HEADER STRUCTURAL PROTEIN 27-SEP-16 5TGC
TITLE STRUCTURE OF THE HETERO-TRIMER OF RTT102-ARP7/9 BOUND TO ATP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACTIN-RELATED PROTEIN 7;
COMPND 3 CHAIN: A, D;
COMPND 4 SYNONYM: ACTIN-LIKE PROTEIN ARP7,CHROMATIN STRUCTURE-REMODELING
COMPND 5 COMPLEX PROTEIN ARP7,SWI/SNF COMPLEX COMPONENT ARP7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ACTIN-LIKE PROTEIN ARP9;
COMPND 9 CHAIN: B, E;
COMPND 10 SYNONYM: CHROMATIN STRUCTURE-REMODELING COMPLEX PROTEIN ARP9,SWI/SNF
COMPND 11 COMPLEX COMPONENT ARP9;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: REGULATOR OF TY1 TRANSPOSITION PROTEIN 102;
COMPND 15 CHAIN: C, F;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: ARP7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 10 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 11 ORGANISM_TAXID: 4932;
SOURCE 12 GENE: ARP9;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 17 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 18 ORGANISM_TAXID: 4932;
SOURCE 19 GENE: RTT102;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CHROMATIN REMODELING COMPLEXES, ACTIN-RELATED PROTEIN, ATP-BINDING
KEYWDS 2 SITE, NUCLEAR ACTIN, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.TUREGUN,R.DOMINGUEZ
REVDAT 7 04-OCT-23 5TGC 1 REMARK
REVDAT 6 25-DEC-19 5TGC 1 REMARK
REVDAT 5 13-JUN-18 5TGC 1 JRNL
REVDAT 4 28-MAR-18 5TGC 1 JRNL
REVDAT 3 07-MAR-18 5TGC 1 REMARK
REVDAT 2 27-SEP-17 5TGC 1 REMARK
REVDAT 1 06-SEP-17 5TGC 0
JRNL AUTH B.TUREGUN,R.W.BAKER,A.E.LESCHZINER,R.DOMINGUEZ
JRNL TITL ACTIN-RELATED PROTEINS REGULATE THE RSC CHROMATIN REMODELER
JRNL TITL 2 BY WEAKENING INTRAMOLECULAR INTERACTIONS OF THE STH1 ATPASE.
JRNL REF COMMUN BIOL V. 1 2018
JRNL REFN ESSN 2399-3642
JRNL PMID 29809203
JRNL DOI 10.1038/S42003-017-0002-6
REMARK 2
REMARK 2 RESOLUTION. 3.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 38745
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.278
REMARK 3 R VALUE (WORKING SET) : 0.276
REMARK 3 FREE R VALUE : 0.322
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1940
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.3691 - 7.8028 0.97 2673 142 0.1782 0.2113
REMARK 3 2 7.8028 - 6.2012 0.99 2684 143 0.2429 0.2991
REMARK 3 3 6.2012 - 5.4196 0.98 2695 142 0.2605 0.3030
REMARK 3 4 5.4196 - 4.9251 0.98 2675 141 0.2406 0.3015
REMARK 3 5 4.9251 - 4.5726 0.97 2665 141 0.2303 0.2679
REMARK 3 6 4.5726 - 4.3034 0.97 2644 139 0.2544 0.3356
REMARK 3 7 4.3034 - 4.0881 0.97 2666 140 0.2907 0.3413
REMARK 3 8 4.0881 - 3.9103 0.97 2648 140 0.3006 0.3226
REMARK 3 9 3.9103 - 3.7599 0.96 2608 135 0.3347 0.3624
REMARK 3 10 3.7599 - 3.6302 0.96 2640 140 0.3481 0.4128
REMARK 3 11 3.6302 - 3.5168 0.96 2625 137 0.3407 0.3909
REMARK 3 12 3.5168 - 3.4163 0.96 2630 140 0.3739 0.4223
REMARK 3 13 3.4163 - 3.3265 0.96 2624 138 0.3905 0.4264
REMARK 3 14 3.3265 - 3.2453 0.84 2328 122 0.4080 0.4584
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.540
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 14502
REMARK 3 ANGLE : 0.940 19640
REMARK 3 CHIRALITY : 0.036 2188
REMARK 3 PLANARITY : 0.004 2486
REMARK 3 DIHEDRAL : 15.255 5435
