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casp_data / casp15 /experiment_structures /T1192.pdb
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HEADER DNA BINDING PROTEIN 21-DEC-23 8RJW
TITLE HUMAN RAD52 OPEN RING - SSDNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA REPAIR PROTEIN RAD52 HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: SSDNA;
COMPND 7 CHAIN: A;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: RAD52;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_TAXID: 9606
KEYWDS SSDNA BINDING PROTEIN, DNA DAMAGE REPAIR, SINGLE-STRAND ANNEALING,
KEYWDS 2 DNA BINDING PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR C.C.LIANG,S.C.WEST
REVDAT 3 29-MAY-24 8RJW 1 JRNL
REVDAT 2 08-MAY-24 8RJW 1 JRNL
REVDAT 1 24-APR-24 8RJW 0
JRNL AUTH C.C.LIANG,L.A.GREENHOUGH,L.MASINO,S.MASLEN,I.BAJRAMI,
JRNL AUTH 2 M.TUPPI,M.SKEHEL,I.A.TAYLOR,S.C.WEST
JRNL TITL MECHANISM OF SINGLE-STRANDED DNA ANNEALING BY RAD52-RPA
JRNL TITL 2 COMPLEX.
JRNL REF NATURE V. 629 697 2024
JRNL REFN ESSN 1476-4687
JRNL PMID 38658755
JRNL DOI 10.1038/S41586-024-07347-7
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : PHENIX
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 8RJ3
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.300
REMARK 3 NUMBER OF PARTICLES : 587046
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 8RJW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-DEC-23.
REMARK 100 THE DEPOSITION ID IS D_1292135580.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : OPEN RING CONFORMATION OF HUMAN
REMARK 245 RAD52 IN COMPLEX WITH SSDNA
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.15
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
REMARK 245 SAMPLE DETAILS : RECOMBINANT RAD52 PURIFIED FROM
REMARK 245 E. COLI, AND THE OPEN RING CONFORMATION WAS SEPARATED BY CATION
REMARK 245 EXCHANGE. THE RAD52-SSDNA COMPLEX WAS RECONSTITUTED IN VITRO.
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X
REMARK 245 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 750.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2250.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4000.00
REMARK 245 ILLUMINATION MODE : SPOT SCAN
REMARK 245 NOMINAL MAGNIFICATION : 105000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 34050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -203.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLY A 3
REMARK 465 THR A 4
REMARK 465 GLU A 5
REMARK 465 GLU A 6
REMARK 465 ALA A 7
REMARK 465 ILE A 8
REMARK 465 LEU A 9
REMARK 465 GLY A 10
REMARK 465 GLY A 11
REMARK 465 ARG A 12
REMARK 465 ASP A 13
REMARK 465 SER A 14
REMARK 465 HIS A 15
REMARK 465 PRO A 16
REMARK 465 ALA A 17
REMARK 465 ALA A 18
REMARK 465 GLY A 19
REMARK 465 GLY A 20
REMARK 465 GLY A 21
REMARK 465 SER A 22
REMARK 465 VAL A 23
REMARK 465 LEU A 24
REMARK 465 CYS A 25
REMARK 465 PHE A 26
REMARK 465 GLY A 27
REMARK 465 GLN A 28
REMARK 465 CYS A 29
REMARK 465 GLN A 30
REMARK 465 TYR A 31
REMARK 465 THR A 32
REMARK 465 ARG A 44
REMARK 465 GLN A 45
REMARK 465 ARG A 46
REMARK 465 LEU A 47
REMARK 465 GLY A 48
REMARK 465 PRO A 49
REMARK 465 GLU A 50
REMARK 465 TYR A 51
REMARK 465 ILE A 52
REMARK 465 SER A 53
REMARK 465 SER A 54
REMARK 465 ARG A 55
REMARK 465 MET A 56
REMARK 465 ALA A 57
REMARK 465 GLY A 58
REMARK 465 GLY A 59
REMARK 465 GLY A 60
REMARK 465 GLN A 61
REMARK 465 LYS A 62
REMARK 465 VAL A 63
REMARK 465 CYS A 64
REMARK 465 LEU A 167
REMARK 465 ASP A 168
REMARK 465 LYS A 169
REMARK 465 ASP A 170
REMARK 465 TYR A 171
REMARK 465 LEU A 172
REMARK 465 ARG A 173
REMARK 465 SER A 174
REMARK 465 LEU A 175
REMARK 465 ASN A 176
REMARK 465 LYS A 177
REMARK 465 LEU A 178
REMARK 465 PRO A 179
REMARK 465 ARG A 180
REMARK 465 GLN A 181
REMARK 465 LEU A 182
REMARK 465 PRO A 183
REMARK 465 LEU A 184
REMARK 465 GLU A 185
REMARK 465 VAL A 186
REMARK 465 ASP A 187
REMARK 465 LEU A 188
REMARK 465 THR A 189
REMARK 465 LYS A 190
REMARK 465 ALA A 191
REMARK 465 LYS A 192
REMARK 465 ARG A 193
REMARK 465 GLN A 194
REMARK 465 ASP A 195
REMARK 465 LEU A 196
REMARK 465 GLU A 197
REMARK 465 PRO A 198
REMARK 465 SER A 199
REMARK 465 VAL A 200
REMARK 465 GLU A 201
REMARK 465 GLU A 202
REMARK 465 ALA A 203
REMARK 465 ARG A 204
REMARK 465 TYR A 205
REMARK 465 ASN A 206
REMARK 465 SER A 207
REMARK 465 CYS A 208
REMARK 465 ARG A 209
REMARK 465 PRO A 210
REMARK 465 ASN A 211
REMARK 465 MET A 212
REMARK 465 ALA A 213
REMARK 465 LEU A 214
REMARK 465 GLY A 215
REMARK 465 HIS A 216
REMARK 465 PRO A 217
REMARK 465 GLN A 218
REMARK 465 LEU A 219
REMARK 465 GLN A 220
REMARK 465 GLN A 221
REMARK 465 VAL A 222
REMARK 465 THR A 223
REMARK 465 SER A 224
REMARK 465 PRO A 225
REMARK 465 SER A 226
REMARK 465 ARG A 227
REMARK 465 PRO A 228
REMARK 465 SER A 229
REMARK 465 HIS A 230
REMARK 465 ALA A 231
REMARK 465 VAL A 232
REMARK 465 ILE A 233
REMARK 465 PRO A 234
REMARK 465 ALA A 235
REMARK 465 ASP A 236
REMARK 465 GLN A 237
REMARK 465 ASP A 238
REMARK 465 CYS A 239
REMARK 465 SER A 240
REMARK 465 SER A 241
REMARK 465 ARG A 242
REMARK 465 SER A 243
REMARK 465 LEU A 244
REMARK 465 SER A 245
REMARK 465 SER A 246
REMARK 465 SER A 247
REMARK 465 ALA A 248
REMARK 465 VAL A 249
REMARK 465 GLU A 250
REMARK 465 SER A 251
REMARK 465 GLU A 252
REMARK 465 ALA A 253
REMARK 465 THR A 254
REMARK 465 HIS A 255
REMARK 465 GLN A 256
REMARK 465 ARG A 257
REMARK 465 LYS A 258
REMARK 465 LEU A 259
REMARK 465 ARG A 260
REMARK 465 GLN A 261
REMARK 465 LYS A 262
REMARK 465 GLN A 263
REMARK 465 LEU A 264
REMARK 465 GLN A 265
REMARK 465 GLN A 266
REMARK 465 GLN A 267
REMARK 465 PHE A 268
REMARK 465 ARG A 269
REMARK 465 GLU A 270
REMARK 465 ARG A 271
REMARK 465 MET A 272
REMARK 465 GLU A 273
REMARK 465 LYS A 274
REMARK 465 GLN A 275
REMARK 465 GLN A 276
REMARK 465 VAL A 277
REMARK 465 ARG A 278
REMARK 465 VAL A 279
REMARK 465 SER A 280
REMARK 465 THR A 281
REMARK 465 PRO A 282
REMARK 465 SER A 283
REMARK 465 ALA A 284
REMARK 465 GLU A 285
REMARK 465 LYS A 286
REMARK 465 SER A 287
REMARK 465 GLU A 288
REMARK 465 ALA A 289
REMARK 465 ALA A 290
REMARK 465 PRO A 291
REMARK 465 PRO A 292
REMARK 465 ALA A 293
REMARK 465 PRO A 294
REMARK 465 PRO A 295
REMARK 465 VAL A 296
REMARK 465 THR A 297
REMARK 465 HIS A 298
REMARK 465 SER A 299
REMARK 465 THR A 300
REMARK 465 PRO A 301
REMARK 465 VAL A 302
REMARK 465 THR A 303
REMARK 465 VAL A 304
REMARK 465 SER A 305
REMARK 465 GLU A 306
REMARK 465 PRO A 307
REMARK 465 LEU A 308
REMARK 465 LEU A 309
REMARK 465 GLU A 310
REMARK 465 LYS A 311
REMARK 465 ASP A 312
REMARK 465 PHE A 313
REMARK 465 LEU A 314
REMARK 465 ALA A 315
REMARK 465 GLY A 316
REMARK 465 VAL A 317
REMARK 465 THR A 318
REMARK 465 GLN A 319
REMARK 465 GLU A 320
REMARK 465 LEU A 321
REMARK 465 ILE A 322
REMARK 465 LYS A 323
REMARK 465 THR A 324
REMARK 465 LEU A 325
REMARK 465 GLU A 326
REMARK 465 ASP A 327
REMARK 465 ASN A 328
REMARK 465 SER A 329
REMARK 465 GLU A 330
REMARK 465 LYS A 331
REMARK 465 TRP A 332
REMARK 465 ALA A 333
REMARK 465 VAL A 334
REMARK 465 THR A 335
REMARK 465 PRO A 336
REMARK 465 ASP A 337
REMARK 465 ALA A 338
REMARK 465 GLY A 339
REMARK 465 ASP A 340
REMARK 465 GLY A 341
REMARK 465 VAL A 342
REMARK 465 VAL A 343
REMARK 465 LYS A 344
REMARK 465 PRO A 345
REMARK 465 SER A 346
REMARK 465 SER A 347
REMARK 465 ARG A 348
REMARK 465 ALA A 349
REMARK 465 ASP A 350
REMARK 465 PRO A 351
REMARK 465 ALA A 352
REMARK 465 GLN A 353
REMARK 465 THR A 354
REMARK 465 SER A 355
REMARK 465 ASP A 356
REMARK 465 THR A 357
REMARK 465 LEU A 358
REMARK 465 ALA A 359
REMARK 465 LEU A 360
REMARK 465 ASN A 361
REMARK 465 ASN A 362
REMARK 465 GLN A 363
REMARK 465 MET A 364
REMARK 465 VAL A 365
REMARK 465 THR A 366
REMARK 465 GLN A 367
REMARK 465 ASN A 368
REMARK 465 ARG A 369
REMARK 465 THR A 370
REMARK 465 PRO A 371
REMARK 465 HIS A 372
REMARK 465 SER A 373
REMARK 465 VAL A 374
REMARK 465 CYS A 375
REMARK 465 HIS A 376
REMARK 465 GLN A 377
REMARK 465 LYS A 378
REMARK 465 PRO A 379
REMARK 465 GLN A 380
REMARK 465 ALA A 381
REMARK 465 LYS A 382
REMARK 465 SER A 383
REMARK 465 GLY A 384
REMARK 465 SER A 385
REMARK 465 TRP A 386
REMARK 465 ASP A 387
REMARK 465 LEU A 388
REMARK 465 GLN A 389
REMARK 465 THR A 390
REMARK 465 TYR A 391
REMARK 465 SER A 392
REMARK 465 ALA A 393
REMARK 465 ASP A 394
REMARK 465 GLN A 395
REMARK 465 ARG A 396
REMARK 465 THR A 397
REMARK 465 THR A 398
REMARK 465 GLY A 399
REMARK 465 ASN A 400
REMARK 465 TRP A 401
REMARK 465 GLU A 402
REMARK 465 SER A 403
REMARK 465 HIS A 404
REMARK 465 ARG A 405
REMARK 465 LYS A 406
REMARK 465 SER A 407
REMARK 465 GLN A 408
REMARK 465 ASP A 409
REMARK 465 MET A 410
REMARK 465 LYS A 411
REMARK 465 LYS A 412
REMARK 465 ARG A 413
REMARK 465 LYS A 414
REMARK 465 TYR A 415
REMARK 465 ASP A 416
REMARK 465 PRO A 417
REMARK 465 SER A 418
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLY B 3
REMARK 465 THR B 4
REMARK 465 GLU B 5
REMARK 465 GLU B 6
REMARK 465 ALA B 7
REMARK 465 ILE B 8
REMARK 465 LEU B 9
REMARK 465 GLY B 10
REMARK 465 GLY B 11
REMARK 465 ARG B 12
REMARK 465 ASP B 13
REMARK 465 SER B 14
REMARK 465 HIS B 15
REMARK 465 PRO B 16
REMARK 465 ALA B 17
REMARK 465 ALA B 18
REMARK 465 GLY B 19
REMARK 465 GLY B 20
REMARK 465 GLY B 21
REMARK 465 SER B 22
REMARK 465 VAL B 23
REMARK 465 LEU B 24
REMARK 465 ALA B 57
REMARK 465 GLY B 58
REMARK 465 GLY B 59
REMARK 465 GLY B 60
REMARK 465 LYS B 177
REMARK 465 LEU B 178
REMARK 465 PRO B 179
REMARK 465 ARG B 180
REMARK 465 GLN B 181
REMARK 465 LEU B 182
REMARK 465 PRO B 183
REMARK 465 LEU B 184
REMARK 465 GLU B 185
REMARK 465 VAL B 186
REMARK 465 ASP B 187
REMARK 465 LEU B 188
REMARK 465 THR B 189
REMARK 465 LYS B 190
REMARK 465 ALA B 191
REMARK 465 LYS B 192
REMARK 465 ARG B 193
REMARK 465 GLN B 194
REMARK 465 ASP B 195
REMARK 465 LEU B 196
REMARK 465 GLU B 197
REMARK 465 PRO B 198
REMARK 465 SER B 199
REMARK 465 VAL B 200
REMARK 465 GLU B 201
REMARK 465 GLU B 202
REMARK 465 ALA B 203
REMARK 465 ARG B 204
REMARK 465 TYR B 205
REMARK 465 ASN B 206
REMARK 465 SER B 207
REMARK 465 CYS B 208
REMARK 465 ARG B 209
REMARK 465 PRO B 210
REMARK 465 ASN B 211
REMARK 465 MET B 212
REMARK 465 ALA B 213
REMARK 465 LEU B 214
REMARK 465 GLY B 215
REMARK 465 HIS B 216
REMARK 465 PRO B 217
REMARK 465 GLN B 218
REMARK 465 LEU B 219
REMARK 465 GLN B 220
REMARK 465 GLN B 221
REMARK 465 VAL B 222
REMARK 465 THR B 223
REMARK 465 SER B 224
REMARK 465 PRO B 225
REMARK 465 SER B 226
REMARK 465 ARG B 227
REMARK 465 PRO B 228
REMARK 465 SER B 229
REMARK 465 HIS B 230
REMARK 465 ALA B 231
REMARK 465 VAL B 232
REMARK 465 ILE B 233
REMARK 465 PRO B 234
REMARK 465 ALA B 235
REMARK 465 ASP B 236
REMARK 465 GLN B 237
REMARK 465 ASP B 238
REMARK 465 CYS B 239
REMARK 465 SER B 240
REMARK 465 SER B 241
REMARK 465 ARG B 242
REMARK 465 SER B 243
REMARK 465 LEU B 244
REMARK 465 SER B 245
REMARK 465 SER B 246
REMARK 465 SER B 247
REMARK 465 ALA B 248
REMARK 465 VAL B 249
REMARK 465 GLU B 250
REMARK 465 SER B 251
REMARK 465 GLU B 252
REMARK 465 ALA B 253
REMARK 465 THR B 254
REMARK 465 HIS B 255
REMARK 465 GLN B 256
REMARK 465 ARG B 257
REMARK 465 LYS B 258
REMARK 465 LEU B 259
REMARK 465 ARG B 260
REMARK 465 GLN B 261
REMARK 465 LYS B 262
REMARK 465 GLN B 263
REMARK 465 LEU B 264
REMARK 465 GLN B 265
REMARK 465 GLN B 266
REMARK 465 GLN B 267
REMARK 465 PHE B 268
REMARK 465 ARG B 269
REMARK 465 GLU B 270
REMARK 465 ARG B 271
REMARK 465 MET B 272
REMARK 465 GLU B 273
REMARK 465 LYS B 274
REMARK 465 GLN B 275
REMARK 465 GLN B 276
REMARK 465 VAL B 277
REMARK 465 ARG B 278
REMARK 465 VAL B 279
REMARK 465 SER B 280
REMARK 465 THR B 281
REMARK 465 PRO B 282
REMARK 465 SER B 283
REMARK 465 ALA B 284
REMARK 465 GLU B 285
REMARK 465 LYS B 286
REMARK 465 SER B 287
REMARK 465 GLU B 288
REMARK 465 ALA B 289
REMARK 465 ALA B 290
REMARK 465 PRO B 291
REMARK 465 PRO B 292
REMARK 465 ALA B 293
REMARK 465 PRO B 294
REMARK 465 PRO B 295
REMARK 465 VAL B 296
REMARK 465 THR B 297
REMARK 465 HIS B 298
REMARK 465 SER B 299
REMARK 465 THR B 300
REMARK 465 PRO B 301
REMARK 465 VAL B 302
REMARK 465 THR B 303
REMARK 465 VAL B 304
REMARK 465 SER B 305
REMARK 465 GLU B 306
REMARK 465 PRO B 307
REMARK 465 LEU B 308
REMARK 465 LEU B 309
REMARK 465 GLU B 310
REMARK 465 LYS B 311
REMARK 465 ASP B 312
REMARK 465 PHE B 313
REMARK 465 LEU B 314
REMARK 465 ALA B 315
REMARK 465 GLY B 316
REMARK 465 VAL B 317
REMARK 465 THR B 318
REMARK 465 GLN B 319
REMARK 465 GLU B 320
REMARK 465 LEU B 321
REMARK 465 ILE B 322
REMARK 465 LYS B 323
REMARK 465 THR B 324
REMARK 465 LEU B 325
REMARK 465 GLU B 326
REMARK 465 ASP B 327
REMARK 465 ASN B 328
REMARK 465 SER B 329
REMARK 465 GLU B 330
REMARK 465 LYS B 331
REMARK 465 TRP B 332
REMARK 465 ALA B 333
REMARK 465 VAL B 334
REMARK 465 THR B 335
REMARK 465 PRO B 336
REMARK 465 ASP B 337
REMARK 465 ALA B 338
REMARK 465 GLY B 339
REMARK 465 ASP B 340
REMARK 465 GLY B 341
REMARK 465 VAL B 342
REMARK 465 VAL B 343
REMARK 465 LYS B 344
REMARK 465 PRO B 345
REMARK 465 SER B 346
REMARK 465 SER B 347
REMARK 465 ARG B 348
REMARK 465 ALA B 349
REMARK 465 ASP B 350
REMARK 465 PRO B 351
REMARK 465 ALA B 352
REMARK 465 GLN B 353
REMARK 465 THR B 354
REMARK 465 SER B 355
REMARK 465 ASP B 356
REMARK 465 THR B 357
REMARK 465 LEU B 358
REMARK 465 ALA B 359
REMARK 465 LEU B 360
REMARK 465 ASN B 361
REMARK 465 ASN B 362
REMARK 465 GLN B 363
REMARK 465 MET B 364
REMARK 465 VAL B 365
REMARK 465 THR B 366
REMARK 465 GLN B 367
REMARK 465 ASN B 368
REMARK 465 ARG B 369
REMARK 465 THR B 370
REMARK 465 PRO B 371
REMARK 465 HIS B 372
REMARK 465 SER B 373
REMARK 465 VAL B 374
REMARK 465 CYS B 375
REMARK 465 HIS B 376
REMARK 465 GLN B 377
REMARK 465 LYS B 378
REMARK 465 PRO B 379
REMARK 465 GLN B 380
REMARK 465 ALA B 381
REMARK 465 LYS B 382
REMARK 465 SER B 383
REMARK 465 GLY B 384
REMARK 465 SER B 385
REMARK 465 TRP B 386
REMARK 465 ASP B 387
REMARK 465 LEU B 388
REMARK 465 GLN B 389
REMARK 465 THR B 390
REMARK 465 TYR B 391
REMARK 465 SER B 392
REMARK 465 ALA B 393
REMARK 465 ASP B 394
REMARK 465 GLN B 395
REMARK 465 ARG B 396
REMARK 465 THR B 397
REMARK 465 THR B 398
REMARK 465 GLY B 399
REMARK 465 ASN B 400
REMARK 465 TRP B 401
REMARK 465 GLU B 402
REMARK 465 SER B 403
REMARK 465 HIS B 404
REMARK 465 ARG B 405
REMARK 465 LYS B 406
REMARK 465 SER B 407
REMARK 465 GLN B 408
REMARK 465 ASP B 409
REMARK 465 MET B 410
REMARK 465 LYS B 411
REMARK 465 LYS B 412
REMARK 465 ARG B 413
REMARK 465 LYS B 414
REMARK 465 TYR B 415
REMARK 465 ASP B 416
REMARK 465 PRO B 417
REMARK 465 SER B 418
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLY C 3
REMARK 465 THR C 4
REMARK 465 GLU C 5
REMARK 465 GLU C 6
REMARK 465 ALA C 7
REMARK 465 ILE C 8
REMARK 465 LEU C 9
REMARK 465 GLY C 10
REMARK 465 GLY C 11
REMARK 465 ARG C 12
REMARK 465 ASP C 13
REMARK 465 SER C 14
REMARK 465 HIS C 15
REMARK 465 PRO C 16
REMARK 465 ALA C 17
REMARK 465 ALA C 18
REMARK 465 GLY C 19
REMARK 465 GLY C 20
REMARK 465 GLY C 21
REMARK 465 SER C 22
REMARK 465 VAL C 23
REMARK 465 LEU C 24
REMARK 465 PRO C 179
REMARK 465 ARG C 180
REMARK 465 GLN C 181
REMARK 465 LEU C 182
REMARK 465 PRO C 183
REMARK 465 LEU C 184
REMARK 465 GLU C 185
REMARK 465 VAL C 186
REMARK 465 ASP C 187
REMARK 465 LEU C 188
REMARK 465 THR C 189
REMARK 465 LYS C 190
REMARK 465 ALA C 191
REMARK 465 LYS C 192
REMARK 465 ARG C 193
REMARK 465 GLN C 194
REMARK 465 ASP C 195
REMARK 465 LEU C 196
REMARK 465 GLU C 197
REMARK 465 PRO C 198
REMARK 465 SER C 199
REMARK 465 VAL C 200
REMARK 465 GLU C 201
REMARK 465 GLU C 202
REMARK 465 ALA C 203
REMARK 465 ARG C 204
REMARK 465 TYR C 205
REMARK 465 ASN C 206
REMARK 465 SER C 207
REMARK 465 CYS C 208
REMARK 465 ARG C 209
REMARK 465 PRO C 210
REMARK 465 ASN C 211
REMARK 465 MET C 212
REMARK 465 ALA C 213
REMARK 465 LEU C 214
REMARK 465 GLY C 215
REMARK 465 HIS C 216
REMARK 465 PRO C 217
REMARK 465 GLN C 218
REMARK 465 LEU C 219
REMARK 465 GLN C 220
REMARK 465 GLN C 221
REMARK 465 VAL C 222
REMARK 465 THR C 223
REMARK 465 SER C 224
REMARK 465 PRO C 225
REMARK 465 SER C 226
REMARK 465 ARG C 227
REMARK 465 PRO C 228
REMARK 465 SER C 229
REMARK 465 HIS C 230
REMARK 465 ALA C 231
REMARK 465 VAL C 232
REMARK 465 ILE C 233
REMARK 465 PRO C 234
REMARK 465 ALA C 235
REMARK 465 ASP C 236
REMARK 465 GLN C 237
REMARK 465 ASP C 238
REMARK 465 CYS C 239
REMARK 465 SER C 240
REMARK 465 SER C 241
REMARK 465 ARG C 242
REMARK 465 SER C 243
REMARK 465 LEU C 244
REMARK 465 SER C 245
REMARK 465 SER C 246
REMARK 465 SER C 247
REMARK 465 ALA C 248
REMARK 465 VAL C 249
REMARK 465 GLU C 250
REMARK 465 SER C 251
REMARK 465 GLU C 252
REMARK 465 ALA C 253
REMARK 465 THR C 254
REMARK 465 HIS C 255
REMARK 465 GLN C 256
REMARK 465 ARG C 257
REMARK 465 LYS C 258
REMARK 465 LEU C 259
REMARK 465 ARG C 260
REMARK 465 GLN C 261
REMARK 465 LYS C 262
REMARK 465 GLN C 263
REMARK 465 LEU C 264
REMARK 465 GLN C 265
REMARK 465 GLN C 266
REMARK 465 GLN C 267
REMARK 465 PHE C 268
REMARK 465 ARG C 269
REMARK 465 GLU C 270
REMARK 465 ARG C 271
REMARK 465 MET C 272
REMARK 465 GLU C 273
REMARK 465 LYS C 274
REMARK 465 GLN C 275
REMARK 465 GLN C 276
REMARK 465 VAL C 277
REMARK 465 ARG C 278
REMARK 465 VAL C 279
REMARK 465 SER C 280
REMARK 465 THR C 281
REMARK 465 PRO C 282
REMARK 465 SER C 283
REMARK 465 ALA C 284
REMARK 465 GLU C 285
REMARK 465 LYS C 286
REMARK 465 SER C 287
REMARK 465 GLU C 288
REMARK 465 ALA C 289
REMARK 465 ALA C 290
REMARK 465 PRO C 291
REMARK 465 PRO C 292
REMARK 465 ALA C 293
REMARK 465 PRO C 294
REMARK 465 PRO C 295
REMARK 465 VAL C 296
REMARK 465 THR C 297
REMARK 465 HIS C 298
REMARK 465 SER C 299
REMARK 465 THR C 300
REMARK 465 PRO C 301
REMARK 465 VAL C 302
REMARK 465 THR C 303
REMARK 465 VAL C 304
REMARK 465 SER C 305
REMARK 465 GLU C 306
REMARK 465 PRO C 307
REMARK 465 LEU C 308
REMARK 465 LEU C 309
REMARK 465 GLU C 310
REMARK 465 LYS C 311
REMARK 465 ASP C 312
REMARK 465 PHE C 313
REMARK 465 LEU C 314
REMARK 465 ALA C 315
REMARK 465 GLY C 316
REMARK 465 VAL C 317
REMARK 465 THR C 318
REMARK 465 GLN C 319
REMARK 465 GLU C 320
REMARK 465 LEU C 321
REMARK 465 ILE C 322
REMARK 465 LYS C 323
REMARK 465 THR C 324
REMARK 465 LEU C 325
REMARK 465 GLU C 326
REMARK 465 ASP C 327
REMARK 465 ASN C 328
REMARK 465 SER C 329
REMARK 465 GLU C 330
REMARK 465 LYS C 331
REMARK 465 TRP C 332
REMARK 465 ALA C 333
REMARK 465 VAL C 334
REMARK 465 THR C 335
REMARK 465 PRO C 336
REMARK 465 ASP C 337
REMARK 465 ALA C 338
REMARK 465 GLY C 339
REMARK 465 ASP C 340
REMARK 465 GLY C 341
REMARK 465 VAL C 342
REMARK 465 VAL C 343
REMARK 465 LYS C 344
REMARK 465 PRO C 345
REMARK 465 SER C 346
REMARK 465 SER C 347
REMARK 465 ARG C 348
REMARK 465 ALA C 349
REMARK 465 ASP C 350
REMARK 465 PRO C 351
REMARK 465 ALA C 352
REMARK 465 GLN C 353
REMARK 465 THR C 354
REMARK 465 SER C 355
REMARK 465 ASP C 356
REMARK 465 THR C 357
REMARK 465 LEU C 358
REMARK 465 ALA C 359
REMARK 465 LEU C 360
REMARK 465 ASN C 361
REMARK 465 ASN C 362
REMARK 465 GLN C 363
REMARK 465 MET C 364
REMARK 465 VAL C 365
REMARK 465 THR C 366
REMARK 465 GLN C 367
REMARK 465 ASN C 368
REMARK 465 ARG C 369
REMARK 465 THR C 370
REMARK 465 PRO C 371
REMARK 465 HIS C 372
REMARK 465 SER C 373
REMARK 465 VAL C 374
REMARK 465 CYS C 375
REMARK 465 HIS C 376
REMARK 465 GLN C 377
REMARK 465 LYS C 378
REMARK 465 PRO C 379
REMARK 465 GLN C 380
REMARK 465 ALA C 381
REMARK 465 LYS C 382
REMARK 465 SER C 383
REMARK 465 GLY C 384
REMARK 465 SER C 385
REMARK 465 TRP C 386
REMARK 465 ASP C 387
REMARK 465 LEU C 388
REMARK 465 GLN C 389
REMARK 465 THR C 390
REMARK 465 TYR C 391
REMARK 465 SER C 392
REMARK 465 ALA C 393
REMARK 465 ASP C 394
REMARK 465 GLN C 395
REMARK 465 ARG C 396
REMARK 465 THR C 397
REMARK 465 THR C 398
REMARK 465 GLY C 399
REMARK 465 ASN C 400
REMARK 465 TRP C 401
REMARK 465 GLU C 402
REMARK 465 SER C 403
REMARK 465 HIS C 404
REMARK 465 ARG C 405
REMARK 465 LYS C 406
REMARK 465 SER C 407
REMARK 465 GLN C 408
REMARK 465 ASP C 409
REMARK 465 MET C 410
REMARK 465 LYS C 411
REMARK 465 LYS C 412
REMARK 465 ARG C 413
REMARK 465 LYS C 414
REMARK 465 TYR C 415
REMARK 465 ASP C 416
REMARK 465 PRO C 417
REMARK 465 SER C 418
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 GLY D 3
REMARK 465 THR D 4
REMARK 465 GLU D 5
REMARK 465 GLU D 6
REMARK 465 ALA D 7
REMARK 465 ILE D 8
REMARK 465 LEU D 9
REMARK 465 GLY D 10
REMARK 465 GLY D 11
REMARK 465 ARG D 12
REMARK 465 ASP D 13
REMARK 465 SER D 14
REMARK 465 HIS D 15
REMARK 465 PRO D 16
REMARK 465 ALA D 17
REMARK 465 ALA D 18
REMARK 465 GLY D 19
REMARK 465 GLY D 20
REMARK 465 GLY D 21
REMARK 465 SER D 22
REMARK 465 VAL D 23
REMARK 465 LEU D 24
REMARK 465 GLY D 58
REMARK 465 GLY D 59
REMARK 465 GLY D 60
REMARK 465 TYR D 205
REMARK 465 ASN D 206
REMARK 465 SER D 207
REMARK 465 CYS D 208
REMARK 465 ARG D 209
REMARK 465 PRO D 210
REMARK 465 ASN D 211
REMARK 465 MET D 212
REMARK 465 ALA D 213
REMARK 465 LEU D 214
REMARK 465 GLY D 215
REMARK 465 HIS D 216
REMARK 465 PRO D 217
REMARK 465 GLN D 218
REMARK 465 LEU D 219
REMARK 465 GLN D 220
REMARK 465 GLN D 221
REMARK 465 VAL D 222
REMARK 465 THR D 223
REMARK 465 SER D 224
REMARK 465 PRO D 225
REMARK 465 SER D 226
REMARK 465 ARG D 227
REMARK 465 PRO D 228
REMARK 465 SER D 229
REMARK 465 HIS D 230
REMARK 465 ALA D 231
REMARK 465 VAL D 232
REMARK 465 ILE D 233
REMARK 465 PRO D 234
REMARK 465 ALA D 235
REMARK 465 ASP D 236
REMARK 465 GLN D 237
REMARK 465 ASP D 238
REMARK 465 CYS D 239
REMARK 465 SER D 240
REMARK 465 SER D 241
REMARK 465 ARG D 242
REMARK 465 SER D 243
REMARK 465 LEU D 244
REMARK 465 SER D 245
REMARK 465 SER D 246
REMARK 465 SER D 247
REMARK 465 ALA D 248
REMARK 465 VAL D 249
REMARK 465 GLU D 250
REMARK 465 SER D 251
REMARK 465 GLU D 252
REMARK 465 ALA D 253
REMARK 465 THR D 254
REMARK 465 HIS D 255
REMARK 465 GLN D 256
REMARK 465 ARG D 257
REMARK 465 LYS D 258
REMARK 465 LEU D 259
REMARK 465 ARG D 260
REMARK 465 GLN D 261
REMARK 465 LYS D 262
REMARK 465 GLN D 263
REMARK 465 LEU D 264
REMARK 465 GLN D 265
REMARK 465 GLN D 266
REMARK 465 GLN D 267
REMARK 465 PHE D 268
REMARK 465 ARG D 269
REMARK 465 GLU D 270
REMARK 465 ARG D 271
REMARK 465 MET D 272
REMARK 465 GLU D 273
REMARK 465 LYS D 274
REMARK 465 GLN D 275
REMARK 465 GLN D 276
REMARK 465 VAL D 277
REMARK 465 ARG D 278
REMARK 465 VAL D 279
REMARK 465 SER D 280
REMARK 465 THR D 281
REMARK 465 PRO D 282
REMARK 465 SER D 283
REMARK 465 ALA D 284
REMARK 465 GLU D 285
REMARK 465 LYS D 286
REMARK 465 SER D 287
REMARK 465 GLU D 288
REMARK 465 ALA D 289
REMARK 465 ALA D 290
REMARK 465 PRO D 291
REMARK 465 PRO D 292
REMARK 465 ALA D 293
REMARK 465 PRO D 294
REMARK 465 PRO D 295
REMARK 465 VAL D 296
REMARK 465 THR D 297
REMARK 465 HIS D 298
REMARK 465 SER D 299
REMARK 465 THR D 300
REMARK 465 PRO D 301
REMARK 465 VAL D 302
REMARK 465 THR D 303
REMARK 465 VAL D 304
REMARK 465 SER D 305
REMARK 465 GLU D 306
REMARK 465 PRO D 307
REMARK 465 LEU D 308
REMARK 465 LEU D 309
REMARK 465 GLU D 310
REMARK 465 LYS D 311
REMARK 465 ASP D 312
REMARK 465 PHE D 313
REMARK 465 LEU D 314
REMARK 465 ALA D 315
REMARK 465 GLY D 316
REMARK 465 VAL D 317
REMARK 465 THR D 318
REMARK 465 GLN D 319
REMARK 465 GLU D 320
REMARK 465 LEU D 321
REMARK 465 ILE D 322
REMARK 465 LYS D 323
REMARK 465 THR D 324
REMARK 465 LEU D 325
REMARK 465 GLU D 326
REMARK 465 ASP D 327
REMARK 465 ASN D 328
REMARK 465 SER D 329
REMARK 465 GLU D 330
REMARK 465 LYS D 331
REMARK 465 TRP D 332
REMARK 465 ALA D 333
REMARK 465 VAL D 334
REMARK 465 THR D 335
REMARK 465 PRO D 336
REMARK 465 ASP D 337
REMARK 465 ALA D 338
REMARK 465 GLY D 339
REMARK 465 ASP D 340
