRES 5Y57 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 PMS A 301 10
HET SO4 A 302 5
HET PMS B 301 10
HET SO4 B 302 5
HET PMS C 301 10
HET SO4 C 302 5
HET PMS D 301 10
HET SO4 D 302 5
HET PMS E 301 10
HET SO4 E 302 5
HET PMS F 301 10
HET SO4 F 302 5
HETNAM MSE SELENOMETHIONINE
HETNAM PMS PHENYLMETHANESULFONIC ACID
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 36(C5 H11 N O2 SE)
FORMUL 7 PMS 6(C7 H8 O3 S)
FORMUL 8 SO4 6(O4 S 2-)
FORMUL 19 HOH *430(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 THR A 176 THR A 181 1 6
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 ASP A 249 1 14
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 ALA B 68 1 11
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 PHE B 217 1 12
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 ALA C 28 1 7
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 ALA D 21 ARG D 29 1 9
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 ALA D 68 1 11
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 VAL D 177 GLY D 180 5 4
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 ALA E 28 1 7
HELIX 64 AH1 ASP E 53 THR E 58 1 6
HELIX 65 AH2 THR E 58 ALA E 68 1 11
HELIX 66 AH3 LEU E 79 HIS E 91 1 13
HELIX 67 AH4 PRO E 112 LEU E 117 1 6
HELIX 68 AH5 THR E 125 LEU E 131 1 7
HELIX 69 AH6 ARG E 147 MSE E 156 1 10
HELIX 70 AH7 PRO E 166 PHE E 170 5 5
HELIX 71 AH8 THR E 176 THR E 181 1 6
HELIX 72 AH9 GLY E 187 ILE E 192 1 6
HELIX 73 AI1 PRO E 206 PHE E 217 1 12
HELIX 74 AI2 ALA E 231 MSE E 236 1 6
HELIX 75 AI3 MSE E 236 ALA E 250 1 15
HELIX 76 AI4 PRO E 251 TYR E 254 5 4
HELIX 77 AI5 ARG F 15 ASP F 20 5 6
HELIX 78 AI6 VAL F 22 ALA F 28 1 7
HELIX 79 AI7 GLY F 46 VAL F 51 5 6
HELIX 80 AI8 ASP F 53 THR F 58 1 6
HELIX 81 AI9 THR F 58 ALA F 68 1 11
HELIX 82 AJ1 LEU F 79 HIS F 91 1 13
HELIX 83 AJ2 PRO F 112 LEU F 117 1 6
HELIX 84 AJ3 THR F 125 ILE F 132 1 8
HELIX 85 AJ4 ASP F 144 SER F 146 5 3
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 9
SHEET 4 AA3 6 VAL B 95 LEU B 101 1 O ILE B 99 N LEU B 74
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 ALA B 222 N TYR B 196
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 7
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 LEU C 226 N GLU C 198
SHEET 1 AA6 3 ILE C 132 VAL C 135 0
SHEET 2 AA6 3 GLY C 140 ALA C 143 -1 O GLN C 142 N GLN C 133
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 LEU D 8 O HIS D 34
SHEET 3 AA7 6 GLN D 71 HIS D 77 1 O LEU D 75 N ILE D 9
SHEET 4 AA7 6 VAL D 95 LEU D 101 1 O ILE D 99 N LEU D 74
SHEET 5 AA7 6 ARG D 194 ALA D 199 1 O LEU D 195 N LEU D 98
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 GLN D 142 N GLN D 133
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 SER E 78 1 O LEU E 75 N ILE E 9
SHEET 4 AA9 6 VAL E 95 ALA E 103 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 VAL E 224 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 ASP F 5 ILE F 9 1 N ILE F 6 O ARG F 32
SHEET 3 AB2 6 ILE F 73 HIS F 77 1 O ILE F 73 N ILE F 7
SHEET 4 AB2 6 GLY F 97 LEU F 101 1 O ILE F 99 N LEU F 74
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
LINK C ASP A 53 N MSE A 54 1555 1555 1.33
LINK C MSE A 54 N GLU A 55 1555 1555 1.34
LINK OG ASER A 78 S PMS A 301 1555 1555 1.57
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 MSE A 164 N PRO A 165 1555 1555 1.32
LINK C PRO A 184 N MSE A 185 1555 1555 1.32
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 OG ASER B 78 S PMS B 301 1555 1555 1.57
LINK C PHE B 155 N MSE B 156 1555 1555 1.33
LINK C MSE B 156 N GLY B 157 1555 1555 1.33
LINK C GLY B 163 N MSE B 164 1555 1555 1.32
LINK C MSE B 164 N PRO B 165 1555 1555 1.39
LINK C PRO B 184 N MSE B 185 1555 1555 1.33
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 1.34
LINK C ASP C 53 N MSE C 54 1555 1555 1.33
LINK C MSE C 54 N GLU C 55 1555 1555 1.34