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 3
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 4497
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B
REMARK 3 SELECTION : CHAIN E
REMARK 3 ATOM PAIRS NUMBER : 4331
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN C
REMARK 3 SELECTION : CHAIN F
REMARK 3 ATOM PAIRS NUMBER : 678
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5TGC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000222752.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6 - 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : APEX II CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SAINT V8.34A
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40398
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.245
REMARK 200 RESOLUTION RANGE LOW (A) : 39.366
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : 0.08700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.41800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 4I6M, CHAINS A,B,D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17M AMMONIUM SULFATE, 20% PEG 3350,
REMARK 280 17 MM EDTA, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.5K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 80350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -138.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 THR A 39
REMARK 465 ASP A 40
REMARK 465 GLU A 41
REMARK 465 GLY A 42
REMARK 465 GLY A 43
REMARK 465 GLU A 44
REMARK 465 ALA A 45
REMARK 465 GLU A 203
REMARK 465 GLU A 204
REMARK 465 ASN A 205
REMARK 465 ASP A 206
REMARK 465 MET A 207
REMARK 465 GLU A 208
REMARK 465 ASN A 209
REMARK 465 MET A 210
REMARK 465 ALA A 211
REMARK 465 ASP A 212
REMARK 465 GLU A 213
REMARK 465 LEU A 276
REMARK 465 THR A 277
REMARK 465 GLY A 278
REMARK 465 SER A 279
REMARK 465 PRO A 280
REMARK 465 SER A 346
REMARK 465 MET A 347
REMARK 465 LYS A 348
REMARK 465 ALA A 349
REMARK 465 ASN A 350
REMARK 465 THR A 351
REMARK 465 SER A 352
REMARK 465 THR A 353
REMARK 465 ASN A 354
REMARK 465 PRO A 355
REMARK 465 ASN A 356
REMARK 465 GLY A 357
REMARK 465 LEU A 358
REMARK 465 GLY A 359
REMARK 465 THR A 360
REMARK 465 SER A 361
REMARK 465 HIS A 362
REMARK 465 ILE A 363
REMARK 465 ASN A 364
REMARK 465 THR A 365
REMARK 465 ASN A 366
REMARK 465 VAL A 367
REMARK 465 GLY A 368
REMARK 465 ASP A 369
REMARK 465 ASN A 370
REMARK 465 ASN A 371
REMARK 465 SER A 372
REMARK 465 THR A 373
REMARK 465 ALA A 374
REMARK 465 SER A 375
REMARK 465 SER A 376
REMARK 465 SER A 377
REMARK 465 ASN A 378
REMARK 465 LEU A 463
REMARK 465 LYS A 464
REMARK 465 ARG A 465
REMARK 465 ASP A 466
REMARK 465 ARG A 467
REMARK 465 LYS A 468
REMARK 465 GLN A 469
REMARK 465 SER A 470
REMARK 465 GLN A 471
REMARK 465 ALA A 472
REMARK 465 THR A 473
REMARK 465 ASN A 474
REMARK 465 ALA A 475
REMARK 465 THR A 476
REMARK 465 ASN A 477
REMARK 465 LEU A 478
REMARK 465 VAL A 479
REMARK 465 PRO A 480
REMARK 465 ARG A 481
REMARK 465 GLY A 482
REMARK 465 SER A 483
REMARK 465 HIS A 484
REMARK 465 HIS A 485
REMARK 465 HIS A 486
REMARK 465 HIS A 487
REMARK 465 HIS A 488
REMARK 465 HIS A 489
REMARK 465 MET B 1
REMARK 465 LYS B 227
REMARK 465 LYS B 228