REMARK 465 GLY D 341
REMARK 465 VAL D 342
REMARK 465 VAL D 343
REMARK 465 LYS D 344
REMARK 465 PRO D 345
REMARK 465 SER D 346
REMARK 465 SER D 347
REMARK 465 ARG D 348
REMARK 465 ALA D 349
REMARK 465 ASP D 350
REMARK 465 PRO D 351
REMARK 465 ALA D 352
REMARK 465 GLN D 353
REMARK 465 THR D 354
REMARK 465 SER D 355
REMARK 465 ASP D 356
REMARK 465 THR D 357
REMARK 465 LEU D 358
REMARK 465 ALA D 359
REMARK 465 LEU D 360
REMARK 465 ASN D 361
REMARK 465 ASN D 362
REMARK 465 GLN D 363
REMARK 465 MET D 364
REMARK 465 VAL D 365
REMARK 465 THR D 366
REMARK 465 GLN D 367
REMARK 465 ASN D 368
REMARK 465 ARG D 369
REMARK 465 THR D 370
REMARK 465 PRO D 371
REMARK 465 HIS D 372
REMARK 465 SER D 373
REMARK 465 VAL D 374
REMARK 465 CYS D 375
REMARK 465 HIS D 376
REMARK 465 GLN D 377
REMARK 465 LYS D 378
REMARK 465 PRO D 379
REMARK 465 GLN D 380
REMARK 465 ALA D 381
REMARK 465 LYS D 382
REMARK 465 SER D 383
REMARK 465 GLY D 384
REMARK 465 SER D 385
REMARK 465 TRP D 386
REMARK 465 ASP D 387
REMARK 465 LEU D 388
REMARK 465 GLN D 389
REMARK 465 THR D 390
REMARK 465 TYR D 391
REMARK 465 SER D 392
REMARK 465 ALA D 393
REMARK 465 ASP D 394
REMARK 465 GLN D 395
REMARK 465 ARG D 396
REMARK 465 THR D 397
REMARK 465 THR D 398
REMARK 465 GLY D 399
REMARK 465 ASN D 400
REMARK 465 TRP D 401
REMARK 465 GLU D 402
REMARK 465 SER D 403
REMARK 465 HIS D 404
REMARK 465 ARG D 405
REMARK 465 LYS D 406
REMARK 465 SER D 407
REMARK 465 GLN D 408
REMARK 465 ASP D 409
REMARK 465 MET D 410
REMARK 465 LYS D 411
REMARK 465 LYS D 412
REMARK 465 ARG D 413
REMARK 465 LYS D 414
REMARK 465 TYR D 415
REMARK 465 ASP D 416
REMARK 465 PRO D 417
REMARK 465 SER D 418
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 GLY E 3
REMARK 465 THR E 4
REMARK 465 GLU E 5
REMARK 465 GLU E 6
REMARK 465 ALA E 7
REMARK 465 ILE E 8
REMARK 465 LEU E 9
REMARK 465 GLY E 10
REMARK 465 GLY E 11
REMARK 465 ARG E 12
REMARK 465 ASP E 13
REMARK 465 SER E 14
REMARK 465 HIS E 15
REMARK 465 PRO E 16
REMARK 465 ALA E 17
REMARK 465 ALA E 18
REMARK 465 GLY E 19
REMARK 465 GLY E 20
REMARK 465 GLY E 21
REMARK 465 SER E 22
REMARK 465 VAL E 23
REMARK 465 LEU E 24
REMARK 465 GLY E 58
REMARK 465 GLY E 59
REMARK 465 GLY E 60
REMARK 465 ARG E 180
REMARK 465 GLN E 181
REMARK 465 LEU E 182
REMARK 465 PRO E 183
REMARK 465 LEU E 184
REMARK 465 GLU E 185
REMARK 465 TYR E 205
REMARK 465 ASN E 206
REMARK 465 SER E 207
REMARK 465 CYS E 208
REMARK 465 ARG E 209
REMARK 465 PRO E 210
REMARK 465 ASN E 211
REMARK 465 MET E 212
REMARK 465 ALA E 213
REMARK 465 LEU E 214
REMARK 465 GLY E 215
REMARK 465 HIS E 216
REMARK 465 PRO E 217
REMARK 465 GLN E 218
REMARK 465 LEU E 219
REMARK 465 GLN E 220
REMARK 465 GLN E 221
REMARK 465 VAL E 222
REMARK 465 THR E 223
REMARK 465 SER E 224
REMARK 465 PRO E 225
REMARK 465 SER E 226
REMARK 465 ARG E 227
REMARK 465 PRO E 228
REMARK 465 SER E 229
REMARK 465 HIS E 230
REMARK 465 ALA E 231
REMARK 465 VAL E 232
REMARK 465 ILE E 233
REMARK 465 PRO E 234
REMARK 465 ALA E 235
REMARK 465 ASP E 236
REMARK 465 GLN E 237
REMARK 465 ASP E 238
REMARK 465 CYS E 239
REMARK 465 SER E 240
REMARK 465 SER E 241
REMARK 465 ARG E 242
REMARK 465 SER E 243
REMARK 465 LEU E 244
REMARK 465 SER E 245
REMARK 465 SER E 246
REMARK 465 SER E 247
REMARK 465 ALA E 248
REMARK 465 VAL E 249
REMARK 465 GLU E 250
REMARK 465 SER E 251
REMARK 465 GLU E 252
REMARK 465 ALA E 253
REMARK 465 THR E 254
REMARK 465 HIS E 255
REMARK 465 GLN E 256
REMARK 465 ARG E 257
REMARK 465 LYS E 258
REMARK 465 LEU E 259
REMARK 465 ARG E 260
REMARK 465 GLN E 261
REMARK 465 LYS E 262
REMARK 465 GLN E 263
REMARK 465 LEU E 264
REMARK 465 GLN E 265
REMARK 465 GLN E 266
REMARK 465 GLN E 267
REMARK 465 PHE E 268
REMARK 465 ARG E 269
REMARK 465 GLU E 270
REMARK 465 ARG E 271
REMARK 465 MET E 272
REMARK 465 GLU E 273
REMARK 465 LYS E 274
REMARK 465 GLN E 275
REMARK 465 GLN E 276
REMARK 465 VAL E 277
REMARK 465 ARG E 278
REMARK 465 VAL E 279
REMARK 465 SER E 280
REMARK 465 THR E 281
REMARK 465 PRO E 282
REMARK 465 SER E 283
REMARK 465 ALA E 284
REMARK 465 GLU E 285
REMARK 465 LYS E 286
REMARK 465 SER E 287
REMARK 465 GLU E 288
REMARK 465 ALA E 289
REMARK 465 ALA E 290
REMARK 465 PRO E 291
REMARK 465 PRO E 292
REMARK 465 ALA E 293
REMARK 465 PRO E 294
REMARK 465 PRO E 295
REMARK 465 VAL E 296
REMARK 465 THR E 297
REMARK 465 HIS E 298
REMARK 465 SER E 299
REMARK 465 THR E 300
REMARK 465 PRO E 301
REMARK 465 VAL E 302
REMARK 465 THR E 303
REMARK 465 VAL E 304
REMARK 465 SER E 305
REMARK 465 GLU E 306
REMARK 465 PRO E 307
REMARK 465 LEU E 308
REMARK 465 LEU E 309
REMARK 465 GLU E 310
REMARK 465 LYS E 311
REMARK 465 ASP E 312
REMARK 465 PHE E 313
REMARK 465 LEU E 314
REMARK 465 ALA E 315
REMARK 465 GLY E 316
REMARK 465 VAL E 317
REMARK 465 THR E 318
REMARK 465 GLN E 319
REMARK 465 GLU E 320
REMARK 465 LEU E 321
REMARK 465 ILE E 322
REMARK 465 LYS E 323
REMARK 465 THR E 324
REMARK 465 LEU E 325
REMARK 465 GLU E 326
REMARK 465 ASP E 327
REMARK 465 ASN E 328
REMARK 465 SER E 329
REMARK 465 GLU E 330
REMARK 465 LYS E 331
REMARK 465 TRP E 332
REMARK 465 ALA E 333
REMARK 465 VAL E 334
REMARK 465 THR E 335
REMARK 465 PRO E 336
REMARK 465 ASP E 337
REMARK 465 ALA E 338
REMARK 465 GLY E 339
REMARK 465 ASP E 340
REMARK 465 GLY E 341
REMARK 465 VAL E 342
REMARK 465 VAL E 343
REMARK 465 LYS E 344
REMARK 465 PRO E 345
REMARK 465 SER E 346
REMARK 465 SER E 347
REMARK 465 ARG E 348
REMARK 465 ALA E 349
REMARK 465 ASP E 350
REMARK 465 PRO E 351
REMARK 465 ALA E 352
REMARK 465 GLN E 353
REMARK 465 THR E 354
REMARK 465 SER E 355
REMARK 465 ASP E 356
REMARK 465 THR E 357
REMARK 465 LEU E 358
REMARK 465 ALA E 359
REMARK 465 LEU E 360
REMARK 465 ASN E 361
REMARK 465 ASN E 362
REMARK 465 GLN E 363
REMARK 465 MET E 364
REMARK 465 VAL E 365
REMARK 465 THR E 366
REMARK 465 GLN E 367
REMARK 465 ASN E 368
REMARK 465 ARG E 369
REMARK 465 THR E 370
REMARK 465 PRO E 371
REMARK 465 HIS E 372
REMARK 465 SER E 373
REMARK 465 VAL E 374
REMARK 465 CYS E 375
REMARK 465 HIS E 376
REMARK 465 GLN E 377
REMARK 465 LYS E 378
REMARK 465 PRO E 379
REMARK 465 GLN E 380
REMARK 465 ALA E 381
REMARK 465 LYS E 382
REMARK 465 SER E 383
REMARK 465 GLY E 384
REMARK 465 SER E 385
REMARK 465 TRP E 386
REMARK 465 ASP E 387
REMARK 465 LEU E 388
REMARK 465 GLN E 389
REMARK 465 THR E 390
REMARK 465 TYR E 391
REMARK 465 SER E 392
REMARK 465 ALA E 393
REMARK 465 ASP E 394
REMARK 465 GLN E 395
REMARK 465 ARG E 396
REMARK 465 THR E 397
REMARK 465 THR E 398
REMARK 465 GLY E 399
REMARK 465 ASN E 400
REMARK 465 TRP E 401
REMARK 465 GLU E 402
REMARK 465 SER E 403
REMARK 465 HIS E 404
REMARK 465 ARG E 405
REMARK 465 LYS E 406
REMARK 465 SER E 407
REMARK 465 GLN E 408
REMARK 465 ASP E 409
REMARK 465 MET E 410
REMARK 465 LYS E 411
REMARK 465 LYS E 412
REMARK 465 ARG E 413
REMARK 465 LYS E 414
REMARK 465 TYR E 415
REMARK 465 ASP E 416
REMARK 465 PRO E 417
REMARK 465 SER E 418
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 GLY F 3
REMARK 465 THR F 4
REMARK 465 GLU F 5
REMARK 465 GLU F 6
REMARK 465 ALA F 7
REMARK 465 ILE F 8
REMARK 465 LEU F 9
REMARK 465 GLY F 10
REMARK 465 GLY F 11
REMARK 465 ARG F 12
REMARK 465 ASP F 13
REMARK 465 SER F 14
REMARK 465 HIS F 15
REMARK 465 PRO F 16
REMARK 465 ALA F 17
REMARK 465 ALA F 18
REMARK 465 GLY F 19
REMARK 465 GLY F 20
REMARK 465 GLY F 21
REMARK 465 SER F 22
REMARK 465 VAL F 23
REMARK 465 LEU F 24
REMARK 465 CYS F 25
REMARK 465 GLY F 58
REMARK 465 GLY F 59
REMARK 465 GLY F 60
REMARK 465 LYS F 177
REMARK 465 LEU F 178
REMARK 465 PRO F 179
REMARK 465 ARG F 180
REMARK 465 GLN F 181
REMARK 465 LEU F 182
REMARK 465 PRO F 183
REMARK 465 LEU F 184
REMARK 465 GLU F 185
REMARK 465 TYR F 205
REMARK 465 ASN F 206
REMARK 465 SER F 207
REMARK 465 CYS F 208
REMARK 465 ARG F 209
REMARK 465 PRO F 210
REMARK 465 ASN F 211
REMARK 465 MET F 212
REMARK 465 ALA F 213
REMARK 465 LEU F 214
REMARK 465 GLY F 215
REMARK 465 HIS F 216
REMARK 465 PRO F 217
REMARK 465 GLN F 218
REMARK 465 LEU F 219
REMARK 465 GLN F 220
REMARK 465 GLN F 221
REMARK 465 VAL F 222
REMARK 465 THR F 223
REMARK 465 SER F 224
REMARK 465 PRO F 225
REMARK 465 SER F 226
REMARK 465 ARG F 227
REMARK 465 PRO F 228
REMARK 465 SER F 229
REMARK 465 HIS F 230
REMARK 465 ALA F 231
REMARK 465 VAL F 232
REMARK 465 ILE F 233
REMARK 465 PRO F 234
REMARK 465 ALA F 235
REMARK 465 ASP F 236
REMARK 465 GLN F 237
REMARK 465 ASP F 238
REMARK 465 CYS F 239
REMARK 465 SER F 240
REMARK 465 SER F 241
REMARK 465 ARG F 242
REMARK 465 SER F 243
REMARK 465 LEU F 244
REMARK 465 SER F 245
REMARK 465 SER F 246
REMARK 465 SER F 247
REMARK 465 ALA F 248
REMARK 465 VAL F 249
REMARK 465 GLU F 250
REMARK 465 SER F 251
REMARK 465 GLU F 252
REMARK 465 ALA F 253
REMARK 465 THR F 254
REMARK 465 HIS F 255
REMARK 465 GLN F 256
REMARK 465 ARG F 257
REMARK 465 LYS F 258
REMARK 465 LEU F 259
REMARK 465 ARG F 260
REMARK 465 GLN F 261
REMARK 465 LYS F 262
REMARK 465 GLN F 263
REMARK 465 LEU F 264
REMARK 465 GLN F 265
REMARK 465 GLN F 266
REMARK 465 GLN F 267
REMARK 465 PHE F 268
REMARK 465 ARG F 269
REMARK 465 GLU F 270
REMARK 465 ARG F 271
REMARK 465 MET F 272
REMARK 465 GLU F 273
REMARK 465 LYS F 274
REMARK 465 GLN F 275
REMARK 465 GLN F 276
REMARK 465 VAL F 277
REMARK 465 ARG F 278
REMARK 465 VAL F 279
REMARK 465 SER F 280
REMARK 465 THR F 281
REMARK 465 PRO F 282
REMARK 465 SER F 283
REMARK 465 ALA F 284
REMARK 465 GLU F 285
REMARK 465 LYS F 286
REMARK 465 SER F 287
REMARK 465 GLU F 288
REMARK 465 ALA F 289
REMARK 465 ALA F 290
REMARK 465 PRO F 291
REMARK 465 PRO F 292
REMARK 465 ALA F 293
REMARK 465 PRO F 294
REMARK 465 PRO F 295
REMARK 465 VAL F 296
REMARK 465 THR F 297
REMARK 465 HIS F 298
REMARK 465 SER F 299
REMARK 465 THR F 300
REMARK 465 PRO F 301
REMARK 465 VAL F 302
REMARK 465 THR F 303
REMARK 465 VAL F 304
REMARK 465 SER F 305
REMARK 465 GLU F 306
REMARK 465 PRO F 307
REMARK 465 LEU F 308
REMARK 465 LEU F 309
REMARK 465 GLU F 310
REMARK 465 LYS F 311
REMARK 465 ASP F 312
REMARK 465 PHE F 313
REMARK 465 LEU F 314
REMARK 465 ALA F 315
REMARK 465 GLY F 316
REMARK 465 VAL F 317
REMARK 465 THR F 318
REMARK 465 GLN F 319
REMARK 465 GLU F 320
REMARK 465 LEU F 321
REMARK 465 ILE F 322
REMARK 465 LYS F 323
REMARK 465 THR F 324
REMARK 465 LEU F 325
REMARK 465 GLU F 326
REMARK 465 ASP F 327
REMARK 465 ASN F 328
REMARK 465 SER F 329
REMARK 465 GLU F 330
REMARK 465 LYS F 331
REMARK 465 TRP F 332
REMARK 465 ALA F 333
REMARK 465 VAL F 334
REMARK 465 THR F 335
REMARK 465 PRO F 336
REMARK 465 ASP F 337
REMARK 465 ALA F 338
REMARK 465 GLY F 339
REMARK 465 ASP F 340
REMARK 465 GLY F 341
REMARK 465 VAL F 342
REMARK 465 VAL F 343
REMARK 465 LYS F 344
REMARK 465 PRO F 345
REMARK 465 SER F 346
REMARK 465 SER F 347
REMARK 465 ARG F 348
REMARK 465 ALA F 349
REMARK 465 ASP F 350
REMARK 465 PRO F 351
REMARK 465 ALA F 352
REMARK 465 GLN F 353
REMARK 465 THR F 354
REMARK 465 SER F 355
REMARK 465 ASP F 356
REMARK 465 THR F 357
REMARK 465 LEU F 358
REMARK 465 ALA F 359
REMARK 465 LEU F 360
REMARK 465 ASN F 361
REMARK 465 ASN F 362
REMARK 465 GLN F 363
REMARK 465 MET F 364
REMARK 465 VAL F 365
REMARK 465 THR F 366
REMARK 465 GLN F 367
REMARK 465 ASN F 368
REMARK 465 ARG F 369
REMARK 465 THR F 370
REMARK 465 PRO F 371
REMARK 465 HIS F 372
REMARK 465 SER F 373
REMARK 465 VAL F 374
REMARK 465 CYS F 375
REMARK 465 HIS F 376
REMARK 465 GLN F 377
REMARK 465 LYS F 378
REMARK 465 PRO F 379
REMARK 465 GLN F 380
REMARK 465 ALA F 381
REMARK 465 LYS F 382
REMARK 465 SER F 383
REMARK 465 GLY F 384
REMARK 465 SER F 385
REMARK 465 TRP F 386
REMARK 465 ASP F 387
REMARK 465 LEU F 388
REMARK 465 GLN F 389
REMARK 465 THR F 390
REMARK 465 TYR F 391
REMARK 465 SER F 392
REMARK 465 ALA F 393
REMARK 465 ASP F 394
REMARK 465 GLN F 395
REMARK 465 ARG F 396
REMARK 465 THR F 397
REMARK 465 THR F 398
REMARK 465 GLY F 399
REMARK 465 ASN F 400
REMARK 465 TRP F 401
REMARK 465 GLU F 402
REMARK 465 SER F 403
REMARK 465 HIS F 404
REMARK 465 ARG F 405
REMARK 465 LYS F 406
REMARK 465 SER F 407
REMARK 465 GLN F 408
REMARK 465 ASP F 409
REMARK 465 MET F 410
REMARK 465 LYS F 411
REMARK 465 LYS F 412
REMARK 465 ARG F 413
REMARK 465 LYS F 414
REMARK 465 TYR F 415
REMARK 465 ASP F 416
REMARK 465 PRO F 417
REMARK 465 SER F 418
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 GLY G 3
REMARK 465 THR G 4
REMARK 465 GLU G 5
REMARK 465 GLU G 6
REMARK 465 ALA G 7
REMARK 465 ILE G 8
REMARK 465 LEU G 9
REMARK 465 GLY G 10
REMARK 465 GLY G 11
REMARK 465 ARG G 12
REMARK 465 ASP G 13
REMARK 465 SER G 14
REMARK 465 HIS G 15
REMARK 465 PRO G 16
REMARK 465 ALA G 17
REMARK 465 ALA G 18
REMARK 465 GLY G 19
REMARK 465 GLY G 20
REMARK 465 GLY G 21
REMARK 465 SER G 22
REMARK 465 VAL G 23
REMARK 465 LEU G 24
REMARK 465 CYS G 25
REMARK 465 ARG G 55
REMARK 465 MET G 56
REMARK 465 ALA G 57
REMARK 465 GLY G 58
REMARK 465 GLY G 59
REMARK 465 GLY G 60
REMARK 465 GLN G 61
REMARK 465 ASP G 168
REMARK 465 LYS G 169
REMARK 465 ASP G 170
REMARK 465 TYR G 171
REMARK 465 LEU G 172
REMARK 465 ARG G 173
REMARK 465 SER G 174
REMARK 465 LEU G 175
REMARK 465 ASN G 176
REMARK 465 LYS G 177
REMARK 465 LEU G 178
REMARK 465 PRO G 179
REMARK 465 ARG G 180
REMARK 465 GLN G 181
REMARK 465 LEU G 182
REMARK 465 PRO G 183
REMARK 465 LEU G 184
REMARK 465 GLU G 185
REMARK 465 VAL G 186
REMARK 465 ASP G 187
REMARK 465 LEU G 188
REMARK 465 THR G 189
REMARK 465 LYS G 190
REMARK 465 ALA G 191
REMARK 465 LYS G 192
REMARK 465 ARG G 193
REMARK 465 GLN G 194
REMARK 465 ASP G 195
REMARK 465 LEU G 196
REMARK 465 GLU G 197
REMARK 465 PRO G 198
REMARK 465 SER G 199
REMARK 465 VAL G 200
REMARK 465 GLU G 201
REMARK 465 GLU G 202
REMARK 465 ALA G 203
REMARK 465 ARG G 204
REMARK 465 TYR G 205
REMARK 465 ASN G 206
REMARK 465 SER G 207
REMARK 465 CYS G 208
REMARK 465 ARG G 209
REMARK 465 PRO G 210
REMARK 465 ASN G 211
REMARK 465 MET G 212
REMARK 465 ALA G 213
REMARK 465 LEU G 214
REMARK 465 GLY G 215
REMARK 465 HIS G 216
REMARK 465 PRO G 217
REMARK 465 GLN G 218
REMARK 465 LEU G 219
REMARK 465 GLN G 220
REMARK 465 GLN G 221
REMARK 465 VAL G 222
REMARK 465 THR G 223
REMARK 465 SER G 224
REMARK 465 PRO G 225
REMARK 465 SER G 226
REMARK 465 ARG G 227
REMARK 465 PRO G 228
REMARK 465 SER G 229
REMARK 465 HIS G 230
REMARK 465 ALA G 231
REMARK 465 VAL G 232
REMARK 465 ILE G 233
REMARK 465 PRO G 234
REMARK 465 ALA G 235
REMARK 465 ASP G 236
REMARK 465 GLN G 237
REMARK 465 ASP G 238
REMARK 465 CYS G 239
REMARK 465 SER G 240
REMARK 465 SER G 241
REMARK 465 ARG G 242
REMARK 465 SER G 243
REMARK 465 LEU G 244
REMARK 465 SER G 245
REMARK 465 SER G 246
REMARK 465 SER G 247
REMARK 465 ALA G 248
REMARK 465 VAL G 249
REMARK 465 GLU G 250
REMARK 465 SER G 251
REMARK 465 GLU G 252
REMARK 465 ALA G 253
REMARK 465 THR G 254
REMARK 465 HIS G 255
REMARK 465 GLN G 256
REMARK 465 ARG G 257
REMARK 465 LYS G 258
REMARK 465 LEU G 259
REMARK 465 ARG G 260
REMARK 465 GLN G 261
REMARK 465 LYS G 262
REMARK 465 GLN G 263
REMARK 465 LEU G 264
REMARK 465 GLN G 265
REMARK 465 GLN G 266
REMARK 465 GLN G 267
REMARK 465 PHE G 268
REMARK 465 ARG G 269
REMARK 465 GLU G 270
REMARK 465 ARG G 271
REMARK 465 MET G 272
REMARK 465 GLU G 273
REMARK 465 LYS G 274
REMARK 465 GLN G 275
REMARK 465 GLN G 276
REMARK 465 VAL G 277
REMARK 465 ARG G 278
REMARK 465 VAL G 279
REMARK 465 SER G 280
REMARK 465 THR G 281
REMARK 465 PRO G 282
REMARK 465 SER G 283
REMARK 465 ALA G 284
REMARK 465 GLU G 285
REMARK 465 LYS G 286
REMARK 465 SER G 287
REMARK 465 GLU G 288
REMARK 465 ALA G 289
REMARK 465 ALA G 290
REMARK 465 PRO G 291
REMARK 465 PRO G 292
REMARK 465 ALA G 293
REMARK 465 PRO G 294
REMARK 465 PRO G 295
REMARK 465 VAL G 296
REMARK 465 THR G 297
REMARK 465 HIS G 298
REMARK 465 SER G 299
REMARK 465 THR G 300
REMARK 465 PRO G 301
REMARK 465 VAL G 302
REMARK 465 THR G 303
REMARK 465 VAL G 304
REMARK 465 SER G 305
REMARK 465 GLU G 306
REMARK 465 PRO G 307
REMARK 465 LEU G 308
REMARK 465 LEU G 309
REMARK 465 GLU G 310
REMARK 465 LYS G 311
REMARK 465 ASP G 312
REMARK 465 PHE G 313
REMARK 465 LEU G 314
REMARK 465 ALA G 315
REMARK 465 GLY G 316
REMARK 465 VAL G 317
REMARK 465 THR G 318
REMARK 465 GLN G 319
REMARK 465 GLU G 320
REMARK 465 LEU G 321
REMARK 465 ILE G 322
REMARK 465 LYS G 323
REMARK 465 THR G 324
REMARK 465 LEU G 325
REMARK 465 GLU G 326
REMARK 465 ASP G 327
REMARK 465 ASN G 328
REMARK 465 SER G 329
REMARK 465 GLU G 330
REMARK 465 LYS G 331
REMARK 465 TRP G 332
REMARK 465 ALA G 333
REMARK 465 VAL G 334
REMARK 465 THR G 335
REMARK 465 PRO G 336
REMARK 465 ASP G 337
REMARK 465 ALA G 338
REMARK 465 GLY G 339
REMARK 465 ASP G 340
REMARK 465 GLY G 341
REMARK 465 VAL G 342
REMARK 465 VAL G 343
REMARK 465 LYS G 344
REMARK 465 PRO G 345
REMARK 465 SER G 346
REMARK 465 SER G 347
REMARK 465 ARG G 348
REMARK 465 ALA G 349
REMARK 465 ASP G 350
REMARK 465 PRO G 351
REMARK 465 ALA G 352
REMARK 465 GLN G 353
REMARK 465 THR G 354
REMARK 465 SER G 355
REMARK 465 ASP G 356
REMARK 465 THR G 357
REMARK 465 LEU G 358
REMARK 465 ALA G 359
REMARK 465 LEU G 360
REMARK 465 ASN G 361
REMARK 465 ASN G 362
REMARK 465 GLN G 363
REMARK 465 MET G 364
REMARK 465 VAL G 365
REMARK 465 THR G 366
REMARK 465 GLN G 367
REMARK 465 ASN G 368
REMARK 465 ARG G 369
REMARK 465 THR G 370
REMARK 465 PRO G 371
REMARK 465 HIS G 372
REMARK 465 SER G 373
REMARK 465 VAL G 374
REMARK 465 CYS G 375
REMARK 465 HIS G 376
REMARK 465 GLN G 377
REMARK 465 LYS G 378
REMARK 465 PRO G 379
REMARK 465 GLN G 380
REMARK 465 ALA G 381
REMARK 465 LYS G 382
REMARK 465 SER G 383
REMARK 465 GLY G 384
REMARK 465 SER G 385
REMARK 465 TRP G 386
REMARK 465 ASP G 387
REMARK 465 LEU G 388
REMARK 465 GLN G 389
REMARK 465 THR G 390
REMARK 465 TYR G 391
REMARK 465 SER G 392
REMARK 465 ALA G 393
REMARK 465 ASP G 394
REMARK 465 GLN G 395
REMARK 465 ARG G 396
REMARK 465 THR G 397
REMARK 465 THR G 398
REMARK 465 GLY G 399
REMARK 465 ASN G 400
REMARK 465 TRP G 401
REMARK 465 GLU G 402
REMARK 465 SER G 403
REMARK 465 HIS G 404
REMARK 465 ARG G 405
REMARK 465 LYS G 406
REMARK 465 SER G 407
REMARK 465 GLN G 408
REMARK 465 ASP G 409
REMARK 465 MET G 410
REMARK 465 LYS G 411
REMARK 465 LYS G 412
REMARK 465 ARG G 413
REMARK 465 LYS G 414
REMARK 465 TYR G 415
REMARK 465 ASP G 416
REMARK 465 PRO G 417
REMARK 465 SER G 418
REMARK 465 MET H 1
REMARK 465 SER H 2
REMARK 465 GLY H 3
REMARK 465 THR H 4
REMARK 465 GLU H 5
REMARK 465 GLU H 6
REMARK 465 ALA H 7
REMARK 465 ILE H 8
REMARK 465 LEU H 9
REMARK 465 GLY H 10
REMARK 465 GLY H 11
REMARK 465 ARG H 12
REMARK 465 ASP H 13
REMARK 465 SER H 14
REMARK 465 HIS H 15
REMARK 465 PRO H 16
REMARK 465 ALA H 17
REMARK 465 ALA H 18
REMARK 465 GLY H 19
REMARK 465 GLY H 20
REMARK 465 GLY H 21
REMARK 465 SER H 22
REMARK 465 VAL H 23
REMARK 465 LEU H 24
REMARK 465 CYS H 25
REMARK 465 PHE H 26
REMARK 465 GLY H 27
REMARK 465 GLN H 28
REMARK 465 CYS H 29
REMARK 465 GLN H 30
REMARK 465 TYR H 31
REMARK 465 THR H 32
REMARK 465 ALA H 33
REMARK 465 GLU H 34
REMARK 465 GLU H 35
REMARK 465 PRO H 49
REMARK 465 GLU H 50
REMARK 465 TYR H 51
REMARK 465 ILE H 52
REMARK 465 SER H 53
REMARK 465 SER H 54
REMARK 465 ARG H 55
REMARK 465 MET H 56
REMARK 465 ALA H 57
REMARK 465 GLY H 58
REMARK 465 GLY H 59
REMARK 465 GLY H 60
REMARK 465 GLN H 61
REMARK 465 LYS H 62
REMARK 465 VAL H 63
REMARK 465 CYS H 64
REMARK 465 GLY H 163
REMARK 465 ASN H 164
REMARK 465 CYS H 165
REMARK 465 ILE H 166
REMARK 465 LEU H 167
REMARK 465 ASP H 168
REMARK 465 LYS H 169
REMARK 465 ASP H 170
REMARK 465 TYR H 171
REMARK 465 LEU H 172
REMARK 465 ARG H 173
REMARK 465 SER H 174
REMARK 465 LEU H 175
REMARK 465 ASN H 176
REMARK 465 LYS H 177
REMARK 465 LEU H 178
REMARK 465 PRO H 179
REMARK 465 ARG H 180
REMARK 465 GLN H 181
REMARK 465 LEU H 182
REMARK 465 PRO H 183
REMARK 465 LEU H 184
REMARK 465 GLU H 185
REMARK 465 VAL H 186
REMARK 465 ASP H 187
REMARK 465 LEU H 188
REMARK 465 THR H 189
REMARK 465 LYS H 190
REMARK 465 ALA H 191
REMARK 465 LYS H 192
REMARK 465 ARG H 193
REMARK 465 GLN H 194
REMARK 465 ASP H 195
REMARK 465 LEU H 196
REMARK 465 GLU H 197
REMARK 465 PRO H 198
REMARK 465 SER H 199
REMARK 465 VAL H 200
REMARK 465 GLU H 201
REMARK 465 GLU H 202
REMARK 465 ALA H 203
REMARK 465 ARG H 204
REMARK 465 TYR H 205
REMARK 465 ASN H 206
REMARK 465 SER H 207
REMARK 465 CYS H 208
REMARK 465 ARG H 209
REMARK 465 PRO H 210
REMARK 465 ASN H 211
REMARK 465 MET H 212
REMARK 465 ALA H 213
REMARK 465 LEU H 214
REMARK 465 GLY H 215
REMARK 465 HIS H 216
REMARK 465 PRO H 217
REMARK 465 GLN H 218
REMARK 465 LEU H 219
REMARK 465 GLN H 220
REMARK 465 GLN H 221
REMARK 465 VAL H 222
REMARK 465 THR H 223
REMARK 465 SER H 224
REMARK 465 PRO H 225
REMARK 465 SER H 226
REMARK 465 ARG H 227
REMARK 465 PRO H 228
REMARK 465 SER H 229
REMARK 465 HIS H 230
REMARK 465 ALA H 231
REMARK 465 VAL H 232
REMARK 465 ILE H 233
REMARK 465 PRO H 234
REMARK 465 ALA H 235
REMARK 465 ASP H 236
REMARK 465 GLN H 237
REMARK 465 ASP H 238
REMARK 465 CYS H 239
REMARK 465 SER H 240
REMARK 465 SER H 241
REMARK 465 ARG H 242
REMARK 465 SER H 243
REMARK 465 LEU H 244
REMARK 465 SER H 245
REMARK 465 SER H 246
REMARK 465 SER H 247
REMARK 465 ALA H 248
REMARK 465 VAL H 249
REMARK 465 GLU H 250
REMARK 465 SER H 251
REMARK 465 GLU H 252
REMARK 465 ALA H 253
REMARK 465 THR H 254
REMARK 465 HIS H 255
REMARK 465 GLN H 256
REMARK 465 ARG H 257
REMARK 465 LYS H 258
REMARK 465 LEU H 259
REMARK 465 ARG H 260
REMARK 465 GLN H 261
REMARK 465 LYS H 262
REMARK 465 GLN H 263
REMARK 465 LEU H 264
REMARK 465 GLN H 265
REMARK 465 GLN H 266
REMARK 465 GLN H 267
REMARK 465 PHE H 268
REMARK 465 ARG H 269
REMARK 465 GLU H 270
REMARK 465 ARG H 271
REMARK 465 MET H 272
REMARK 465 GLU H 273
REMARK 465 LYS H 274
REMARK 465 GLN H 275
REMARK 465 GLN H 276
REMARK 465 VAL H 277
REMARK 465 ARG H 278
REMARK 465 VAL H 279
REMARK 465 SER H 280
REMARK 465 THR H 281
REMARK 465 PRO H 282
REMARK 465 SER H 283
REMARK 465 ALA H 284
REMARK 465 GLU H 285
REMARK 465 LYS H 286
REMARK 465 SER H 287
REMARK 465 GLU H 288
REMARK 465 ALA H 289
REMARK 465 ALA H 290
REMARK 465 PRO H 291
REMARK 465 PRO H 292
REMARK 465 ALA H 293
REMARK 465 PRO H 294
REMARK 465 PRO H 295
REMARK 465 VAL H 296
REMARK 465 THR H 297
REMARK 465 HIS H 298
REMARK 465 SER H 299
REMARK 465 THR H 300
REMARK 465 PRO H 301
REMARK 465 VAL H 302
REMARK 465 THR H 303
REMARK 465 VAL H 304
REMARK 465 SER H 305
REMARK 465 GLU H 306
REMARK 465 PRO H 307
REMARK 465 LEU H 308
REMARK 465 LEU H 309
REMARK 465 GLU H 310
REMARK 465 LYS H 311
REMARK 465 ASP H 312
REMARK 465 PHE H 313
REMARK 465 LEU H 314
REMARK 465 ALA H 315
REMARK 465 GLY H 316
REMARK 465 VAL H 317
REMARK 465 THR H 318
REMARK 465 GLN H 319
REMARK 465 GLU H 320
REMARK 465 LEU H 321
REMARK 465 ILE H 322
REMARK 465 LYS H 323
REMARK 465 THR H 324
REMARK 465 LEU H 325
REMARK 465 GLU H 326
REMARK 465 ASP H 327
REMARK 465 ASN H 328
REMARK 465 SER H 329
REMARK 465 GLU H 330
REMARK 465 LYS H 331
REMARK 465 TRP H 332
REMARK 465 ALA H 333
REMARK 465 VAL H 334
REMARK 465 THR H 335
REMARK 465 PRO H 336
REMARK 465 ASP H 337
REMARK 465 ALA H 338
REMARK 465 GLY H 339
REMARK 465 ASP H 340
REMARK 465 GLY H 341
REMARK 465 VAL H 342
REMARK 465 VAL H 343
REMARK 465 LYS H 344
REMARK 465 PRO H 345
REMARK 465 SER H 346
REMARK 465 SER H 347
REMARK 465 ARG H 348
REMARK 465 ALA H 349
REMARK 465 ASP H 350
REMARK 465 PRO H 351
REMARK 465 ALA H 352
REMARK 465 GLN H 353
REMARK 465 THR H 354
REMARK 465 SER H 355
REMARK 465 ASP H 356
REMARK 465 THR H 357
REMARK 465 LEU H 358
REMARK 465 ALA H 359
REMARK 465 LEU H 360
REMARK 465 ASN H 361
REMARK 465 ASN H 362
REMARK 465 GLN H 363
REMARK 465 MET H 364
REMARK 465 VAL H 365
REMARK 465 THR H 366
REMARK 465 GLN H 367
