HEADER HYDROLASE 02-NOV-09 3KIO
TITLE MOUSE RNASE H2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE H2 SUBUNIT A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RNASE H2 SUBUNIT A, RIBONUCLEASE HI SUBUNIT A,
COMPND 5 RIBONUCLEASE HI LARGE SUBUNIT, RNASE HI LARGE SUBUNIT;
COMPND 6 EC: 3.1.26.4;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: RIBONUCLEASE H2 SUBUNIT B;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: RNASE H2 SUBUNIT B, RIBONUCLEASE HI SUBUNIT B,
COMPND 12 DELETED IN LYMPHOCYTIC LEUKEMIA 8 HOMOLOG;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: RIBONUCLEASE H2 SUBUNIT C;
COMPND 16 CHAIN: C;
COMPND 17 SYNONYM: RNASE H2 SUBUNIT C, RIBONUCLEASE HI SUBUNIT C;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: RNASE H2A, RNASEH2A, RNASEHI;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET26;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 12 ORGANISM_COMMON: MOUSE;
SOURCE 13 ORGANISM_TAXID: 10090;
SOURCE 14 GENE: DLEU8, RNASE H2B, RNASEH2B;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PCDFDUET;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 21 ORGANISM_COMMON: MOUSE;
SOURCE 22 ORGANISM_TAXID: 10090;
SOURCE 23 GENE: AYP1, RNASE H2C, RNASEH2C;
SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 27 EXPRESSION_SYSTEM_PLASMID: PCDFDUET
KEYWDS RIBONUCLEASE, AICARDI-GOUTIERES SYNDROME, RNASE H2, PROTEIN
KEYWDS 2 COMPLEX, AUTOIMMUNE DISEASE, ENDONUCLEASE, HYDROLASE,
KEYWDS 3 METAL-BINDING, NUCLEASE, NUCLEUS, PHOSPHOPROTEIN,
KEYWDS 4 ACETYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR N.SHABAN,S.HARVEY,F.W.PERRINO,T.HOLLIS
REVDAT 2 16-FEB-10 3KIO 1 JRNL
REVDAT 1 17-NOV-09 3KIO 0
JRNL AUTH N.M.SHABAN,S.HARVEY,F.W.PERRINO,T.HOLLIS
JRNL TITL THE STRUCTURE OF THE MAMMALIAN RNASE H2 COMPLEX
JRNL TITL 2 PROVIDES INSIGHT INTO RNA:DNA HYBRID PROCESSING TO
JRNL TITL 3 PREVENT IMMUNE DYSFUNCTION.
JRNL REF J.BIOL.CHEM. V. 285 3617 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 19923215
JRNL DOI 10.1074/JBC.M109.059048
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.4_113)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.050
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 22814
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.305
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1692
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 24.6195 - 6.2175 1.00 3113 164 0.2704 0.2624
REMARK 3 2 6.2175 - 4.9482 1.00 3089 173 0.2426 0.3321
REMARK 3 3 4.9482 - 4.3265 0.98 3090 167 0.1986 0.3030
REMARK 3 4 4.3265 - 3.9327 0.99 3032 181 0.2127 0.2943
REMARK 3 5 3.9327 - 3.6518 0.99 3093 174 0.2285 0.3076
REMARK 3 6 3.6518 - 3.4371 0.99 3075 171 0.2119 0.2907
REMARK 3 7 3.4371 - 3.2654 0.99 3144 150 0.2126 0.3240
REMARK 3 8 3.2654 - 3.1235 1.00 3092 146 0.2151 0.3020
REMARK 3 9 3.1235 - 3.0035 1.00 3105 176 0.2177 0.3126
REMARK 3 10 3.0035 - 2.9000 1.00 3041 190 0.2510 0.3125
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 : 0.28
REMARK 3 B_SOL : 42.77
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.470
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
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 3877
REMARK 3 ANGLE : 1.352 5275
REMARK 3 CHIRALITY : 0.085 603
REMARK 3 PLANARITY : 0.007 693
REMARK 3 DIHEDRAL : 21.759 1352
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN C AND RESID 136:144)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.0703 0.2527 9.4353
REMARK 3 T TENSOR
REMARK 3 T11: 1.6721 T22: 1.5083
REMARK 3 T33: 0.8612 T12: -0.4955
REMARK 3 T13: -0.4067 T23: 0.1466
REMARK 3 L TENSOR
REMARK 3 L11: 0.1490 L22: 0.3461
REMARK 3 L33: 0.1014 L12: 0.1985
REMARK 3 L13: 0.0608 L23: 0.0326
REMARK 3 S TENSOR
REMARK 3 S11: -2.1638 S12: -1.5602 S13: -0.9935
REMARK 3 S21: 0.4454 S22: -1.7393 S23: 0.0141
REMARK 3 S31: 0.4219 S32: -1.8300 S33: -0.0273
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 3KIO COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-NOV-09.