REMARK 465 LEU B 229
REMARK 465 SER B 230
REMARK 465 SER B 231
REMARK 465 PHE B 232
REMARK 465 ASP B 233
REMARK 465 PHE B 234
REMARK 465 GLY B 235
REMARK 465 ASN B 236
REMARK 465 GLU B 237
REMARK 465 ASN B 238
REMARK 465 GLU B 239
REMARK 465 ASP B 240
REMARK 465 GLU B 241
REMARK 465 ASP B 242
REMARK 465 GLU B 243
REMARK 465 GLY B 244
REMARK 465 THR B 245
REMARK 465 LEU B 246
REMARK 465 ASN B 247
REMARK 465 VAL B 248
REMARK 465 ALA B 249
REMARK 465 GLU B 250
REMARK 465 ILE B 251
REMARK 465 ILE B 252
REMARK 465 THR B 253
REMARK 465 SER B 254
REMARK 465 GLY B 255
REMARK 465 ARG B 256
REMARK 465 ASP B 257
REMARK 465 THR B 258
REMARK 465 ARG B 259
REMARK 465 GLU B 260
REMARK 465 VAL B 261
REMARK 465 LEU B 262
REMARK 465 GLU B 263
REMARK 465 GLU B 264
REMARK 465 ARG B 265
REMARK 465 GLU B 266
REMARK 465 ARG B 267
REMARK 465 GLY B 268
REMARK 465 GLN B 269
REMARK 465 LYS B 270
REMARK 465 VAL B 271
REMARK 465 LYS B 272
REMARK 465 ASN B 273
REMARK 465 ALA B 379
REMARK 465 ALA B 380
REMARK 465 THR B 381
REMARK 465 LYS B 382
REMARK 465 LYS B 383
REMARK 465 LYS B 384
REMARK 465 SER B 385
REMARK 465 LYS B 386
REMARK 465 PHE B 387
REMARK 465 MET B 388
REMARK 465 THR B 389
REMARK 465 ASN B 390
REMARK 465 SER B 391
REMARK 465 THR B 392
REMARK 465 ALA B 393
REMARK 465 PHE B 394
REMARK 465 PHE B 416
REMARK 465 PRO B 417
REMARK 465 GLU B 418
REMARK 465 TRP B 419
REMARK 465 LYS B 420
REMARK 465 ASP B 445
REMARK 465 THR B 446
REMARK 465 PHE B 467
REMARK 465 SER C 0
REMARK 465 SER C 36
REMARK 465 SER C 37
REMARK 465 ASN C 38
REMARK 465 VAL C 39
REMARK 465 GLN C 40
REMARK 465 GLN C 41
REMARK 465 PRO C 42
REMARK 465 GLN C 43
REMARK 465 GLN C 44
REMARK 465 GLN C 45
REMARK 465 LEU C 46
REMARK 465 GLY C 47
REMARK 465 ASP C 48
REMARK 465 MET C 49
REMARK 465 GLU C 50
REMARK 465 ASN C 51
REMARK 465 ASN C 52
REMARK 465 LEU C 53
REMARK 465 LYS C 71
REMARK 465 ASN C 72
REMARK 465 LEU C 73
REMARK 465 GLN C 74
REMARK 465 ARG C 75
REMARK 465 ILE C 91
REMARK 465 LEU C 92
REMARK 465 LYS C 93
REMARK 465 LYS C 94
REMARK 465 SER C 95
REMARK 465 LEU C 96
REMARK 465 MET C 97
REMARK 465 THR C 98
REMARK 465 SER C 99
REMARK 465 HIS C 100
REMARK 465 THR C 101
REMARK 465 LYS C 102
REMARK 465 GLY C 103
REMARK 465 ASP C 104
REMARK 465 THR C 105
REMARK 465 SER C 106
REMARK 465 LYS C 107
REMARK 465 ALA C 108
REMARK 465 THR C 109
REMARK 465 GLY C 110
REMARK 465 ALA C 111
REMARK 465 PRO C 112
REMARK 465 SER C 113
REMARK 465 ALA C 114
REMARK 465 ASN C 115
REMARK 465 GLN C 116
REMARK 465 GLY C 117
REMARK 465 ASP C 118
REMARK 465 GLU C 119
REMARK 465 ALA C 120
REMARK 465 LEU C 121
REMARK 465 SER C 122
REMARK 465 VAL C 123
REMARK 465 ASP C 124
REMARK 465 ASP C 125
REMARK 465 ILE C 126
REMARK 465 ARG C 127
REMARK 465 GLY C 128
REMARK 465 ALA C 129
REMARK 465 VAL C 130
REMARK 465 GLY C 131
REMARK 465 ASN C 132
REMARK 465 SER C 133
REMARK 465 GLU C 134
REMARK 465 ALA C 135
REMARK 465 ILE C 136
REMARK 465 PRO C 137
REMARK 465 GLY C 138
REMARK 465 LEU C 139
REMARK 465 SER C 140
REMARK 465 ALA C 141
REMARK 465 GLY C 142
REMARK 465 VAL C 143
REMARK 465 ASN C 144
REMARK 465 ASN C 145
REMARK 465 ASP C 146
REMARK 465 ASN C 147
REMARK 465 THR C 148