REMARK 465 ASN H 368
REMARK 465 ARG H 369
REMARK 465 THR H 370
REMARK 465 PRO H 371
REMARK 465 HIS H 372
REMARK 465 SER H 373
REMARK 465 VAL H 374
REMARK 465 CYS H 375
REMARK 465 HIS H 376
REMARK 465 GLN H 377
REMARK 465 LYS H 378
REMARK 465 PRO H 379
REMARK 465 GLN H 380
REMARK 465 ALA H 381
REMARK 465 LYS H 382
REMARK 465 SER H 383
REMARK 465 GLY H 384
REMARK 465 SER H 385
REMARK 465 TRP H 386
REMARK 465 ASP H 387
REMARK 465 LEU H 388
REMARK 465 GLN H 389
REMARK 465 THR H 390
REMARK 465 TYR H 391
REMARK 465 SER H 392
REMARK 465 ALA H 393
REMARK 465 ASP H 394
REMARK 465 GLN H 395
REMARK 465 ARG H 396
REMARK 465 THR H 397
REMARK 465 THR H 398
REMARK 465 GLY H 399
REMARK 465 ASN H 400
REMARK 465 TRP H 401
REMARK 465 GLU H 402
REMARK 465 SER H 403
REMARK 465 HIS H 404
REMARK 465 ARG H 405
REMARK 465 LYS H 406
REMARK 465 SER H 407
REMARK 465 GLN H 408
REMARK 465 ASP H 409
REMARK 465 MET H 410
REMARK 465 LYS H 411
REMARK 465 LYS H 412
REMARK 465 ARG H 413
REMARK 465 LYS H 414
REMARK 465 TYR H 415
REMARK 465 ASP H 416
REMARK 465 PRO H 417
REMARK 465 SER H 418
REMARK 465 MET I 1
REMARK 465 SER I 2
REMARK 465 GLY I 3
REMARK 465 THR I 4
REMARK 465 GLU I 5
REMARK 465 GLU I 6
REMARK 465 ALA I 7
REMARK 465 ILE I 8
REMARK 465 LEU I 9
REMARK 465 GLY I 10
REMARK 465 GLY I 11
REMARK 465 ARG I 12
REMARK 465 ASP I 13
REMARK 465 SER I 14
REMARK 465 HIS I 15
REMARK 465 PRO I 16
REMARK 465 ALA I 17
REMARK 465 ALA I 18
REMARK 465 GLY I 19
REMARK 465 GLY I 20
REMARK 465 GLY I 21
REMARK 465 SER I 22
REMARK 465 VAL I 23
REMARK 465 LEU I 24
REMARK 465 CYS I 25
REMARK 465 PHE I 26
REMARK 465 GLY I 27
REMARK 465 GLN I 28
REMARK 465 CYS I 29
REMARK 465 GLN I 30
REMARK 465 TYR I 31
REMARK 465 THR I 32
REMARK 465 ALA I 33
REMARK 465 GLU I 34
REMARK 465 GLU I 35
REMARK 465 TYR I 36
REMARK 465 GLN I 37
REMARK 465 ALA I 38
REMARK 465 ILE I 39
REMARK 465 GLN I 40
REMARK 465 LYS I 41
REMARK 465 ALA I 42
REMARK 465 LEU I 43
REMARK 465 ARG I 44
REMARK 465 GLN I 45
REMARK 465 ARG I 46
REMARK 465 LEU I 47
REMARK 465 GLY I 48
REMARK 465 PRO I 49
REMARK 465 GLU I 50
REMARK 465 TYR I 51
REMARK 465 ILE I 52
REMARK 465 SER I 53
REMARK 465 SER I 54
REMARK 465 ARG I 55
REMARK 465 MET I 56
REMARK 465 ALA I 57
REMARK 465 GLY I 58
REMARK 465 GLY I 59
REMARK 465 GLY I 60
REMARK 465 GLN I 61
REMARK 465 LYS I 62
REMARK 465 VAL I 63
REMARK 465 CYS I 64
REMARK 465 TYR I 65
REMARK 465 ILE I 66
REMARK 465 GLU I 77
REMARK 465 MET I 78
REMARK 465 PHE I 79
REMARK 465 GLY I 80
REMARK 465 TYR I 81
REMARK 465 ASN I 82
REMARK 465 GLY I 83
REMARK 465 THR I 89
REMARK 465 GLN I 90
REMARK 465 GLN I 91
REMARK 465 ASN I 92
REMARK 465 VAL I 93
REMARK 465 ASP I 94
REMARK 465 ASN I 99
REMARK 465 GLN I 114
REMARK 465 LEU I 115
REMARK 465 LYS I 116
REMARK 465 ASP I 117
REMARK 465 GLY I 118
REMARK 465 SER I 119
REMARK 465 GLY I 131
REMARK 465 LEU I 132
REMARK 465 LYS I 133
REMARK 465 ARG I 156
REMARK 465 SER I 157
REMARK 465 PHE I 158
REMARK 465 GLY I 159
REMARK 465 ASN I 160
REMARK 465 ALA I 161
REMARK 465 LEU I 162
REMARK 465 GLY I 163
REMARK 465 ASN I 164
REMARK 465 CYS I 165
REMARK 465 ILE I 166
REMARK 465 LEU I 167
REMARK 465 ASP I 168
REMARK 465 LYS I 169
REMARK 465 ASP I 170
REMARK 465 TYR I 171
REMARK 465 LEU I 172
REMARK 465 ARG I 173
REMARK 465 SER I 174
REMARK 465 LEU I 175
REMARK 465 ASN I 176
REMARK 465 LYS I 177
REMARK 465 LEU I 178
REMARK 465 PRO I 179
REMARK 465 ARG I 180
REMARK 465 GLN I 181
REMARK 465 LEU I 182
REMARK 465 PRO I 183
REMARK 465 LEU I 184
REMARK 465 GLU I 185
REMARK 465 VAL I 186
REMARK 465 ASP I 187
REMARK 465 LEU I 188
REMARK 465 THR I 189
REMARK 465 LYS I 190
REMARK 465 ALA I 191
REMARK 465 LYS I 192
REMARK 465 ARG I 193
REMARK 465 GLN I 194
REMARK 465 ASP I 195
REMARK 465 LEU I 196
REMARK 465 GLU I 197
REMARK 465 PRO I 198
REMARK 465 SER I 199
REMARK 465 VAL I 200
REMARK 465 GLU I 201
REMARK 465 GLU I 202
REMARK 465 ALA I 203
REMARK 465 ARG I 204
REMARK 465 TYR I 205
REMARK 465 ASN I 206
REMARK 465 SER I 207
REMARK 465 CYS I 208
REMARK 465 ARG I 209
REMARK 465 PRO I 210
REMARK 465 ASN I 211
REMARK 465 MET I 212
REMARK 465 ALA I 213
REMARK 465 LEU I 214
REMARK 465 GLY I 215
REMARK 465 HIS I 216
REMARK 465 PRO I 217
REMARK 465 GLN I 218
REMARK 465 LEU I 219
REMARK 465 GLN I 220
REMARK 465 GLN I 221
REMARK 465 VAL I 222
REMARK 465 THR I 223
REMARK 465 SER I 224
REMARK 465 PRO I 225
REMARK 465 SER I 226
REMARK 465 ARG I 227
REMARK 465 PRO I 228
REMARK 465 SER I 229
REMARK 465 HIS I 230
REMARK 465 ALA I 231
REMARK 465 VAL I 232
REMARK 465 ILE I 233
REMARK 465 PRO I 234
REMARK 465 ALA I 235
REMARK 465 ASP I 236
REMARK 465 GLN I 237
REMARK 465 ASP I 238
REMARK 465 CYS I 239
REMARK 465 SER I 240
REMARK 465 SER I 241
REMARK 465 ARG I 242
REMARK 465 SER I 243
REMARK 465 LEU I 244
REMARK 465 SER I 245
REMARK 465 SER I 246
REMARK 465 SER I 247
REMARK 465 ALA I 248
REMARK 465 VAL I 249
REMARK 465 GLU I 250
REMARK 465 SER I 251
REMARK 465 GLU I 252
REMARK 465 ALA I 253
REMARK 465 THR I 254
REMARK 465 HIS I 255
REMARK 465 GLN I 256
REMARK 465 ARG I 257
REMARK 465 LYS I 258
REMARK 465 LEU I 259
REMARK 465 ARG I 260
REMARK 465 GLN I 261
REMARK 465 LYS I 262
REMARK 465 GLN I 263
REMARK 465 LEU I 264
REMARK 465 GLN I 265
REMARK 465 GLN I 266
REMARK 465 GLN I 267
REMARK 465 PHE I 268
REMARK 465 ARG I 269
REMARK 465 GLU I 270
REMARK 465 ARG I 271
REMARK 465 MET I 272
REMARK 465 GLU I 273
REMARK 465 LYS I 274
REMARK 465 GLN I 275
REMARK 465 GLN I 276
REMARK 465 VAL I 277
REMARK 465 ARG I 278
REMARK 465 VAL I 279
REMARK 465 SER I 280
REMARK 465 THR I 281
REMARK 465 PRO I 282
REMARK 465 SER I 283
REMARK 465 ALA I 284
REMARK 465 GLU I 285
REMARK 465 LYS I 286
REMARK 465 SER I 287
REMARK 465 GLU I 288
REMARK 465 ALA I 289
REMARK 465 ALA I 290
REMARK 465 PRO I 291
REMARK 465 PRO I 292
REMARK 465 ALA I 293
REMARK 465 PRO I 294
REMARK 465 PRO I 295
REMARK 465 VAL I 296
REMARK 465 THR I 297
REMARK 465 HIS I 298
REMARK 465 SER I 299
REMARK 465 THR I 300
REMARK 465 PRO I 301
REMARK 465 VAL I 302
REMARK 465 THR I 303
REMARK 465 VAL I 304
REMARK 465 SER I 305
REMARK 465 GLU I 306
REMARK 465 PRO I 307
REMARK 465 LEU I 308
REMARK 465 LEU I 309
REMARK 465 GLU I 310
REMARK 465 LYS I 311
REMARK 465 ASP I 312
REMARK 465 PHE I 313
REMARK 465 LEU I 314
REMARK 465 ALA I 315
REMARK 465 GLY I 316
REMARK 465 VAL I 317
REMARK 465 THR I 318
REMARK 465 GLN I 319
REMARK 465 GLU I 320
REMARK 465 LEU I 321
REMARK 465 ILE I 322
REMARK 465 LYS I 323
REMARK 465 THR I 324
REMARK 465 LEU I 325
REMARK 465 GLU I 326
REMARK 465 ASP I 327
REMARK 465 ASN I 328
REMARK 465 SER I 329
REMARK 465 GLU I 330
REMARK 465 LYS I 331
REMARK 465 TRP I 332
REMARK 465 ALA I 333
REMARK 465 VAL I 334
REMARK 465 THR I 335
REMARK 465 PRO I 336
REMARK 465 ASP I 337
REMARK 465 ALA I 338
REMARK 465 GLY I 339
REMARK 465 ASP I 340
REMARK 465 GLY I 341
REMARK 465 VAL I 342
REMARK 465 VAL I 343
REMARK 465 LYS I 344
REMARK 465 PRO I 345
REMARK 465 SER I 346
REMARK 465 SER I 347
REMARK 465 ARG I 348
REMARK 465 ALA I 349
REMARK 465 ASP I 350
REMARK 465 PRO I 351
REMARK 465 ALA I 352
REMARK 465 GLN I 353
REMARK 465 THR I 354
REMARK 465 SER I 355
REMARK 465 ASP I 356
REMARK 465 THR I 357
REMARK 465 LEU I 358
REMARK 465 ALA I 359
REMARK 465 LEU I 360
REMARK 465 ASN I 361
REMARK 465 ASN I 362
REMARK 465 GLN I 363
REMARK 465 MET I 364
REMARK 465 VAL I 365
REMARK 465 THR I 366
REMARK 465 GLN I 367
REMARK 465 ASN I 368
REMARK 465 ARG I 369
REMARK 465 THR I 370
REMARK 465 PRO I 371
REMARK 465 HIS I 372
REMARK 465 SER I 373
REMARK 465 VAL I 374
REMARK 465 CYS I 375
REMARK 465 HIS I 376
REMARK 465 GLN I 377
REMARK 465 LYS I 378
REMARK 465 PRO I 379
REMARK 465 GLN I 380
REMARK 465 ALA I 381
REMARK 465 LYS I 382
REMARK 465 SER I 383
REMARK 465 GLY I 384
REMARK 465 SER I 385
REMARK 465 TRP I 386
REMARK 465 ASP I 387
REMARK 465 LEU I 388
REMARK 465 GLN I 389
REMARK 465 THR I 390
REMARK 465 TYR I 391
REMARK 465 SER I 392
REMARK 465 ALA I 393
REMARK 465 ASP I 394
REMARK 465 GLN I 395
REMARK 465 ARG I 396
REMARK 465 THR I 397
REMARK 465 THR I 398
REMARK 465 GLY I 399
REMARK 465 ASN I 400
REMARK 465 TRP I 401
REMARK 465 GLU I 402
REMARK 465 SER I 403
REMARK 465 HIS I 404
REMARK 465 ARG I 405
REMARK 465 LYS I 406
REMARK 465 SER I 407
REMARK 465 GLN I 408
REMARK 465 ASP I 409
REMARK 465 MET I 410
REMARK 465 LYS I 411
REMARK 465 LYS I 412
REMARK 465 ARG I 413
REMARK 465 LYS I 414
REMARK 465 TYR I 415
REMARK 465 ASP I 416
REMARK 465 PRO I 417
REMARK 465 SER I 418
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 HH12 ARG E 55 O5' DT J 9 1.47
REMARK 500 OD1 ASP B 117 H SER B 119 1.57
REMARK 500 HG1 THR F 148 OP1 DT J 7 1.58
REMARK 500 HG1 THR E 148 OP1 DT J 11 1.59
REMARK 500 O LEU D 47 HH TYR D 171 1.60
REMARK 500 O LEU B 47 OH TYR B 171 1.89
REMARK 500 O LEU E 47 OH TYR E 171 1.90
REMARK 500 OG1 THR G 148 OP1 DT J 3 1.92
REMARK 500 OG SER B 53 OE2 GLU B 67 1.94
REMARK 500 OP2 DT J 17 O HOH J 101 1.96
REMARK 500 NZ LYS G 152 OP1 DT J 2 2.06
REMARK 500 OG1 THR F 148 OP1 DT J 7 2.09
REMARK 500 NZ LYS E 192 OE2 GLU E 197 2.14
REMARK 500 O LEU C 47 OH TYR C 171 2.14
REMARK 500 O HOH J 107 O HOH J 109 2.15
REMARK 500 NH1 ARG E 55 O5' DT J 9 2.16
REMARK 500 OD1 ASP B 149 O HOH B 501 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DT J 3 O4' - C1' - N1 ANGL. DEV. = 1.9 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 94 -60.94 -91.00
REMARK 500 SER A 134 140.98 -170.42
REMARK 500 GLN C 28 22.08 -140.06
REMARK 500 GLN E 90 137.01 -170.64
REMARK 500 PHE E 95 143.44 -171.00
REMARK 500 GLN F 28 21.01 -140.95
REMARK 500 PRO F 49 1.88 -69.64
REMARK 500 PHE F 95 148.81 -171.10
REMARK 500 GLN H 37 -6.03 73.52
REMARK 500 SER H 134 137.04 74.33
REMARK 500 VAL I 107 -58.79 -128.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 502 O
REMARK 620 2 HOH B 504 O 81.9
REMARK 620 3 GLU C 140 OE2 104.0 140.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 601 O
REMARK 620 2 HOH J 105 O 142.6
REMARK 620 3 HOH J 106 O 90.6 86.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR D 126 O
REMARK 620 2 ASP D 149 OD2 87.5
REMARK 620 3 GLU E 140 OE2 88.4 102.7
REMARK 620 4 HOH E 503 O 146.3 119.3 67.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E 501 O
REMARK 620 2 HOH E 504 O 61.1
REMARK 620 3 GLU F 140 OE2 62.3 78.0
REMARK 620 4 HOH F 606 O 81.1 142.2 84.1
REMARK 620 5 HOH J 111 O 98.4 112.1 151.8 72.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH F 601 O
REMARK 620 2 HOH J 108 O 108.6
REMARK 620 N 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8RJ3 RELATED DB: PDB
REMARK 900 RELATED ID: 8RIL RELATED DB: PDB
REMARK 900 RELATED ID: EMD-19253 RELATED DB: EMDB
REMARK 900 HUMAN RAD52 OPEN RING - SSDNA COMPLEX
DBREF 8RJW A 1 418 UNP P43351 RAD52_HUMAN 1 418
DBREF 8RJW B 1 418 UNP P43351 RAD52_HUMAN 1 418
DBREF 8RJW C 1 418 UNP P43351 RAD52_HUMAN 1 418
DBREF 8RJW D 1 418 UNP P43351 RAD52_HUMAN 1 418
DBREF 8RJW E 1 418 UNP P43351 RAD52_HUMAN 1 418
DBREF 8RJW F 1 418 UNP P43351 RAD52_HUMAN 1 418
DBREF 8RJW G 1 418 UNP P43351 RAD52_HUMAN 1 418
DBREF 8RJW H 1 418 UNP P43351 RAD52_HUMAN 1 418
DBREF 8RJW I 1 418 UNP P43351 RAD52_HUMAN 1 418
DBREF 8RJW J 1 23 PDB 8RJW 8RJW 1 23
SEQRES 1 A 418 MET SER GLY THR GLU GLU ALA ILE LEU GLY GLY ARG ASP
SEQRES 2 A 418 SER HIS PRO ALA ALA GLY GLY GLY SER VAL LEU CYS PHE
SEQRES 3 A 418 GLY GLN CYS GLN TYR THR ALA GLU GLU TYR GLN ALA ILE
SEQRES 4 A 418 GLN LYS ALA LEU ARG GLN ARG LEU GLY PRO GLU TYR ILE
SEQRES 5 A 418 SER SER ARG MET ALA GLY GLY GLY GLN LYS VAL CYS TYR
SEQRES 6 A 418 ILE GLU GLY HIS ARG VAL ILE ASN LEU ALA ASN GLU MET
SEQRES 7 A 418 PHE GLY TYR ASN GLY TRP ALA HIS SER ILE THR GLN GLN
SEQRES 8 A 418 ASN VAL ASP PHE VAL ASP LEU ASN ASN GLY LYS PHE TYR
SEQRES 9 A 418 VAL GLY VAL CYS ALA PHE VAL ARG VAL GLN LEU LYS ASP
SEQRES 10 A 418 GLY SER TYR HIS GLU ASP VAL GLY TYR GLY VAL SER GLU
SEQRES 11 A 418 GLY LEU LYS SER LYS ALA LEU SER LEU GLU LYS ALA ARG
SEQRES 12 A 418 LYS GLU ALA VAL THR ASP GLY LEU LYS ARG ALA LEU ARG
SEQRES 13 A 418 SER PHE GLY ASN ALA LEU GLY ASN CYS ILE LEU ASP LYS
SEQRES 14 A 418 ASP TYR LEU ARG SER LEU ASN LYS LEU PRO ARG GLN LEU
SEQRES 15 A 418 PRO LEU GLU VAL ASP LEU THR LYS ALA LYS ARG GLN ASP
SEQRES 16 A 418 LEU GLU PRO SER VAL GLU GLU ALA ARG TYR ASN SER CYS
SEQRES 17 A 418 ARG PRO ASN MET ALA LEU GLY HIS PRO GLN LEU GLN GLN
SEQRES 18 A 418 VAL THR SER PRO SER ARG PRO SER HIS ALA VAL ILE PRO
SEQRES 19 A 418 ALA ASP GLN ASP CYS SER SER ARG SER LEU SER SER SER
SEQRES 20 A 418 ALA VAL GLU SER GLU ALA THR HIS GLN ARG LYS LEU ARG
SEQRES 21 A 418 GLN LYS GLN LEU GLN GLN GLN PHE ARG GLU ARG MET GLU
SEQRES 22 A 418 LYS GLN GLN VAL ARG VAL SER THR PRO SER ALA GLU LYS
SEQRES 23 A 418 SER GLU ALA ALA PRO PRO ALA PRO PRO VAL THR HIS SER
SEQRES 24 A 418 THR PRO VAL THR VAL SER GLU PRO LEU LEU GLU LYS ASP
SEQRES 25 A 418 PHE LEU ALA GLY VAL THR GLN GLU LEU ILE LYS THR LEU
SEQRES 26 A 418 GLU ASP ASN SER GLU LYS TRP ALA VAL THR PRO ASP ALA
SEQRES 27 A 418 GLY ASP GLY VAL VAL LYS PRO SER SER ARG ALA ASP PRO
SEQRES 28 A 418 ALA GLN THR SER ASP THR LEU ALA LEU ASN ASN GLN MET
SEQRES 29 A 418 VAL THR GLN ASN ARG THR PRO HIS SER VAL CYS HIS GLN
SEQRES 30 A 418 LYS PRO GLN ALA LYS SER GLY SER TRP ASP LEU GLN THR
SEQRES 31 A 418 TYR SER ALA ASP GLN ARG THR THR GLY ASN TRP GLU SER
SEQRES 32 A 418 HIS ARG LYS SER GLN ASP MET LYS LYS ARG LYS TYR ASP
SEQRES 33 A 418 PRO SER
SEQRES 1 B 418 MET SER GLY THR GLU GLU ALA ILE LEU GLY GLY ARG ASP
SEQRES 2 B 418 SER HIS PRO ALA ALA GLY GLY GLY SER VAL LEU CYS PHE
SEQRES 3 B 418 GLY GLN CYS GLN TYR THR ALA GLU GLU TYR GLN ALA ILE
SEQRES 4 B 418 GLN LYS ALA LEU ARG GLN ARG LEU GLY PRO GLU TYR ILE
SEQRES 5 B 418 SER SER ARG MET ALA GLY GLY GLY GLN LYS VAL CYS TYR
SEQRES 6 B 418 ILE GLU GLY HIS ARG VAL ILE ASN LEU ALA ASN GLU MET
SEQRES 7 B 418 PHE GLY TYR ASN GLY TRP ALA HIS SER ILE THR GLN GLN
SEQRES 8 B 418 ASN VAL ASP PHE VAL ASP LEU ASN ASN GLY LYS PHE TYR
SEQRES 9 B 418 VAL GLY VAL CYS ALA PHE VAL ARG VAL GLN LEU LYS ASP
SEQRES 10 B 418 GLY SER TYR HIS GLU ASP VAL GLY TYR GLY VAL SER GLU
SEQRES 11 B 418 GLY LEU LYS SER LYS ALA LEU SER LEU GLU LYS ALA ARG
SEQRES 12 B 418 LYS GLU ALA VAL THR ASP GLY LEU LYS ARG ALA LEU ARG
SEQRES 13 B 418 SER PHE GLY ASN ALA LEU GLY ASN CYS ILE LEU ASP LYS
SEQRES 14 B 418 ASP TYR LEU ARG SER LEU ASN LYS LEU PRO ARG GLN LEU
SEQRES 15 B 418 PRO LEU GLU VAL ASP LEU THR LYS ALA LYS ARG GLN ASP
SEQRES 16 B 418 LEU GLU PRO SER VAL GLU GLU ALA ARG TYR ASN SER CYS
SEQRES 17 B 418 ARG PRO ASN MET ALA LEU GLY HIS PRO GLN LEU GLN GLN
SEQRES 18 B 418 VAL THR SER PRO SER ARG PRO SER HIS ALA VAL ILE PRO
SEQRES 19 B 418 ALA ASP GLN ASP CYS SER SER ARG SER LEU SER SER SER
SEQRES 20 B 418 ALA VAL GLU SER GLU ALA THR HIS GLN ARG LYS LEU ARG
SEQRES 21 B 418 GLN LYS GLN LEU GLN GLN GLN PHE ARG GLU ARG MET GLU
SEQRES 22 B 418 LYS GLN GLN VAL ARG VAL SER THR PRO SER ALA GLU LYS
SEQRES 23 B 418 SER GLU ALA ALA PRO PRO ALA PRO PRO VAL THR HIS SER
SEQRES 24 B 418 THR PRO VAL THR VAL SER GLU PRO LEU LEU GLU LYS ASP
SEQRES 25 B 418 PHE LEU ALA GLY VAL THR GLN GLU LEU ILE LYS THR LEU
SEQRES 26 B 418 GLU ASP ASN SER GLU LYS TRP ALA VAL THR PRO ASP ALA
SEQRES 27 B 418 GLY ASP GLY VAL VAL LYS PRO SER SER ARG ALA ASP PRO
SEQRES 28 B 418 ALA GLN THR SER ASP THR LEU ALA LEU ASN ASN GLN MET
SEQRES 29 B 418 VAL THR GLN ASN ARG THR PRO HIS SER VAL CYS HIS GLN
SEQRES 30 B 418 LYS PRO GLN ALA LYS SER GLY SER TRP ASP LEU GLN THR
SEQRES 31 B 418 TYR SER ALA ASP GLN ARG THR THR GLY ASN TRP GLU SER
SEQRES 32 B 418 HIS ARG LYS SER GLN ASP MET LYS LYS ARG LYS TYR ASP
SEQRES 33 B 418 PRO SER
SEQRES 1 C 418 MET SER GLY THR GLU GLU ALA ILE LEU GLY GLY ARG ASP
SEQRES 2 C 418 SER HIS PRO ALA ALA GLY GLY GLY SER VAL LEU CYS PHE
SEQRES 3 C 418 GLY GLN CYS GLN TYR THR ALA GLU GLU TYR GLN ALA ILE
SEQRES 4 C 418 GLN LYS ALA LEU ARG GLN ARG LEU GLY PRO GLU TYR ILE
SEQRES 5 C 418 SER SER ARG MET ALA GLY GLY GLY GLN LYS VAL CYS TYR
SEQRES 6 C 418 ILE GLU GLY HIS ARG VAL ILE ASN LEU ALA ASN GLU MET
SEQRES 7 C 418 PHE GLY TYR ASN GLY TRP ALA HIS SER ILE THR GLN GLN
SEQRES 8 C 418 ASN VAL ASP PHE VAL ASP LEU ASN ASN GLY LYS PHE TYR
SEQRES 9 C 418 VAL GLY VAL CYS ALA PHE VAL ARG VAL GLN LEU LYS ASP
SEQRES 10 C 418 GLY SER TYR HIS GLU ASP VAL GLY TYR GLY VAL SER GLU
SEQRES 11 C 418 GLY LEU LYS SER LYS ALA LEU SER LEU GLU LYS ALA ARG
SEQRES 12 C 418 LYS GLU ALA VAL THR ASP GLY LEU LYS ARG ALA LEU ARG
SEQRES 13 C 418 SER PHE GLY ASN ALA LEU GLY ASN CYS ILE LEU ASP LYS
SEQRES 14 C 418 ASP TYR LEU ARG SER LEU ASN LYS LEU PRO ARG GLN LEU
SEQRES 15 C 418 PRO LEU GLU VAL ASP LEU THR LYS ALA LYS ARG GLN ASP
SEQRES 16 C 418 LEU GLU PRO SER VAL GLU GLU ALA ARG TYR ASN SER CYS
SEQRES 17 C 418 ARG PRO ASN MET ALA LEU GLY HIS PRO GLN LEU GLN GLN
SEQRES 18 C 418 VAL THR SER PRO SER ARG PRO SER HIS ALA VAL ILE PRO
SEQRES 19 C 418 ALA ASP GLN ASP CYS SER SER ARG SER LEU SER SER SER
SEQRES 20 C 418 ALA VAL GLU SER GLU ALA THR HIS GLN ARG LYS LEU ARG
SEQRES 21 C 418 GLN LYS GLN LEU GLN GLN GLN PHE ARG GLU ARG MET GLU
SEQRES 22 C 418 LYS GLN GLN VAL ARG VAL SER THR PRO SER ALA GLU LYS
SEQRES 23 C 418 SER GLU ALA ALA PRO PRO ALA PRO PRO VAL THR HIS SER
SEQRES 24 C 418 THR PRO VAL THR VAL SER GLU PRO LEU LEU GLU LYS ASP
SEQRES 25 C 418 PHE LEU ALA GLY VAL THR GLN GLU LEU ILE LYS THR LEU
SEQRES 26 C 418 GLU ASP ASN SER GLU LYS TRP ALA VAL THR PRO ASP ALA
SEQRES 27 C 418 GLY ASP GLY VAL VAL LYS PRO SER SER ARG ALA ASP PRO
SEQRES 28 C 418 ALA GLN THR SER ASP THR LEU ALA LEU ASN ASN GLN MET
SEQRES 29 C 418 VAL THR GLN ASN ARG THR PRO HIS SER VAL CYS HIS GLN
SEQRES 30 C 418 LYS PRO GLN ALA LYS SER GLY SER TRP ASP LEU GLN THR
SEQRES 31 C 418 TYR SER ALA ASP GLN ARG THR THR GLY ASN TRP GLU SER
SEQRES 32 C 418 HIS ARG LYS SER GLN ASP MET LYS LYS ARG LYS TYR ASP
SEQRES 33 C 418 PRO SER
SEQRES 1 D 418 MET SER GLY THR GLU GLU ALA ILE LEU GLY GLY ARG ASP
SEQRES 2 D 418 SER HIS PRO ALA ALA GLY GLY GLY SER VAL LEU CYS PHE
SEQRES 3 D 418 GLY GLN CYS GLN TYR THR ALA GLU GLU TYR GLN ALA ILE
SEQRES 4 D 418 GLN LYS ALA LEU ARG GLN ARG LEU GLY PRO GLU TYR ILE
SEQRES 5 D 418 SER SER ARG MET ALA GLY GLY GLY GLN LYS VAL CYS TYR
SEQRES 6 D 418 ILE GLU GLY HIS ARG VAL ILE ASN LEU ALA ASN GLU MET
SEQRES 7 D 418 PHE GLY TYR ASN GLY TRP ALA HIS SER ILE THR GLN GLN
SEQRES 8 D 418 ASN VAL ASP PHE VAL ASP LEU ASN ASN GLY LYS PHE TYR
SEQRES 9 D 418 VAL GLY VAL CYS ALA PHE VAL ARG VAL GLN LEU LYS ASP
SEQRES 10 D 418 GLY SER TYR HIS GLU ASP VAL GLY TYR GLY VAL SER GLU
SEQRES 11 D 418 GLY LEU LYS SER LYS ALA LEU SER LEU GLU LYS ALA ARG
SEQRES 12 D 418 LYS GLU ALA VAL THR ASP GLY LEU LYS ARG ALA LEU ARG
SEQRES 13 D 418 SER PHE GLY ASN ALA LEU GLY ASN CYS ILE LEU ASP LYS
SEQRES 14 D 418 ASP TYR LEU ARG SER LEU ASN LYS LEU PRO ARG GLN LEU
SEQRES 15 D 418 PRO LEU GLU VAL ASP LEU THR LYS ALA LYS ARG GLN ASP
SEQRES 16 D 418 LEU GLU PRO SER VAL GLU GLU ALA ARG TYR ASN SER CYS
SEQRES 17 D 418 ARG PRO ASN MET ALA LEU GLY HIS PRO GLN LEU GLN GLN
SEQRES 18 D 418 VAL THR SER PRO SER ARG PRO SER HIS ALA VAL ILE PRO
SEQRES 19 D 418 ALA ASP GLN ASP CYS SER SER ARG SER LEU SER SER SER
SEQRES 20 D 418 ALA VAL GLU SER GLU ALA THR HIS GLN ARG LYS LEU ARG
SEQRES 21 D 418 GLN LYS GLN LEU GLN GLN GLN PHE ARG GLU ARG MET GLU
SEQRES 22 D 418 LYS GLN GLN VAL ARG VAL SER THR PRO SER ALA GLU LYS
SEQRES 23 D 418 SER GLU ALA ALA PRO PRO ALA PRO PRO VAL THR HIS SER
SEQRES 24 D 418 THR PRO VAL THR VAL SER GLU PRO LEU LEU GLU LYS ASP
SEQRES 25 D 418 PHE LEU ALA GLY VAL THR GLN GLU LEU ILE LYS THR LEU
SEQRES 26 D 418 GLU ASP ASN SER GLU LYS TRP ALA VAL THR PRO ASP ALA
SEQRES 27 D 418 GLY ASP GLY VAL VAL LYS PRO SER SER ARG ALA ASP PRO
SEQRES 28 D 418 ALA GLN THR SER ASP THR LEU ALA LEU ASN ASN GLN MET
SEQRES 29 D 418 VAL THR GLN ASN ARG THR PRO HIS SER VAL CYS HIS GLN
SEQRES 30 D 418 LYS PRO GLN ALA LYS SER GLY SER TRP ASP LEU GLN THR
SEQRES 31 D 418 TYR SER ALA ASP GLN ARG THR THR GLY ASN TRP GLU SER
SEQRES 32 D 418 HIS ARG LYS SER GLN ASP MET LYS LYS ARG LYS TYR ASP
SEQRES 33 D 418 PRO SER
SEQRES 1 E 418 MET SER GLY THR GLU GLU ALA ILE LEU GLY GLY ARG ASP
SEQRES 2 E 418 SER HIS PRO ALA ALA GLY GLY GLY SER VAL LEU CYS PHE
SEQRES 3 E 418 GLY GLN CYS GLN TYR THR ALA GLU GLU TYR GLN ALA ILE
SEQRES 4 E 418 GLN LYS ALA LEU ARG GLN ARG LEU GLY PRO GLU TYR ILE
SEQRES 5 E 418 SER SER ARG MET ALA GLY GLY GLY GLN LYS VAL CYS TYR
SEQRES 6 E 418 ILE GLU GLY HIS ARG VAL ILE ASN LEU ALA ASN GLU MET
SEQRES 7 E 418 PHE GLY TYR ASN GLY TRP ALA HIS SER ILE THR GLN GLN
SEQRES 8 E 418 ASN VAL ASP PHE VAL ASP LEU ASN ASN GLY LYS PHE TYR
SEQRES 9 E 418 VAL GLY VAL CYS ALA PHE VAL ARG VAL GLN LEU LYS ASP
SEQRES 10 E 418 GLY SER TYR HIS GLU ASP VAL GLY TYR GLY VAL SER GLU
SEQRES 11 E 418 GLY LEU LYS SER LYS ALA LEU SER LEU GLU LYS ALA ARG
SEQRES 12 E 418 LYS GLU ALA VAL THR ASP GLY LEU LYS ARG ALA LEU ARG
SEQRES 13 E 418 SER PHE GLY ASN ALA LEU GLY ASN CYS ILE LEU ASP LYS
SEQRES 14 E 418 ASP TYR LEU ARG SER LEU ASN LYS LEU PRO ARG GLN LEU
SEQRES 15 E 418 PRO LEU GLU VAL ASP LEU THR LYS ALA LYS ARG GLN ASP
SEQRES 16 E 418 LEU GLU PRO SER VAL GLU GLU ALA ARG TYR ASN SER CYS
SEQRES 17 E 418 ARG PRO ASN MET ALA LEU GLY HIS PRO GLN LEU GLN GLN
SEQRES 18 E 418 VAL THR SER PRO SER ARG PRO SER HIS ALA VAL ILE PRO
SEQRES 19 E 418 ALA ASP GLN ASP CYS SER SER ARG SER LEU SER SER SER
SEQRES 20 E 418 ALA VAL GLU SER GLU ALA THR HIS GLN ARG LYS LEU ARG
SEQRES 21 E 418 GLN LYS GLN LEU GLN GLN GLN PHE ARG GLU ARG MET GLU
SEQRES 22 E 418 LYS GLN GLN VAL ARG VAL SER THR PRO SER ALA GLU LYS
SEQRES 23 E 418 SER GLU ALA ALA PRO PRO ALA PRO PRO VAL THR HIS SER
SEQRES 24 E 418 THR PRO VAL THR VAL SER GLU PRO LEU LEU GLU LYS ASP
SEQRES 25 E 418 PHE LEU ALA GLY VAL THR GLN GLU LEU ILE LYS THR LEU
SEQRES 26 E 418 GLU ASP ASN SER GLU LYS TRP ALA VAL THR PRO ASP ALA
SEQRES 27 E 418 GLY ASP GLY VAL VAL LYS PRO SER SER ARG ALA ASP PRO
SEQRES 28 E 418 ALA GLN THR SER ASP THR LEU ALA LEU ASN ASN GLN MET
SEQRES 29 E 418 VAL THR GLN ASN ARG THR PRO HIS SER VAL CYS HIS GLN
SEQRES 30 E 418 LYS PRO GLN ALA LYS SER GLY SER TRP ASP LEU GLN THR
SEQRES 31 E 418 TYR SER ALA ASP GLN ARG THR THR GLY ASN TRP GLU SER
SEQRES 32 E 418 HIS ARG LYS SER GLN ASP MET LYS LYS ARG LYS TYR ASP
SEQRES 33 E 418 PRO SER
SEQRES 1 F 418 MET SER GLY THR GLU GLU ALA ILE LEU GLY GLY ARG ASP
SEQRES 2 F 418 SER HIS PRO ALA ALA GLY GLY GLY SER VAL LEU CYS PHE
SEQRES 3 F 418 GLY GLN CYS GLN TYR THR ALA GLU GLU TYR GLN ALA ILE
SEQRES 4 F 418 GLN LYS ALA LEU ARG GLN ARG LEU GLY PRO GLU TYR ILE
SEQRES 5 F 418 SER SER ARG MET ALA GLY GLY GLY GLN LYS VAL CYS TYR
SEQRES 6 F 418 ILE GLU GLY HIS ARG VAL ILE ASN LEU ALA ASN GLU MET
SEQRES 7 F 418 PHE GLY TYR ASN GLY TRP ALA HIS SER ILE THR GLN GLN
SEQRES 8 F 418 ASN VAL ASP PHE VAL ASP LEU ASN ASN GLY LYS PHE TYR
SEQRES 9 F 418 VAL GLY VAL CYS ALA PHE VAL ARG VAL GLN LEU LYS ASP
SEQRES 10 F 418 GLY SER TYR HIS GLU ASP VAL GLY TYR GLY VAL SER GLU
SEQRES 11 F 418 GLY LEU LYS SER LYS ALA LEU SER LEU GLU LYS ALA ARG
SEQRES 12 F 418 LYS GLU ALA VAL THR ASP GLY LEU LYS ARG ALA LEU ARG
SEQRES 13 F 418 SER PHE GLY ASN ALA LEU GLY ASN CYS ILE LEU ASP LYS
SEQRES 14 F 418 ASP TYR LEU ARG SER LEU ASN LYS LEU PRO ARG GLN LEU
SEQRES 15 F 418 PRO LEU GLU VAL ASP LEU THR LYS ALA LYS ARG GLN ASP
SEQRES 16 F 418 LEU GLU PRO SER VAL GLU GLU ALA ARG TYR ASN SER CYS
SEQRES 17 F 418 ARG PRO ASN MET ALA LEU GLY HIS PRO GLN LEU GLN GLN
SEQRES 18 F 418 VAL THR SER PRO SER ARG PRO SER HIS ALA VAL ILE PRO
SEQRES 19 F 418 ALA ASP GLN ASP CYS SER SER ARG SER LEU SER SER SER