REMARK 100 THE RCSB ID CODE IS RCSB056040.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9798, 0.979, 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23731
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 9.400
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.37000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 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 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 139.64350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.21050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 139.64350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 20.21050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 SER A 68
REMARK 465 LYS A 69
REMARK 465 GLU A 259
REMARK 465 ALA A 260
REMARK 465 GLU A 261
REMARK 465 GLU A 262
REMARK 465 ASP A 263
REMARK 465 PRO A 264
REMARK 465 GLU A 265
REMARK 465 ARG A 266
REMARK 465 PRO A 267
REMARK 465 GLY A 268
REMARK 465 LYS A 269
REMARK 465 ILE A 270
REMARK 465 THR A 271
REMARK 465 SER A 272
REMARK 465 TYR A 273
REMARK 465 PHE A 274
REMARK 465 SER A 275
REMARK 465 GLN A 276
REMARK 465 GLY A 277
REMARK 465 PRO A 278
REMARK 465 GLN A 279
REMARK 465 THR A 280
REMARK 465 CYS A 281
REMARK 465 ARG A 282
REMARK 465 PRO A 283
REMARK 465 GLN A 284
REMARK 465 ALA A 285
REMARK 465 PRO A 286
REMARK 465 HIS A 287
REMARK 465 ARG A 288
REMARK 465 TYR A 289
REMARK 465 PHE A 290
REMARK 465 GLN A 291
REMARK 465 GLU A 292
REMARK 465 ARG A 293
REMARK 465 GLY A 294
REMARK 465 LEU A 295
REMARK 465 GLU A 296
REMARK 465 ALA A 297
REMARK 465 ALA A 298
REMARK 465 SER A 299
REMARK 465 SER A 300
REMARK 465 LEU A 301
REMARK 465 MSE B -23
REMARK 465 GLY B -22
REMARK 465 SER B -21
REMARK 465 SER B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 SER B -13
REMARK 465 GLN B -12
REMARK 465 ASP B -11
REMARK 465 PRO B -10
REMARK 465 ASN B -9
REMARK 465 SER B -8
REMARK 465 LEU B -7
REMARK 465 GLU B -6
REMARK 465 VAL B -5
REMARK 465 LEU B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 GLY B -1
REMARK 465 PRO B 0
REMARK 465 MSE B 1
REMARK 465 ALA B 2
REMARK 465 GLY B 3
REMARK 465 GLY B 4
REMARK 465 ARG B 5
REMARK 465 ASP B 6
REMARK 465 ARG B 7
REMARK 465 GLY B 8
REMARK 465 ASP B 9
REMARK 465 ALA B 26
REMARK 465 SER B 27
REMARK 465 LYS B 28
REMARK 465 LYS B 29
REMARK 465 LYS B 30
REMARK 465 LYS B 103
REMARK 465 ALA B 104
REMARK 465 GLY B 105
REMARK 465 LYS B 106
REMARK 465 GLU B 107
REMARK 465 GLY B 108
REMARK 465 LYS B 109
REMARK 465 TYR B 110
REMARK 465 GLN B 111
REMARK 465 PRO B 112
REMARK 465 LEU B 113
REMARK 465 ASP B 114
REMARK 465 GLN B 115
REMARK 465 VAL B 116
REMARK 465 VAL B 117
REMARK 465 VAL B 118
REMARK 465 ASP B 119
REMARK 465 ASP B 120
REMARK 465 THR B 121
REMARK 465 PHE B 122
REMARK 465 PRO B 123
REMARK 465 ASP B 124
REMARK 465 CYS B 125
REMARK 465 THR B 126
REMARK 465 LEU B 127
REMARK 465 LEU B 128
REMARK 465 LEU B 129
REMARK 465 ARG B 130
REMARK 465 PHE B 131
REMARK 465 PRO B 132
REMARK 465 GLU B 133
REMARK 465 LEU B 134
REMARK 465 GLU B 135
REMARK 465 LYS B 136
REMARK 465 SER B 137