REMARK 465 LYS C 149
REMARK 465 GLU C 150
REMARK 465 SER C 151
REMARK 465 LYS C 152
REMARK 465 ASP C 153
REMARK 465 VAL C 154
REMARK 465 LYS C 155
REMARK 465 MET C 156
REMARK 465 ASN C 157
REMARK 465 MET D 0
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 ASN D 205
REMARK 465 ASP D 206
REMARK 465 MET D 207
REMARK 465 GLU D 208
REMARK 465 ASN D 209
REMARK 465 MET D 210
REMARK 465 ALA D 211
REMARK 465 ASP D 212
REMARK 465 GLU D 213
REMARK 465 GLN D 214
REMARK 465 TYR D 273
REMARK 465 THR D 274
REMARK 465 ALA D 275
REMARK 465 LEU D 276
REMARK 465 THR D 277
REMARK 465 ASN D 356
REMARK 465 GLY D 357
REMARK 465 LEU D 358
REMARK 465 GLY D 359
REMARK 465 THR D 360
REMARK 465 SER D 361
REMARK 465 HIS D 362
REMARK 465 ILE D 363
REMARK 465 ASN D 364
REMARK 465 THR D 365
REMARK 465 ASN D 366
REMARK 465 VAL D 367
REMARK 465 GLY D 368
REMARK 465 ASP D 369
REMARK 465 ASN D 370
REMARK 465 ASN D 371
REMARK 465 SER D 372
REMARK 465 THR D 373
REMARK 465 ALA D 374
REMARK 465 SER D 375
REMARK 465 SER D 376
REMARK 465 SER D 377
REMARK 465 LYS D 468
REMARK 465 GLN D 469
REMARK 465 SER D 470
REMARK 465 GLN D 471
REMARK 465 ALA D 472
REMARK 465 THR D 473
REMARK 465 ASN D 474
REMARK 465 ALA D 475
REMARK 465 THR D 476
REMARK 465 ASN D 477
REMARK 465 LEU D 478
REMARK 465 VAL D 479
REMARK 465 PRO D 480
REMARK 465 ARG D 481
REMARK 465 GLY D 482
REMARK 465 SER D 483
REMARK 465 HIS D 484
REMARK 465 HIS D 485
REMARK 465 HIS D 486
REMARK 465 HIS D 487
REMARK 465 HIS D 488
REMARK 465 HIS D 489
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 ASP E 224
REMARK 465 ASP E 225
REMARK 465 ALA E 226
REMARK 465 LYS E 227
REMARK 465 LYS E 228
REMARK 465 LEU E 229
REMARK 465 SER E 230
REMARK 465 SER E 231
REMARK 465 PHE E 232
REMARK 465 ASP E 233
REMARK 465 PHE E 234
REMARK 465 GLY E 235
REMARK 465 ASN E 236
REMARK 465 GLU E 237
REMARK 465 ASN E 238
REMARK 465 GLU E 239
REMARK 465 ASP E 240
REMARK 465 GLU E 241
REMARK 465 ASP E 242
REMARK 465 GLU E 243
REMARK 465 GLY E 244
REMARK 465 THR E 245
REMARK 465 LEU E 246
REMARK 465 ASN E 247
REMARK 465 VAL E 248
REMARK 465 ALA E 249
REMARK 465 GLU E 250
REMARK 465 ILE E 251
REMARK 465 ILE E 252
REMARK 465 THR E 253
REMARK 465 SER E 254
REMARK 465 GLY E 255
REMARK 465 ARG E 256
REMARK 465 ASP E 257
REMARK 465 THR E 258
REMARK 465 ARG E 259
REMARK 465 GLU E 260
REMARK 465 VAL E 261
REMARK 465 LEU E 262
REMARK 465 GLU E 263
REMARK 465 GLU E 264
REMARK 465 ARG E 265
REMARK 465 GLU E 266
REMARK 465 ARG E 267
REMARK 465 GLY E 268
REMARK 465 GLN E 269
REMARK 465 LYS E 270
REMARK 465 VAL E 271
REMARK 465 LYS E 272
REMARK 465 ASN E 273
REMARK 465 VAL E 274
REMARK 465 LYS E 374
REMARK 465 SER E 375
REMARK 465 VAL E 376
REMARK 465 LEU E 377
REMARK 465 PRO E 378
REMARK 465 ALA E 379
REMARK 465 ALA E 380
REMARK 465 THR E 381
REMARK 465 LYS E 382
REMARK 465 LYS E 383
REMARK 465 LYS E 384
REMARK 465 SER E 385
REMARK 465 LYS E 386
REMARK 465 PHE E 387
REMARK 465 MET E 388
REMARK 465 THR E 389
REMARK 465 ASN E 390
REMARK 465 SER E 391
REMARK 465 THR E 392
REMARK 465 ALA E 393
REMARK 465 PHE E 394
REMARK 465 ASP E 445
REMARK 465 THR E 446
REMARK 465 SER F 0
REMARK 465 SER F 37