SEQRES 20 F 418 ALA VAL GLU SER GLU ALA THR HIS GLN ARG LYS LEU ARG
SEQRES 21 F 418 GLN LYS GLN LEU GLN GLN GLN PHE ARG GLU ARG MET GLU
SEQRES 22 F 418 LYS GLN GLN VAL ARG VAL SER THR PRO SER ALA GLU LYS
SEQRES 23 F 418 SER GLU ALA ALA PRO PRO ALA PRO PRO VAL THR HIS SER
SEQRES 24 F 418 THR PRO VAL THR VAL SER GLU PRO LEU LEU GLU LYS ASP
SEQRES 25 F 418 PHE LEU ALA GLY VAL THR GLN GLU LEU ILE LYS THR LEU
SEQRES 26 F 418 GLU ASP ASN SER GLU LYS TRP ALA VAL THR PRO ASP ALA
SEQRES 27 F 418 GLY ASP GLY VAL VAL LYS PRO SER SER ARG ALA ASP PRO
SEQRES 28 F 418 ALA GLN THR SER ASP THR LEU ALA LEU ASN ASN GLN MET
SEQRES 29 F 418 VAL THR GLN ASN ARG THR PRO HIS SER VAL CYS HIS GLN
SEQRES 30 F 418 LYS PRO GLN ALA LYS SER GLY SER TRP ASP LEU GLN THR
SEQRES 31 F 418 TYR SER ALA ASP GLN ARG THR THR GLY ASN TRP GLU SER
SEQRES 32 F 418 HIS ARG LYS SER GLN ASP MET LYS LYS ARG LYS TYR ASP
SEQRES 33 F 418 PRO SER
SEQRES 1 G 418 MET SER GLY THR GLU GLU ALA ILE LEU GLY GLY ARG ASP
SEQRES 2 G 418 SER HIS PRO ALA ALA GLY GLY GLY SER VAL LEU CYS PHE
SEQRES 3 G 418 GLY GLN CYS GLN TYR THR ALA GLU GLU TYR GLN ALA ILE
SEQRES 4 G 418 GLN LYS ALA LEU ARG GLN ARG LEU GLY PRO GLU TYR ILE
SEQRES 5 G 418 SER SER ARG MET ALA GLY GLY GLY GLN LYS VAL CYS TYR
SEQRES 6 G 418 ILE GLU GLY HIS ARG VAL ILE ASN LEU ALA ASN GLU MET
SEQRES 7 G 418 PHE GLY TYR ASN GLY TRP ALA HIS SER ILE THR GLN GLN
SEQRES 8 G 418 ASN VAL ASP PHE VAL ASP LEU ASN ASN GLY LYS PHE TYR
SEQRES 9 G 418 VAL GLY VAL CYS ALA PHE VAL ARG VAL GLN LEU LYS ASP
SEQRES 10 G 418 GLY SER TYR HIS GLU ASP VAL GLY TYR GLY VAL SER GLU
SEQRES 11 G 418 GLY LEU LYS SER LYS ALA LEU SER LEU GLU LYS ALA ARG
SEQRES 12 G 418 LYS GLU ALA VAL THR ASP GLY LEU LYS ARG ALA LEU ARG
SEQRES 13 G 418 SER PHE GLY ASN ALA LEU GLY ASN CYS ILE LEU ASP LYS
SEQRES 14 G 418 ASP TYR LEU ARG SER LEU ASN LYS LEU PRO ARG GLN LEU
SEQRES 15 G 418 PRO LEU GLU VAL ASP LEU THR LYS ALA LYS ARG GLN ASP
SEQRES 16 G 418 LEU GLU PRO SER VAL GLU GLU ALA ARG TYR ASN SER CYS
SEQRES 17 G 418 ARG PRO ASN MET ALA LEU GLY HIS PRO GLN LEU GLN GLN
SEQRES 18 G 418 VAL THR SER PRO SER ARG PRO SER HIS ALA VAL ILE PRO
SEQRES 19 G 418 ALA ASP GLN ASP CYS SER SER ARG SER LEU SER SER SER
SEQRES 20 G 418 ALA VAL GLU SER GLU ALA THR HIS GLN ARG LYS LEU ARG
SEQRES 21 G 418 GLN LYS GLN LEU GLN GLN GLN PHE ARG GLU ARG MET GLU
SEQRES 22 G 418 LYS GLN GLN VAL ARG VAL SER THR PRO SER ALA GLU LYS
SEQRES 23 G 418 SER GLU ALA ALA PRO PRO ALA PRO PRO VAL THR HIS SER
SEQRES 24 G 418 THR PRO VAL THR VAL SER GLU PRO LEU LEU GLU LYS ASP
SEQRES 25 G 418 PHE LEU ALA GLY VAL THR GLN GLU LEU ILE LYS THR LEU
SEQRES 26 G 418 GLU ASP ASN SER GLU LYS TRP ALA VAL THR PRO ASP ALA
SEQRES 27 G 418 GLY ASP GLY VAL VAL LYS PRO SER SER ARG ALA ASP PRO
SEQRES 28 G 418 ALA GLN THR SER ASP THR LEU ALA LEU ASN ASN GLN MET
SEQRES 29 G 418 VAL THR GLN ASN ARG THR PRO HIS SER VAL CYS HIS GLN
SEQRES 30 G 418 LYS PRO GLN ALA LYS SER GLY SER TRP ASP LEU GLN THR
SEQRES 31 G 418 TYR SER ALA ASP GLN ARG THR THR GLY ASN TRP GLU SER
SEQRES 32 G 418 HIS ARG LYS SER GLN ASP MET LYS LYS ARG LYS TYR ASP
SEQRES 33 G 418 PRO SER
SEQRES 1 H 418 MET SER GLY THR GLU GLU ALA ILE LEU GLY GLY ARG ASP
SEQRES 2 H 418 SER HIS PRO ALA ALA GLY GLY GLY SER VAL LEU CYS PHE
SEQRES 3 H 418 GLY GLN CYS GLN TYR THR ALA GLU GLU TYR GLN ALA ILE
SEQRES 4 H 418 GLN LYS ALA LEU ARG GLN ARG LEU GLY PRO GLU TYR ILE
SEQRES 5 H 418 SER SER ARG MET ALA GLY GLY GLY GLN LYS VAL CYS TYR
SEQRES 6 H 418 ILE GLU GLY HIS ARG VAL ILE ASN LEU ALA ASN GLU MET
SEQRES 7 H 418 PHE GLY TYR ASN GLY TRP ALA HIS SER ILE THR GLN GLN
SEQRES 8 H 418 ASN VAL ASP PHE VAL ASP LEU ASN ASN GLY LYS PHE TYR
SEQRES 9 H 418 VAL GLY VAL CYS ALA PHE VAL ARG VAL GLN LEU LYS ASP
SEQRES 10 H 418 GLY SER TYR HIS GLU ASP VAL GLY TYR GLY VAL SER GLU
SEQRES 11 H 418 GLY LEU LYS SER LYS ALA LEU SER LEU GLU LYS ALA ARG
SEQRES 12 H 418 LYS GLU ALA VAL THR ASP GLY LEU LYS ARG ALA LEU ARG
SEQRES 13 H 418 SER PHE GLY ASN ALA LEU GLY ASN CYS ILE LEU ASP LYS
SEQRES 14 H 418 ASP TYR LEU ARG SER LEU ASN LYS LEU PRO ARG GLN LEU
SEQRES 15 H 418 PRO LEU GLU VAL ASP LEU THR LYS ALA LYS ARG GLN ASP
SEQRES 16 H 418 LEU GLU PRO SER VAL GLU GLU ALA ARG TYR ASN SER CYS
SEQRES 17 H 418 ARG PRO ASN MET ALA LEU GLY HIS PRO GLN LEU GLN GLN
SEQRES 18 H 418 VAL THR SER PRO SER ARG PRO SER HIS ALA VAL ILE PRO
SEQRES 19 H 418 ALA ASP GLN ASP CYS SER SER ARG SER LEU SER SER SER
SEQRES 20 H 418 ALA VAL GLU SER GLU ALA THR HIS GLN ARG LYS LEU ARG
SEQRES 21 H 418 GLN LYS GLN LEU GLN GLN GLN PHE ARG GLU ARG MET GLU
SEQRES 22 H 418 LYS GLN GLN VAL ARG VAL SER THR PRO SER ALA GLU LYS
SEQRES 23 H 418 SER GLU ALA ALA PRO PRO ALA PRO PRO VAL THR HIS SER
SEQRES 24 H 418 THR PRO VAL THR VAL SER GLU PRO LEU LEU GLU LYS ASP
SEQRES 25 H 418 PHE LEU ALA GLY VAL THR GLN GLU LEU ILE LYS THR LEU
SEQRES 26 H 418 GLU ASP ASN SER GLU LYS TRP ALA VAL THR PRO ASP ALA
SEQRES 27 H 418 GLY ASP GLY VAL VAL LYS PRO SER SER ARG ALA ASP PRO
SEQRES 28 H 418 ALA GLN THR SER ASP THR LEU ALA LEU ASN ASN GLN MET
SEQRES 29 H 418 VAL THR GLN ASN ARG THR PRO HIS SER VAL CYS HIS GLN
SEQRES 30 H 418 LYS PRO GLN ALA LYS SER GLY SER TRP ASP LEU GLN THR
SEQRES 31 H 418 TYR SER ALA ASP GLN ARG THR THR GLY ASN TRP GLU SER
SEQRES 32 H 418 HIS ARG LYS SER GLN ASP MET LYS LYS ARG LYS TYR ASP
SEQRES 33 H 418 PRO SER
SEQRES 1 I 418 MET SER GLY THR GLU GLU ALA ILE LEU GLY GLY ARG ASP
SEQRES 2 I 418 SER HIS PRO ALA ALA GLY GLY GLY SER VAL LEU CYS PHE
SEQRES 3 I 418 GLY GLN CYS GLN TYR THR ALA GLU GLU TYR GLN ALA ILE
SEQRES 4 I 418 GLN LYS ALA LEU ARG GLN ARG LEU GLY PRO GLU TYR ILE
SEQRES 5 I 418 SER SER ARG MET ALA GLY GLY GLY GLN LYS VAL CYS TYR
SEQRES 6 I 418 ILE GLU GLY HIS ARG VAL ILE ASN LEU ALA ASN GLU MET
SEQRES 7 I 418 PHE GLY TYR ASN GLY TRP ALA HIS SER ILE THR GLN GLN
SEQRES 8 I 418 ASN VAL ASP PHE VAL ASP LEU ASN ASN GLY LYS PHE TYR
SEQRES 9 I 418 VAL GLY VAL CYS ALA PHE VAL ARG VAL GLN LEU LYS ASP
SEQRES 10 I 418 GLY SER TYR HIS GLU ASP VAL GLY TYR GLY VAL SER GLU
SEQRES 11 I 418 GLY LEU LYS SER LYS ALA LEU SER LEU GLU LYS ALA ARG
SEQRES 12 I 418 LYS GLU ALA VAL THR ASP GLY LEU LYS ARG ALA LEU ARG
SEQRES 13 I 418 SER PHE GLY ASN ALA LEU GLY ASN CYS ILE LEU ASP LYS
SEQRES 14 I 418 ASP TYR LEU ARG SER LEU ASN LYS LEU PRO ARG GLN LEU
SEQRES 15 I 418 PRO LEU GLU VAL ASP LEU THR LYS ALA LYS ARG GLN ASP
SEQRES 16 I 418 LEU GLU PRO SER VAL GLU GLU ALA ARG TYR ASN SER CYS
SEQRES 17 I 418 ARG PRO ASN MET ALA LEU GLY HIS PRO GLN LEU GLN GLN
SEQRES 18 I 418 VAL THR SER PRO SER ARG PRO SER HIS ALA VAL ILE PRO
SEQRES 19 I 418 ALA ASP GLN ASP CYS SER SER ARG SER LEU SER SER SER
SEQRES 20 I 418 ALA VAL GLU SER GLU ALA THR HIS GLN ARG LYS LEU ARG
SEQRES 21 I 418 GLN LYS GLN LEU GLN GLN GLN PHE ARG GLU ARG MET GLU
SEQRES 22 I 418 LYS GLN GLN VAL ARG VAL SER THR PRO SER ALA GLU LYS
SEQRES 23 I 418 SER GLU ALA ALA PRO PRO ALA PRO PRO VAL THR HIS SER
SEQRES 24 I 418 THR PRO VAL THR VAL SER GLU PRO LEU LEU GLU LYS ASP
SEQRES 25 I 418 PHE LEU ALA GLY VAL THR GLN GLU LEU ILE LYS THR LEU
SEQRES 26 I 418 GLU ASP ASN SER GLU LYS TRP ALA VAL THR PRO ASP ALA
SEQRES 27 I 418 GLY ASP GLY VAL VAL LYS PRO SER SER ARG ALA ASP PRO
SEQRES 28 I 418 ALA GLN THR SER ASP THR LEU ALA LEU ASN ASN GLN MET
SEQRES 29 I 418 VAL THR GLN ASN ARG THR PRO HIS SER VAL CYS HIS GLN
SEQRES 30 I 418 LYS PRO GLN ALA LYS SER GLY SER TRP ASP LEU GLN THR
SEQRES 31 I 418 TYR SER ALA ASP GLN ARG THR THR GLY ASN TRP GLU SER
SEQRES 32 I 418 HIS ARG LYS SER GLN ASP MET LYS LYS ARG LYS TYR ASP
SEQRES 33 I 418 PRO SER
SEQRES 1 J 23 DT DT DT DT DT DT DT DT DT DT DT DT DT
SEQRES 2 J 23 DT DT DT DT DT DT DT DT DT DT
HET MG C 501 1
HET MG D 501 1
HET MG D 502 1
HET MG F 501 1
HET MG G 501 1
HETNAM MG MAGNESIUM ION
FORMUL 11 MG 5(MG 2+)
FORMUL 16 HOH *39(H2 O)
HELIX 1 AA1 ALA A 33 LEU A 43 1 11
HELIX 2 AA2 GLU A 67 GLY A 80 1 14
HELIX 3 AA3 SER A 138 SER A 157 1 20
HELIX 4 AA4 GLY A 159 GLY A 163 5 5
HELIX 5 AA5 THR B 32 ARG B 44 1 13
HELIX 6 AA6 GLU B 67 PHE B 79 1 13
HELIX 7 AA7 SER B 134 ARG B 156 1 23
HELIX 8 AA8 SER B 157 LEU B 167 5 11
HELIX 9 AA9 ASP B 168 ASN B 176 1 9
HELIX 10 AB1 THR C 32 ARG C 44 1 13
HELIX 11 AB2 GLU C 67 GLY C 80 1 14
HELIX 12 AB3 SER C 134 ARG C 156 1 23
HELIX 13 AB4 SER C 157 LEU C 167 5 11
HELIX 14 AB5 ASP C 168 ASN C 176 1 9
HELIX 15 AB6 THR D 32 ARG D 44 1 13
HELIX 16 AB7 GLU D 67 GLY D 80 1 14
HELIX 17 AB8 LYS D 135 ARG D 156 1 22
HELIX 18 AB9 SER D 157 LEU D 167 5 11
HELIX 19 AC1 ASP D 168 ASN D 176 1 9
HELIX 20 AC2 GLU D 197 ARG D 204 1 8
HELIX 21 AC3 THR E 32 GLN E 45 1 14
HELIX 22 AC4 GLY E 48 ILE E 52 5 5
HELIX 23 AC5 GLU E 67 GLY E 80 1 14
HELIX 24 AC6 SER E 134 ARG E 156 1 23
HELIX 25 AC7 SER E 157 GLY E 159 5 3
HELIX 26 AC8 GLY E 163 LEU E 167 5 5
HELIX 27 AC9 ASP E 168 ASN E 176 1 9
HELIX 28 AD1 GLU E 197 ARG E 204 1 8
HELIX 29 AD2 THR F 32 ARG F 44 1 13
HELIX 30 AD3 GLU F 67 GLY F 80 1 14
HELIX 31 AD4 SER F 134 SER F 157 1 24
HELIX 32 AD5 PHE F 158 GLY F 163 5 6
HELIX 33 AD6 ASP F 168 ASN F 176 1 9
HELIX 34 AD7 GLU F 197 ARG F 204 1 8
HELIX 35 AD8 THR G 32 GLN G 45 1 14
HELIX 36 AD9 GLU G 67 GLY G 80 1 14
HELIX 37 AE1 SER G 134 ARG G 156 1 23
HELIX 38 AE2 SER G 157 GLY G 163 5 7
HELIX 39 AE3 ALA H 38 LEU H 43 1 6
HELIX 40 AE4 GLU H 67 PHE H 79 1 13
HELIX 41 AE5 SER H 134 ARG H 156 1 23
HELIX 42 AE6 SER H 157 GLY H 159 5 3
HELIX 43 AE7 GLY I 68 ASN I 76 1 9
HELIX 44 AE8 LYS I 135 LEU I 155 1 21
SHEET 1 AA1 3 TRP A 84 VAL A 93 0
SHEET 2 AA1 3 TYR A 104 LEU A 115 -1 O PHE A 110 N THR A 89
SHEET 3 AA1 3 TYR A 120 VAL A 124 -1 O HIS A 121 N VAL A 113
SHEET 1 AA2 3 TRP A 84 VAL A 93 0
SHEET 2 AA2 3 TYR A 104 LEU A 115 -1 O PHE A 110 N THR A 89
SHEET 3 AA2 3 GLY A 127 GLU A 130 -1 O GLY A 127 N VAL A 107
SHEET 1 AA3 2 SER B 53 ARG B 55 0
SHEET 2 AA3 2 VAL B 63 TYR B 65 -1 O TYR B 65 N SER B 53
SHEET 1 AA4 3 TRP B 84 ASN B 99 0
SHEET 2 AA4 3 LYS B 102 LEU B 115 -1 O TYR B 104 N ASP B 97
SHEET 3 AA4 3 TYR B 120 GLU B 130 -1 O GLY B 125 N ALA B 109
SHEET 1 AA5 2 SER C 53 MET C 56 0
SHEET 2 AA5 2 LYS C 62 TYR C 65 -1 O TYR C 65 N SER C 53
SHEET 1 AA6 3 TRP C 84 ASN C 99 0
SHEET 2 AA6 3 LYS C 102 LEU C 115 -1 O TYR C 104 N ASP C 97
SHEET 3 AA6 3 TYR C 120 GLU C 130 -1 O GLY C 127 N VAL C 107
SHEET 1 AA7 2 SER D 53 ARG D 55 0
SHEET 2 AA7 2 VAL D 63 TYR D 65 -1 O TYR D 65 N SER D 53
SHEET 1 AA8 3 TRP D 84 ASN D 99 0
SHEET 2 AA8 3 LYS D 102 LEU D 115 -1 O PHE D 110 N THR D 89
SHEET 3 AA8 3 TYR D 120 GLU D 130 -1 O GLY D 125 N ALA D 109
SHEET 1 AA9 2 SER E 53 ARG E 55 0
SHEET 2 AA9 2 VAL E 63 TYR E 65 -1 O TYR E 65 N SER E 53
SHEET 1 AB1 3 TRP E 84 ASN E 99 0
SHEET 2 AB1 3 LYS E 102 LEU E 115 -1 O GLN E 114 N ALA E 85
SHEET 3 AB1 3 TYR E 120 LEU E 132 -1 O GLY E 125 N ALA E 109
SHEET 1 AB2 2 SER F 53 ARG F 55 0
SHEET 2 AB2 2 VAL F 63 TYR F 65 -1 O TYR F 65 N SER F 53
SHEET 1 AB3 3 TRP F 84 ASN F 99 0
SHEET 2 AB3 3 LYS F 102 LEU F 115 -1 O ARG F 112 N SER F 87
SHEET 3 AB3 3 TYR F 120 LEU F 132 -1 O GLY F 127 N VAL F 107
SHEET 1 AB4 3 TRP G 84 ASN G 99 0
SHEET 2 AB4 3 LYS G 102 LEU G 115 -1 O GLN G 114 N ALA G 85
SHEET 3 AB4 3 TYR G 120 LEU G 132 -1 O ASP G 123 N VAL G 111
SHEET 1 AB5 3 TRP H 84 ASN H 99 0
SHEET 2 AB5 3 LYS H 102 LEU H 115 -1 O PHE H 110 N THR H 89
SHEET 3 AB5 3 TYR H 120 LEU H 132 -1 O ASP H 123 N VAL H 111
LINK O HOH B 502 MG MG C 501 1555 1555 2.02
LINK O HOH B 504 MG MG C 501 1555 1555 2.75
LINK OE2 GLU C 140 MG MG C 501 1555 1555 2.62
LINK O HOH C 601 MG MG D 501 1555 1555 1.79
LINK O TYR D 126 MG MG D 502 1555 1555 2.98
LINK OD2 ASP D 149 MG MG D 502 1555 1555 2.37
LINK MG MG D 501 O HOH J 105 1555 1555 1.82
LINK MG MG D 501 O HOH J 106 1555 1555 2.99
LINK MG MG D 502 OE2 GLU E 140 1555 1555 2.44
LINK MG MG D 502 O HOH E 503 1555 1555 1.90
LINK O HOH E 501 MG MG F 501 1555 1555 2.89
LINK O HOH E 504 MG MG F 501 1555 1555 2.46
LINK OE2 GLU F 140 MG MG F 501 1555 1555 2.68
LINK MG MG F 501 O HOH F 606 1555 1555 2.56
LINK MG MG F 501 O HOH J 111 1555 1555 1.94
LINK O HOH F 601 MG MG G 501 1555 1555 2.84
LINK MG MG G 501 O HOH J 108 1555 1555 2.63
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
ATOM 1 N ALA A 33 178.293 190.284 151.586 1.00 85.46 N
ATOM 2 CA ALA A 33 178.515 190.155 153.054 1.00 86.18 C
ATOM 3 C ALA A 33 178.043 191.407 153.784 1.00 87.27 C
ATOM 4 O ALA A 33 177.306 191.320 154.764 1.00 87.33 O
ATOM 5 CB ALA A 33 179.983 189.893 153.347 1.00 86.11 C
ATOM 6 H ALA A 33 177.429 190.427 151.428 1.00 85.54 H
ATOM 7 HA ALA A 33 178.003 189.401 153.387 1.00 85.09 H
ATOM 8 HB1 ALA A 33 180.250 189.069 152.911 1.00 85.69 H
ATOM 9 HB2 ALA A 33 180.509 190.634 153.006 1.00 86.04 H
ATOM 10 HB3 ALA A 33 180.104 189.815 154.306 1.00 86.44 H
ATOM 11 N GLU A 34 178.468 192.574 153.293 1.00 84.11 N
ATOM 12 CA GLU A 34 178.094 193.828 153.938 1.00 83.13 C
ATOM 13 C GLU A 34 176.583 193.967 154.058 1.00 85.19 C
ATOM 14 O GLU A 34 176.087 194.576 155.015 1.00 84.24 O
ATOM 15 CB GLU A 34 178.689 195.005 153.160 1.00 87.28 C
ATOM 16 CG GLU A 34 178.082 195.244 151.778 1.00 90.67 C
ATOM 17 CD GLU A 34 178.717 194.382 150.705 1.00 90.54 C
ATOM 18 OE1 GLU A 34 179.403 193.399 151.056 1.00 89.03 O
ATOM 19 OE2 GLU A 34 178.528 194.685 149.508 1.00 90.01 O
ATOM 20 H GLU A 34 178.968 192.662 152.599 1.00 85.85 H
ATOM 21 HA GLU A 34 178.468 193.846 154.832 1.00 84.08 H
ATOM 22 HB2 GLU A 34 178.557 195.814 153.680 1.00 86.84 H
ATOM 23 HB3 GLU A 34 179.638 194.848 153.041 1.00 86.93 H
ATOM 24 HG2 GLU A 34 177.132 195.059 151.790 1.00 89.07 H
ATOM 25 HG3 GLU A 34 178.229 196.171 151.533 1.00 89.22 H
ATOM 26 N GLU A 35 175.837 193.406 153.105 1.00 89.60 N
ATOM 27 CA GLU A 35 174.382 193.465 153.175 1.00 87.27 C
ATOM 28 C GLU A 35 173.868 192.780 154.431 1.00 86.86 C
ATOM 29 O GLU A 35 172.874 193.215 155.020 1.00 80.36 O
ATOM 30 CB GLU A 35 173.771 192.829 151.926 1.00 88.48 C
ATOM 31 CG GLU A 35 174.136 191.361 151.727 1.00 91.67 C
ATOM 32 CD GLU A 35 173.136 190.407 152.357 1.00 92.16 C
ATOM 33 OE1 GLU A 35 171.971 190.805 152.563 1.00 90.86 O
ATOM 34 OE2 GLU A 35 173.519 189.254 152.647 1.00 87.47 O
ATOM 35 H GLU A 35 176.146 192.992 152.417 1.00 88.11 H
ATOM 36 HA GLU A 35 174.105 194.394 153.205 1.00 86.12 H
ATOM 37 HB2 GLU A 35 172.806 192.898 151.981 1.00 87.57 H
ATOM 38 HB3 GLU A 35 174.086 193.315 151.148 1.00 88.38 H
ATOM 39 HG2 GLU A 35 174.170 191.172 150.776 1.00 90.24 H
ATOM 40 HG3 GLU A 35 175.003 191.191 152.128 1.00 89.22 H
ATOM 41 N TYR A 36 174.533 191.705 154.860 1.00 89.53 N
ATOM 42 CA TYR A 36 174.094 190.998 156.059 1.00 89.41 C
ATOM 43 C TYR A 36 174.189 191.896 157.286 1.00 83.53 C
ATOM 44 O TYR A 36 173.233 192.005 158.064 1.00 84.29 O
ATOM 45 CB TYR A 36 174.923 189.727 156.252 1.00 91.55 C
ATOM 46 CG TYR A 36 174.952 189.225 157.678 1.00 95.09 C
ATOM 47 CD1 TYR A 36 173.946 188.400 158.165 1.00 95.43 C
ATOM 48 CD2 TYR A 36 175.988 189.569 158.536 1.00 91.74 C
ATOM 49 CE1 TYR A 36 173.969 187.937 159.467 1.00 96.24 C
ATOM 50 CE2 TYR A 36 176.020 189.111 159.840 1.00 91.19 C
ATOM 51 CZ TYR A 36 175.008 188.296 160.300 1.00 93.07 C
ATOM 52 OH TYR A 36 175.036 187.838 161.596 1.00 90.22 O
ATOM 53 H TYR A 36 175.228 191.371 154.479 1.00 88.34 H
ATOM 54 HA TYR A 36 173.166 190.737 155.949 1.00 90.02 H
ATOM 55 HB2 TYR A 36 174.550 189.024 155.697 1.00 90.88 H
ATOM 56 HB3 TYR A 36 175.838 189.905 155.984 1.00 89.67 H
ATOM 57 HD1 TYR A 36 173.244 188.157 157.606 1.00 93.04 H
ATOM 58 HD2 TYR A 36 176.671 190.119 158.229 1.00 90.93 H
ATOM 59 HE1 TYR A 36 173.288 187.387 159.780 1.00 94.96 H
ATOM 60 HE2 TYR A 36 176.719 189.351 160.403 1.00 91.12 H
ATOM 61 HH TYR A 36 175.721 188.126 161.988 1.00 91.77 H
ATOM 62 N GLN A 37 175.337 192.546 157.479 1.00 79.51 N
ATOM 63 CA GLN A 37 175.482 193.451 158.614 1.00 78.84 C
ATOM 64 C GLN A 37 174.514 194.620 158.509 1.00 81.05 C
ATOM 65 O GLN A 37 173.921 195.036 159.511 1.00 81.11 O
ATOM 66 CB GLN A 37 176.921 193.957 158.715 1.00 83.56 C
ATOM 67 CG GLN A 37 177.937 192.890 159.101 1.00 87.35 C
ATOM 68 CD GLN A 37 178.416 192.071 157.920 1.00 90.36 C
ATOM 69 OE1 GLN A 37 178.263 192.473 156.769 1.00 91.57 O
ATOM 70 NE2 GLN A 37 179.002 190.913 158.202 1.00 89.22 N
ATOM 71 H GLN A 37 176.032 192.483 156.977 1.00 84.70 H
ATOM 72 HA GLN A 37 175.278 192.967 159.430 1.00 82.32 H
ATOM 73 HB2 GLN A 37 177.184 194.322 157.856 1.00 84.81 H
ATOM 74 HB3 GLN A 37 176.957 194.653 159.389 1.00 83.13 H
ATOM 75 HG2 GLN A 37 178.710 193.321 159.498 1.00 87.07 H
ATOM 76 HG3 GLN A 37 177.531 192.284 159.739 1.00 87.11 H
ATOM 77 HE21 GLN A 37 179.091 190.665 159.021 1.00 89.40 H
ATOM 78 HE22 GLN A 37 179.291 190.411 157.566 1.00 88.77 H
ATOM 79 N ALA A 38 174.341 195.167 157.304 1.00 82.62 N
ATOM 80 CA ALA A 38 173.410 196.277 157.130 1.00 77.72 C
ATOM 81 C ALA A 38 172.001 195.877 157.551 1.00 76.27 C
ATOM 82 O ALA A 38 171.343 196.588 158.319 1.00 74.81 O
ATOM 83 CB ALA A 38 173.424 196.747 155.676 1.00 81.76 C
ATOM 84 H ALA A 38 174.744 194.919 156.586 1.00 83.22 H
ATOM 85 HA ALA A 38 173.692 197.017 157.689 1.00 78.18 H
ATOM 86 HB1 ALA A 38 174.321 197.037 155.447 1.00 81.76 H
ATOM 87 HB2 ALA A 38 173.158 196.010 155.104 1.00 81.88 H
ATOM 88 HB3 ALA A 38 172.802 197.485 155.577 1.00 81.38 H
ATOM 89 N ILE A 39 171.525 194.728 157.065 1.00 72.56 N
ATOM 90 CA ILE A 39 170.174 194.286 157.390 1.00 66.98 C
ATOM 91 C ILE A 39 170.051 193.995 158.877 1.00 69.34 C
ATOM 92 O ILE A 39 169.059 194.369 159.513 1.00 69.83 O
ATOM 93 CB ILE A 39 169.792 193.064 156.541 1.00 67.46 C
ATOM 94 CG1 ILE A 39 169.620 193.474 155.078 1.00 72.78 C
ATOM 95 CG2 ILE A 39 168.514 192.443 157.061 1.00 66.25 C
ATOM 96 CD1 ILE A 39 169.721 192.327 154.103 1.00 73.57 C
ATOM 97 H ILE A 39 171.961 194.194 156.551 1.00 75.54 H
ATOM 98 HA ILE A 39 169.553 195.000 157.177 1.00 70.04 H
ATOM 99 HB ILE A 39 170.504 192.408 156.599 1.00 72.63 H
ATOM 100 HG12 ILE A 39 168.745 193.879 154.969 1.00 72.52 H
ATOM 101 HG13 ILE A 39 170.309 194.117 154.850 1.00 74.54 H
ATOM 102 HG21 ILE A 39 168.129 191.885 156.368 1.00 67.99 H
ATOM 103 HG22 ILE A 39 167.893 193.151 157.297 1.00 67.93 H
ATOM 104 HG23 ILE A 39 168.716 191.906 157.843 1.00 68.18 H
ATOM 105 HD11 ILE A 39 169.712 192.679 153.199 1.00 76.47 H
ATOM 106 HD12 ILE A 39 170.550 191.850 154.265 1.00 77.52 H
ATOM 107 HD13 ILE A 39 168.966 191.732 154.235 1.00 74.20 H
ATOM 108 N GLN A 40 171.048 193.327 159.458 1.00 72.81 N
ATOM 109 CA GLN A 40 170.977 193.001 160.878 1.00 76.55 C
ATOM 110 C GLN A 40 170.902 194.263 161.725 1.00 76.79 C
ATOM 111 O GLN A 40 170.116 194.336 162.676 1.00 77.53 O
ATOM 112 CB GLN A 40 172.182 192.154 161.284 1.00 77.49 C
ATOM 113 CG GLN A 40 172.227 191.801 162.761 1.00 79.34 C
ATOM 114 CD GLN A 40 171.017 191.007 163.208 1.00 84.61 C
ATOM 115 OE1 GLN A 40 170.954 189.792 163.024 1.00 86.66 O
ATOM 116 NE2 GLN A 40 170.047 191.692 163.802 1.00 83.22 N
ATOM 117 H GLN A 40 171.762 193.057 159.061 1.00 75.30 H
ATOM 118 HA GLN A 40 170.174 192.482 161.042 1.00 76.89 H
ATOM 119 HB2 GLN A 40 172.161 191.323 160.783 1.00 80.43 H
ATOM 120 HB3 GLN A 40 172.992 192.643 161.072 1.00 78.19 H
ATOM 121 HG2 GLN A 40 173.015 191.263 162.930 1.00 80.86 H
ATOM 122 HG3 GLN A 40 172.266 192.615 163.286 1.00 79.28 H
ATOM 123 HE21 GLN A 40 170.126 192.541 163.914 1.00 82.10 H
ATOM 124 HE22 GLN A 40 169.339 191.287 164.074 1.00 83.38 H
ATOM 125 N LYS A 41 171.714 195.270 161.396 1.00 76.68 N
ATOM 126 CA LYS A 41 171.650 196.529 162.128 1.00 75.66 C
ATOM 127 C LYS A 41 170.302 197.207 161.924 1.00 75.29 C
ATOM 128 O LYS A 41 169.739 197.784 162.861 1.00 77.66 O
ATOM 129 CB LYS A 41 172.788 197.450 161.687 1.00 76.45 C
ATOM 130 CG LYS A 41 174.020 197.381 162.578 1.00 77.40 C
ATOM 131 CD LYS A 41 174.612 195.978 162.602 1.00 79.16 C
ATOM 132 CE LYS A 41 175.855 195.909 163.474 1.00 75.35 C
ATOM 133 NZ LYS A 41 176.425 194.534 163.524 1.00 73.97 N
ATOM 134 H LYS A 41 172.299 195.247 160.766 1.00 76.97 H
ATOM 135 HA LYS A 41 171.756 196.351 163.075 1.00 76.33 H
ATOM 136 HB2 LYS A 41 173.059 197.206 160.788 1.00 76.73 H
ATOM 137 HB3 LYS A 41 172.468 198.366 161.696 1.00 76.88 H
ATOM 138 HG2 LYS A 41 174.695 197.990 162.240 1.00 77.55 H
ATOM 139 HG3 LYS A 41 173.773 197.622 163.485 1.00 76.78 H
ATOM 140 HD2 LYS A 41 173.958 195.359 162.960 1.00 78.29 H
ATOM 141 HD3 LYS A 41 174.860 195.721 161.700 1.00 78.56 H
ATOM 142 HE2 LYS A 41 176.531 196.504 163.113 1.00 75.21 H
ATOM 143 HE3 LYS A 41 175.624 196.174 164.379 1.00 75.82 H
ATOM 144 HZ1 LYS A 41 176.656 194.270 162.706 1.00 75.03 H
ATOM 145 HZ2 LYS A 41 175.823 193.966 163.852 1.00 75.35 H
ATOM 146 HZ3 LYS A 41 177.146 194.523 164.046 1.00 73.95 H
ATOM 147 N ALA A 42 169.767 197.146 160.702 1.00 74.38 N
ATOM 148 CA ALA A 42 168.476 197.770 160.428 1.00 74.74 C
ATOM 149 C ALA A 42 167.366 197.125 161.248 1.00 71.19 C
ATOM 150 O ALA A 42 166.476 197.818 161.755 1.00 70.23 O
ATOM 151 CB ALA A 42 168.161 197.684 158.936 1.00 71.64 C
ATOM 152 H ALA A 42 170.126 196.755 160.026 1.00 74.27 H
ATOM 153 HA ALA A 42 168.522 198.708 160.671 1.00 74.33 H
ATOM 154 HB1 ALA A 42 168.856 198.146 158.440 1.00 72.94 H
ATOM 155 HB2 ALA A 42 167.302 198.103 158.770 1.00 70.85 H
ATOM 156 HB3 ALA A 42 168.131 196.751 158.673 1.00 73.19 H
ATOM 157 N LEU A 43 167.400 195.804 161.388 1.00 66.93 N
ATOM 158 CA LEU A 43 166.368 195.078 162.123 1.00 60.60 C
ATOM 159 C LEU A 43 166.447 195.350 163.624 1.00 55.12 C
ATOM 160 O LEU A 43 167.450 195.852 164.128 1.00 49.17 O
ATOM 161 CB LEU A 43 166.493 193.577 161.857 1.00 61.54 C
ATOM 162 CG LEU A 43 166.118 193.109 160.449 1.00 58.76 C
ATOM 163 CD1 LEU A 43 166.590 191.689 160.224 1.00 61.78 C
ATOM 164 CD2 LEU A 43 164.622 193.207 160.229 1.00 57.32 C
ATOM 165 H LEU A 43 168.016 195.300 161.064 1.00 68.50 H
ATOM 166 HA LEU A 43 165.497 195.367 161.811 1.00 62.94 H
ATOM 167 HB2 LEU A 43 167.413 193.315 162.013 1.00 65.32 H
ATOM 168 HB3 LEU A 43 165.915 193.109 162.480 1.00 61.62 H
ATOM 169 HG LEU A 43 166.557 193.679 159.798 1.00 62.95 H
ATOM 170 HD11 LEU A 43 167.554 191.658 160.326 1.00 66.45 H
ATOM 171 HD12 LEU A 43 166.169 191.110 160.878 1.00 62.80 H
ATOM 172 HD13 LEU A 43 166.342 191.413 159.328 1.00 62.67 H
ATOM 173 HD21 LEU A 43 164.405 192.825 159.364 1.00 60.72 H
ATOM 174 HD22 LEU A 43 164.167 192.716 160.931 1.00 58.59 H
ATOM 175 HD23 LEU A 43 164.361 194.139 160.255 1.00 61.55 H
ATOM 176 N TYR A 65 148.867 198.781 168.159 1.00 57.09 N
ATOM 177 CA TYR A 65 149.239 197.775 167.174 1.00 61.51 C
ATOM 178 C TYR A 65 149.928 198.425 165.982 1.00 60.04 C
ATOM 179 O TYR A 65 150.314 199.590 166.044 1.00 61.95 O
ATOM 180 CB TYR A 65 148.008 196.988 166.720 1.00 64.43 C
ATOM 181 CG TYR A 65 146.968 197.818 166.006 1.00 66.56 C
ATOM 182 CD1 TYR A 65 145.949 198.445 166.711 1.00 68.79 C
ATOM 183 CD2 TYR A 65 146.997 197.969 164.626 1.00 67.07 C
ATOM 184 CE1 TYR A 65 144.993 199.203 166.063 1.00 69.37 C
ATOM 185 CE2 TYR A 65 146.045 198.726 163.969 1.00 70.93 C
ATOM 186 CZ TYR A 65 145.045 199.340 164.692 1.00 74.82 C
ATOM 187 OH TYR A 65 144.095 200.093 164.043 1.00 74.78 O
ATOM 188 H TYR A 65 148.287 199.350 167.877 1.00 61.31 H
ATOM 189 HA TYR A 65 149.862 197.151 167.579 1.00 62.02 H
ATOM 190 HB2 TYR A 65 148.288 196.281 166.118 1.00 64.46 H
ATOM 191 HB3 TYR A 65 147.585 196.600 167.502 1.00 64.85 H
ATOM 192 HD1 TYR A 65 145.911 198.355 167.636 1.00 67.79 H
ATOM 193 HD2 TYR A 65 147.670 197.556 164.135 1.00 67.23 H
ATOM 194 HE1 TYR A 65 144.317 199.618 166.549 1.00 68.45 H