REMARK 465 LEU B 138
REMARK 465 ARG B 139
REMARK 465 HIS B 140
REMARK 465 VAL B 141
REMARK 465 THR B 142
REMARK 465 GLU B 143
REMARK 465 GLU B 144
REMARK 465 LYS B 145
REMARK 465 VAL B 182
REMARK 465 GLY B 183
REMARK 465 ALA B 184
REMARK 465 ARG B 185
REMARK 465 VAL B 186
REMARK 465 GLN B 187
REMARK 465 SER B 188
REMARK 465 SER B 189
REMARK 465 ALA B 190
REMARK 465 TYR B 191
REMARK 465 PHE B 192
REMARK 465 SER B 193
REMARK 465 GLY B 194
REMARK 465 GLY B 195
REMARK 465 GLN B 196
REMARK 465 VAL B 197
REMARK 465 SER B 198
REMARK 465 ARG B 199
REMARK 465 ASP B 200
REMARK 465 LYS B 201
REMARK 465 GLU B 202
REMARK 465 GLU B 203
REMARK 465 ASP B 204
REMARK 465 TYR B 205
REMARK 465 VAL B 206
REMARK 465 ARG B 207
REMARK 465 TYR B 208
REMARK 465 ALA B 209
REMARK 465 HIS B 210
REMARK 465 GLY B 211
REMARK 465 LEU B 212
REMARK 465 ILE B 213
REMARK 465 SER B 214
REMARK 465 ASP B 215
REMARK 465 TYR B 216
REMARK 465 ILE B 217
REMARK 465 PRO B 218
REMARK 465 LYS B 219
REMARK 465 GLU B 220
REMARK 465 LEU B 221
REMARK 465 SER B 222
REMARK 465 ASP B 223
REMARK 465 ASP B 224
REMARK 465 LEU B 225
REMARK 465 SER B 226
REMARK 465 LYS B 227
REMARK 465 PHE B 228
REMARK 465 LEU B 229
REMARK 465 LYS B 230
REMARK 465 LEU B 231
REMARK 465 PRO B 232
REMARK 465 GLU B 233
REMARK 465 PRO B 234
REMARK 465 PRO B 235
REMARK 465 ALA B 236
REMARK 465 SER B 237
REMARK 465 LEU B 238
REMARK 465 PRO B 239
REMARK 465 ASN B 240
REMARK 465 PRO B 241
REMARK 465 PRO B 242
REMARK 465 SER B 243
REMARK 465 LYS B 244
REMARK 465 LYS B 245
REMARK 465 LEU B 246
REMARK 465 LYS B 247
REMARK 465 LEU B 248
REMARK 465 SER B 249
REMARK 465 ASP B 250
REMARK 465 GLU B 251
REMARK 465 PRO B 252
REMARK 465 VAL B 253
REMARK 465 GLU B 254
REMARK 465 ALA B 255
REMARK 465 LYS B 256
REMARK 465 GLU B 257
REMARK 465 ASP B 258
REMARK 465 TYR B 259
REMARK 465 THR B 260
REMARK 465 LYS B 261
REMARK 465 PHE B 262
REMARK 465 ASN B 263
REMARK 465 THR B 264
REMARK 465 LYS B 265
REMARK 465 ASP B 266
REMARK 465 LEU B 283
REMARK 465 ALA B 284
REMARK 465 LYS B 285
REMARK 465 VAL B 286
REMARK 465 ASP B 287
REMARK 465 LYS B 288
REMARK 465 SER B 289
REMARK 465 GLY B 290
REMARK 465 MSE B 291
REMARK 465 LYS B 292
REMARK 465 SER B 293
REMARK 465 ILE B 294
REMARK 465 ASP B 295
REMARK 465 ALA B 296
REMARK 465 PHE B 297
REMARK 465 PHE B 298
REMARK 465 GLY B 299
REMARK 465 ALA B 300
REMARK 465 LYS B 301
REMARK 465 ASN B 302
REMARK 465 LYS B 303
REMARK 465 LYS B 304
REMARK 465 THR B 305
REMARK 465 GLY B 306
REMARK 465 LYS B 307
REMARK 465 ILE B 308
REMARK 465 MSE C 1
REMARK 465 LYS C 2
REMARK 465 ASN C 3
REMARK 465 PRO C 4
REMARK 465 GLU C 5
REMARK 465 GLU C 6
REMARK 465 ALA C 7
REMARK 465 ALA C 8
REMARK 465 GLU C 9
REMARK 465 GLY C 10
REMARK 465 LYS C 11
REMARK 465 GLN C 12
REMARK 465 ASP C 120
REMARK 465 PHE C 121
REMARK 465 ASP C 122
REMARK 465 ARG C 123
REMARK 465 LEU C 124
REMARK 465 ILE C 125
REMARK 465 GLY C 126
REMARK 465 ALA C 127
REMARK 465 THR C 128
REMARK 465 GLY C 129
REMARK 465 SER C 130
REMARK 465 PHE C 131
REMARK 465 SER C 132
REMARK 465 HIS C 133
REMARK 465 PHE C 134