REMARK 465 ASN F 38
REMARK 465 VAL F 39
REMARK 465 GLN F 40
REMARK 465 GLN F 41
REMARK 465 PRO F 42
REMARK 465 GLN F 43
REMARK 465 GLN F 44
REMARK 465 GLN F 45
REMARK 465 LEU F 46
REMARK 465 GLY F 47
REMARK 465 ASP F 48
REMARK 465 MET F 49
REMARK 465 GLU F 50
REMARK 465 ASN F 51
REMARK 465 ASN F 52
REMARK 465 LEU F 53
REMARK 465 GLU F 68
REMARK 465 ASP F 69
REMARK 465 GLU F 70
REMARK 465 LYS F 71
REMARK 465 ASN F 72
REMARK 465 LEU F 73
REMARK 465 GLN F 74
REMARK 465 ARG F 75
REMARK 465 GLU F 76
REMARK 465 ARG F 89
REMARK 465 ARG F 90
REMARK 465 ILE F 91
REMARK 465 LEU F 92
REMARK 465 LYS F 93
REMARK 465 LYS F 94
REMARK 465 SER F 95
REMARK 465 LEU F 96
REMARK 465 MET F 97
REMARK 465 THR F 98
REMARK 465 SER F 99
REMARK 465 HIS F 100
REMARK 465 THR F 101
REMARK 465 LYS F 102
REMARK 465 GLY F 103
REMARK 465 ASP F 104
REMARK 465 THR F 105
REMARK 465 SER F 106
REMARK 465 LYS F 107
REMARK 465 ALA F 108
REMARK 465 THR F 109
REMARK 465 GLY F 110
REMARK 465 ALA F 111
REMARK 465 PRO F 112
REMARK 465 SER F 113
REMARK 465 ALA F 114
REMARK 465 ASN F 115
REMARK 465 GLN F 116
REMARK 465 GLY F 117
REMARK 465 ASP F 118
REMARK 465 GLU F 119
REMARK 465 ALA F 120
REMARK 465 LEU F 121
REMARK 465 SER F 122
REMARK 465 VAL F 123
REMARK 465 ASP F 124
REMARK 465 ASP F 125
REMARK 465 ILE F 126
REMARK 465 ARG F 127
REMARK 465 GLY F 128
REMARK 465 ALA F 129
REMARK 465 VAL F 130
REMARK 465 GLY F 131
REMARK 465 ASN F 132
REMARK 465 SER F 133
REMARK 465 GLU F 134
REMARK 465 ALA F 135
REMARK 465 ILE F 136
REMARK 465 PRO F 137
REMARK 465 GLY F 138
REMARK 465 LEU F 139
REMARK 465 SER F 140
REMARK 465 ALA F 141
REMARK 465 GLY F 142
REMARK 465 VAL F 143
REMARK 465 ASN F 144
REMARK 465 ASN F 145
REMARK 465 ASP F 146
REMARK 465 ASN F 147
REMARK 465 THR F 148
REMARK 465 LYS F 149
REMARK 465 GLU F 150
REMARK 465 SER F 151
REMARK 465 LYS F 152
REMARK 465 ASP F 153
REMARK 465 VAL F 154
REMARK 465 LYS F 155
REMARK 465 MET F 156
REMARK 465 ASN F 157
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ARG B 312 OG1 THR B 316 2.11
REMARK 500 O LYS E 437 OG1 THR E 441 2.12
REMARK 500 OE1 GLN E 22 OG1 THR E 31 2.16
REMARK 500 O TRP E 419 OG SER E 422 2.16
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 GLU A 25 -12.02 83.68
REMARK 500 THR A 93 -66.39 -95.18
REMARK 500 PHE A 128 -71.48 -94.88
REMARK 500 THR A 226 -77.64 -116.16
REMARK 500 GLN A 269 -172.20 55.08
REMARK 500 GLN A 270 -178.04 156.69
REMARK 500 GLN A 272 74.82 42.24
REMARK 500 SER A 320 -57.96 -132.81
REMARK 500 ASP A 321 -7.83 93.93
REMARK 500 GLN B 17 -63.39 -104.53
REMARK 500 GLU B 27 -15.33 70.20
REMARK 500 ASP B 59 -0.46 68.24
REMARK 500 ASN B 60 -163.27 -71.92
REMARK 500 ALA B 62 -103.81 58.53
REMARK 500 GLU B 63 -155.20 63.59
REMARK 500 ALA B 104 -75.32 -123.52
REMARK 500 GLU D 25 -11.05 82.79
REMARK 500 ASP D 40 -73.70 -116.09
REMARK 500 GLU D 41 -63.54 -97.12
REMARK 500 THR D 93 -66.12 -95.16
REMARK 500 PHE D 128 -64.62 -94.63
REMARK 500 THR D 226 -78.96 -116.72
REMARK 500 GLN D 269 -78.91 -126.53
REMARK 500 THR D 353 -15.55 84.38
REMARK 500 GLN E 17 -62.86 -102.80
REMARK 500 GLU E 27 -18.92 66.47
REMARK 500 ASN E 60 -72.65 -80.17
REMARK 500 LYS E 61 158.41 177.40