ATOM 195 HE2 TYR A 65 146.078 198.819 163.044 1.00 70.23 H
ATOM 196 HH TYR A 65 144.243 200.092 163.216 1.00 73.43 H
ATOM 197 N ILE A 66 150.088 197.668 164.900 1.00 59.09 N
ATOM 198 CA ILE A 66 150.757 198.140 163.695 1.00 62.44 C
ATOM 199 C ILE A 66 149.822 197.942 162.511 1.00 67.27 C
ATOM 200 O ILE A 66 149.232 196.867 162.353 1.00 62.77 O
ATOM 201 CB ILE A 66 152.094 197.412 163.461 1.00 60.29 C
ATOM 202 CG1 ILE A 66 152.850 198.057 162.297 1.00 62.14 C
ATOM 203 CG2 ILE A 66 151.858 195.932 163.196 1.00 59.87 C
ATOM 204 CD1 ILE A 66 154.338 197.797 162.319 1.00 60.22 C
ATOM 205 H ILE A 66 149.812 196.856 164.839 1.00 61.10 H
ATOM 206 HA ILE A 66 150.940 199.089 163.780 1.00 62.50 H
ATOM 207 HB ILE A 66 152.634 197.498 164.262 1.00 60.68 H
ATOM 208 HG12 ILE A 66 152.500 197.706 161.463 1.00 61.84 H
ATOM 209 HG13 ILE A 66 152.717 199.017 162.331 1.00 60.75 H
ATOM 210 HG21 ILE A 66 152.706 195.464 163.255 1.00 61.42 H
ATOM 211 HG22 ILE A 66 151.243 195.585 163.861 1.00 59.88 H
ATOM 212 HG23 ILE A 66 151.482 195.822 162.309 1.00 60.84 H
ATOM 213 HD11 ILE A 66 154.720 198.219 163.105 1.00 60.95 H
ATOM 214 HD12 ILE A 66 154.735 198.170 161.517 1.00 60.71 H
ATOM 215 HD13 ILE A 66 154.491 196.840 162.350 1.00 59.79 H
ATOM 216 N GLU A 67 149.686 198.978 161.686 1.00 73.60 N
ATOM 217 CA GLU A 67 148.815 198.904 160.521 1.00 70.14 C
ATOM 218 C GLU A 67 149.341 197.881 159.521 1.00 65.80 C
ATOM 219 O GLU A 67 150.551 197.732 159.334 1.00 66.28 O
ATOM 220 CB GLU A 67 148.698 200.277 159.861 1.00 73.72 C
ATOM 221 CG GLU A 67 148.262 201.388 160.808 1.00 76.15 C
ATOM 222 CD GLU A 67 149.426 202.201 161.344 1.00 79.35 C
ATOM 223 OE1 GLU A 67 150.488 201.611 161.630 1.00 74.37 O
ATOM 224 OE2 GLU A 67 149.279 203.434 161.480 1.00 76.35 O
ATOM 225 H GLU A 67 150.088 199.732 161.781 1.00 70.79 H
ATOM 226 HA GLU A 67 147.929 198.626 160.801 1.00 68.73 H
ATOM 227 HB2 GLU A 67 149.562 200.521 159.495 1.00 73.59 H
ATOM 228 HB3 GLU A 67 148.044 200.224 159.147 1.00 72.73 H
ATOM 229 HG2 GLU A 67 147.668 201.991 160.335 1.00 75.66 H
ATOM 230 HG3 GLU A 67 147.800 200.994 161.565 1.00 73.50 H
ATOM 231 N GLY A 68 148.416 197.185 158.866 1.00 59.73 N
ATOM 232 CA GLY A 68 148.753 196.059 158.018 1.00 58.96 C
ATOM 233 C GLY A 68 149.762 196.338 156.921 1.00 65.90 C
ATOM 234 O GLY A 68 150.886 195.831 156.971 1.00 68.56 O
ATOM 235 H GLY A 68 147.573 197.352 158.901 1.00 63.61 H
ATOM 236 HA2 GLY A 68 149.111 195.349 158.573 1.00 62.24 H
ATOM 237 HA3 GLY A 68 147.943 195.729 157.599 1.00 60.74 H
ATOM 238 N HIS A 69 149.381 197.142 155.924 1.00 63.60 N
ATOM 239 CA HIS A 69 150.227 197.307 154.745 1.00 61.89 C
ATOM 240 C HIS A 69 151.573 197.932 155.076 1.00 61.10 C
ATOM 241 O HIS A 69 152.521 197.788 154.295 1.00 59.62 O
ATOM 242 CB HIS A 69 149.513 198.151 153.693 1.00 66.02 C
ATOM 243 CG HIS A 69 149.929 197.836 152.289 1.00 68.32 C
ATOM 244 ND1 HIS A 69 151.209 198.051 151.827 1.00 67.66 N
ATOM 245 CD2 HIS A 69 149.235 197.318 151.249 1.00 69.87 C
ATOM 246 CE1 HIS A 69 151.286 197.680 150.561 1.00 68.85 C
ATOM 247 NE2 HIS A 69 150.102 197.232 150.186 1.00 71.35 N
ATOM 248 H HIS A 69 148.650 197.595 155.907 1.00 64.02 H
ATOM 249 HA HIS A 69 150.393 196.437 154.355 1.00 63.54 H
ATOM 250 HB2 HIS A 69 148.558 197.996 153.762 1.00 65.90 H
ATOM 251 HB3 HIS A 69 149.708 199.087 153.858 1.00 66.31 H
ATOM 252 HD2 HIS A 69 148.339 197.068 151.252 1.00 69.00 H
ATOM 253 HE1 HIS A 69 152.045 197.727 150.025 1.00 68.43 H
ATOM 254 HE2 HIS A 69 149.905 196.934 149.403 1.00 70.91 H
ATOM 255 N ARG A 70 151.688 198.615 156.214 1.00 62.64 N
ATOM 256 CA ARG A 70 152.979 199.180 156.587 1.00 66.30 C
ATOM 257 C ARG A 70 154.008 198.084 156.829 1.00 64.81 C
ATOM 258 O ARG A 70 155.185 198.252 156.500 1.00 63.65 O
ATOM 259 CB ARG A 70 152.832 200.067 157.822 1.00 70.53 C
ATOM 260 CG ARG A 70 151.986 201.307 157.585 1.00 71.26 C
ATOM 261 CD ARG A 70 151.861 202.141 158.845 1.00 75.95 C
ATOM 262 NE ARG A 70 153.139 202.713 159.252 1.00 80.32 N
ATOM 263 CZ ARG A 70 153.619 203.872 158.821 1.00 76.72 C
ATOM 264 NH1 ARG A 70 152.953 204.619 157.955 1.00 78.71 N
ATOM 265 NH2 ARG A 70 154.798 204.292 159.270 1.00 71.39 N
ATOM 266 H ARG A 70 151.051 198.762 156.773 1.00 64.38 H
ATOM 267 HA ARG A 70 153.300 199.735 155.859 1.00 66.47 H
ATOM 268 HB2 ARG A 70 152.411 199.553 158.529 1.00 68.56 H
ATOM 269 HB3 ARG A 70 153.713 200.358 158.106 1.00 70.53 H
ATOM 270 HG2 ARG A 70 152.403 201.852 156.899 1.00 72.08 H
ATOM 271 HG3 ARG A 70 151.096 201.040 157.307 1.00 69.62 H
ATOM 272 HD2 ARG A 70 151.231 202.863 158.694 1.00 75.97 H
ATOM 273 HD3 ARG A 70 151.550 201.571 159.562 1.00 74.27 H
ATOM 274 HE ARG A 70 153.604 202.279 159.831 1.00 77.89 H
ATOM 275 HH11 ARG A 70 152.190 204.361 157.655 1.00 77.97 H
ATOM 276 HH12 ARG A 70 153.286 205.367 157.691 1.00 77.95 H
ATOM 277 HH21 ARG A 70 155.239 203.815 159.833 1.00 73.18 H
ATOM 278 HH22 ARG A 70 155.119 205.042 158.998 1.00 72.85 H
ATOM 279 N VAL A 71 153.586 196.949 157.389 1.00 63.50 N
ATOM 280 CA VAL A 71 154.525 195.856 157.622 1.00 56.56 C
ATOM 281 C VAL A 71 154.958 195.225 156.303 1.00 52.70 C
ATOM 282 O VAL A 71 156.123 194.848 156.139 1.00 59.23 O
ATOM 283 CB VAL A 71 153.913 194.819 158.578 1.00 54.28 C
ATOM 284 CG1 VAL A 71 154.837 193.626 158.724 1.00 51.97 C
ATOM 285 CG2 VAL A 71 153.656 195.453 159.929 1.00 57.62 C
ATOM 286 H VAL A 71 152.778 196.791 157.638 1.00 62.71 H
ATOM 287 HA VAL A 71 155.318 196.215 158.048 1.00 58.96 H
ATOM 288 HB VAL A 71 153.067 194.510 158.219 1.00 57.47 H
ATOM 289 HG11 VAL A 71 154.785 193.082 157.923 1.00 54.14 H
ATOM 290 HG12 VAL A 71 154.557 193.105 159.493 1.00 55.05 H
ATOM 291 HG13 VAL A 71 155.744 193.943 158.854 1.00 54.16 H
ATOM 292 HG21 VAL A 71 154.491 195.806 160.274 1.00 57.58 H
ATOM 293 HG22 VAL A 71 153.307 194.779 160.532 1.00 59.84 H
ATOM 294 HG23 VAL A 71 153.011 196.169 159.824 1.00 59.60 H
ATOM 295 N ILE A 72 154.038 195.087 155.348 1.00 51.03 N
ATOM 296 CA ILE A 72 154.420 194.550 154.045 1.00 56.42 C
ATOM 297 C ILE A 72 155.365 195.506 153.328 1.00 58.84 C
ATOM 298 O ILE A 72 156.273 195.075 152.606 1.00 59.32 O
ATOM 299 CB ILE A 72 153.176 194.235 153.194 1.00 57.53 C
ATOM 300 CG1 ILE A 72 152.334 193.143 153.862 1.00 58.34 C
ATOM 301 CG2 ILE A 72 153.587 193.822 151.780 1.00 52.91 C
ATOM 302 CD1 ILE A 72 151.297 193.646 154.838 1.00 60.87 C
ATOM 303 H ILE A 72 153.210 195.302 155.424 1.00 57.05 H
ATOM 304 HA ILE A 72 154.898 193.718 154.183 1.00 56.72 H
ATOM 305 HB ILE A 72 152.638 195.039 153.132 1.00 59.62 H
ATOM 306 HG12 ILE A 72 151.868 192.643 153.173 1.00 57.40 H
ATOM 307 HG13 ILE A 72 152.927 192.549 154.348 1.00 58.10 H
ATOM 308 HG21 ILE A 72 153.915 194.600 151.303 1.00 54.65 H
ATOM 309 HG22 ILE A 72 152.814 193.459 151.320 1.00 54.37 H
ATOM 310 HG23 ILE A 72 154.282 193.148 151.838 1.00 54.91 H
ATOM 311 HD11 ILE A 72 150.710 192.911 155.075 1.00 59.84 H
ATOM 312 HD12 ILE A 72 151.738 193.980 155.633 1.00 60.14 H
ATOM 313 HD13 ILE A 72 150.784 194.350 154.415 1.00 61.31 H
ATOM 314 N ASN A 73 155.162 196.814 153.491 1.00 61.14 N
ATOM 315 CA ASN A 73 156.121 197.769 152.943 1.00 58.50 C
ATOM 316 C ASN A 73 157.471 197.653 153.642 1.00 60.58 C
ATOM 317 O ASN A 73 158.522 197.735 152.996 1.00 62.13 O
ATOM 318 CB ASN A 73 155.577 199.191 153.059 1.00 58.27 C
ATOM 319 CG ASN A 73 154.922 199.669 151.779 1.00 62.46 C
ATOM 320 OD1 ASN A 73 154.718 198.895 150.845 1.00 62.26 O
ATOM 321 ND2 ASN A 73 154.591 200.954 151.729 1.00 68.76 N
ATOM 322 H ASN A 73 154.495 197.164 153.905 1.00 60.81 H
ATOM 323 HA ASN A 73 156.259 197.571 152.004 1.00 59.31 H
ATOM 324 HB2 ASN A 73 154.913 199.221 153.766 1.00 59.94 H
ATOM 325 HB3 ASN A 73 156.309 199.794 153.264 1.00 60.26 H
ATOM 326 HD21 ASN A 73 154.750 201.466 152.402 1.00 66.13 H
ATOM 327 HD22 ASN A 73 154.217 201.274 151.024 1.00 67.32 H
ATOM 328 N LEU A 74 157.463 197.465 154.965 1.00 57.26 N
ATOM 329 CA LEU A 74 158.713 197.302 155.700 1.00 54.69 C
ATOM 330 C LEU A 74 159.483 196.089 155.201 1.00 53.71 C
ATOM 331 O LEU A 74 160.690 196.166 154.942 1.00 56.49 O
ATOM 332 CB LEU A 74 158.430 197.170 157.197 1.00 52.16 C
ATOM 333 CG LEU A 74 158.053 198.439 157.955 1.00 53.18 C
ATOM 334 CD1 LEU A 74 157.574 198.095 159.350 1.00 53.09 C
ATOM 335 CD2 LEU A 74 159.230 199.397 158.019 1.00 54.71 C
ATOM 336 H LEU A 74 156.755 197.428 155.451 1.00 57.43 H
ATOM 337 HA LEU A 74 159.266 198.086 155.563 1.00 56.10 H
ATOM 338 HB2 LEU A 74 157.703 196.539 157.313 1.00 54.23 H
ATOM 339 HB3 LEU A 74 159.229 196.818 157.619 1.00 54.60 H
ATOM 340 HG LEU A 74 157.329 198.885 157.489 1.00 56.12 H
ATOM 341 HD11 LEU A 74 157.355 198.916 159.819 1.00 54.13 H
ATOM 342 HD12 LEU A 74 158.282 197.626 159.819 1.00 53.77 H
ATOM 343 HD13 LEU A 74 156.789 197.530 159.285 1.00 56.01 H
ATOM 344 HD21 LEU A 74 158.995 200.146 158.589 1.00 55.02 H
ATOM 345 HD22 LEU A 74 159.431 199.712 157.125 1.00 55.16 H
ATOM 346 HD23 LEU A 74 159.996 198.930 158.387 1.00 54.59 H
ATOM 347 N ALA A 75 158.797 194.956 155.054 1.00 50.55 N
ATOM 348 CA ALA A 75 159.451 193.765 154.530 1.00 56.49 C
ATOM 349 C ALA A 75 159.961 194.008 153.117 1.00 56.84 C
ATOM 350 O ALA A 75 161.024 193.507 152.736 1.00 58.54 O
ATOM 351 CB ALA A 75 158.486 192.580 154.558 1.00 56.29 C
ATOM 352 H ALA A 75 157.965 194.854 155.248 1.00 55.02 H
ATOM 353 HA ALA A 75 160.211 193.547 155.091 1.00 56.79 H
ATOM 354 HB1 ALA A 75 158.211 192.419 155.474 1.00 56.25 H
ATOM 355 HB2 ALA A 75 157.712 192.790 154.012 1.00 56.61 H
ATOM 356 HB3 ALA A 75 158.937 191.797 154.205 1.00 56.62 H
ATOM 357 N ASN A 76 159.213 194.774 152.327 1.00 50.90 N
ATOM 358 CA ASN A 76 159.655 195.090 150.976 1.00 55.35 C
ATOM 359 C ASN A 76 160.939 195.913 150.995 1.00 55.98 C
ATOM 360 O ASN A 76 161.839 195.693 150.176 1.00 56.93 O
ATOM 361 CB ASN A 76 158.548 195.832 150.232 1.00 55.32 C
ATOM 362 CG ASN A 76 157.764 194.927 149.312 1.00 53.82 C
ATOM 363 OD1 ASN A 76 158.337 194.160 148.541 1.00 56.81 O
ATOM 364 ND2 ASN A 76 156.442 195.001 149.397 1.00 56.95 N
ATOM 365 H ASN A 76 158.456 195.118 152.548 1.00 54.05 H
ATOM 366 HA ASN A 76 159.836 194.264 150.501 1.00 55.69 H
ATOM 367 HB2 ASN A 76 157.931 196.214 150.876 1.00 56.49 H
ATOM 368 HB3 ASN A 76 158.944 196.535 149.695 1.00 56.21 H
ATOM 369 HD21 ASN A 76 156.076 195.548 149.951 1.00 56.86 H
ATOM 370 HD22 ASN A 76 155.951 194.505 148.895 1.00 56.58 H
ATOM 371 N GLU A 77 161.038 196.878 151.911 1.00 55.90 N
ATOM 372 CA GLU A 77 162.243 197.695 151.998 1.00 56.36 C
ATOM 373 C GLU A 77 163.397 196.936 152.644 1.00 59.88 C
ATOM 374 O GLU A 77 164.535 197.012 152.167 1.00 62.78 O
ATOM 375 CB GLU A 77 161.952 198.974 152.782 1.00 61.07 C
ATOM 376 CG GLU A 77 161.003 199.932 152.077 1.00 67.38 C
ATOM 377 CD GLU A 77 161.569 200.463 150.775 1.00 72.44 C
ATOM 378 OE1 GLU A 77 162.804 200.627 150.684 1.00 71.72 O
ATOM 379 OE2 GLU A 77 160.779 200.718 149.841 1.00 76.27 O
ATOM 380 H GLU A 77 160.429 197.076 152.485 1.00 57.53 H
ATOM 381 HA GLU A 77 162.518 197.945 151.103 1.00 59.56 H
ATOM 382 HB2 GLU A 77 161.552 198.734 153.632 1.00 59.79 H
ATOM 383 HB3 GLU A 77 162.787 199.444 152.933 1.00 62.87 H
ATOM 384 HG2 GLU A 77 160.175 199.467 151.877 1.00 63.68 H
ATOM 385 HG3 GLU A 77 160.827 200.688 152.659 1.00 66.84 H
ATOM 386 N MET A 78 163.126 196.202 153.725 1.00 61.04 N
ATOM 387 CA MET A 78 164.199 195.540 154.462 1.00 49.96 C
ATOM 388 C MET A 78 164.883 194.481 153.609 1.00 51.93 C
ATOM 389 O MET A 78 166.116 194.397 153.576 1.00 49.70 O
ATOM 390 CB MET A 78 163.644 194.915 155.738 1.00 44.50 C
ATOM 391 CG MET A 78 164.702 194.476 156.717 1.00 45.11 C
ATOM 392 SD MET A 78 165.448 195.845 157.610 1.00 45.61 S
ATOM 393 CE MET A 78 164.050 196.440 158.549 1.00 45.63 C
ATOM 394 H MET A 78 162.339 196.074 154.048 1.00 57.42 H
ATOM 395 HA MET A 78 164.856 196.205 154.719 1.00 52.22 H
ATOM 396 HB2 MET A 78 163.076 195.564 156.181 1.00 49.80 H
ATOM 397 HB3 MET A 78 163.122 194.133 155.499 1.00 49.22 H
ATOM 398 HG2 MET A 78 164.299 193.880 157.367 1.00 48.45 H
ATOM 399 HG3 MET A 78 165.406 194.013 156.237 1.00 49.32 H
ATOM 400 HE1 MET A 78 164.373 197.011 159.263 1.00 51.09 H
ATOM 401 HE2 MET A 78 163.467 196.945 157.960 1.00 48.48 H
ATOM 402 HE3 MET A 78 163.571 195.683 158.919 1.00 48.63 H
ATOM 403 N PHE A 79 164.097 193.664 152.904 1.00 54.08 N
ATOM 404 CA PHE A 79 164.631 192.539 152.151 1.00 51.24 C
ATOM 405 C PHE A 79 164.478 192.668 150.645 1.00 53.03 C
ATOM 406 O PHE A 79 165.191 191.977 149.912 1.00 60.67 O
ATOM 407 CB PHE A 79 163.959 191.237 152.602 1.00 49.84 C
ATOM 408 CG PHE A 79 163.967 191.038 154.085 1.00 51.04 C
ATOM 409 CD1 PHE A 79 165.159 190.885 154.770 1.00 57.33 C
ATOM 410 CD2 PHE A 79 162.784 191.008 154.797 1.00 53.70 C
ATOM 411 CE1 PHE A 79 165.169 190.702 156.138 1.00 61.21 C
ATOM 412 CE2 PHE A 79 162.786 190.825 156.164 1.00 57.38 C
ATOM 413 CZ PHE A 79 163.980 190.672 156.836 1.00 59.50 C
ATOM 414 H PHE A 79 163.242 193.745 152.849 1.00 53.91 H
ATOM 415 HA PHE A 79 165.579 192.458 152.341 1.00 53.60 H
ATOM 416 HB2 PHE A 79 163.035 191.244 152.309 1.00 53.22 H
ATOM 417 HB3 PHE A 79 164.426 190.488 152.199 1.00 51.96 H
ATOM 418 HD1 PHE A 79 165.963 190.904 154.303 1.00 56.54 H
ATOM 419 HD2 PHE A 79 161.975 191.110 154.349 1.00 54.19 H
ATOM 420 HE1 PHE A 79 165.976 190.599 156.588 1.00 59.36 H
ATOM 421 HE2 PHE A 79 161.983 190.806 156.632 1.00 56.38 H
ATOM 422 HZ PHE A 79 163.984 190.549 157.758 1.00 59.02 H
ATOM 423 N GLY A 80 163.582 193.518 150.166 1.00 47.40 N
ATOM 424 CA GLY A 80 163.425 193.726 148.745 1.00 50.42 C
ATOM 425 C GLY A 80 162.228 192.981 148.181 1.00 55.64 C
ATOM 426 O GLY A 80 161.687 192.052 148.785 1.00 61.53 O
ATOM 427 H GLY A 80 163.049 193.988 150.651 1.00 52.29 H
ATOM 428 HA2 GLY A 80 163.309 194.672 148.566 1.00 53.32 H
ATOM 429 HA3 GLY A 80 164.221 193.424 148.281 1.00 52.07 H
ATOM 430 N TYR A 81 161.814 193.403 146.986 1.00 60.80 N
ATOM 431 CA TYR A 81 160.626 192.825 146.368 1.00 65.83 C
ATOM 432 C TYR A 81 160.825 191.356 146.026 1.00 66.44 C
ATOM 433 O TYR A 81 159.855 190.591 145.997 1.00 68.87 O
ATOM 434 CB TYR A 81 160.254 193.623 145.118 1.00 68.17 C
ATOM 435 CG TYR A 81 161.048 193.259 143.885 1.00 71.23 C
ATOM 436 CD1 TYR A 81 160.618 192.256 143.025 1.00 75.31 C
ATOM 437 CD2 TYR A 81 162.230 193.918 143.580 1.00 74.72 C
ATOM 438 CE1 TYR A 81 161.341 191.923 141.897 1.00 77.75 C
ATOM 439 CE2 TYR A 81 162.961 193.591 142.454 1.00 80.10 C
ATOM 440 CZ TYR A 81 162.513 192.593 141.616 1.00 81.04 C
ATOM 441 OH TYR A 81 163.237 192.264 140.494 1.00 82.31 O
ATOM 442 H TYR A 81 162.199 194.014 146.519 1.00 61.80 H
ATOM 443 HA TYR A 81 159.887 192.888 146.993 1.00 64.15 H
ATOM 444 HB2 TYR A 81 159.317 193.469 144.920 1.00 68.56 H
ATOM 445 HB3 TYR A 81 160.400 194.565 145.295 1.00 66.90 H
ATOM 446 HD1 TYR A 81 159.828 191.803 143.212 1.00 74.50 H
ATOM 447 HD2 TYR A 81 162.536 194.592 144.143 1.00 72.76 H
ATOM 448 HE1 TYR A 81 161.040 191.249 141.331 1.00 77.30 H
ATOM 449 HE2 TYR A 81 163.752 194.042 142.262 1.00 79.06 H
ATOM 450 HH TYR A 81 163.912 192.761 140.431 1.00 81.47 H
ATOM 451 N ASN A 82 162.065 190.941 145.767 1.00 66.09 N
ATOM 452 CA ASN A 82 162.376 189.561 145.415 1.00 67.83 C
ATOM 453 C ASN A 82 163.191 188.856 146.494 1.00 57.41 C
ATOM 454 O ASN A 82 163.881 187.876 146.201 1.00 54.13 O
ATOM 455 CB ASN A 82 163.115 189.515 144.078 1.00 72.52 C
ATOM 456 CG ASN A 82 164.464 190.208 144.129 1.00 77.65 C
ATOM 457 OD1 ASN A 82 164.923 190.628 145.191 1.00 75.35 O
ATOM 458 ND2 ASN A 82 165.107 190.331 142.974 1.00 78.88 N
ATOM 459 H ASN A 82 162.756 191.453 145.790 1.00 66.98 H
ATOM 460 HA ASN A 82 161.547 189.070 145.308 1.00 67.75 H
ATOM 461 HB2 ASN A 82 163.264 188.588 143.831 1.00 71.32 H
ATOM 462 HB3 ASN A 82 162.576 189.955 143.403 1.00 71.96 H
ATOM 463 HD21 ASN A 82 164.755 190.026 142.251 1.00 76.65 H
ATOM 464 HD22 ASN A 82 165.875 190.717 142.948 1.00 77.06 H
ATOM 465 N GLY A 83 163.128 189.334 147.731 1.00 51.79 N
ATOM 466 CA GLY A 83 163.935 188.770 148.792 1.00 52.14 C
ATOM 467 C GLY A 83 163.166 187.917 149.777 1.00 49.31 C
ATOM 468 O GLY A 83 163.766 187.324 150.678 1.00 48.65 O
ATOM 469 H GLY A 83 162.625 189.986 147.978 1.00 56.49 H
ATOM 470 HA2 GLY A 83 164.639 188.225 148.408 1.00 54.60 H
ATOM 471 HA3 GLY A 83 164.352 189.493 149.286 1.00 53.50 H
ATOM 472 N TRP A 84 161.846 187.841 149.630 1.00 47.26 N
ATOM 473 CA TRP A 84 161.029 187.130 150.601 1.00 49.98 C
ATOM 474 C TRP A 84 159.784 186.588 149.916 1.00 49.32 C
ATOM 475 O TRP A 84 159.402 187.035 148.831 1.00 52.27 O
ATOM 476 CB TRP A 84 160.641 188.043 151.765 1.00 49.11 C
ATOM 477 CG TRP A 84 159.688 189.121 151.368 1.00 56.02 C
ATOM 478 CD1 TRP A 84 159.895 190.100 150.443 1.00 56.15 C
ATOM 479 CD2 TRP A 84 158.377 189.339 151.898 1.00 53.35 C
ATOM 480 NE1 TRP A 84 158.789 190.909 150.355 1.00 55.48 N
ATOM 481 CE2 TRP A 84 157.844 190.464 151.241 1.00 55.30 C
ATOM 482 CE3 TRP A 84 157.600 188.691 152.863 1.00 51.33 C
ATOM 483 CZ2 TRP A 84 156.572 190.953 151.516 1.00 61.56 C
ATOM 484 CZ3 TRP A 84 156.338 189.179 153.134 1.00 50.09 C
ATOM 485 CH2 TRP A 84 155.836 190.299 152.464 1.00 55.51 C
ATOM 486 H TRP A 84 161.403 188.191 148.981 1.00 51.22 H
ATOM 487 HA TRP A 84 161.530 186.380 150.957 1.00 51.25 H
ATOM 488 HB2 TRP A 84 160.219 187.510 152.456 1.00 50.69 H
ATOM 489 HB3 TRP A 84 161.441 188.465 152.114 1.00 50.92 H
ATOM 490 HD1 TRP A 84 160.669 190.201 149.937 1.00 55.64 H
ATOM 491 HE1 TRP A 84 158.705 191.587 149.833 1.00 56.06 H
ATOM 492 HE3 TRP A 84 157.927 187.945 153.312 1.00 53.13 H
ATOM 493 HZ2 TRP A 84 156.235 191.698 151.073 1.00 58.80 H
ATOM 494 HZ3 TRP A 84 155.812 188.755 153.774 1.00 52.92 H
ATOM 495 HH2 TRP A 84 154.982 190.605 152.668 1.00 55.99 H
ATOM 496 N ALA A 85 159.156 185.610 150.564 1.00 37.95 N
ATOM 497 CA ALA A 85 157.925 185.025 150.055 1.00 36.51 C
ATOM 498 C ALA A 85 157.174 184.391 151.213 1.00 38.47 C
ATOM 499 O ALA A 85 157.728 184.178 152.294 1.00 40.97 O
ATOM 500 CB ALA A 85 158.201 183.995 148.958 1.00 37.88 C
ATOM 501 H ALA A 85 159.426 185.267 151.305 1.00 41.60 H
ATOM 502 HA ALA A 85 157.369 185.726 149.680 1.00 40.59 H
ATOM 503 HB1 ALA A 85 158.664 184.431 148.225 1.00 39.12 H
ATOM 504 HB2 ALA A 85 157.357 183.632 148.647 1.00 39.08 H
ATOM 505 HB3 ALA A 85 158.752 183.285 149.323 1.00 39.19 H
ATOM 506 N HIS A 86 155.900 184.092 150.971 1.00 39.91 N
ATOM 507 CA HIS A 86 155.042 183.505 151.989 1.00 35.05 C
ATOM 508 C HIS A 86 154.070 182.539 151.331 1.00 31.72 C
ATOM 509 O HIS A 86 153.851 182.572 150.119 1.00 35.23 O
ATOM 510 CB HIS A 86 154.291 184.583 152.779 1.00 37.62 C
ATOM 511 CG HIS A 86 153.405 185.446 151.935 1.00 43.50 C
ATOM 512 ND1 HIS A 86 152.099 185.119 151.647 1.00 44.53 N
ATOM 513 CD2 HIS A 86 153.644 186.625 151.312 1.00 45.84 C
ATOM 514 CE1 HIS A 86 151.570 186.061 150.886 1.00 39.99 C
ATOM 515 NE2 HIS A 86 152.487 186.985 150.667 1.00 38.07 N
ATOM 516 H HIS A 86 155.507 184.221 150.217 1.00 39.36 H
ATOM 517 HA HIS A 86 155.589 183.003 152.612 1.00 37.53 H
ATOM 518 HB2 HIS A 86 153.734 184.151 153.445 1.00 37.65 H
ATOM 519 HB3 HIS A 86 154.938 185.159 153.216 1.00 40.26 H
ATOM 520 HD2 HIS A 86 154.443 187.101 151.320 1.00 44.58 H
ATOM 521 HE1 HIS A 86 150.699 186.070 150.558 1.00 40.06 H
ATOM 522 HE2 HIS A 86 152.377 187.697 150.198 1.00 40.11 H
ATOM 523 N SER A 87 153.508 181.655 152.149 1.00 36.13 N
ATOM 524 CA SER A 87 152.551 180.671 151.671 1.00 36.36 C
ATOM 525 C SER A 87 151.713 180.200 152.848 1.00 36.39 C
ATOM 526 O SER A 87 152.136 180.274 154.004 1.00 39.95 O
ATOM 527 CB SER A 87 153.252 179.491 150.995 1.00 43.75 C
ATOM 528 OG SER A 87 154.219 179.945 150.064 1.00 44.98 O
ATOM 529 H SER A 87 153.669 181.606 152.992 1.00 37.76 H
ATOM 530 HA SER A 87 151.960 181.086 151.024 1.00 37.41 H
ATOM 531 HB2 SER A 87 153.695 178.957 151.673 1.00 41.65 H
ATOM 532 HB3 SER A 87 152.592 178.956 150.529 1.00 41.58 H
ATOM 533 HG SER A 87 154.604 179.289 149.706 1.00 43.17 H
ATOM 534 N ILE A 88 150.518 179.713 152.536 1.00 39.26 N
ATOM 535 CA ILE A 88 149.552 179.275 153.535 1.00 37.65 C
ATOM 536 C ILE A 88 149.633 177.760 153.637 1.00 42.34 C
ATOM 537 O ILE A 88 149.609 177.060 152.617 1.00 48.00 O
ATOM 538 CB ILE A 88 148.131 179.733 153.167 1.00 41.51 C
ATOM 539 CG1 ILE A 88 147.186 179.562 154.352 1.00 45.91 C
ATOM 540 CG2 ILE A 88 147.608 178.957 151.964 1.00 49.49 C
ATOM 541 CD1 ILE A 88 147.387 180.585 155.431 1.00 43.15 C
ATOM 542 H ILE A 88 150.238 179.624 151.728 1.00 40.17 H
ATOM 543 HA ILE A 88 149.783 179.653 154.397 1.00 39.35 H
ATOM 544 HB ILE A 88 148.164 180.673 152.932 1.00 41.24 H
ATOM 545 HG12 ILE A 88 146.272 179.639 154.036 1.00 45.97 H
ATOM 546 HG13 ILE A 88 147.326 178.686 154.744 1.00 44.71 H
ATOM 547 HG21 ILE A 88 146.848 179.430 151.591 1.00 46.68 H
ATOM 548 HG22 ILE A 88 148.312 178.890 151.300 1.00 46.26 H
ATOM 549 HG23 ILE A 88 147.338 178.071 152.250 1.00 46.64 H
ATOM 550 HD11 ILE A 88 146.522 180.821 155.799 1.00 44.59 H
ATOM 551 HD12 ILE A 88 147.953 180.211 156.123 1.00 42.96 H
ATOM 552 HD13 ILE A 88 147.804 181.372 155.047 1.00 42.56 H
ATOM 553 N THR A 89 149.737 177.250 154.862 1.00 45.32 N
ATOM 554 CA THR A 89 149.970 175.829 155.089 1.00 44.86 C
ATOM 555 C THR A 89 148.723 175.092 155.560 1.00 47.70 C
ATOM 556 O THR A 89 148.348 174.076 154.968 1.00 49.93 O
ATOM 557 CB THR A 89 151.098 175.637 156.110 1.00 48.33 C
ATOM 558 OG1 THR A 89 150.619 175.948 157.422 1.00 52.66 O
ATOM 559 CG2 THR A 89 152.283 176.530 155.778 1.00 44.00 C
ATOM 560 H THR A 89 149.676 177.713 155.585 1.00 44.98 H
ATOM 561 HA THR A 89 150.256 175.422 154.257 1.00 45.43 H
ATOM 562 HB THR A 89 151.396 174.714 156.088 1.00 48.53 H
ATOM 563 HG1 THR A 89 151.236 175.847 157.984 1.00 52.15 H
ATOM 564 HG21 THR A 89 153.030 176.316 156.359 1.00 45.68 H
ATOM 565 HG22 THR A 89 152.552 176.393 154.856 1.00 43.76 H
ATOM 566 HG23 THR A 89 152.045 177.462 155.902 1.00 45.31 H
ATOM 567 N GLN A 90 148.075 175.574 156.616 1.00 46.43 N
ATOM 568 CA GLN A 90 146.906 174.918 157.181 1.00 44.05 C
ATOM 569 C GLN A 90 145.822 175.943 157.471 1.00 49.32 C
ATOM 570 O GLN A 90 146.110 177.062 157.905 1.00 49.01 O
ATOM 571 CB GLN A 90 147.262 174.166 158.463 1.00 45.61 C
ATOM 572 CG GLN A 90 146.119 173.365 159.048 1.00 49.78 C
ATOM 573 CD GLN A 90 146.542 172.537 160.243 1.00 57.27 C
ATOM 574 OE1 GLN A 90 147.698 172.580 160.663 1.00 56.60 O
ATOM 575 NE2 GLN A 90 145.606 171.777 160.798 1.00 59.35 N
ATOM 576 H GLN A 90 148.299 176.295 157.029 1.00 46.70 H
ATOM 577 HA GLN A 90 146.554 174.279 156.542 1.00 46.93 H
ATOM 578 HB2 GLN A 90 147.987 173.550 158.271 1.00 47.53 H
ATOM 579 HB3 GLN A 90 147.547 174.808 159.132 1.00 47.85 H
ATOM 580 HG2 GLN A 90 145.421 173.973 159.338 1.00 50.03 H
ATOM 581 HG3 GLN A 90 145.775 172.762 158.371 1.00 50.67 H
ATOM 582 HE21 GLN A 90 144.808 171.773 160.476 1.00 57.45 H
ATOM 583 HE22 GLN A 90 145.797 171.288 161.479 1.00 58.46 H
ATOM 584 N GLN A 91 144.574 175.549 157.229 1.00 51.39 N
ATOM 585 CA GLN A 91 143.407 176.361 157.537 1.00 41.16 C
ATOM 586 C GLN A 91 142.401 175.507 158.289 1.00 41.30 C
ATOM 587 O GLN A 91 142.293 174.301 158.058 1.00 45.71 O
ATOM 588 CB GLN A 91 142.764 176.927 156.273 1.00 39.06 C
ATOM 589 CG GLN A 91 143.619 177.939 155.545 1.00 45.93 C
ATOM 590 CD GLN A 91 142.800 179.053 154.928 1.00 53.08 C
ATOM 591 OE1 GLN A 91 142.161 179.834 155.633 1.00 45.08 O
ATOM 592 NE2 GLN A 91 142.816 179.135 153.602 1.00 51.59 N
ATOM 593 H GLN A 91 144.375 174.790 156.875 1.00 49.36 H