REMARK 465 THR C 135
REMARK 465 PRO C 145
REMARK 465 ASP C 146
REMARK 465 ALA C 147
REMARK 465 LYS C 148
REMARK 465 VAL C 149
REMARK 465 HIS C 150
REMARK 465 ARG C 151
REMARK 465 ALA C 152
REMARK 465 LEU C 153
REMARK 465 GLY C 154
REMARK 465 TRP C 155
REMARK 465 PRO C 156
REMARK 465 SER C 157
REMARK 465 LEU C 158
REMARK 465 ALA C 159
REMARK 465 ALA C 160
REMARK 465 ALA C 161
REMARK 465 ILE C 162
REMARK 465 HIS C 163
REMARK 465 ALA C 164
REMARK 465 GLN C 165
REMARK 465 VAL C 166
REMARK 465 PRO C 167
REMARK 465 GLU C 168
REMARK 465 ASP C 169
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 A 8 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 218 CG CD CE NZ
REMARK 470 LYS A 223 CG CD CE NZ
REMARK 470 SER A 258 OG
REMARK 470 LYS B 24 CG CD CE NZ
REMARK 470 LYS B 31 CG CD CE NZ
REMARK 470 LYS B 32 CG CD CE NZ
REMARK 470 SER B 33 OG
REMARK 470 SER B 34 OG
REMARK 470 LEU B 40 CG CD1 CD2
REMARK 470 ASN B 42 CG OD1 ND2
REMARK 470 SER B 45 OG
REMARK 470 ILE B 53 CG1 CG2 CD1
REMARK 470 LYS B 64 CG CD CE NZ
REMARK 470 LYS B 69 CG CD CE NZ
REMARK 470 ASP B 92 CG OD1
REMARK 470 LEU B 94 CG CD1 CD2
REMARK 470 PHE B 95 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 96 CG CD1 CD2
REMARK 470 HIS B 99 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 146 CG CD OE1 OE2
REMARK 470 SER B 149 OG
REMARK 470 LYS B 150 CG CD CE NZ
REMARK 470 LYS B 151 CG CD CE NZ
REMARK 470 TYR B 152 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR B 153 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 154 CG CD CE NZ
REMARK 470 TYR B 155 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER B 156 OG
REMARK 470 SER B 157 OG
REMARK 470 GLU B 158 CG CD OE1 OE2
REMARK 470 LYS B 159 CG CD CE NZ
REMARK 470 THR B 160 OG1 CG2
REMARK 470 LYS B 166 CG CD CE NZ
REMARK 470 LEU B 175 CG CD1 CD2
REMARK 470 LYS B 176 CG CD CE NZ
REMARK 470 ASN B 179 CG OD1 ND2
REMARK 470 VAL B 180 CG1 CG2
REMARK 470 ASN B 181 CG OD1 ND2
REMARK 470 THR B 269 OG1 CG2
REMARK 470 LYS B 271 CG CD CE NZ
REMARK 470 LYS B 272 CG CD CE NZ
REMARK 470 ASN B 273 CG OD1 ND2
REMARK 470 LYS B 275 CG CD CE NZ
REMARK 470 THR B 277 OG1 CG2
REMARK 470 GLN B 280 CG CD OE1 NE2
REMARK 470 LYS B 281 CG CD CE NZ
REMARK 470 ARG C 13 CG CD NE CZ NH1 NH2
REMARK 470 HIS C 15 CG ND1 CD2 CE1 NE2
REMARK 470 ARG C 22 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 91 CG CD OE1 OE2
REMARK 470 ILE C 94 CG1 CG2 CD1
REMARK 470 LEU C 97 CG CD1 CD2
REMARK 470 GLU C 109 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 ASP C 55 O ASP C 57 2.10
REMARK 500 O LYS A 111 O HOH A 339 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR A 112 CE2 TYR A 112 CD2 -0.094
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS A 64 N - CA - CB ANGL. DEV. = -13.6 DEGREES
REMARK 500 LYS A 64 N - CA - C ANGL. DEV. = 20.9 DEGREES
REMARK 500 LYS A 111 CB - CA - C ANGL. DEV. = -12.7 DEGREES
REMARK 500 PRO A 215 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 PRO A 232 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 GLY C 58 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 2 -13.97 54.30