LINK OG ASER C 78 S PMS C 301 1555 1555 1.56
LINK OG BSER C 78 S PMS C 301 1555 1555 1.47
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 1.34
LINK C PRO C 184 N MSE C 185 1555 1555 1.33
LINK C MSE C 185 N GLU C 186 1555 1555 1.34
LINK C GLN C 212 N MSE C 213 1555 1555 1.33
LINK C MSE C 213 N GLN C 214 1555 1555 1.34
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 OG ASER D 78 S PMS D 301 1555 1555 1.54
LINK OG BSER D 78 S PMS D 301 1555 1555 1.63
LINK C PHE D 155 N MSE D 156 1555 1555 1.33
LINK C MSE D 156 N GLY D 157 1555 1555 1.33
LINK C GLY D 163 N MSE D 164 1555 1555 1.31
LINK C MSE D 164 N PRO D 165 1555 1555 1.32
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 1.34
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 OG ASER E 78 S PMS E 301 1555 1555 1.56
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 1.33
LINK C PRO E 184 N MSE E 185 1555 1555 1.32
LINK C MSE E 185 N GLU E 186 1555 1555 1.34
LINK C GLN E 212 N MSE E 213 1555 1555 1.31
LINK C MSE E 213 N GLN E 214 1555 1555 1.31
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 1.33
LINK C MSE F 54 N GLU F 55 1555 1555 1.34
LINK OG ASER F 78 S PMS F 301 1555 1555 1.51
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 1.33
LINK C MSE F 164 N PRO F 165 1555 1555 1.33
LINK C PRO F 184 N MSE F 185 1555 1555 1.33
LINK C MSE F 185 N GLU F 186 1555 1555 1.33
LINK C GLN F 212 N MSE F 213 1555 1555 1.33
LINK C MSE F 213 N GLN F 214 1555 1555 1.34
LINK C SER F 235 N MSE F 236 1555 1555 1.32
LINK C MSE F 236 N PRO F 237 1555 1555 1.34
CISPEP 1 GLU A 120 PRO A 121 0 -9.92
CISPEP 2 GLU B 120 PRO B 121 0 0.42
CISPEP 3 GLU C 120 PRO C 121 0 -3.59
CISPEP 4 GLU D 120 PRO D 121 0 -5.03
CISPEP 5 GLU E 120 PRO E 121 0 -6.44
CISPEP 6 GLU F 120 PRO F 121 0 8.29
SITE 1 AC1 6 ALA A 12 SER A 78 LEU A 79 ALA A 128
SITE 2 AC1 6 PHE A 179 HIS A 230
SITE 1 AC2 5 MSE A 236 PRO A 237 GLU A 238 ARG A 239
SITE 2 AC2 5 HOH A 421
SITE 1 AC3 5 SER B 235 MSE B 236 PRO B 237 GLU B 238
SITE 2 AC3 5 ARG B 239
SITE 1 AC4 6 SER C 235 MSE C 236 PRO C 237 GLU C 238
SITE 2 AC4 6 ARG C 239 HOH C 421
SITE 1 AC5 5 SER D 235 MSE D 236 PRO D 237 GLU D 238
SITE 2 AC5 5 ARG D 239
SITE 1 AC6 5 SER E 235 MSE E 236 PRO E 237 GLU E 238
SITE 2 AC6 5 ARG E 239
SITE 1 AC7 4 MSE F 236 PRO F 237 GLU F 238 ARG F 239
SITE 1 AC8 12 ALA B 12 HIS B 77 LEU B 79 GLY B 80
SITE 2 AC8 12 GLY B 81 LEU B 101 THR B 102 ALA B 103
SITE 3 AC8 12 VAL B 104 ALA B 128 HIS B 230 HOH B 413
SITE 1 AC9 12 ALA C 12 HIS C 77 LEU C 79 GLY C 80
SITE 2 AC9 12 GLY C 81 LEU C 101 THR C 102 ALA C 103
SITE 3 AC9 12 VAL C 104 ALA C 128 VAL C 204 HIS C 230
SITE 1 AD1 12 ALA C 12 HIS C 77 LEU C 79 GLY C 80
SITE 2 AD1 12 GLY C 81 LEU C 101 THR C 102 ALA C 103
SITE 3 AD1 12 VAL C 104 ALA C 128 VAL C 204 HIS C 230
SITE 1 AD2 11 ALA D 12 HIS D 77 LEU D 79 GLY D 80
SITE 2 AD2 11 GLY D 81 LEU D 101 THR D 102 ALA D 103
SITE 3 AD2 11 VAL D 104 PHE D 179 HIS D 230
SITE 1 AD3 11 ALA D 12 HIS D 77 LEU D 79 GLY D 80
SITE 2 AD3 11 GLY D 81 LEU D 101 THR D 102 ALA D 103
SITE 3 AD3 11 VAL D 104 PHE D 179 HIS D 230
SITE 1 AD4 14 ALA E 12 HIS E 77 LEU E 79 GLY E 80
SITE 2 AD4 14 GLY E 81 LEU E 101 THR E 102 ALA E 103
SITE 3 AD4 14 VAL E 104 ALA E 128 ILE E 132 PHE E 179
SITE 4 AD4 14 VAL E 204 HIS E 230
SITE 1 AD5 12 ALA F 12 HIS F 77 LEU F 79 GLY F 80
SITE 2 AD5 12 GLY F 81 LEU F 101 THR F 102 ALA F 103
SITE 3 AD5 12 VAL F 104 VAL F 116 THR F 125 ALA F 128
CRYST1 168.453 168.453 123.593 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 0.005936 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005936 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008091 0.00000
TER 1917 TYR A 254
TER 3838 TYR B 254
TER 5762 TYR C 254
TER 7683 TYR D 254
TER 9583 TYR E 254
TER 11457 TYR F 254
MASTER 698 0 48 92 51 0 35 611935 6 458 138
END |