ATOM 594 HA GLN A 91 143.668 177.101 158.107 1.00 43.78 H
ATOM 595 HB2 GLN A 91 142.585 176.196 155.661 1.00 42.62 H
ATOM 596 HB3 GLN A 91 141.932 177.362 156.516 1.00 42.27 H
ATOM 597 HG2 GLN A 91 144.242 178.337 156.173 1.00 45.88 H
ATOM 598 HG3 GLN A 91 144.103 177.492 154.834 1.00 45.10 H
ATOM 599 HE21 GLN A 91 143.274 178.571 153.142 1.00 49.51 H
ATOM 600 HE22 GLN A 91 142.367 179.751 153.204 1.00 48.94 H
ATOM 601 N ASN A 92 141.666 176.139 159.197 1.00 38.34 N
ATOM 602 CA ASN A 92 140.724 175.417 160.035 1.00 41.07 C
ATOM 603 C ASN A 92 139.605 176.358 160.451 1.00 45.38 C
ATOM 604 O ASN A 92 139.759 177.581 160.441 1.00 48.78 O
ATOM 605 CB ASN A 92 141.419 174.830 161.268 1.00 43.61 C
ATOM 606 CG ASN A 92 140.624 173.721 161.913 1.00 48.06 C
ATOM 607 OD1 ASN A 92 140.245 173.813 163.079 1.00 52.34 O
ATOM 608 ND2 ASN A 92 140.368 172.659 161.158 1.00 49.84 N
ATOM 609 H ASN A 92 141.694 176.986 159.345 1.00 41.77 H
ATOM 610 HA ASN A 92 140.336 174.689 159.527 1.00 43.99 H
ATOM 611 HB2 ASN A 92 142.281 174.471 161.005 1.00 44.71 H
ATOM 612 HB3 ASN A 92 141.537 175.532 161.925 1.00 44.66 H
ATOM 613 HD21 ASN A 92 140.651 172.630 160.346 1.00 48.07 H
ATOM 614 HD22 ASN A 92 139.919 172.001 161.481 1.00 49.55 H
ATOM 615 N VAL A 93 138.470 175.767 160.816 1.00 43.74 N
ATOM 616 CA VAL A 93 137.298 176.502 161.273 1.00 39.11 C
ATOM 617 C VAL A 93 136.888 175.921 162.614 1.00 41.68 C
ATOM 618 O VAL A 93 136.826 174.697 162.769 1.00 48.73 O
ATOM 619 CB VAL A 93 136.140 176.420 160.263 1.00 40.03 C
ATOM 620 CG1 VAL A 93 134.988 177.310 160.701 1.00 43.17 C
ATOM 621 CG2 VAL A 93 136.623 176.803 158.873 1.00 38.52 C
ATOM 622 H VAL A 93 138.353 174.915 160.807 1.00 44.44 H
ATOM 623 HA VAL A 93 137.529 177.435 161.399 1.00 42.13 H
ATOM 624 HB VAL A 93 135.815 175.507 160.227 1.00 41.51 H
ATOM 625 HG11 VAL A 93 134.606 176.955 161.518 1.00 42.21 H
ATOM 626 HG12 VAL A 93 134.317 177.322 160.000 1.00 42.24 H
ATOM 627 HG13 VAL A 93 135.324 178.207 160.852 1.00 41.32 H
ATOM 628 HG21 VAL A 93 137.056 177.669 158.917 1.00 40.26 H
ATOM 629 HG22 VAL A 93 135.861 176.844 158.275 1.00 39.83 H
ATOM 630 HG23 VAL A 93 137.252 176.133 158.561 1.00 38.36 H
ATOM 631 N ASP A 94 136.610 176.791 163.581 1.00 46.12 N
ATOM 632 CA ASP A 94 136.471 176.354 164.965 1.00 50.42 C
ATOM 633 C ASP A 94 135.035 175.988 165.331 1.00 55.60 C
ATOM 634 O ASP A 94 134.760 174.842 165.699 1.00 61.79 O
ATOM 635 CB ASP A 94 136.987 177.448 165.909 1.00 57.97 C
ATOM 636 CG ASP A 94 138.497 177.416 166.078 1.00 60.02 C
ATOM 637 OD1 ASP A 94 139.126 176.410 165.688 1.00 60.81 O
ATOM 638 OD2 ASP A 94 139.055 178.399 166.610 1.00 53.94 O
ATOM 639 H ASP A 94 136.498 177.635 163.462 1.00 48.69 H
ATOM 640 HA ASP A 94 137.015 175.562 165.098 1.00 51.45 H
ATOM 641 HB2 ASP A 94 136.745 178.316 165.549 1.00 56.75 H
ATOM 642 HB3 ASP A 94 136.585 177.327 166.783 1.00 56.63 H
ATOM 643 N PHE A 95 134.111 176.943 165.236 1.00 53.64 N
ATOM 644 CA PHE A 95 132.816 176.810 165.890 1.00 59.28 C
ATOM 645 C PHE A 95 131.679 177.056 164.904 1.00 69.13 C
ATOM 646 O PHE A 95 131.893 177.357 163.725 1.00 67.65 O
ATOM 647 CB PHE A 95 132.718 177.753 167.095 1.00 60.52 C
ATOM 648 CG PHE A 95 133.286 179.119 166.851 1.00 59.37 C
ATOM 649 CD1 PHE A 95 132.539 180.096 166.226 1.00 62.95 C
ATOM 650 CD2 PHE A 95 134.569 179.428 167.266 1.00 57.66 C
ATOM 651 CE1 PHE A 95 133.064 181.353 166.011 1.00 62.84 C
ATOM 652 CE2 PHE A 95 135.097 180.683 167.052 1.00 54.08 C
ATOM 653 CZ PHE A 95 134.344 181.644 166.423 1.00 58.15 C
ATOM 654 H PHE A 95 134.211 177.676 164.797 1.00 54.66 H
ATOM 655 HA PHE A 95 132.722 175.903 166.221 1.00 59.11 H
ATOM 656 HB2 PHE A 95 131.789 177.855 167.355 1.00 61.47 H
ATOM 657 HB3 PHE A 95 133.223 177.360 167.818 1.00 58.49 H
ATOM 658 HD1 PHE A 95 131.673 179.904 165.944 1.00 61.81 H
ATOM 659 HD2 PHE A 95 135.083 178.780 167.691 1.00 58.45 H
ATOM 660 HE1 PHE A 95 132.556 182.004 165.587 1.00 61.86 H
ATOM 661 HE2 PHE A 95 135.962 180.878 167.332 1.00 55.28 H
ATOM 662 HZ PHE A 95 134.698 182.492 166.278 1.00 58.31 H
ATOM 663 N VAL A 96 130.456 176.929 165.424 1.00 79.51 N
ATOM 664 CA VAL A 96 129.226 176.858 164.639 1.00 81.63 C
ATOM 665 C VAL A 96 128.835 178.221 164.090 1.00 70.09 C
ATOM 666 O VAL A 96 129.381 179.252 164.494 1.00 64.65 O
ATOM 667 CB VAL A 96 128.077 176.278 165.483 1.00 84.22 C
ATOM 668 CG1 VAL A 96 128.510 174.985 166.158 1.00 81.22 C
ATOM 669 CG2 VAL A 96 127.611 177.298 166.513 1.00 78.26 C
ATOM 670 H VAL A 96 130.310 176.881 166.270 1.00 74.28 H
ATOM 671 HA VAL A 96 129.370 176.265 163.886 1.00 77.58 H
ATOM 672 HB VAL A 96 127.328 176.076 164.901 1.00 81.45 H
ATOM 673 HG11 VAL A 96 128.909 174.402 165.493 1.00 78.50 H
ATOM 674 HG12 VAL A 96 127.732 174.557 166.549 1.00 81.14 H
ATOM 675 HG13 VAL A 96 129.158 175.189 166.850 1.00 77.93 H
ATOM 676 HG21 VAL A 96 128.386 177.738 166.895 1.00 76.04 H
ATOM 677 HG22 VAL A 96 127.116 176.838 167.209 1.00 79.40 H
ATOM 678 HG23 VAL A 96 127.040 177.951 166.079 1.00 75.11 H
ATOM 679 N ASP A 97 127.866 178.228 163.179 1.00 72.88 N
ATOM 680 CA ASP A 97 127.489 179.415 162.433 1.00 79.51 C
ATOM 681 C ASP A 97 125.972 179.560 162.447 1.00 81.62 C
ATOM 682 O ASP A 97 125.241 178.609 162.735 1.00 87.71 O
ATOM 683 CB ASP A 97 128.006 179.320 160.993 1.00 81.60 C
ATOM 684 CG ASP A 97 129.521 179.343 160.920 1.00 70.75 C
ATOM 685 OD1 ASP A 97 130.150 179.951 161.807 1.00 69.53 O
ATOM 686 OD2 ASP A 97 130.084 178.735 159.986 1.00 62.13 O
ATOM 687 H ASP A 97 127.400 177.535 162.975 1.00 75.45 H
ATOM 688 HA ASP A 97 127.877 180.201 162.848 1.00 76.61 H
ATOM 689 HB2 ASP A 97 127.699 178.487 160.600 1.00 78.66 H
ATOM 690 HB3 ASP A 97 127.669 180.072 160.483 1.00 79.20 H
ATOM 691 N LEU A 98 125.500 180.769 162.130 1.00 75.88 N
ATOM 692 CA LEU A 98 124.070 181.062 162.012 1.00 75.61 C
ATOM 693 C LEU A 98 123.339 180.791 163.332 1.00 75.60 C
ATOM 694 O LEU A 98 122.500 179.897 163.449 1.00 78.38 O
ATOM 695 CB LEU A 98 123.449 180.251 160.868 1.00 77.39 C
ATOM 696 CG LEU A 98 121.965 180.492 160.575 1.00 85.24 C
ATOM 697 CD1 LEU A 98 121.702 181.926 160.138 1.00 82.76 C
ATOM 698 CD2 LEU A 98 121.472 179.510 159.522 1.00 83.37 C
ATOM 699 H LEU A 98 126.001 181.450 161.975 1.00 76.59 H
ATOM 700 HA LEU A 98 123.964 182.003 161.803 1.00 77.09 H
ATOM 701 HB2 LEU A 98 123.938 180.455 160.055 1.00 78.20 H
ATOM 702 HB3 LEU A 98 123.550 179.309 161.074 1.00 78.35 H
ATOM 703 HG LEU A 98 121.452 180.334 161.383 1.00 83.65 H
ATOM 704 HD11 LEU A 98 120.747 182.047 160.019 1.00 82.18 H
ATOM 705 HD12 LEU A 98 122.028 182.532 160.821 1.00 81.08 H
ATOM 706 HD13 LEU A 98 122.162 182.090 159.301 1.00 82.70 H
ATOM 707 HD21 LEU A 98 120.532 179.677 159.351 1.00 80.75 H
ATOM 708 HD22 LEU A 98 121.984 179.636 158.709 1.00 83.12 H
ATOM 709 HD23 LEU A 98 121.593 178.607 159.853 1.00 82.73 H
ATOM 710 N ASN A 99 123.691 181.593 164.334 1.00 72.49 N
ATOM 711 CA ASN A 99 123.063 181.535 165.648 1.00 72.67 C
ATOM 712 C ASN A 99 122.320 182.839 165.892 1.00 77.71 C
ATOM 713 O ASN A 99 122.922 183.916 165.854 1.00 77.54 O
ATOM 714 CB ASN A 99 124.102 181.294 166.745 1.00 81.91 C
ATOM 715 CG ASN A 99 123.471 181.040 168.100 1.00 82.54 C
ATOM 716 OD1 ASN A 99 123.236 181.968 168.874 1.00 88.79 O
ATOM 717 ND2 ASN A 99 123.195 179.775 168.396 1.00 76.41 N
ATOM 718 H ASN A 99 124.304 182.193 164.273 1.00 75.81 H
ATOM 719 HA ASN A 99 122.422 180.808 165.671 1.00 74.44 H
ATOM 720 HB2 ASN A 99 124.635 180.518 166.511 1.00 80.07 H
ATOM 721 HB3 ASN A 99 124.670 182.077 166.820 1.00 81.33 H
ATOM 722 HD21 ASN A 99 123.375 179.152 167.830 1.00 76.87 H
ATOM 723 HD22 ASN A 99 122.837 179.578 169.153 1.00 78.90 H
ATOM 724 N ASN A 100 121.016 182.737 166.157 1.00 87.32 N
ATOM 725 CA ASN A 100 120.173 183.905 166.419 1.00 88.27 C
ATOM 726 C ASN A 100 120.234 184.904 165.266 1.00 85.19 C
ATOM 727 O ASN A 100 120.340 186.115 165.473 1.00 82.69 O
ATOM 728 CB ASN A 100 120.565 184.574 167.738 1.00 87.72 C
ATOM 729 CG ASN A 100 119.553 185.604 168.192 1.00 90.68 C
ATOM 730 OD1 ASN A 100 118.571 185.871 167.501 1.00 88.28 O
ATOM 731 ND2 ASN A 100 119.786 186.187 169.362 1.00 92.41 N
ATOM 732 H ASN A 100 120.591 181.990 166.192 1.00 84.52 H
ATOM 733 HA ASN A 100 119.253 183.609 166.503 1.00 87.23 H
ATOM 734 HB2 ASN A 100 120.635 183.896 168.428 1.00 86.40 H
ATOM 735 HB3 ASN A 100 121.419 185.021 167.624 1.00 86.14 H
ATOM 736 HD21 ASN A 100 120.483 185.973 169.818 1.00 90.56 H
ATOM 737 HD22 ASN A 100 119.239 186.778 169.664 1.00 90.98 H
ATOM 738 N GLY A 101 120.164 184.397 164.044 1.00 83.23 N
ATOM 739 CA GLY A 101 120.261 185.253 162.863 1.00 80.90 C
ATOM 740 C GLY A 101 121.677 185.627 162.499 1.00 85.35 C
ATOM 741 O GLY A 101 122.094 185.439 161.353 1.00 86.09 O
ATOM 742 H GLY A 101 120.060 183.562 163.868 1.00 83.43 H
ATOM 743 HA2 GLY A 101 119.864 184.796 162.105 1.00 80.91 H
ATOM 744 HA3 GLY A 101 119.763 186.071 163.020 1.00 82.30 H
ATOM 745 N LYS A 102 122.436 186.155 163.456 1.00 87.06 N
ATOM 746 CA LYS A 102 123.826 186.511 163.222 1.00 84.74 C
ATOM 747 C LYS A 102 124.696 185.256 163.174 1.00 82.53 C
ATOM 748 O LYS A 102 124.289 184.162 163.575 1.00 84.17 O
ATOM 749 CB LYS A 102 124.321 187.455 164.317 1.00 87.85 C
ATOM 750 CG LYS A 102 123.582 188.783 164.374 1.00 89.44 C
ATOM 751 CD LYS A 102 123.972 189.583 165.607 1.00 89.33 C
ATOM 752 CE LYS A 102 123.331 190.962 165.605 1.00 90.24 C
ATOM 753 NZ LYS A 102 123.685 191.745 166.821 1.00 89.63 N
ATOM 754 H LYS A 102 122.164 186.319 164.255 1.00 85.57 H
ATOM 755 HA LYS A 102 123.906 186.965 162.370 1.00 84.60 H
ATOM 756 HB2 LYS A 102 124.213 187.019 165.177 1.00 87.13 H
ATOM 757 HB3 LYS A 102 125.260 187.645 164.163 1.00 88.08 H
ATOM 758 HG2 LYS A 102 123.804 189.306 163.588 1.00 88.92 H
ATOM 759 HG3 LYS A 102 122.627 188.617 164.409 1.00 87.61 H
ATOM 760 HD2 LYS A 102 123.673 189.112 166.400 1.00 89.46 H
ATOM 761 HD3 LYS A 102 124.935 189.694 165.628 1.00 88.58 H
ATOM 762 HE2 LYS A 102 123.639 191.455 164.828 1.00 90.76 H
ATOM 763 HE3 LYS A 102 122.366 190.865 165.578 1.00 89.82 H
ATOM 764 HZ1 LYS A 102 123.294 192.543 166.794 1.00 90.25 H
ATOM 765 HZ2 LYS A 102 124.567 191.856 166.866 1.00 89.51 H
ATOM 766 HZ3 LYS A 102 123.411 191.314 167.550 1.00 89.71 H
ATOM 767 N PHE A 103 125.915 185.427 162.674 1.00 76.98 N
ATOM 768 CA PHE A 103 126.885 184.350 162.566 1.00 71.58 C
ATOM 769 C PHE A 103 128.059 184.608 163.500 1.00 70.90 C
ATOM 770 O PHE A 103 128.442 185.756 163.739 1.00 68.28 O
ATOM 771 CB PHE A 103 127.433 184.218 161.142 1.00 74.90 C
ATOM 772 CG PHE A 103 126.444 183.702 160.142 1.00 72.72 C
ATOM 773 CD1 PHE A 103 125.287 184.403 159.861 1.00 75.08 C
ATOM 774 CD2 PHE A 103 126.679 182.515 159.477 1.00 69.97 C
ATOM 775 CE1 PHE A 103 124.389 183.929 158.931 1.00 75.02 C
ATOM 776 CE2 PHE A 103 125.784 182.038 158.552 1.00 69.66 C
ATOM 777 CZ PHE A 103 124.639 182.745 158.277 1.00 71.89 C
ATOM 778 H PHE A 103 126.209 186.181 162.383 1.00 78.09 H
ATOM 779 HA PHE A 103 126.472 183.510 162.815 1.00 74.42 H
ATOM 780 HB2 PHE A 103 127.728 185.092 160.841 1.00 75.12 H
ATOM 781 HB3 PHE A 103 128.185 183.606 161.155 1.00 74.81 H
ATOM 782 HD1 PHE A 103 125.117 185.206 160.298 1.00 76.04 H
ATOM 783 HD2 PHE A 103 127.455 182.034 159.656 1.00 71.90 H
ATOM 784 HE1 PHE A 103 123.612 184.408 158.749 1.00 76.09 H
ATOM 785 HE2 PHE A 103 125.954 181.237 158.112 1.00 71.75 H
ATOM 786 HZ PHE A 103 124.030 182.421 157.653 1.00 73.65 H
ATOM 787 N TYR A 104 128.630 183.525 164.020 1.00 74.70 N
ATOM 788 CA TYR A 104 129.928 183.545 164.686 1.00 67.85 C
ATOM 789 C TYR A 104 130.844 182.597 163.928 1.00 61.47 C
ATOM 790 O TYR A 104 130.579 181.392 163.873 1.00 69.16 O
ATOM 791 CB TYR A 104 129.814 183.119 166.152 1.00 67.07 C
ATOM 792 CG TYR A 104 128.983 184.040 167.018 1.00 74.83 C
ATOM 793 CD1 TYR A 104 128.706 185.342 166.625 1.00 81.74 C
ATOM 794 CD2 TYR A 104 128.466 183.601 168.225 1.00 74.09 C
ATOM 795 CE1 TYR A 104 127.945 186.181 167.414 1.00 85.21 C
ATOM 796 CE2 TYR A 104 127.702 184.431 169.021 1.00 82.97 C
ATOM 797 CZ TYR A 104 127.445 185.720 168.611 1.00 89.41 C
ATOM 798 OH TYR A 104 126.685 186.552 169.401 1.00 92.04 O
ATOM 799 H TYR A 104 128.273 182.743 163.998 1.00 73.69 H
ATOM 800 HA TYR A 104 130.309 184.435 164.643 1.00 70.00 H
ATOM 801 HB2 TYR A 104 129.408 182.239 166.187 1.00 69.50 H
ATOM 802 HB3 TYR A 104 130.705 183.082 166.533 1.00 67.47 H
ATOM 803 HD1 TYR A 104 129.043 185.659 165.819 1.00 78.04 H
ATOM 804 HD2 TYR A 104 128.637 182.731 168.506 1.00 75.10 H
ATOM 805 HE1 TYR A 104 127.771 187.052 167.138 1.00 82.69 H
ATOM 806 HE2 TYR A 104 127.364 184.122 169.830 1.00 82.81 H
ATOM 807 HH TYR A 104 126.445 186.148 170.097 1.00 89.46 H
ATOM 808 N VAL A 105 131.917 183.130 163.351 1.00 56.96 N
ATOM 809 CA VAL A 105 132.849 182.343 162.554 1.00 57.12 C
ATOM 810 C VAL A 105 134.243 182.504 163.143 1.00 61.38 C
ATOM 811 O VAL A 105 134.669 183.625 163.441 1.00 60.49 O
ATOM 812 CB VAL A 105 132.844 182.766 161.074 1.00 55.06 C
ATOM 813 CG1 VAL A 105 133.866 181.962 160.293 1.00 57.54 C
ATOM 814 CG2 VAL A 105 131.461 182.611 160.472 1.00 58.20 C
ATOM 815 H VAL A 105 132.129 183.961 163.408 1.00 60.91 H
ATOM 816 HA VAL A 105 132.606 181.405 162.602 1.00 60.41 H
ATOM 817 HB VAL A 105 133.094 183.700 161.014 1.00 57.15 H
ATOM 818 HG11 VAL A 105 133.645 182.004 159.350 1.00 57.44 H
ATOM 819 HG12 VAL A 105 134.748 182.336 160.443 1.00 58.88 H
ATOM 820 HG13 VAL A 105 133.839 181.040 160.596 1.00 58.84 H
ATOM 821 HG21 VAL A 105 131.469 182.971 159.571 1.00 57.95 H
ATOM 822 HG22 VAL A 105 131.232 181.669 160.449 1.00 61.82 H
ATOM 823 HG23 VAL A 105 130.821 183.096 161.016 1.00 61.97 H
ATOM 824 N GLY A 106 134.948 181.386 163.311 1.00 61.12 N
ATOM 825 CA GLY A 106 136.322 181.406 163.775 1.00 47.89 C
ATOM 826 C GLY A 106 137.234 180.591 162.884 1.00 37.31 C
ATOM 827 O GLY A 106 137.053 179.379 162.755 1.00 48.76 O
ATOM 828 H GLY A 106 134.643 180.596 163.159 1.00 57.78 H
ATOM 829 HA2 GLY A 106 136.647 182.318 163.796 1.00 52.73 H
ATOM 830 HA3 GLY A 106 136.371 181.041 164.671 1.00 50.96 H
ATOM 831 N VAL A 107 138.215 181.239 162.263 1.00 32.74 N
ATOM 832 CA VAL A 107 139.148 180.583 161.356 1.00 35.36 C
ATOM 833 C VAL A 107 140.567 180.871 161.826 1.00 42.54 C
ATOM 834 O VAL A 107 140.909 182.023 162.115 1.00 46.90 O
ATOM 835 CB VAL A 107 138.954 181.053 159.905 1.00 32.82 C
ATOM 836 CG1 VAL A 107 139.772 180.200 158.955 1.00 32.33 C
ATOM 837 CG2 VAL A 107 137.487 181.007 159.535 1.00 43.51 C
ATOM 838 H VAL A 107 138.363 182.081 162.355 1.00 38.76 H
ATOM 839 HA VAL A 107 139.006 179.625 161.388 1.00 39.78 H
ATOM 840 HB VAL A 107 139.258 181.970 159.824 1.00 35.93 H
ATOM 841 HG11 VAL A 107 140.423 179.690 159.460 1.00 37.10 H
ATOM 842 HG12 VAL A 107 139.181 179.597 158.478 1.00 37.00 H
ATOM 843 HG13 VAL A 107 140.229 180.781 158.327 1.00 34.54 H
ATOM 844 HG21 VAL A 107 137.065 181.833 159.817 1.00 43.52 H
ATOM 845 HG22 VAL A 107 137.074 180.255 159.988 1.00 42.49 H
ATOM 846 HG23 VAL A 107 137.401 180.901 158.575 1.00 41.51 H
ATOM 847 N CYS A 108 141.387 179.825 161.903 1.00 40.29 N
ATOM 848 CA CYS A 108 142.783 179.928 162.300 1.00 37.17 C
ATOM 849 C CYS A 108 143.662 179.398 161.178 1.00 39.41 C
ATOM 850 O CYS A 108 143.366 178.355 160.589 1.00 47.21 O
ATOM 851 CB CYS A 108 143.047 179.148 163.585 1.00 43.43 C
ATOM 852 SG CYS A 108 142.957 177.364 163.392 1.00 60.99 S
ATOM 853 H CYS A 108 141.145 179.020 161.723 1.00 41.39 H
ATOM 854 HA CYS A 108 143.010 180.858 162.453 1.00 40.19 H
ATOM 855 HB2 CYS A 108 143.936 179.367 163.906 1.00 44.86 H
ATOM 856 HB3 CYS A 108 142.387 179.407 164.247 1.00 44.73 H
ATOM 857 HG CYS A 108 142.252 176.916 164.254 1.00 52.08 H
ATOM 858 N ALA A 109 144.743 180.119 160.886 1.00 42.71 N
ATOM 859 CA ALA A 109 145.605 179.811 159.755 1.00 41.90 C
ATOM 860 C ALA A 109 147.064 179.770 160.186 1.00 44.07 C
ATOM 861 O ALA A 109 147.472 180.451 161.131 1.00 45.97 O
ATOM 862 CB ALA A 109 145.440 180.839 158.635 1.00 39.78 C
ATOM 863 H ALA A 109 145.000 180.803 161.339 1.00 43.13 H
ATOM 864 HA ALA A 109 145.371 178.940 159.401 1.00 44.05 H
ATOM 865 HB1 ALA A 109 144.525 180.813 158.314 1.00 42.76 H
ATOM 866 HB2 ALA A 109 145.646 181.721 158.983 1.00 42.77 H
ATOM 867 HB3 ALA A 109 146.051 180.615 157.916 1.00 41.58 H
ATOM 868 N PHE A 110 147.843 178.956 159.478 1.00 40.19 N
ATOM 869 CA PHE A 110 149.284 178.857 159.660 1.00 34.48 C
ATOM 870 C PHE A 110 149.955 179.430 158.421 1.00 34.77 C
ATOM 871 O PHE A 110 149.682 178.978 157.306 1.00 38.03 O
ATOM 872 CB PHE A 110 149.718 177.406 159.857 1.00 38.13 C
ATOM 873 CG PHE A 110 149.264 176.791 161.148 1.00 35.90 C
ATOM 874 CD1 PHE A 110 148.504 177.495 162.056 1.00 37.32 C
ATOM 875 CD2 PHE A 110 149.602 175.488 161.441 1.00 44.20 C
ATOM 876 CE1 PHE A 110 148.095 176.911 163.229 1.00 35.88 C
ATOM 877 CE2 PHE A 110 149.196 174.903 162.612 1.00 45.15 C
ATOM 878 CZ PHE A 110 148.443 175.617 163.505 1.00 38.71 C
ATOM 879 H PHE A 110 147.545 178.433 158.864 1.00 41.62 H
ATOM 880 HA PHE A 110 149.561 179.379 160.429 1.00 37.25 H
ATOM 881 HB2 PHE A 110 149.343 176.876 159.138 1.00 41.42 H
ATOM 882 HB3 PHE A 110 150.686 177.362 159.830 1.00 40.16 H
ATOM 883 HD1 PHE A 110 148.264 178.375 161.878 1.00 38.73 H
ATOM 884 HD2 PHE A 110 150.113 174.999 160.838 1.00 43.68 H
ATOM 885 HE1 PHE A 110 147.584 177.396 163.837 1.00 39.27 H
ATOM 886 HE2 PHE A 110 149.432 174.023 162.798 1.00 44.38 H
ATOM 887 HZ PHE A 110 148.168 175.217 164.296 1.00 39.80 H
ATOM 888 N VAL A 111 150.835 180.407 158.612 1.00 37.07 N
ATOM 889 CA VAL A 111 151.504 181.088 157.509 1.00 36.05 C
ATOM 890 C VAL A 111 153.006 180.929 157.677 1.00 32.25 C
ATOM 891 O VAL A 111 153.532 181.050 158.788 1.00 32.06 O
ATOM 892 CB VAL A 111 151.124 182.581 157.432 1.00 33.10 C
ATOM 893 CG1 VAL A 111 151.783 183.228 156.231 1.00 33.14 C
ATOM 894 CG2 VAL A 111 149.614 182.751 157.369 1.00 34.88 C
ATOM 895 H VAL A 111 151.067 180.699 159.387 1.00 36.10 H
ATOM 896 HA VAL A 111 151.249 180.670 156.672 1.00 37.43 H
ATOM 897 HB VAL A 111 151.444 183.031 158.230 1.00 33.95 H
ATOM 898 HG11 VAL A 111 152.067 182.537 155.613 1.00 34.32 H
ATOM 899 HG12 VAL A 111 151.148 183.819 155.798 1.00 34.84 H
ATOM 900 HG13 VAL A 111 152.551 183.738 156.533 1.00 33.83 H
ATOM 901 HG21 VAL A 111 149.377 183.587 157.801 1.00 36.40 H
ATOM 902 HG22 VAL A 111 149.179 182.014 157.824 1.00 36.11 H
ATOM 903 HG23 VAL A 111 149.335 182.773 156.440 1.00 36.35 H
ATOM 904 N ARG A 112 153.692 180.650 156.572 1.00 31.81 N
ATOM 905 CA ARG A 112 155.127 180.408 156.567 1.00 30.64 C
ATOM 906 C ARG A 112 155.803 181.416 155.652 1.00 28.37 C
ATOM 907 O ARG A 112 155.536 181.441 154.448 1.00 34.46 O
ATOM 908 CB ARG A 112 155.439 178.982 156.111 1.00 37.52 C
ATOM 909 CG ARG A 112 156.914 178.625 156.172 1.00 40.72 C
ATOM 910 CD ARG A 112 157.142 177.161 155.875 1.00 38.25 C
ATOM 911 NE ARG A 112 158.387 176.948 155.146 1.00 34.59 N
ATOM 912 CZ ARG A 112 159.284 176.012 155.428 1.00 46.12 C
ATOM 913 NH1 ARG A 112 159.110 175.158 156.423 1.00 48.49 N
ATOM 914 NH2 ARG A 112 160.386 175.930 154.688 1.00 46.34 N
ATOM 915 H ARG A 112 153.334 180.595 155.792 1.00 34.70 H
ATOM 916 HA ARG A 112 155.480 180.525 157.463 1.00 32.40 H
ATOM 917 HB2 ARG A 112 154.957 178.358 156.675 1.00 36.03 H
ATOM 918 HB3 ARG A 112 155.149 178.880 155.191 1.00 35.61 H
ATOM 919 HG2 ARG A 112 157.392 179.143 155.506 1.00 39.32 H
ATOM 920 HG3 ARG A 112 157.262 178.820 157.055 1.00 39.05 H
ATOM 921 HD2 ARG A 112 157.177 176.679 156.712 1.00 39.06 H
ATOM 922 HD3 ARG A 112 156.412 176.829 155.329 1.00 39.05 H
ATOM 923 HE ARG A 112 158.553 177.471 154.484 1.00 36.51 H
ATOM 924 HH11 ARG A 112 158.406 175.192 156.913 1.00 46.93 H
ATOM 925 HH12 ARG A 112 159.709 174.561 156.581 1.00 46.28 H
ATOM 926 HH21 ARG A 112 160.509 176.480 154.039 1.00 45.32 H
ATOM 927 HH22 ARG A 112 160.975 175.328 154.860 1.00 45.93 H
ATOM 928 N VAL A 113 156.692 182.224 156.222 1.00 33.14 N
ATOM 929 CA VAL A 113 157.442 183.237 155.490 1.00 36.44 C
ATOM 930 C VAL A 113 158.877 182.748 155.356 1.00 35.09 C
ATOM 931 O VAL A 113 159.496 182.362 156.352 1.00 29.64 O
ATOM 932 CB VAL A 113 157.384 184.599 156.203 1.00 36.67 C
ATOM 933 CG1 VAL A 113 158.140 185.646 155.414 1.00 34.81 C
ATOM 934 CG2 VAL A 113 155.944 185.026 156.412 1.00 38.01 C
ATOM 935 H VAL A 113 156.884 182.201 157.060 1.00 33.65 H
ATOM 936 HA VAL A 113 157.068 183.340 154.601 1.00 36.22 H
ATOM 937 HB VAL A 113 157.803 184.519 157.074 1.00 36.06 H
ATOM 938 HG11 VAL A 113 159.090 185.457 155.464 1.00 36.95 H
ATOM 939 HG12 VAL A 113 157.958 186.519 155.795 1.00 35.14 H
ATOM 940 HG13 VAL A 113 157.845 185.620 154.490 1.00 36.53 H
ATOM 941 HG21 VAL A 113 155.488 185.023 155.556 1.00 36.79 H
ATOM 942 HG22 VAL A 113 155.932 185.918 156.791 1.00 38.33 H
ATOM 943 HG23 VAL A 113 155.514 184.402 157.018 1.00 36.86 H
ATOM 944 N GLN A 114 159.399 182.752 154.127 1.00 36.93 N
ATOM 945 CA GLN A 114 160.714 182.197 153.829 1.00 36.46 C
ATOM 946 C GLN A 114 161.502 183.154 152.948 1.00 35.21 C
ATOM 947 O GLN A 114 160.979 183.653 151.949 1.00 39.84 O
ATOM 948 CB GLN A 114 160.587 180.836 153.135 1.00 38.95 C
ATOM 949 CG GLN A 114 161.914 180.146 152.867 1.00 42.52 C
ATOM 950 CD GLN A 114 161.739 178.783 152.235 1.00 45.99 C
ATOM 951 OE1 GLN A 114 160.619 178.355 151.957 1.00 44.97 O
ATOM 952 NE2 GLN A 114 162.848 178.092 152.002 1.00 46.93 N
ATOM 953 H GLN A 114 158.999 183.077 153.438 1.00 37.81 H
ATOM 954 HA GLN A 114 161.201 182.072 154.657 1.00 36.71 H
ATOM 955 HB2 GLN A 114 160.059 180.249 153.697 1.00 38.78 H
ATOM 956 HB3 GLN A 114 160.143 180.962 152.282 1.00 38.87 H
ATOM 957 HG2 GLN A 114 162.439 180.691 152.260 1.00 42.88 H
ATOM 958 HG3 GLN A 114 162.388 180.031 153.705 1.00 41.92 H
ATOM 959 HE21 GLN A 114 163.614 178.424 152.209 1.00 46.15 H
ATOM 960 HE22 GLN A 114 162.801 177.311 151.644 1.00 46.19 H
ATOM 961 N LEU A 115 162.764 183.389 153.309 1.00 32.73 N
ATOM 962 CA LEU A 115 163.629 184.310 152.593 1.00 31.63 C
ATOM 963 C LEU A 115 164.350 183.592 151.456 1.00 35.42 C
ATOM 964 O LEU A 115 164.198 182.385 151.250 1.00 43.96 O
ATOM 965 CB LEU A 115 164.637 184.945 153.545 1.00 34.29 C
ATOM 966 CG LEU A 115 164.073 185.755 154.707 1.00 37.60 C
ATOM 967 CD1 LEU A 115 165.201 186.196 155.614 1.00 39.97 C
ATOM 968 CD2 LEU A 115 163.291 186.955 154.201 1.00 43.83 C
ATOM 969 H LEU A 115 163.145 183.015 153.983 1.00 35.73 H
ATOM 970 HA LEU A 115 163.090 185.017 152.206 1.00 36.91 H
ATOM 971 HB2 LEU A 115 165.179 184.237 153.926 1.00 35.68 H
ATOM 972 HB3 LEU A 115 165.204 185.541 153.031 1.00 36.55 H
ATOM 973 HG LEU A 115 163.471 185.197 155.223 1.00 37.26 H
ATOM 974 HD11 LEU A 115 164.898 186.941 156.156 1.00 43.30 H
ATOM 975 HD12 LEU A 115 165.459 185.454 156.183 1.00 39.80 H
ATOM 976 HD13 LEU A 115 165.953 186.473 155.068 1.00 40.60 H
ATOM 977 HD21 LEU A 115 163.864 187.482 153.622 1.00 44.93 H
ATOM 978 HD22 LEU A 115 163.006 187.489 154.959 1.00 45.55 H
ATOM 979 HD23 LEU A 115 162.518 186.643 153.707 1.00 43.38 H
ATOM 980 N LYS A 116 165.149 184.348 150.700 1.00 32.82 N
ATOM 981 CA LYS A 116 165.852 183.761 149.563 1.00 38.89 C
ATOM 982 C LYS A 116 166.873 182.726 150.012 1.00 44.35 C
ATOM 983 O LYS A 116 166.978 181.651 149.410 1.00 46.65 O
ATOM 984 CB LYS A 116 166.530 184.853 148.741 1.00 39.22 C
ATOM 985 CG LYS A 116 165.630 185.476 147.698 1.00 49.34 C
ATOM 986 CD LYS A 116 165.425 184.537 146.518 1.00 53.47 C
ATOM 987 CE LYS A 116 164.580 185.176 145.429 1.00 58.73 C