REMARK 500 GLU A 61 -73.69 -64.03
REMARK 500 LEU A 63 -124.91 -77.72
REMARK 500 VAL A 65 -71.01 -81.01
REMARK 500 ASP A 86 49.73 -87.43
REMARK 500 GLU A 148 -70.38 -52.29
REMARK 500 LYS A 168 54.00 -144.59
REMARK 500 GLN A 201 37.31 -95.71
REMARK 500 ASN A 213 -21.43 85.85
REMARK 500 HIS A 224 46.87 -143.26
REMARK 500 ARG A 236 83.92 -65.43
REMARK 500 ASP A 257 85.33 -60.36
REMARK 500 ALA B 11 106.18 145.34
REMARK 500 ALA B 12 106.54 -54.29
REMARK 500 LYS B 32 -158.87 -112.01
REMARK 500 PRO B 43 177.35 -53.64
REMARK 500 SER B 45 -42.50 81.77
REMARK 500 GLU B 47 98.18 61.72
REMARK 500 MSE B 55 1.82 -62.53
REMARK 500 CYS B 56 48.53 -84.29
REMARK 500 LEU B 57 81.09 71.37
REMARK 500 GLN B 58 -111.72 72.87
REMARK 500 ASN B 76 -134.47 54.65
REMARK 500 ASP B 92 -87.15 133.71
REMARK 500 PRO B 93 -127.66 -81.43
REMARK 500 ASN B 148 167.01 178.27
REMARK 500 LYS B 150 148.26 64.39
REMARK 500 LYS B 151 26.30 43.63
REMARK 500 SER B 156 -114.76 -66.26
REMARK 500 SER B 157 74.35 60.48
REMARK 500 GLU B 158 177.31 -43.40
REMARK 500 LYS B 159 104.60 -51.38
REMARK 500 VAL B 180 -146.17 -70.93
REMARK 500 LYS B 268 -105.29 -149.30
REMARK 500 THR B 269 -176.31 -57.15
REMARK 500 LYS B 272 33.70 -68.86
REMARK 500 LYS B 281 -74.76 -89.17
REMARK 500 ARG C 22 108.02 -162.25
REMARK 500 ALA C 24 141.24 -39.34
REMARK 500 ARG C 40 146.73 -177.86
REMARK 500 PRO C 43 44.95 -74.73
REMARK 500 LEU C 59 141.37 -172.36
REMARK 500 GLU C 88 -83.76 133.18
REMARK 500 LYS C 89 84.60 -153.29
REMARK 500 GLU C 91 100.06 64.44
REMARK 500 ASP C 105 -26.25 52.99
REMARK 500 ASP C 108 35.86 92.36
REMARK 500 GLU C 109 -134.43 -59.55
REMARK 500 ALA C 110 -94.53 33.75
REMARK 500 PRO C 113 -23.46 -37.70
REMARK 500
REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP B 92 PRO B 93 -146.25
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3KIO A 1 301 UNP Q9CWY8 RNH2A_MOUSE 1 301
DBREF 3KIO B 1 308 UNP Q80ZV0 RNH2B_MOUSE 1 308
DBREF 3KIO C 1 169 UNP Q9CQ18 RNH2C_MOUSE 1 166
SEQADV 3KIO MSE B -23 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO GLY B -22 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO SER B -21 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO SER B -20 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO HIS B -19 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO HIS B -18 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO HIS B -17 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO HIS B -16 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO HIS B -15 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO HIS B -14 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO SER B -13 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO GLN B -12 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO ASP B -11 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO PRO B -10 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO ASN B -9 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO SER B -8 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO LEU B -7 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO GLU B -6 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO VAL B -5 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO LEU B -4 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO PHE B -3 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO GLN B -2 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO GLY B -1 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO PRO B 0 UNP Q80ZV0 EXPRESSION TAG
SEQADV 3KIO PRO B 239 UNP Q80ZV0 THR 239 VARIANT
SEQADV 3KIO GLU C 9 UNP Q9CQ18 ASP 9 VARIANT
SEQRES 1 A 301 MSE ASP LEU SER GLU LEU GLU ARG ASP ASN THR GLY ARG
SEQRES 2 A 301 CYS ARG LEU SER SER PRO VAL PRO ALA VAL CYS LEU LYS
SEQRES 3 A 301 GLU PRO CYS VAL LEU GLY VAL ASP GLU ALA GLY ARG GLY
SEQRES 4 A 301 PRO VAL LEU GLY PRO MSE VAL TYR ALA ILE CYS TYR CYS
SEQRES 5 A 301 PRO LEU SER ARG LEU ALA ASP LEU GLU ALA LEU LYS VAL
SEQRES 6 A 301 ALA ASP SER LYS THR LEU THR GLU ASN GLU ARG GLU ARG
SEQRES 7 A 301 LEU PHE ALA LYS MSE GLU GLU ASP GLY ASP PHE VAL GLY
SEQRES 8 A 301 TRP ALA LEU ASP VAL LEU SER PRO ASN LEU ILE SER THR
SEQRES 9 A 301 SER MSE LEU GLY ARG VAL LYS TYR ASN LEU ASN SER LEU
SEQRES 10 A 301 SER HIS ASP THR ALA ALA GLY LEU ILE GLN TYR ALA LEU
SEQRES 11 A 301 ASP GLN ASN VAL ASN VAL THR GLN VAL PHE VAL ASP THR
SEQRES 12 A 301 VAL GLY MSE PRO GLU THR TYR GLN ALA ARG LEU GLN GLN
SEQRES 13 A 301 HIS PHE PRO GLY ILE GLU VAL THR VAL LYS ALA LYS ALA
SEQRES 14 A 301 ASP SER LEU PHE PRO VAL VAL SER ALA ALA SER ILE PHE
SEQRES 15 A 301 ALA LYS VAL ALA ARG ASP LYS ALA VAL LYS ASN TRP GLN
SEQRES 16 A 301 PHE VAL GLU ASN LEU GLN ASP LEU ASP SER ASP TYR GLY
SEQRES 17 A 301 SER GLY TYR PRO ASN ASP PRO LYS THR LYS ALA TRP LEU
SEQRES 18 A 301 ARG LYS HIS VAL ASP PRO VAL PHE GLY PHE PRO GLN PHE
SEQRES 19 A 301 VAL ARG PHE SER TRP SER THR ALA GLN ALA ILE LEU GLU
SEQRES 20 A 301 LYS GLU ALA GLU ASP VAL ILE TRP GLU ASP SER GLU ALA
SEQRES 21 A 301 GLU GLU ASP PRO GLU ARG PRO GLY LYS ILE THR SER TYR
SEQRES 22 A 301 PHE SER GLN GLY PRO GLN THR CYS ARG PRO GLN ALA PRO
SEQRES 23 A 301 HIS ARG TYR PHE GLN GLU ARG GLY LEU GLU ALA ALA SER
SEQRES 24 A 301 SER LEU
SEQRES 1 B 332 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 B 332 PRO ASN SER LEU GLU VAL LEU PHE GLN GLY PRO MSE ALA
SEQRES 3 B 332 GLY GLY ARG ASP ARG GLY ASP LEU ALA ALA ARG GLN LEU
SEQRES 4 B 332 VAL PHE LEU LEU PRO GLU HIS LEU LYS ASP ALA SER LYS
SEQRES 5 B 332 LYS LYS LYS LYS SER SER LEU LEU PHE VAL LYS LEU ALA
SEQRES 6 B 332 ASN PRO HIS SER GLY GLU GLY ALA THR TYR LEU ILE ASP
SEQRES 7 B 332 MSE CYS LEU GLN GLN LEU PHE GLU ILE LYS VAL PHE LYS
SEQRES 8 B 332 GLU LYS HIS HIS SER TRP PHE ILE ASN GLN SER VAL GLN
SEQRES 9 B 332 SER GLY GLY LEU LEU HIS PHE ALA THR PRO MSE ASP PRO
SEQRES 10 B 332 LEU PHE LEU LEU LEU HIS TYR LEU LEU LYS ALA GLY LYS
SEQRES 11 B 332 GLU GLY LYS TYR GLN PRO LEU ASP GLN VAL VAL VAL ASP
SEQRES 12 B 332 ASP THR PHE PRO ASP CYS THR LEU LEU LEU ARG PHE PRO
SEQRES 13 B 332 GLU LEU GLU LYS SER LEU ARG HIS VAL THR GLU GLU LYS
SEQRES 14 B 332 GLU VAL ASN SER LYS LYS TYR TYR LYS TYR SER SER GLU
SEQRES 15 B 332 LYS THR LEU LYS TRP LEU GLU LYS LYS VAL ASN GLN THR
SEQRES 16 B 332 VAL VAL ALA LEU LYS ALA ASN ASN VAL ASN VAL GLY ALA
SEQRES 17 B 332 ARG VAL GLN SER SER ALA TYR PHE SER GLY GLY GLN VAL
SEQRES 18 B 332 SER ARG ASP LYS GLU GLU ASP TYR VAL ARG TYR ALA HIS
SEQRES 19 B 332 GLY LEU ILE SER ASP TYR ILE PRO LYS GLU LEU SER ASP
SEQRES 20 B 332 ASP LEU SER LYS PHE LEU LYS LEU PRO GLU PRO PRO ALA
SEQRES 21 B 332 SER LEU PRO ASN PRO PRO SER LYS LYS LEU LYS LEU SER
SEQRES 22 B 332 ASP GLU PRO VAL GLU ALA LYS GLU ASP TYR THR LYS PHE
SEQRES 23 B 332 ASN THR LYS ASP LEU LYS THR GLY LYS LYS ASN SER LYS
SEQRES 24 B 332 MSE THR ALA ALA GLN LYS ALA LEU ALA LYS VAL ASP LYS
SEQRES 25 B 332 SER GLY MSE LYS SER ILE ASP ALA PHE PHE GLY ALA LYS
SEQRES 26 B 332 ASN LYS LYS THR GLY LYS ILE
SEQRES 1 C 166 MSE LYS ASN PRO GLU GLU ALA ALA GLU GLY LYS GLN ARG
SEQRES 2 C 166 ILE HIS LEU ARG PRO GLY SER LEU ARG GLY ALA ALA PRO
SEQRES 3 C 166 ALA LYS LEU HIS LEU LEU PRO CYS ASP VAL LEU VAL SER
SEQRES 4 C 166 ARG PRO ALA PRO VAL ASP ARG PHE PHE THR PRO ALA VAL
SEQRES 5 C 166 ARG HIS ASP ALA ASP GLY LEU GLN ALA SER PHE ARG GLY
SEQRES 6 C 166 ARG GLY LEU ARG GLY GLU GLU VAL ALA VAL PRO PRO GLY
SEQRES 7 C 166 PHE ALA GLY PHE VAL MSE VAL THR GLU GLU LYS GLY GLU
SEQRES 8 C 166 GLY LEU ILE GLY LYS LEU ASN PHE SER GLY ASP ALA GLU
SEQRES 9 C 166 ASP LYS ALA ASP GLU ALA GLN GLU PRO LEU GLU ARG ASP
SEQRES 10 C 166 PHE ASP ARG LEU ILE GLY ALA THR GLY SER PHE SER HIS
SEQRES 11 C 166 PHE THR LEU TRP GLY LEU GLU THR VAL PRO GLY PRO ASP
SEQRES 12 C 166 ALA LYS VAL HIS ARG ALA LEU GLY TRP PRO SER LEU ALA
SEQRES 13 C 166 ALA ALA ILE HIS ALA GLN VAL PRO GLU ASP
MODRES 3KIO MSE A 1 MET SELENOMETHIONINE
MODRES 3KIO MSE A 45 MET SELENOMETHIONINE
MODRES 3KIO MSE A 83 MET SELENOMETHIONINE
MODRES 3KIO MSE A 106 MET SELENOMETHIONINE
MODRES 3KIO MSE A 146 MET SELENOMETHIONINE
MODRES 3KIO MSE B 55 MET SELENOMETHIONINE
MODRES 3KIO MSE B 91 MET SELENOMETHIONINE
MODRES 3KIO MSE B 276 MET SELENOMETHIONINE
MODRES 3KIO MSE C 84 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 45 8
HET MSE A 83 8
HET MSE A 106 8
HET MSE A 146 8
HET MSE B 55 8
HET MSE B 91 8
HET MSE B 276 8
HET MSE C 84 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 9(C5 H11 N O2 SE)
FORMUL 4 HOH *60(H2 O)
HELIX 1 1 LEU A 6 ASN A 10 5 5
HELIX 2 2 ALA A 22 GLU A 27 1 6
HELIX 3 3 SER A 55 LEU A 60 5 6
HELIX 4 4 THR A 72 ASP A 86 1 15
HELIX 5 5 SER A 98 LEU A 107 1 10
HELIX 6 6 ASN A 113 GLN A 132 1 20
HELIX 7 7 PRO A 147 HIS A 157 1 11
HELIX 8 8 LYS A 168 LEU A 172 5 5
HELIX 9 9 PHE A 173 GLN A 201 1 29
HELIX 10 10 ASP A 214 LYS A 223 1 10
HELIX 11 11 TRP A 239 ALA A 250 1 12
HELIX 12 12 HIS B 22 ASP B 25 5 4
HELIX 13 13 LEU B 94 LEU B 98 5 5
HELIX 14 14 LYS B 151 SER B 156 1 6
HELIX 15 15 THR B 160 LEU B 175 1 16
HELIX 16 16 ASN B 273 ALA B 278 1 6
HELIX 17 17 PRO C 43 PHE C 48 1 6
HELIX 18 18 THR C 49 VAL C 52 5 4
HELIX 19 19 GLU C 112 ARG C 116 5 5
SHEET 1 A 6 ARG A 13 SER A 17 0