ATOM 988 NZ LYS A 116 164.342 184.248 144.290 1.00 61.64 N
ATOM 989 H LYS A 116 165.298 185.186 150.822 1.00 36.93 H
ATOM 990 HA LYS A 116 165.206 183.314 148.995 1.00 40.97 H
ATOM 991 HB2 LYS A 116 166.827 185.558 149.338 1.00 41.02 H
ATOM 992 HB3 LYS A 116 167.294 184.469 148.282 1.00 40.73 H
ATOM 993 HG2 LYS A 116 164.764 185.665 148.093 1.00 48.06 H
ATOM 994 HG3 LYS A 116 166.037 186.293 147.370 1.00 50.17 H
ATOM 995 HD2 LYS A 116 166.287 184.308 146.138 1.00 50.79 H
ATOM 996 HD3 LYS A 116 164.970 183.736 146.821 1.00 49.60 H
ATOM 997 HE2 LYS A 116 163.719 185.426 145.800 1.00 56.09 H
ATOM 998 HE3 LYS A 116 165.038 185.961 145.090 1.00 59.17 H
ATOM 999 HZ1 LYS A 116 163.847 184.649 143.669 1.00 60.08 H
ATOM 1000 HZ2 LYS A 116 165.119 184.006 143.928 1.00 61.42 H
ATOM 1001 HZ3 LYS A 116 163.916 183.520 144.574 1.00 60.43 H
ATOM 1002 N ASP A 117 167.636 183.027 151.064 1.00 40.46 N
ATOM 1003 CA ASP A 117 168.669 182.097 151.506 1.00 30.73 C
ATOM 1004 C ASP A 117 168.066 180.779 151.966 1.00 26.55 C
ATOM 1005 O ASP A 117 168.585 179.705 151.643 1.00 38.68 O
ATOM 1006 CB ASP A 117 169.514 182.742 152.607 1.00 28.76 C
ATOM 1007 CG ASP A 117 168.789 182.845 153.936 1.00 31.76 C
ATOM 1008 OD1 ASP A 117 167.860 182.059 154.204 1.00 32.08 O
ATOM 1009 OD2 ASP A 117 169.157 183.735 154.729 1.00 32.13 O
ATOM 1010 H ASP A 117 167.576 183.748 151.529 1.00 37.78 H
ATOM 1011 HA ASP A 117 169.257 181.907 150.758 1.00 33.02 H
ATOM 1012 HB2 ASP A 117 170.313 182.209 152.743 1.00 30.04 H
ATOM 1013 HB3 ASP A 117 169.759 183.639 152.330 1.00 31.44 H
ATOM 1014 N GLY A 118 166.968 180.837 152.708 1.00 20.98 N
ATOM 1015 CA GLY A 118 166.317 179.630 153.167 1.00 28.60 C
ATOM 1016 C GLY A 118 165.709 179.750 154.545 1.00 28.69 C
ATOM 1017 O GLY A 118 164.981 178.855 154.982 1.00 37.68 O
ATOM 1018 H GLY A 118 166.584 181.565 152.957 1.00 29.28 H
ATOM 1019 HA2 GLY A 118 165.610 179.394 152.546 1.00 32.53 H
ATOM 1020 HA3 GLY A 118 166.960 178.904 153.186 1.00 31.64 H
ATOM 1021 N SER A 119 165.990 180.843 155.242 1.00 22.15 N
ATOM 1022 CA SER A 119 165.387 181.052 156.546 1.00 22.78 C
ATOM 1023 C SER A 119 163.881 181.227 156.404 1.00 32.38 C
ATOM 1024 O SER A 119 163.382 181.697 155.379 1.00 40.82 O
ATOM 1025 CB SER A 119 165.997 182.276 157.221 1.00 24.99 C
ATOM 1026 OG SER A 119 167.403 182.275 157.080 1.00 28.36 O
ATOM 1027 H SER A 119 166.518 181.471 154.987 1.00 27.64 H
ATOM 1028 HA SER A 119 165.549 180.278 157.107 1.00 25.47 H
ATOM 1029 HB2 SER A 119 165.637 183.078 156.810 1.00 28.09 H
ATOM 1030 HB3 SER A 119 165.774 182.258 158.165 1.00 26.05 H
ATOM 1031 HG SER A 119 167.718 183.011 157.332 1.00 30.11 H
ATOM 1032 N TYR A 120 163.155 180.838 157.445 1.00 32.42 N
ATOM 1033 CA TYR A 120 161.705 180.913 157.419 1.00 28.87 C
ATOM 1034 C TYR A 120 161.176 180.954 158.845 1.00 34.90 C
ATOM 1035 O TYR A 120 161.880 180.609 159.797 1.00 37.61 O
ATOM 1036 CB TYR A 120 161.112 179.724 156.669 1.00 33.16 C
ATOM 1037 CG TYR A 120 161.509 178.403 157.280 1.00 35.49 C
ATOM 1038 CD1 TYR A 120 160.884 177.934 158.422 1.00 38.94 C
ATOM 1039 CD2 TYR A 120 162.517 177.635 156.731 1.00 34.43 C
ATOM 1040 CE1 TYR A 120 161.245 176.745 158.995 1.00 34.17 C
ATOM 1041 CE2 TYR A 120 162.885 176.432 157.301 1.00 37.73 C
ATOM 1042 CZ TYR A 120 162.242 175.995 158.435 1.00 35.25 C
ATOM 1043 OH TYR A 120 162.593 174.802 159.013 1.00 38.91 O
ATOM 1044 H TYR A 120 163.481 180.525 158.176 1.00 32.89 H
ATOM 1045 HA TYR A 120 161.458 181.733 156.972 1.00 32.03 H
ATOM 1046 HB2 TYR A 120 160.145 179.790 156.698 1.00 35.46 H
ATOM 1047 HB3 TYR A 120 161.418 179.740 155.747 1.00 35.25 H
ATOM 1048 HD1 TYR A 120 160.209 178.441 158.810 1.00 37.41 H
ATOM 1049 HD2 TYR A 120 162.953 177.932 155.965 1.00 35.91 H
ATOM 1050 HE1 TYR A 120 160.812 176.448 159.761 1.00 35.92 H
ATOM 1051 HE2 TYR A 120 163.562 175.920 156.922 1.00 37.97 H
ATOM 1052 HH TYR A 120 162.032 174.589 159.602 1.00 38.03 H
ATOM 1053 N HIS A 121 159.915 181.365 158.979 1.00 39.61 N
ATOM 1054 CA HIS A 121 159.233 181.350 160.267 1.00 34.88 C
ATOM 1055 C HIS A 121 157.756 181.062 160.045 1.00 32.90 C
ATOM 1056 O HIS A 121 157.152 181.584 159.108 1.00 35.96 O
ATOM 1057 CB HIS A 121 159.400 182.680 161.011 1.00 40.99 C
ATOM 1058 CG HIS A 121 160.812 182.977 161.411 1.00 39.06 C
ATOM 1059 ND1 HIS A 121 161.476 182.265 162.384 1.00 32.06 N
ATOM 1060 CD2 HIS A 121 161.682 183.917 160.975 1.00 36.57 C
ATOM 1061 CE1 HIS A 121 162.695 182.750 162.527 1.00 31.51 C
ATOM 1062 NE2 HIS A 121 162.846 183.752 161.682 1.00 33.46 N
ATOM 1063 H HIS A 121 159.430 181.659 158.332 1.00 36.35 H
ATOM 1064 HA HIS A 121 159.602 180.644 160.819 1.00 35.13 H
ATOM 1065 HB2 HIS A 121 159.098 183.400 160.436 1.00 37.57 H
ATOM 1066 HB3 HIS A 121 158.861 182.657 161.817 1.00 39.51 H
ATOM 1067 HD1 HIS A 121 161.152 181.609 162.824 1.00 32.79 H
ATOM 1068 HD2 HIS A 121 161.522 184.552 160.319 1.00 36.40 H
ATOM 1069 HE1 HIS A 121 163.339 182.436 163.120 1.00 32.66 H
ATOM 1070 HE2 HIS A 121 163.558 184.227 161.591 1.00 34.83 H
ATOM 1071 N GLU A 122 157.183 180.235 160.914 1.00 34.67 N
ATOM 1072 CA GLU A 122 155.775 179.871 160.856 1.00 32.66 C
ATOM 1073 C GLU A 122 155.069 180.364 162.108 1.00 42.00 C
ATOM 1074 O GLU A 122 155.522 180.097 163.225 1.00 34.09 O
ATOM 1075 CB GLU A 122 155.590 178.360 160.739 1.00 37.60 C
ATOM 1076 CG GLU A 122 155.570 177.830 159.329 1.00 42.90 C
ATOM 1077 CD GLU A 122 155.550 176.318 159.289 1.00 57.57 C
ATOM 1078 OE1 GLU A 122 154.578 175.725 159.800 1.00 67.25 O
ATOM 1079 OE2 GLU A 122 156.509 175.720 158.758 1.00 57.33 O
ATOM 1080 H GLU A 122 157.603 179.862 161.565 1.00 36.69 H
ATOM 1081 HA GLU A 122 155.363 180.291 160.086 1.00 35.98 H
ATOM 1082 HB2 GLU A 122 156.323 177.930 161.199 1.00 40.10 H
ATOM 1083 HB3 GLU A 122 154.751 178.115 161.159 1.00 39.82 H
ATOM 1084 HG2 GLU A 122 154.776 178.156 158.878 1.00 41.23 H
ATOM 1085 HG3 GLU A 122 156.366 178.133 158.869 1.00 41.79 H
ATOM 1086 N ASP A 123 153.950 181.061 161.920 1.00 48.19 N
ATOM 1087 CA ASP A 123 153.157 181.561 163.032 1.00 43.47 C
ATOM 1088 C ASP A 123 151.683 181.350 162.723 1.00 39.83 C
ATOM 1089 O ASP A 123 151.298 181.050 161.591 1.00 36.62 O
ATOM 1090 CB ASP A 123 153.454 183.039 163.314 1.00 41.05 C
ATOM 1091 CG ASP A 123 153.449 183.360 164.799 1.00 44.01 C
ATOM 1092 OD1 ASP A 123 152.814 182.614 165.574 1.00 46.70 O
ATOM 1093 OD2 ASP A 123 154.099 184.350 165.194 1.00 45.18 O
ATOM 1094 H ASP A 123 153.628 181.258 161.147 1.00 41.17 H
ATOM 1095 HA ASP A 123 153.372 181.051 163.828 1.00 42.95 H
ATOM 1096 HB2 ASP A 123 154.330 183.259 162.962 1.00 41.61 H
ATOM 1097 HB3 ASP A 123 152.776 183.585 162.887 1.00 42.90 H
ATOM 1098 N VAL A 124 150.858 181.513 163.754 1.00 37.13 N
ATOM 1099 CA VAL A 124 149.433 181.206 163.705 1.00 33.40 C
ATOM 1100 C VAL A 124 148.645 182.508 163.677 1.00 44.38 C
ATOM 1101 O VAL A 124 148.875 183.401 164.502 1.00 47.44 O
ATOM 1102 CB VAL A 124 149.002 180.339 164.900 1.00 27.55 C
ATOM 1103 CG1 VAL A 124 149.265 181.050 166.201 1.00 27.25 C
ATOM 1104 CG2 VAL A 124 147.538 179.988 164.789 1.00 37.30 C
ATOM 1105 H VAL A 124 151.113 181.816 164.516 1.00 39.55 H
ATOM 1106 HA VAL A 124 149.238 180.716 162.891 1.00 36.66 H
ATOM 1107 HB VAL A 124 149.513 179.515 164.897 1.00 33.10 H
ATOM 1108 HG11 VAL A 124 150.185 181.353 166.224 1.00 32.41 H
ATOM 1109 HG12 VAL A 124 149.107 180.431 166.931 1.00 30.17 H
ATOM 1110 HG13 VAL A 124 148.663 181.806 166.280 1.00 31.43 H
ATOM 1111 HG21 VAL A 124 147.330 179.299 165.439 1.00 37.24 H
ATOM 1112 HG22 VAL A 124 147.006 180.780 164.965 1.00 37.29 H
ATOM 1113 HG23 VAL A 124 147.360 179.661 163.893 1.00 38.52 H
ATOM 1114 N GLY A 125 147.720 182.617 162.721 1.00 45.57 N
ATOM 1115 CA GLY A 125 146.757 183.695 162.693 1.00 38.93 C
ATOM 1116 C GLY A 125 145.427 183.272 163.302 1.00 41.69 C
ATOM 1117 O GLY A 125 145.265 182.174 163.827 1.00 51.03 O
ATOM 1118 H GLY A 125 147.635 182.063 162.069 1.00 42.93 H
ATOM 1119 HA2 GLY A 125 147.100 184.454 163.190 1.00 40.98 H
ATOM 1120 HA3 GLY A 125 146.604 183.970 161.776 1.00 41.55 H
ATOM 1121 N TYR A 126 144.460 184.181 163.224 1.00 35.86 N
ATOM 1122 CA TYR A 126 143.121 183.879 163.707 1.00 35.61 C
ATOM 1123 C TYR A 126 142.159 184.911 163.147 1.00 32.65 C
ATOM 1124 O TYR A 126 142.526 186.068 162.940 1.00 38.20 O
ATOM 1125 CB TYR A 126 143.059 183.874 165.235 1.00 34.00 C
ATOM 1126 CG TYR A 126 141.842 183.172 165.785 1.00 44.41 C
ATOM 1127 CD1 TYR A 126 141.805 181.788 165.882 1.00 46.64 C
ATOM 1128 CD2 TYR A 126 140.722 183.885 166.183 1.00 51.27 C
ATOM 1129 CE1 TYR A 126 140.698 181.135 166.377 1.00 48.18 C
ATOM 1130 CE2 TYR A 126 139.606 183.240 166.680 1.00 57.38 C
ATOM 1131 CZ TYR A 126 139.599 181.864 166.773 1.00 57.99 C
ATOM 1132 OH TYR A 126 138.490 181.217 167.265 1.00 62.78 O
ATOM 1133 H TYR A 126 144.553 184.972 162.900 1.00 37.55 H
ATOM 1134 HA TYR A 126 142.853 183.004 163.387 1.00 40.12 H
ATOM 1135 HB2 TYR A 126 143.846 183.426 165.582 1.00 38.96 H
ATOM 1136 HB3 TYR A 126 143.037 184.793 165.545 1.00 38.35 H
ATOM 1137 HD1 TYR A 126 142.546 181.292 165.617 1.00 45.77 H
ATOM 1138 HD2 TYR A 126 140.725 184.813 166.122 1.00 47.08 H
ATOM 1139 HE1 TYR A 126 140.690 180.207 166.440 1.00 48.78 H
ATOM 1140 HE2 TYR A 126 138.862 183.730 166.948 1.00 55.01 H
ATOM 1141 HH TYR A 126 137.852 181.758 167.336 1.00 58.40 H
ATOM 1142 N GLY A 127 140.927 184.480 162.908 1.00 35.36 N
ATOM 1143 CA GLY A 127 139.923 185.358 162.342 1.00 41.83 C
ATOM 1144 C GLY A 127 138.573 185.201 163.004 1.00 44.76 C
ATOM 1145 O GLY A 127 138.164 184.085 163.335 1.00 51.03 O
ATOM 1146 H GLY A 127 140.650 183.682 163.066 1.00 39.91 H
ATOM 1147 HA2 GLY A 127 140.204 186.281 162.440 1.00 40.37 H
ATOM 1148 HA3 GLY A 127 139.824 185.166 161.396 1.00 41.79 H
ATOM 1149 N VAL A 128 137.872 186.311 163.203 1.00 44.56 N
ATOM 1150 CA VAL A 128 136.575 186.320 163.866 1.00 52.12 C
ATOM 1151 C VAL A 128 135.620 187.170 163.044 1.00 58.51 C
ATOM 1152 O VAL A 128 135.971 188.278 162.624 1.00 62.68 O
ATOM 1153 CB VAL A 128 136.675 186.855 165.309 1.00 50.26 C
ATOM 1154 CG1 VAL A 128 135.350 186.685 166.035 1.00 56.95 C
ATOM 1155 CG2 VAL A 128 137.793 186.149 166.057 1.00 45.84 C
ATOM 1156 H VAL A 128 138.134 187.092 162.956 1.00 47.78 H
ATOM 1157 HA VAL A 128 136.226 185.416 163.901 1.00 51.87 H
ATOM 1158 HB VAL A 128 136.883 187.802 165.282 1.00 50.92 H
ATOM 1159 HG11 VAL A 128 134.716 186.255 165.441 1.00 55.79 H
ATOM 1160 HG12 VAL A 128 135.480 186.139 166.825 1.00 53.92 H
ATOM 1161 HG13 VAL A 128 135.018 187.560 166.291 1.00 54.12 H
ATOM 1162 HG21 VAL A 128 138.633 186.589 165.855 1.00 48.25 H
ATOM 1163 HG22 VAL A 128 137.827 185.224 165.766 1.00 48.85 H
ATOM 1164 HG23 VAL A 128 137.621 186.189 167.010 1.00 47.66 H
ATOM 1165 N SER A 129 134.417 186.648 162.810 1.00 64.83 N
ATOM 1166 CA SER A 129 133.341 187.381 162.157 1.00 67.94 C
ATOM 1167 C SER A 129 132.107 187.319 163.041 1.00 65.85 C
ATOM 1168 O SER A 129 131.691 186.232 163.454 1.00 71.06 O
ATOM 1169 CB SER A 129 133.028 186.804 160.775 1.00 66.16 C
ATOM 1170 OG SER A 129 131.744 187.204 160.338 1.00 60.44 O
ATOM 1171 H SER A 129 134.197 185.845 163.028 1.00 60.96 H
ATOM 1172 HA SER A 129 133.596 188.311 162.052 1.00 64.13 H
ATOM 1173 HB2 SER A 129 133.690 187.124 160.143 1.00 65.59 H
ATOM 1174 HB3 SER A 129 133.056 185.838 160.823 1.00 64.91 H
ATOM 1175 HG SER A 129 131.600 186.912 159.564 1.00 61.34 H
ATOM 1176 N GLU A 130 131.530 188.479 163.336 1.00 68.57 N
ATOM 1177 CA GLU A 130 130.346 188.544 164.177 1.00 78.27 C
ATOM 1178 C GLU A 130 129.475 189.701 163.714 1.00 83.21 C
ATOM 1179 O GLU A 130 129.952 190.661 163.104 1.00 84.54 O
ATOM 1180 CB GLU A 130 130.713 188.709 165.656 1.00 78.14 C
ATOM 1181 CG GLU A 130 131.615 187.615 166.197 1.00 76.37 C
ATOM 1182 CD GLU A 130 131.684 187.614 167.713 1.00 83.04 C
ATOM 1183 OE1 GLU A 130 131.270 188.619 168.328 1.00 83.81 O
ATOM 1184 OE2 GLU A 130 132.155 186.611 168.289 1.00 83.68 O
ATOM 1185 H GLU A 130 131.808 189.245 163.059 1.00 70.39 H
ATOM 1186 HA GLU A 130 129.839 187.724 164.080 1.00 75.51 H
ATOM 1187 HB2 GLU A 130 131.174 189.555 165.771 1.00 78.04 H
ATOM 1188 HB3 GLU A 130 129.897 188.707 166.182 1.00 78.43 H
ATOM 1189 HG2 GLU A 130 131.273 186.753 165.912 1.00 75.39 H
ATOM 1190 HG3 GLU A 130 132.513 187.747 165.855 1.00 73.59 H
ATOM 1191 N GLY A 131 128.185 189.595 164.012 1.00 85.79 N
ATOM 1192 CA GLY A 131 127.206 190.600 163.641 1.00 81.00 C
ATOM 1193 C GLY A 131 126.629 190.419 162.253 1.00 77.79 C
ATOM 1194 O GLY A 131 125.414 190.507 162.071 1.00 82.84 O
ATOM 1195 H GLY A 131 127.848 188.931 164.441 1.00 82.36 H
ATOM 1196 HA2 GLY A 131 126.474 190.581 164.276 1.00 82.59 H
ATOM 1197 HA3 GLY A 131 127.619 191.477 163.683 1.00 81.97 H
ATOM 1198 N LEU A 132 127.483 190.162 161.266 1.00 72.08 N
ATOM 1199 CA LEU A 132 127.017 190.015 159.895 1.00 74.67 C
ATOM 1200 C LEU A 132 126.074 188.824 159.791 1.00 79.68 C
ATOM 1201 O LEU A 132 126.449 187.693 160.115 1.00 77.23 O
ATOM 1202 CB LEU A 132 128.209 189.845 158.956 1.00 74.42 C
ATOM 1203 CG LEU A 132 127.919 190.013 157.464 1.00 76.84 C
ATOM 1204 CD1 LEU A 132 129.167 190.479 156.729 1.00 74.99 C
ATOM 1205 CD2 LEU A 132 127.391 188.725 156.856 1.00 75.67 C
ATOM 1206 H LEU A 132 128.333 190.070 161.365 1.00 75.46 H
ATOM 1207 HA LEU A 132 126.532 190.813 159.632 1.00 76.05 H
ATOM 1208 HB2 LEU A 132 128.880 190.503 159.195 1.00 74.80 H
ATOM 1209 HB3 LEU A 132 128.573 188.955 159.085 1.00 75.93 H
ATOM 1210 HG LEU A 132 127.237 190.694 157.353 1.00 75.93 H
ATOM 1211 HD11 LEU A 132 129.443 191.336 157.089 1.00 74.91 H
ATOM 1212 HD12 LEU A 132 128.962 190.568 155.785 1.00 75.17 H
ATOM 1213 HD13 LEU A 132 129.870 189.823 156.855 1.00 75.12 H
ATOM 1214 HD21 LEU A 132 127.905 187.977 157.197 1.00 75.66 H
ATOM 1215 HD22 LEU A 132 127.477 188.773 155.891 1.00 76.00 H
ATOM 1216 HD23 LEU A 132 126.458 188.624 157.099 1.00 75.55 H
ATOM 1217 N LYS A 133 124.850 189.081 159.336 1.00 83.17 N
ATOM 1218 CA LYS A 133 123.805 188.059 159.287 1.00 83.55 C
ATOM 1219 C LYS A 133 123.781 187.377 157.919 1.00 78.28 C
ATOM 1220 O LYS A 133 122.809 187.449 157.170 1.00 79.32 O
ATOM 1221 CB LYS A 133 122.450 188.679 159.612 1.00 85.17 C
ATOM 1222 CG LYS A 133 122.250 189.020 161.079 1.00 88.89 C
ATOM 1223 CD LYS A 133 120.892 189.661 161.318 1.00 92.83 C
ATOM 1224 CE LYS A 133 120.641 189.896 162.799 1.00 96.14 C
ATOM 1225 NZ LYS A 133 119.312 190.518 163.050 1.00 99.41 N
ATOM 1226 H LYS A 133 124.596 189.850 159.047 1.00 81.58 H
ATOM 1227 HA LYS A 133 123.992 187.382 159.956 1.00 81.73 H
ATOM 1228 HB2 LYS A 133 122.354 189.499 159.103 1.00 84.25 H
ATOM 1229 HB3 LYS A 133 121.754 188.053 159.358 1.00 84.46 H
ATOM 1230 HG2 LYS A 133 122.293 188.207 161.604 1.00 87.28 H
ATOM 1231 HG3 LYS A 133 122.938 189.642 161.362 1.00 86.50 H
ATOM 1232 HD2 LYS A 133 120.858 190.517 160.864 1.00 91.95 H
ATOM 1233 HD3 LYS A 133 120.197 189.074 160.981 1.00 91.26 H
ATOM 1234 HE2 LYS A 133 120.668 189.045 163.264 1.00 92.04 H
ATOM 1235 HE3 LYS A 133 121.324 190.490 163.148 1.00 93.86 H
ATOM 1236 HZ1 LYS A 133 119.196 190.647 163.923 1.00 97.58 H
ATOM 1237 HZ2 LYS A 133 119.260 191.303 162.632 1.00 98.59 H
ATOM 1238 HZ3 LYS A 133 118.665 189.986 162.748 1.00 98.11 H
ATOM 1239 N SER A 134 124.882 186.703 157.598 1.00 74.22 N
ATOM 1240 CA SER A 134 124.952 185.952 156.353 1.00 74.91 C
ATOM 1241 C SER A 134 126.208 185.097 156.350 1.00 76.69 C
ATOM 1242 O SER A 134 127.263 185.535 156.815 1.00 77.08 O
ATOM 1243 CB SER A 134 124.950 186.888 155.137 1.00 73.81 C
ATOM 1244 OG SER A 134 124.947 186.150 153.929 1.00 72.13 O
ATOM 1245 H SER A 134 125.594 186.666 158.079 1.00 75.55 H
ATOM 1246 HA SER A 134 124.182 185.365 156.288 1.00 75.20 H
ATOM 1247 HB2 SER A 134 124.158 187.446 155.166 1.00 75.05 H
ATOM 1248 HB3 SER A 134 125.746 187.440 155.163 1.00 75.36 H
ATOM 1249 HG SER A 134 124.943 186.674 153.273 1.00 73.24 H
ATOM 1250 N LYS A 135 126.082 183.877 155.824 1.00 73.58 N
ATOM 1251 CA LYS A 135 127.252 183.032 155.627 1.00 70.55 C
ATOM 1252 C LYS A 135 128.137 183.561 154.509 1.00 73.55 C
ATOM 1253 O LYS A 135 129.365 183.447 154.584 1.00 72.18 O
ATOM 1254 CB LYS A 135 126.815 181.601 155.318 1.00 66.14 C
ATOM 1255 CG LYS A 135 127.961 180.611 155.234 1.00 68.72 C
ATOM 1256 CD LYS A 135 127.474 179.205 154.933 1.00 69.25 C
ATOM 1257 CE LYS A 135 126.749 178.590 156.119 1.00 69.57 C
ATOM 1258 NZ LYS A 135 127.668 178.344 157.264 1.00 72.82 N
ATOM 1259 H LYS A 135 125.338 183.523 155.576 1.00 72.88 H
ATOM 1260 HA LYS A 135 127.774 183.018 156.444 1.00 71.86 H
ATOM 1261 HB2 LYS A 135 126.208 181.303 156.010 1.00 67.75 H
ATOM 1262 HB3 LYS A 135 126.360 181.596 154.461 1.00 68.71 H
ATOM 1263 HG2 LYS A 135 128.563 180.878 154.522 1.00 69.23 H
ATOM 1264 HG3 LYS A 135 128.432 180.595 156.082 1.00 69.18 H
ATOM 1265 HD2 LYS A 135 126.858 179.235 154.184 1.00 69.56 H
ATOM 1266 HD3 LYS A 135 128.235 178.644 154.718 1.00 69.66 H
ATOM 1267 HE2 LYS A 135 126.045 179.186 156.417 1.00 69.74 H
ATOM 1268 HE3 LYS A 135 126.371 177.738 155.850 1.00 69.51 H
ATOM 1269 HZ1 LYS A 135 127.223 177.966 157.936 1.00 72.34 H
ATOM 1270 HZ2 LYS A 135 128.328 177.802 157.013 1.00 72.51 H
ATOM 1271 HZ3 LYS A 135 128.017 179.113 157.545 1.00 71.73 H
ATOM 1272 N ALA A 136 127.537 184.141 153.472 1.00 82.23 N
ATOM 1273 CA ALA A 136 128.302 184.629 152.335 1.00 81.50 C
ATOM 1274 C ALA A 136 129.184 185.800 152.749 1.00 82.35 C
ATOM 1275 O ALA A 136 128.737 186.712 153.451 1.00 83.00 O
ATOM 1276 CB ALA A 136 127.361 185.051 151.208 1.00 82.45 C
ATOM 1277 H ALA A 136 126.688 184.263 153.406 1.00 79.27 H
ATOM 1278 HA ALA A 136 128.874 183.919 152.004 1.00 78.43 H
ATOM 1279 HB1 ALA A 136 126.831 184.285 150.937 1.00 80.70 H
ATOM 1280 HB2 ALA A 136 126.781 185.758 151.531 1.00 79.85 H
ATOM 1281 HB3 ALA A 136 127.888 185.371 150.459 1.00 82.08 H
ATOM 1282 N LEU A 137 130.440 185.769 152.313 1.00 81.45 N
ATOM 1283 CA LEU A 137 131.425 186.818 152.560 1.00 84.52 C
ATOM 1284 C LEU A 137 131.725 187.018 154.042 1.00 79.80 C
ATOM 1285 O LEU A 137 132.442 187.960 154.401 1.00 75.00 O
ATOM 1286 CB LEU A 137 130.986 188.151 151.937 1.00 87.43 C
ATOM 1287 CG LEU A 137 131.368 188.366 150.469 1.00 86.02 C
ATOM 1288 CD1 LEU A 137 132.875 188.518 150.310 1.00 81.82 C
ATOM 1289 CD2 LEU A 137 130.850 187.227 149.602 1.00 83.63 C
ATOM 1290 H LEU A 137 130.758 185.118 151.850 1.00 81.63 H
ATOM 1291 HA LEU A 137 132.256 186.557 152.134 1.00 84.31 H
ATOM 1292 HB2 LEU A 137 130.020 188.219 151.995 1.00 85.35 H
ATOM 1293 HB3 LEU A 137 131.387 188.873 152.444 1.00 85.20 H
ATOM 1294 HG LEU A 137 130.955 189.186 150.156 1.00 84.19 H
ATOM 1295 HD11 LEU A 137 133.192 189.192 150.932 1.00 83.97 H
ATOM 1296 HD12 LEU A 137 133.070 188.790 149.400 1.00 83.61 H
ATOM 1297 HD13 LEU A 137 133.302 187.667 150.499 1.00 83.66 H
ATOM 1298 HD21 LEU A 137 131.022 187.437 148.671 1.00 83.49 H
ATOM 1299 HD22 LEU A 137 131.309 186.408 149.846 1.00 82.99 H
ATOM 1300 HD23 LEU A 137 129.896 187.128 149.748 1.00 83.95 H
ATOM 1301 N SER A 138 131.203 186.157 154.916 1.00 75.87 N
ATOM 1302 CA SER A 138 131.530 186.217 156.338 1.00 71.91 C
ATOM 1303 C SER A 138 132.714 185.309 156.656 1.00 61.13 C
ATOM 1304 O SER A 138 133.751 185.772 157.144 1.00 57.56 O
ATOM 1305 CB SER A 138 130.311 185.827 157.179 1.00 70.03 C
ATOM 1306 OG SER A 138 130.604 185.901 158.563 1.00 65.46 O
ATOM 1307 H SER A 138 130.660 185.524 154.713 1.00 75.93 H
ATOM 1308 HA SER A 138 131.776 187.126 156.571 1.00 72.51 H
ATOM 1309 HB2 SER A 138 129.582 186.434 156.978 1.00 72.14 H
ATOM 1310 HB3 SER A 138 130.054 184.917 156.959 1.00 71.23 H
ATOM 1311 HG SER A 138 129.927 185.687 159.012 1.00 67.05 H
ATOM 1312 N LEU A 139 132.572 184.014 156.375 1.00 57.59 N
ATOM 1313 CA LEU A 139 133.702 183.114 156.549 1.00 64.77 C
ATOM 1314 C LEU A 139 134.875 183.548 155.685 1.00 63.93 C
ATOM 1315 O LEU A 139 136.033 183.354 156.069 1.00 61.97 O
ATOM 1316 CB LEU A 139 133.291 181.674 156.232 1.00 61.87 C
ATOM 1317 CG LEU A 139 133.196 181.254 154.765 1.00 62.83 C
ATOM 1318 CD1 LEU A 139 133.054 179.747 154.667 1.00 61.67 C
ATOM 1319 CD2 LEU A 139 132.034 181.947 154.072 1.00 67.03 C
ATOM 1320 H LEU A 139 131.851 183.642 156.090 1.00 63.71 H
ATOM 1321 HA LEU A 139 133.989 183.147 157.474 1.00 63.42 H
ATOM 1322 HB2 LEU A 139 133.934 181.083 156.653 1.00 60.03 H
ATOM 1323 HB3 LEU A 139 132.417 181.521 156.626 1.00 61.93 H
ATOM 1324 HG LEU A 139 134.012 181.502 154.303 1.00 62.81 H
ATOM 1325 HD11 LEU A 139 132.989 179.496 153.732 1.00 63.72 H
ATOM 1326 HD12 LEU A 139 133.833 179.330 155.068 1.00 61.92 H
ATOM 1327 HD13 LEU A 139 132.252 179.474 155.139 1.00 62.12 H
ATOM 1328 HD21 LEU A 139 131.953 181.600 153.169 1.00 67.09 H
ATOM 1329 HD22 LEU A 139 131.220 181.767 154.568 1.00 67.88 H
ATOM 1330 HD23 LEU A 139 132.202 182.901 154.046 1.00 68.33 H
ATOM 1331 N GLU A 140 134.602 184.159 154.531 1.00 55.21 N
ATOM 1332 CA GLU A 140 135.686 184.710 153.726 1.00 57.40 C
ATOM 1333 C GLU A 140 136.388 185.847 154.462 1.00 57.57 C
ATOM 1334 O GLU A 140 137.621 185.963 154.416 1.00 52.59 O
ATOM 1335 CB GLU A 140 135.148 185.186 152.377 1.00 53.89 C
ATOM 1336 CG GLU A 140 136.174 185.152 151.256 1.00 51.70 C
ATOM 1337 CD GLU A 140 135.540 185.054 149.886 1.00 51.23 C
ATOM 1338 OE1 GLU A 140 134.679 184.174 149.690 1.00 51.89 O
ATOM 1339 OE2 GLU A 140 135.905 185.855 149.002 1.00 51.78 O
ATOM 1340 H GLU A 140 133.816 184.265 154.200 1.00 59.29 H
ATOM 1341 HA GLU A 140 136.340 184.013 153.561 1.00 58.08 H
ATOM 1342 HB2 GLU A 140 134.406 184.617 152.118 1.00 57.93 H
ATOM 1343 HB3 GLU A 140 134.842 186.102 152.469 1.00 58.89 H
ATOM 1344 HG2 GLU A 140 136.703 185.963 151.283 1.00 53.54 H
ATOM 1345 HG3 GLU A 140 136.747 184.379 151.374 1.00 52.30 H
ATOM 1346 N LYS A 141 135.619 186.700 155.146 1.00 55.69 N
ATOM 1347 CA LYS A 141 136.226 187.774 155.926 1.00 53.10 C
ATOM 1348 C LYS A 141 137.093 187.212 157.043 1.00 53.08 C
ATOM 1349 O LYS A 141 138.204 187.701 157.287 1.00 51.31 O
ATOM 1350 CB LYS A 141 135.142 188.685 156.501 1.00 55.41 C
ATOM 1351 CG LYS A 141 134.840 189.898 155.636 1.00 59.60 C
ATOM 1352 CD LYS A 141 133.787 190.799 156.266 1.00 68.50 C
ATOM 1353 CE LYS A 141 134.334 191.546 157.472 1.00 70.43 C
ATOM 1354 NZ LYS A 141 133.351 192.521 158.022 1.00 71.99 N
ATOM 1355 H LYS A 141 134.760 186.677 155.172 1.00 58.58 H
ATOM 1356 HA LYS A 141 136.790 188.307 155.345 1.00 55.86 H
ATOM 1357 HB2 LYS A 141 134.322 188.176 156.597 1.00 60.09 H
ATOM 1358 HB3 LYS A 141 135.434 189.003 157.369 1.00 56.46 H
ATOM 1359 HG2 LYS A 141 135.651 190.416 155.519 1.00 58.99 H
ATOM 1360 HG3 LYS A 141 134.507 189.600 154.775 1.00 62.88 H
ATOM 1361 HD2 LYS A 141 133.492 191.451 155.612 1.00 68.05 H
ATOM 1362 HD3 LYS A 141 133.038 190.257 156.559 1.00 66.84 H
ATOM 1363 HE2 LYS A 141 134.549 190.910 158.172 1.00 67.22 H
ATOM 1364 HE3 LYS A 141 135.129 192.035 157.209 1.00 68.35 H
ATOM 1365 HZ1 LYS A 141 133.699 192.939 158.726 1.00 71.03 H
ATOM 1366 HZ2 LYS A 141 133.142 193.124 157.402 1.00 70.58 H
ATOM 1367 HZ3 LYS A 141 132.610 192.096 158.274 1.00 71.90 H
ATOM 1368 N ALA A 142 136.600 186.181 157.732 1.00 53.40 N
ATOM 1369 CA ALA A 142 137.401 185.547 158.773 1.00 46.18 C
ATOM 1370 C ALA A 142 138.676 184.954 158.193 1.00 42.03 C
ATOM 1371 O ALA A 142 139.749 185.063 158.794 1.00 42.04 O
ATOM 1372 CB ALA A 142 136.584 184.471 159.483 1.00 50.12 C
ATOM 1373 H ALA A 142 135.820 185.838 157.618 1.00 55.10 H
ATOM 1374 HA ALA A 142 137.652 186.215 159.430 1.00 49.78 H
ATOM 1375 HB1 ALA A 142 135.793 184.880 159.870 1.00 52.68 H
ATOM 1376 HB2 ALA A 142 136.324 183.795 158.838 1.00 51.73 H
ATOM 1377 HB3 ALA A 142 137.126 184.073 160.182 1.00 48.22 H
ATOM 1378 N ARG A 143 138.577 184.320 157.026 1.00 37.88 N
ATOM 1379 CA ARG A 143 139.757 183.762 156.374 1.00 41.33 C
ATOM 1380 C ARG A 143 140.794 184.840 156.083 1.00 41.97 C
ATOM 1381 O ARG A 143 141.985 184.674 156.382 1.00 42.94 O
ATOM 1382 CB ARG A 143 139.338 183.059 155.085 1.00 43.95 C
ATOM 1383 CG ARG A 143 140.487 182.502 154.266 1.00 50.87 C
ATOM 1384 CD ARG A 143 140.845 183.444 153.122 1.00 48.92 C
ATOM 1385 NE ARG A 143 141.763 182.833 152.169 1.00 49.35 N
ATOM 1386 CZ ARG A 143 142.354 183.482 151.176 1.00 51.62 C
ATOM 1387 NH1 ARG A 143 142.142 184.771 150.970 1.00 50.84 N
ATOM 1388 NH2 ARG A 143 143.178 182.821 150.369 1.00 54.17 N
ATOM 1389 H ARG A 143 137.843 184.202 156.594 1.00 45.78 H
ATOM 1390 HA ARG A 143 140.162 183.104 156.959 1.00 43.99 H
ATOM 1391 HB2 ARG A 143 138.754 182.319 155.313 1.00 45.02 H
ATOM 1392 HB3 ARG A 143 138.858 183.693 154.530 1.00 47.64 H
ATOM 1393 HG2 ARG A 143 141.267 182.397 154.833 1.00 49.11 H
ATOM 1394 HG3 ARG A 143 140.227 181.647 153.888 1.00 49.18 H
ATOM 1395 HD2 ARG A 143 140.037 183.687 152.643 1.00 49.95 H
ATOM 1396 HD3 ARG A 143 141.271 184.236 153.482 1.00 47.68 H
ATOM 1397 HE ARG A 143 141.957 182.002 152.276 1.00 48.81 H
ATOM 1398 HH11 ARG A 143 141.612 185.210 151.485 1.00 50.26 H
ATOM 1399 HH12 ARG A 143 142.537 185.171 150.319 1.00 51.28 H
ATOM 1400 HH21 ARG A 143 143.322 181.982 150.495 1.00 53.48 H
ATOM 1401 HH22 ARG A 143 143.567 183.231 149.721 1.00 53.52 H
ATOM 1402 N LYS A 144 140.360 185.951 155.486 1.00 42.33 N
ATOM 1403 CA LYS A 144 141.292 187.025 155.156 1.00 34.86 C
ATOM 1404 C LYS A 144 141.934 187.605 156.411 1.00 31.81 C
ATOM 1405 O LYS A 144 143.153 187.829 156.452 1.00 32.59 O
ATOM 1406 CB LYS A 144 140.564 188.110 154.370 1.00 36.24 C
ATOM 1407 CG LYS A 144 140.111 187.655 152.997 1.00 39.79 C
ATOM 1408 CD LYS A 144 139.554 188.800 152.177 1.00 46.78 C
ATOM 1409 CE LYS A 144 138.180 189.219 152.667 1.00 50.39 C
ATOM 1410 NZ LYS A 144 137.152 188.191 152.370 1.00 51.08 N
ATOM 1411 H LYS A 144 139.543 186.104 155.265 1.00 44.70 H
ATOM 1412 HA LYS A 144 141.998 186.669 154.594 1.00 38.45 H
ATOM 1413 HB2 LYS A 144 139.779 188.382 154.870 1.00 41.04 H
ATOM 1414 HB3 LYS A 144 141.160 188.866 154.252 1.00 38.33 H
ATOM 1415 HG2 LYS A 144 140.869 187.284 152.519 1.00 40.58 H
ATOM 1416 HG3 LYS A 144 139.418 186.985 153.094 1.00 44.92 H
ATOM 1417 HD2 LYS A 144 140.148 189.564 152.247 1.00 46.06 H
ATOM 1418 HD3 LYS A 144 139.474 188.521 151.251 1.00 46.43 H
ATOM 1419 HE2 LYS A 144 138.206 189.354 153.627 1.00 49.40 H
ATOM 1420 HE3 LYS A 144 137.922 190.041 152.222 1.00 49.49 H
ATOM 1421 HZ1 LYS A 144 137.054 188.105 151.489 1.00 51.77 H
ATOM 1422 HZ2 LYS A 144 136.372 188.428 152.726 1.00 52.93 H
ATOM 1423 HZ3 LYS A 144 137.399 187.407 152.711 1.00 50.64 H
ATOM 1424 N GLU A 145 141.132 187.837 157.453 1.00 30.29 N
ATOM 1425 CA GLU A 145 141.679 188.362 158.697 1.00 32.37 C
ATOM 1426 C GLU A 145 142.696 187.405 159.303 1.00 32.84 C
ATOM 1427 O GLU A 145 143.758 187.831 159.774 1.00 38.74 O
ATOM 1428 CB GLU A 145 140.550 188.634 159.689 1.00 38.56 C
ATOM 1429 CG GLU A 145 140.972 189.438 160.908 1.00 41.14 C
ATOM 1430 CD GLU A 145 141.420 190.844 160.557 1.00 47.01 C
ATOM 1431 OE1 GLU A 145 141.064 191.327 159.462 1.00 46.20 O
ATOM 1432 OE2 GLU A 145 142.129 191.465 161.377 1.00 58.15 O
ATOM 1433 H GLU A 145 140.283 187.700 157.462 1.00 37.05 H
ATOM 1434 HA GLU A 145 142.129 189.201 158.513 1.00 36.48 H
ATOM 1435 HB2 GLU A 145 139.850 189.130 159.236 1.00 40.39 H
ATOM 1436 HB3 GLU A 145 140.200 187.785 160.001 1.00 40.45 H
ATOM 1437 HG2 GLU A 145 140.221 189.506 161.517 1.00 43.17 H
ATOM 1438 HG3 GLU A 145 141.713 188.987 161.344 1.00 40.24 H
ATOM 1439 N ALA A 146 142.386 186.107 159.309 1.00 35.60 N
ATOM 1440 CA ALA A 146 143.300 185.134 159.890 1.00 25.96 C
ATOM 1441 C ALA A 146 144.608 185.084 159.120 1.00 27.65 C
ATOM 1442 O ALA A 146 145.689 185.035 159.720 1.00 35.13 O
ATOM 1443 CB ALA A 146 142.645 183.756 159.922 1.00 30.73 C
ATOM 1444 H ALA A 146 141.662 185.772 158.987 1.00 36.22 H
ATOM 1445 HA ALA A 146 143.501 185.393 160.802 1.00 31.63 H
ATOM 1446 HB1 ALA A 146 141.840 183.802 160.461 1.00 35.14 H
ATOM 1447 HB2 ALA A 146 143.266 183.120 160.309 1.00 34.40 H
ATOM 1448 HB3 ALA A 146 142.422 183.492 159.015 1.00 35.00 H
ATOM 1449 N VAL A 147 144.536 185.101 157.790 1.00 22.82 N
ATOM 1450 CA VAL A 147 145.761 185.074 156.999 1.00 24.98 C
ATOM 1451 C VAL A 147 146.609 186.303 157.291 1.00 31.18 C
ATOM 1452 O VAL A 147 147.833 186.206 157.460 1.00 34.83 O
ATOM 1453 CB VAL A 147 145.436 184.961 155.501 1.00 25.23 C
ATOM 1454 CG1 VAL A 147 146.656 185.300 154.671 1.00 24.62 C
ATOM 1455 CG2 VAL A 147 144.941 183.566 155.177 1.00 34.93 C
ATOM 1456 H VAL A 147 143.809 185.127 157.332 1.00 29.29 H
ATOM 1457 HA VAL A 147 146.278 184.293 157.250 1.00 29.08 H
ATOM 1458 HB VAL A 147 144.733 185.591 155.278 1.00 29.76 H
ATOM 1459 HG11 VAL A 147 146.577 184.874 153.804 1.00 26.52 H
ATOM 1460 HG12 VAL A 147 147.451 184.978 155.125 1.00 27.88 H
ATOM 1461 HG13 VAL A 147 146.703 186.262 154.557 1.00 25.82 H
ATOM 1462 HG21 VAL A 147 144.744 183.100 156.005 1.00 33.89 H
ATOM 1463 HG22 VAL A 147 144.137 183.635 154.638 1.00 37.13 H
ATOM 1464 HG23 VAL A 147 145.627 183.089 154.685 1.00 35.70 H
ATOM 1465 N THR A 148 145.985 187.482 157.344 1.00 29.06 N
ATOM 1466 CA THR A 148 146.759 188.694 157.596 1.00 27.59 C
ATOM 1467 C THR A 148 147.397 188.666 158.979 1.00 27.49 C
ATOM 1468 O THR A 148 148.566 189.043 159.142 1.00 30.33 O
ATOM 1469 CB THR A 148 145.873 189.928 157.437 1.00 30.32 C
ATOM 1470 OG1 THR A 148 145.353 189.975 156.102 1.00 30.93 O
ATOM 1471 CG2 THR A 148 146.664 191.201 157.710 1.00 33.93 C
ATOM 1472 H THR A 148 145.140 187.603 157.241 1.00 31.35 H
ATOM 1473 HA THR A 148 147.472 188.752 156.941 1.00 29.19 H
ATOM 1474 HB THR A 148 145.138 189.882 158.068 1.00 31.47 H
ATOM 1475 HG1 THR A 148 144.845 190.638 156.016 1.00 30.99 H
ATOM 1476 HG21 THR A 148 146.132 191.976 157.471 1.00 32.64 H
ATOM 1477 HG22 THR A 148 146.895 191.258 158.650 1.00 31.82 H
ATOM 1478 HG23 THR A 148 147.478 191.204 157.182 1.00 33.25 H
ATOM 1479 N ASP A 149 146.646 188.230 159.992 1.00 24.69 N
ATOM 1480 CA ASP A 149 147.205 188.157 161.336 1.00 27.34 C
ATOM 1481 C ASP A 149 148.377 187.186 161.384 1.00 32.92 C
ATOM 1482 O ASP A 149 149.409 187.469 162.008 1.00 33.59 O
ATOM 1483 CB ASP A 149 146.122 187.745 162.329 1.00 37.71 C
ATOM 1484 CG ASP A 149 146.585 187.835 163.768 1.00 44.88 C
ATOM 1485 OD1 ASP A 149 147.488 188.649 164.054 1.00 44.65 O
ATOM 1486 OD2 ASP A 149 146.045 187.096 164.615 1.00 45.13 O
ATOM 1487 H ASP A 149 145.827 187.976 159.927 1.00 29.87 H
ATOM 1488 HA ASP A 149 147.530 189.035 161.591 1.00 29.62 H
ATOM 1489 HB2 ASP A 149 145.356 188.330 162.224 1.00 36.42 H
ATOM 1490 HB3 ASP A 149 145.865 186.826 162.153 1.00 36.32 H
ATOM 1491 N GLY A 150 148.244 186.040 160.714 1.00 33.06 N
ATOM 1492 CA GLY A 150 149.344 185.095 160.665 1.00 33.93 C
ATOM 1493 C GLY A 150 150.576 185.667 159.993 1.00 33.80 C
ATOM 1494 O GLY A 150 151.698 185.454 160.453 1.00 40.64 O
ATOM 1495 H GLY A 150 147.538 185.796 160.289 1.00 33.32 H
ATOM 1496 HA2 GLY A 150 149.582 184.831 161.567 1.00 36.65 H
ATOM 1497 HA3 GLY A 150 149.067 184.305 160.176 1.00 34.66 H
ATOM 1498 N LEU A 151 150.390 186.387 158.887 1.00 30.02 N
ATOM 1499 CA LEU A 151 151.538 186.969 158.199 1.00 27.83 C
ATOM 1500 C LEU A 151 152.231 188.006 159.072 1.00 26.80 C
ATOM 1501 O LEU A 151 153.468 188.054 159.134 1.00 34.17 O
ATOM 1502 CB LEU A 151 151.099 187.590 156.876 1.00 27.18 C
ATOM 1503 CG LEU A 151 152.206 188.235 156.048 1.00 27.04 C
ATOM 1504 CD1 LEU A 151 153.245 187.210 155.645 1.00 34.73 C
ATOM 1505 CD2 LEU A 151 151.627 188.915 154.820 1.00 32.86 C
ATOM 1506 H LEU A 151 149.628 186.549 158.523 1.00 31.36 H
ATOM 1507 HA LEU A 151 152.177 186.266 158.005 1.00 30.69 H
ATOM 1508 HB2 LEU A 151 150.696 186.896 156.331 1.00 29.76 H
ATOM 1509 HB3 LEU A 151 150.440 188.277 157.064 1.00 29.68 H
ATOM 1510 HG LEU A 151 152.648 188.915 156.580 1.00 28.71 H
ATOM 1511 HD11 LEU A 151 153.714 186.905 156.437 1.00 34.37 H
ATOM 1512 HD12 LEU A 151 153.871 187.623 155.029 1.00 36.23 H
ATOM 1513 HD13 LEU A 151 152.801 186.464 155.214 1.00 34.08 H
ATOM 1514 HD21 LEU A 151 151.175 188.251 154.276 1.00 31.64 H
ATOM 1515 HD22 LEU A 151 152.348 189.322 154.315 1.00 36.83 H
ATOM 1516 HD23 LEU A 151 150.996 189.595 155.104 1.00 32.42 H
ATOM 1517 N LYS A 152 151.453 188.839 159.762 1.00 30.80 N
ATOM 1518 CA LYS A 152 152.052 189.816 160.664 1.00 31.76 C
ATOM 1519 C LYS A 152 152.843 189.132 161.770 1.00 32.56 C
ATOM 1520 O LYS A 152 153.956 189.556 162.099 1.00 35.24 O
ATOM 1521 CB LYS A 152 150.974 190.713 161.270 1.00 35.07 C
ATOM 1522 CG LYS A 152 150.341 191.683 160.291 1.00 37.67 C
ATOM 1523 CD LYS A 152 149.473 192.699 161.016 1.00 42.37 C
ATOM 1524 CE LYS A 152 148.204 192.064 161.556 1.00 44.15 C
ATOM 1525 NZ LYS A 152 147.295 193.071 162.164 1.00 46.59 N
ATOM 1526 H LYS A 152 150.594 188.859 159.727 1.00 32.32 H
ATOM 1527 HA LYS A 152 152.663 190.378 160.162 1.00 33.46 H
ATOM 1528 HB2 LYS A 152 150.269 190.150 161.625 1.00 35.19 H
ATOM 1529 HB3 LYS A 152 151.370 191.233 161.987 1.00 34.70 H
ATOM 1530 HG2 LYS A 152 151.038 192.161 159.815 1.00 39.22 H
ATOM 1531 HG3 LYS A 152 149.783 191.193 159.668 1.00 34.97 H
ATOM 1532 HD2 LYS A 152 149.969 193.070 161.762 1.00 44.36 H
ATOM 1533 HD3 LYS A 152 149.221 193.403 160.398 1.00 45.15 H
ATOM 1534 HE2 LYS A 152 147.731 191.628 160.830 1.00 39.37 H
ATOM 1535 HE3 LYS A 152 148.437 191.417 162.240 1.00 40.80 H
ATOM 1536 HZ1 LYS A 152 147.705 193.485 162.837 1.00 48.08 H
ATOM 1537 HZ2 LYS A 152 146.562 192.671 162.474 1.00 44.96 H
ATOM 1538 HZ3 LYS A 152 147.058 193.674 161.554 1.00 46.93 H
ATOM 1539 N ARG A 153 152.287 188.075 162.358 1.00 34.41 N
ATOM 1540 CA ARG A 153 152.988 187.390 163.437 1.00 33.32 C
ATOM 1541 C ARG A 153 154.187 186.592 162.941 1.00 33.93 C
ATOM 1542 O ARG A 153 155.104 186.329 163.723 1.00 34.00 O
ATOM 1543 CB ARG A 153 152.025 186.472 164.179 1.00 34.65 C
ATOM 1544 CG ARG A 153 150.872 187.196 164.826 1.00 36.04 C
ATOM 1545 CD ARG A 153 150.151 186.293 165.777 1.00 31.65 C
ATOM 1546 NE ARG A 153 150.767 186.333 167.095 1.00 23.55 N
ATOM 1547 CZ ARG A 153 151.326 185.300 167.705 1.00 29.71 C
ATOM 1548 NH1 ARG A 153 151.389 184.108 167.139 1.00 36.32 N
ATOM 1549 NH2 ARG A 153 151.849 185.471 168.913 1.00 36.44 N
ATOM 1550 H ARG A 153 151.520 187.741 162.156 1.00 34.69 H
ATOM 1551 HA ARG A 153 153.313 188.052 164.067 1.00 33.15 H
ATOM 1552 HB2 ARG A 153 151.659 185.826 163.554 1.00 34.89 H
ATOM 1553 HB3 ARG A 153 152.509 186.014 164.881 1.00 35.27 H
ATOM 1554 HG2 ARG A 153 151.210 187.957 165.324 1.00 34.55 H
ATOM 1555 HG3 ARG A 153 150.246 187.490 164.149 1.00 35.30 H
ATOM 1556 HD2 ARG A 153 149.235 186.599 165.866 1.00 33.44 H
ATOM 1557 HD3 ARG A 153 150.166 185.390 165.430 1.00 34.99 H
ATOM 1558 HE ARG A 153 150.765 187.086 167.512 1.00 27.74 H
ATOM 1559 HH11 ARG A 153 151.059 183.974 166.358 1.00 36.43 H
ATOM 1560 HH12 ARG A 153 151.761 183.457 167.560 1.00 36.13 H
ATOM 1561 HH21 ARG A 153 151.814 186.244 169.288 1.00 33.86 H
ATOM 1562 HH22 ARG A 153 152.217 184.811 169.322 1.00 35.78 H
ATOM 1563 N ALA A 154 154.192 186.183 161.672 1.00 35.36 N
ATOM 1564 CA ALA A 154 155.351 185.502 161.107 1.00 36.47 C
ATOM 1565 C ALA A 154 156.492 186.470 160.819 1.00 35.91 C
ATOM 1566 O ALA A 154 157.654 186.162 161.106 1.00 40.64 O
ATOM 1567 CB ALA A 154 154.956 184.764 159.830 1.00 38.44 C
ATOM 1568 H ALA A 154 153.540 186.289 161.122 1.00 34.92 H
ATOM 1569 HA ALA A 154 155.672 184.845 161.745 1.00 36.82 H
ATOM 1570 HB1 ALA A 154 154.269 184.112 160.041 1.00 36.68 H
ATOM 1571 HB2 ALA A 154 154.617 185.406 159.187 1.00 35.98 H
ATOM 1572 HB3 ALA A 154 155.738 184.316 159.470 1.00 36.23 H
ATOM 1573 N LEU A 155 156.189 187.643 160.253 1.00 37.24 N
ATOM 1574 CA LEU A 155 157.240 188.620 159.983 1.00 28.47 C
ATOM 1575 C LEU A 155 157.823 189.223 161.251 1.00 28.38 C
ATOM 1576 O LEU A 155 158.848 189.905 161.177 1.00 35.76 O
ATOM 1577 CB LEU A 155 156.706 189.745 159.100 1.00 29.22 C
ATOM 1578 CG LEU A 155 156.620 189.464 157.604 1.00 32.85 C
ATOM 1579 CD1 LEU A 155 155.730 190.490 156.931 1.00 36.41 C
ATOM 1580 CD2 LEU A 155 157.999 189.461 156.974 1.00 38.77 C
ATOM 1581 H LEU A 155 155.399 187.890 160.022 1.00 35.79 H
ATOM 1582 HA LEU A 155 157.960 188.181 159.505 1.00 31.69 H
ATOM 1583 HB2 LEU A 155 155.811 189.967 159.402 1.00 32.35 H
ATOM 1584 HB3 LEU A 155 157.282 190.517 159.213 1.00 32.44 H
ATOM 1585 HG LEU A 155 156.225 188.589 157.468 1.00 34.15 H
ATOM 1586 HD11 LEU A 155 155.684 190.293 155.983 1.00 39.48 H
ATOM 1587 HD12 LEU A 155 156.109 191.373 157.067 1.00 41.68 H
ATOM 1588 HD13 LEU A 155 154.844 190.445 157.323 1.00 35.87 H
ATOM 1589 HD21 LEU A 155 157.907 189.327 156.017 1.00 41.59 H
ATOM 1590 HD22 LEU A 155 158.428 190.313 157.149 1.00 38.77 H
ATOM 1591 HD23 LEU A 155 158.522 188.741 157.359 1.00 36.82 H
ATOM 1592 N ARG A 156 157.198 189.000 162.400 1.00 27.35 N
ATOM 1593 CA ARG A 156 157.639 189.636 163.633 1.00 31.81 C
ATOM 1594 C ARG A 156 158.907 188.998 164.180 1.00 39.66 C
ATOM 1595 O ARG A 156 159.794 189.701 164.677 1.00 47.42 O
ATOM 1596 CB ARG A 156 156.517 189.561 164.669 1.00 40.85 C
ATOM 1597 CG ARG A 156 156.976 189.565 166.114 1.00 42.64 C
ATOM 1598 CD ARG A 156 155.802 189.751 167.060 1.00 45.08 C
ATOM 1599 NE ARG A 156 155.238 191.096 166.998 1.00 53.52 N
ATOM 1600 CZ ARG A 156 154.181 191.442 166.274 1.00 54.52 C
ATOM 1601 NH1 ARG A 156 153.536 190.565 165.521 1.00 48.04 N
ATOM 1602 NH2 ARG A 156 153.759 192.703 166.306 1.00 54.26 N
ATOM 1603 H ARG A 156 156.515 188.486 162.493 1.00 32.64 H
ATOM 1604 HA ARG A 156 157.825 190.572 163.458 1.00 34.68 H
ATOM 1605 HB2 ARG A 156 155.937 190.327 164.542 1.00 40.33 H
ATOM 1606 HB3 ARG A 156 156.015 188.744 164.524 1.00 39.68 H
ATOM 1607 HG2 ARG A 156 157.394 188.716 166.323 1.00 41.41 H
ATOM 1608 HG3 ARG A 156 157.600 190.294 166.253 1.00 43.07 H
ATOM 1609 HD2 ARG A 156 155.109 189.110 166.841 1.00 43.48 H
ATOM 1610 HD3 ARG A 156 156.109 189.603 167.968 1.00 45.72 H
ATOM 1611 HE ARG A 156 155.564 191.687 167.531 1.00 51.34 H
ATOM 1612 HH11 ARG A 156 153.794 189.746 165.487 1.00 43.23 H
ATOM 1613 HH12 ARG A 156 152.854 190.816 165.062 1.00 45.36 H
ATOM 1614 HH21 ARG A 156 154.169 193.282 166.791 1.00 53.07 H
ATOM 1615 HH22 ARG A 156 153.075 192.939 165.841 1.00 52.82 H
ATOM 1616 N SER A 157 159.011 187.670 164.100 1.00 40.90 N
ATOM 1617 CA SER A 157 160.109 186.963 164.746 1.00 32.63 C
ATOM 1618 C SER A 157 161.462 187.303 164.142 1.00 31.60 C
ATOM 1619 O SER A 157 162.491 187.000 164.754 1.00 36.84 O
ATOM 1620 CB SER A 157 159.870 185.458 164.668 1.00 34.20 C
ATOM 1621 OG SER A 157 159.624 185.051 163.334 1.00 42.82 O
ATOM 1622 H SER A 157 158.460 187.161 163.679 1.00 38.11 H
ATOM 1623 HA SER A 157 160.132 187.212 165.684 1.00 35.39 H
ATOM 1624 HB2 SER A 157 160.656 184.996 164.999 1.00 35.04 H
ATOM 1625 HB3 SER A 157 159.100 185.232 165.213 1.00 36.50 H
ATOM 1626 HG SER A 157 159.452 184.229 163.312 1.00 40.15 H
ATOM 1627 N PHE A 158 161.491 187.919 162.961 1.00 29.59 N
ATOM 1628 CA PHE A 158 162.765 188.269 162.346 1.00 30.13 C
ATOM 1629 C PHE A 158 163.520 189.296 163.183 1.00 40.96 C
ATOM 1630 O PHE A 158 164.715 189.134 163.451 1.00 45.52 O
ATOM 1631 CB PHE A 158 162.534 188.794 160.932 1.00 32.61 C
ATOM 1632 CG PHE A 158 162.406 187.714 159.903 1.00 31.13 C
ATOM 1633 CD1 PHE A 158 163.524 187.192 159.287 1.00 34.23 C
ATOM 1634 CD2 PHE A 158 161.166 187.223 159.547 1.00 40.84 C
ATOM 1635 CE1 PHE A 158 163.408 186.197 158.341 1.00 31.02 C
ATOM 1636 CE2 PHE A 158 161.048 186.232 158.598 1.00 37.65 C
ATOM 1637 CZ PHE A 158 162.172 185.719 157.997 1.00 29.45 C
ATOM 1638 H PHE A 158 160.798 188.141 162.503 1.00 34.79 H
ATOM 1639 HA PHE A 158 163.314 187.472 162.284 1.00 33.48 H
ATOM 1640 HB2 PHE A 158 161.715 189.313 160.921 1.00 34.84 H
ATOM 1641 HB3 PHE A 158 163.283 189.356 160.680 1.00 35.90 H
ATOM 1642 HD1 PHE A 158 164.367 187.512 159.517 1.00 36.62 H
ATOM 1643 HD2 PHE A 158 160.402 187.566 159.951 1.00 36.99 H
ATOM 1644 HE1 PHE A 158 164.169 185.852 157.934 1.00 33.74 H
ATOM 1645 HE2 PHE A 158 160.207 185.907 158.368 1.00 36.43 H
ATOM 1646 HZ PHE A 158 162.093 185.049 157.357 1.00 32.64 H
ATOM 1647 N GLY A 159 162.845 190.360 163.606 1.00 43.69 N
ATOM 1648 CA GLY A 159 163.524 191.401 164.357 1.00 42.23 C
ATOM 1649 C GLY A 159 162.575 192.511 164.752 1.00 42.57 C
ATOM 1650 O GLY A 159 161.376 192.475 164.460 1.00 43.05 O
ATOM 1651 H GLY A 159 162.007 190.499 163.473 1.00 40.42 H
ATOM 1652 HA2 GLY A 159 163.911 191.023 165.162 1.00 41.18 H
ATOM 1653 HA3 GLY A 159 164.236 191.780 163.818 1.00 44.46 H
ATOM 1654 N ASN A 160 163.147 193.514 165.426 1.00 42.94 N
ATOM 1655 CA ASN A 160 162.350 194.612 165.968 1.00 41.70 C
ATOM 1656 C ASN A 160 161.769 195.502 164.877 1.00 42.45 C
ATOM 1657 O ASN A 160 160.700 196.090 165.066 1.00 39.42 O
ATOM 1658 CB ASN A 160 163.197 195.452 166.917 1.00 38.30 C
ATOM 1659 CG ASN A 160 163.296 194.850 168.288 1.00 40.53 C
ATOM 1660 OD1 ASN A 160 162.285 194.590 168.935 1.00 45.56 O
ATOM 1661 ND2 ASN A 160 164.519 194.625 168.748 1.00 47.19 N
ATOM 1662 H ASN A 160 163.990 193.580 165.581 1.00 42.85 H
ATOM 1663 HA ASN A 160 161.611 194.243 166.474 1.00 42.56 H
ATOM 1664 HB2 ASN A 160 164.094 195.530 166.557 1.00 40.67 H
ATOM 1665 HB3 ASN A 160 162.796 196.331 167.004 1.00 40.16 H
ATOM 1666 HD21 ASN A 160 165.203 194.821 168.265 1.00 46.13 H
ATOM 1667 HD22 ASN A 160 164.628 194.282 169.528 1.00 45.55 H
ATOM 1668 N ALA A 161 162.454 195.628 163.743 1.00 45.64 N
ATOM 1669 CA ALA A 161 161.984 196.525 162.697 1.00 43.32 C
ATOM 1670 C ALA A 161 160.665 196.073 162.091 1.00 44.79 C
ATOM 1671 O ALA A 161 160.028 196.855 161.377 1.00 51.52 O
ATOM 1672 CB ALA A 161 163.037 196.645 161.598 1.00 48.93 C
ATOM 1673 H ALA A 161 163.184 195.211 163.558 1.00 47.61 H
ATOM 1674 HA ALA A 161 161.850 197.407 163.078 1.00 45.33 H
ATOM 1675 HB1 ALA A 161 163.855 196.999 161.981 1.00 50.69 H
ATOM 1676 HB2 ALA A 161 162.707 197.244 160.910 1.00 50.62 H
ATOM 1677 HB3 ALA A 161 163.199 195.767 161.222 1.00 49.63 H
ATOM 1678 N LEU A 162 160.242 194.837 162.350 1.00 42.21 N
ATOM 1679 CA LEU A 162 159.033 194.281 161.756 1.00 42.47 C
ATOM 1680 C LEU A 162 158.050 193.800 162.819 1.00 41.69 C
ATOM 1681 O LEU A 162 157.248 192.899 162.565 1.00 43.18 O
ATOM 1682 CB LEU A 162 159.387 193.140 160.804 1.00 43.30 C
ATOM 1683 CG LEU A 162 160.424 193.455 159.726 1.00 36.55 C
ATOM 1684 CD1 LEU A 162 160.890 192.188 159.050 1.00 42.56 C
ATOM 1685 CD2 LEU A 162 159.848 194.408 158.708 1.00 40.06 C
ATOM 1686 H LEU A 162 160.647 194.291 162.876 1.00 43.01 H
ATOM 1687 HA LEU A 162 158.590 194.970 161.238 1.00 44.41 H
ATOM 1688 HB2 LEU A 162 159.733 192.402 161.330 1.00 41.77 H
ATOM 1689 HB3 LEU A 162 158.577 192.859 160.351 1.00 41.37 H
ATOM 1690 HG LEU A 162 161.194 193.879 160.135 1.00 41.07 H
ATOM 1691 HD11 LEU A 162 161.290 191.606 159.715 1.00 41.02 H
ATOM 1692 HD12 LEU A 162 161.545 192.415 158.372 1.00 44.20 H
ATOM 1693 HD13 LEU A 162 160.128 191.750 158.641 1.00 41.68 H
ATOM 1694 HD21 LEU A 162 159.589 195.227 159.158 1.00 44.94 H
ATOM 1695 HD22 LEU A 162 160.521 194.598 158.036 1.00 45.33 H
ATOM 1696 HD23 LEU A 162 159.073 193.997 158.295 1.00 44.45 H
ATOM 1697 N GLY A 163 158.096 194.388 164.012 1.00 38.75 N
ATOM 1698 CA GLY A 163 157.169 194.011 165.061 1.00 39.08 C
ATOM 1699 C GLY A 163 157.746 194.129 166.455 1.00 47.05 C
ATOM 1700 O GLY A 163 158.240 195.190 166.844 1.00 52.94 O
ATOM 1701 H GLY A 163 158.652 195.005 164.235 1.00 41.92 H
ATOM 1702 HA2 GLY A 163 156.382 194.576 165.010 1.00 41.34 H
ATOM 1703 HA3 GLY A 163 156.891 193.091 164.929 1.00 42.49 H
ATOM 1704 N ASN A 164 157.686 193.038 167.220 1.00 57.15 N
ATOM 1705 CA ASN A 164 158.193 192.985 168.591 1.00 62.98 C
ATOM 1706 C ASN A 164 157.500 194.035 169.466 1.00 74.72 C
ATOM 1707 O ASN A 164 158.102 194.996 169.953 1.00 71.23 O
ATOM 1708 CB ASN A 164 159.717 193.156 168.614 1.00 55.96 C
ATOM 1709 CG ASN A 164 160.452 191.832 168.717 1.00 53.91 C
ATOM 1710 OD1 ASN A 164 160.005 190.910 169.399 1.00 50.85 O
ATOM 1711 ND2 ASN A 164 161.588 191.733 168.036 1.00 52.91 N
ATOM 1712 H ASN A 164 157.347 192.293 166.956 1.00 52.84 H
ATOM 1713 HA ASN A 164 157.987 192.114 168.962 1.00 58.02 H
ATOM 1714 HB2 ASN A 164 160.000 193.593 167.797 1.00 52.58 H
ATOM 1715 HB3 ASN A 164 159.968 193.693 169.381 1.00 55.21 H
ATOM 1716 HD21 ASN A 164 161.869 192.399 167.570 1.00 49.68 H
ATOM 1717 HD22 ASN A 164 162.042 191.004 168.062 1.00 50.52 H
ATOM 1718 N CYS A 165 156.199 193.819 169.645 1.00 81.76 N
ATOM 1719 CA CYS A 165 155.408 194.688 170.504 1.00 89.55 C
ATOM 1720 C CYS A 165 155.954 194.670 171.928 1.00 95.14 C
ATOM 1721 O CYS A 165 156.564 193.694 172.373 1.00 89.55 O
ATOM 1722 CB CYS A 165 153.943 194.250 170.498 1.00 90.16 C
ATOM 1723 SG CYS A 165 152.803 195.459 171.212 1.00101.17 S
ATOM 1724 H CYS A 165 155.754 193.179 169.281 1.00 72.75 H
ATOM 1725 HA CYS A 165 155.455 195.598 170.172 1.00 84.34 H
ATOM 1726 HB2 CYS A 165 153.669 194.093 169.581 1.00 83.44 H
ATOM 1727 HB3 CYS A 165 153.861 193.430 171.009 1.00 87.46 H
ATOM 1728 HG CYS A 165 151.689 195.014 171.171 1.00 97.41 H
ATOM 1729 N ILE A 166 155.733 195.771 172.641 1.00 97.86 N
ATOM 1730 CA ILE A 166 156.268 195.952 173.987 1.00 96.91 C
ATOM 1731 C ILE A 166 157.788 196.041 173.917 1.00 95.52 C
ATOM 1732 O ILE A 166 158.437 196.539 174.836 1.00 94.78 O
ATOM 1733 CB ILE A 166 155.828 194.819 174.938 1.00 99.29 C
ATOM 1734 CG1 ILE A 166 154.301 194.716 174.985 1.00 98.56 C
ATOM 1735 CG2 ILE A 166 156.379 195.059 176.338 1.00 98.96 C
ATOM 1736 CD1 ILE A 166 153.796 193.405 175.552 1.00 97.77 C
ATOM 1737 H ILE A 166 155.270 196.439 172.362 1.00 95.03 H
ATOM 1738 HA ILE A 166 155.936 196.789 174.347 1.00 96.41 H
ATOM 1739 HB ILE A 166 156.184 193.977 174.616 1.00 96.82 H
ATOM 1740 HG12 ILE A 166 153.958 195.432 175.543 1.00 98.27 H
ATOM 1741 HG13 ILE A 166 153.948 194.802 174.087 1.00 97.21 H
ATOM 1742 HG21 ILE A 166 157.336 194.904 176.333 1.00 97.97 H
ATOM 1743 HG22 ILE A 166 155.951 194.446 176.956 1.00 98.37 H
ATOM 1744 HG23 ILE A 166 156.191 195.974 176.598 1.00 97.82 H
ATOM 1745 HD11 ILE A 166 154.196 192.674 175.056 1.00 97.55 H
ATOM 1746 HD12 ILE A 166 152.831 193.375 175.465 1.00 97.85 H
ATOM 1747 HD13 ILE A 166 154.046 193.346 176.487 1.00 97.96 H
TER 1748 ILE A 166
TER 4075 ASN B 176
TER 6476 LEU C 178
TER 9283 ARG D 204
TER 11983 ARG E 204
TER 14617 ARG F 204
TER 16722 LEU G 167
TER 18470 LEU H 162
TER 19506 LEU I 155
TER 20242 DT J 23
CONECT 585320243
CONECT 801620245
CONECT 837820245
CONECT1103920245
CONECT1372820246
CONECT20243 58532024920251
CONECT20244202522028020281
CONECT20245 8016 83781103920260
CONECT2024613728202582026120272
CONECT2024620286
CONECT202472026720283
CONECT2024920243
CONECT2025120243
CONECT2025220244
CONECT2025820246
CONECT2026020245
CONECT2026120246
CONECT2026720247
CONECT2027220246
CONECT2028020244
CONECT2028120244
CONECT2028320247
CONECT2028620246
MASTER 2754 0 5 44 37 0 0 610302 10 23 299
END