SHEET 2 A 6 GLY A 91 LEU A 97 -1 O VAL A 96 N CYS A 14
SHEET 3 A 6 MSE A 45 PRO A 53 -1 N ILE A 49 O ALA A 93
SHEET 4 A 6 CYS A 29 ALA A 36 -1 N ALA A 36 O VAL A 46
SHEET 5 A 6 VAL A 136 ASP A 142 1 O ASP A 142 N VAL A 33
SHEET 6 A 6 GLU A 162 LYS A 166 1 O THR A 164 N VAL A 141
SHEET 1 B 2 VAL A 253 ILE A 254 0
SHEET 2 B 2 ASP C 35 VAL C 36 -1 O ASP C 35 N ILE A 254
SHEET 1 C 8 ILE C 14 LEU C 16 0
SHEET 2 C 8 LEU B 35 LYS B 39 -1 N PHE B 37 O ILE C 14
SHEET 3 C 8 THR B 50 ASP B 54 -1 O ILE B 53 N LEU B 36
SHEET 4 C 8 PHE B 61 PHE B 66 -1 O PHE B 61 N LEU B 52
SHEET 5 C 8 LEU B 85 PRO B 90 -1 O THR B 89 N GLU B 62
SHEET 6 C 8 GLN B 14 PRO B 20 1 N LEU B 18 O ALA B 88
SHEET 7 C 8 PHE C 79 VAL C 85 -1 O MSE C 84 N LEU B 15
SHEET 8 C 8 GLY C 92 LYS C 96 -1 O LEU C 93 N VAL C 83
SHEET 1 D 7 ARG C 40 PRO C 41 0
SHEET 2 D 7 SER B 78 GLN B 80 -1 N VAL B 79 O ARG C 40
SHEET 3 D 7 SER B 72 ILE B 75 -1 N TRP B 73 O GLN B 80
SHEET 4 D 7 LEU C 29 LEU C 32 -1 O HIS C 30 N PHE B 74
SHEET 5 D 7 ASN C 98 GLU C 104 1 O SER C 100 N LEU C 31
SHEET 6 D 7 ARG C 66 ALA C 74 -1 N GLU C 71 O GLY C 101
SHEET 7 D 7 GLN C 60 PHE C 63 -1 N ALA C 61 O LEU C 68
SSBOND 1 CYS A 24 CYS A 29 1555 1555 2.06
LINK C MSE A 1 N ASP A 2 1555 1555 1.33
LINK C PRO A 44 N MSE A 45 1555 1555 1.33
LINK C MSE A 45 N VAL A 46 1555 1555 1.33
LINK C LYS A 82 N MSE A 83 1555 1555 1.33
LINK C MSE A 83 N GLU A 84 1555 1555 1.32
LINK C SER A 105 N MSE A 106 1555 1555 1.33
LINK C MSE A 106 N LEU A 107 1555 1555 1.32
LINK C GLY A 145 N MSE A 146 1555 1555 1.34
LINK C MSE A 146 N PRO A 147 1555 1555 1.34
LINK C ASP B 54 N MSE B 55 1555 1555 1.33
LINK C MSE B 55 N CYS B 56 1555 1555 1.33
LINK C PRO B 90 N MSE B 91 1555 1555 1.33
LINK C MSE B 91 N ASP B 92 1555 1555 1.34
LINK C LYS B 275 N MSE B 276 1555 1555 1.33
LINK C MSE B 276 N THR B 277 1555 1555 1.33
LINK C VAL C 83 N MSE C 84 1555 1555 1.33
LINK C MSE C 84 N VAL C 85 1555 1555 1.33
CRYST1 279.287 40.421 67.820 90.00 90.00 90.00 P 21 21 2 4
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 0.003581 0.000000 0.000000 0.00000
SCALE2 0.000000 0.024740 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014745 0.00000
HETATM 1 N MSE A 1 78.700 0.060 0.551 1.00 87.49 N
ANISOU 1 N MSE A 1 16171 8307 8763 -4584 -6042 5791 N
HETATM 2 CA MSE A 1 78.175 -1.304 0.568 1.00 92.89 C
ANISOU 2 CA MSE A 1 16716 8993 9586 -5052 -4556 5646 C
HETATM 3 C MSE A 1 76.773 -1.265 1.145 1.00103.51 C
ANISOU 3 C MSE A 1 17719 11118 10492 -5094 -4499 4363 C
HETATM 4 O MSE A 1 75.829 -1.821 0.579 1.00 98.80 O
ANISOU 4 O MSE A 1 16961 10653 9926 -5386 -3840 3488 O
HETATM 5 CB MSE A 1 79.056 -2.187 1.434 1.00 88.76 C
ANISOU 5 CB MSE A 1 16286 8217 9223 -5196 -3684 6900 C
HETATM 6 CG MSE A 1 79.127 -3.623 0.994 1.00 87.86 C
ANISOU 6 CG MSE A 1 16194 7696 9495 -5681 -2163 7276 C
HETATM 7 SE MSE A 1 79.699 -4.650 2.356 1.00120.79 SE
ANISOU 7 SE MSE A 1 20249 11958 13686 -5793 -1171 8195 SE
HETATM 8 CE MSE A 1 78.309 -4.498 3.475 1.00 94.82 C
ANISOU 8 CE MSE A 1 16684 9548 9798 -5819 -1190 7152 C
(ATOM LINES ARE NOT SHOWN.)
END