REMARK 500 ALA E 104 -75.57 -124.20
REMARK 500 TYR E 424 -132.15 65.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 501
DBREF 5TGC A 1 477 UNP Q12406 ARP7_YEAST 1 477
DBREF 5TGC B 1 467 UNP Q05123 ARP9_YEAST 1 467
DBREF 5TGC C 1 157 UNP P53330 RT102_YEAST 1 157
DBREF 5TGC D 1 477 UNP Q12406 ARP7_YEAST 1 477
DBREF 5TGC E 1 467 UNP Q05123 ARP9_YEAST 1 467
DBREF 5TGC F 1 157 UNP P53330 RT102_YEAST 1 157
SEQADV 5TGC MET A 0 UNP Q12406 INITIATING METHIONINE
SEQADV 5TGC LEU A 478 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC VAL A 479 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC PRO A 480 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC ARG A 481 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC GLY A 482 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC SER A 483 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC HIS A 484 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC HIS A 485 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC HIS A 486 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC HIS A 487 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC HIS A 488 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC HIS A 489 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC SER C 0 UNP P53330 EXPRESSION TAG
SEQADV 5TGC MET D 0 UNP Q12406 INITIATING METHIONINE
SEQADV 5TGC LEU D 478 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC VAL D 479 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC PRO D 480 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC ARG D 481 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC GLY D 482 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC SER D 483 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC HIS D 484 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC HIS D 485 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC HIS D 486 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC HIS D 487 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC HIS D 488 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC HIS D 489 UNP Q12406 EXPRESSION TAG
SEQADV 5TGC SER F 0 UNP P53330 EXPRESSION TAG
SEQRES 1 A 490 MET MET THR LEU ASN ARG LYS CYS VAL VAL ILE HIS ASN
SEQRES 2 A 490 GLY SER HIS ARG THR VAL ALA GLY PHE SER ASN VAL GLU
SEQRES 3 A 490 LEU PRO GLN CYS ILE ILE PRO SER SER TYR ILE LYS ARG
SEQRES 4 A 490 THR ASP GLU GLY GLY GLU ALA GLU PHE ILE PHE GLY THR
SEQRES 5 A 490 TYR ASN MET ILE ASP ALA ALA ALA GLU LYS ARG ASN GLY
SEQRES 6 A 490 ASP GLU VAL TYR THR LEU VAL ASP SER GLN GLY LEU PRO
SEQRES 7 A 490 TYR ASN TRP ASP ALA LEU GLU MET GLN TRP ARG TYR LEU
SEQRES 8 A 490 TYR ASP THR GLN LEU LYS VAL SER PRO GLU GLU LEU PRO
SEQRES 9 A 490 LEU VAL ILE THR MET PRO ALA THR ASN GLY LYS PRO ASP
SEQRES 10 A 490 MET ALA ILE LEU GLU ARG TYR TYR GLU LEU ALA PHE ASP
SEQRES 11 A 490 LYS LEU ASN VAL PRO VAL PHE GLN ILE VAL ILE GLU PRO
SEQRES 12 A 490 LEU ALA ILE ALA LEU SER MET GLY LYS SER SER ALA PHE
SEQRES 13 A 490 VAL ILE ASP ILE GLY ALA SER GLY CYS ASN VAL THR PRO
SEQRES 14 A 490 ILE ILE ASP GLY ILE VAL VAL LYS ASN ALA VAL VAL ARG
SEQRES 15 A 490 SER LYS PHE GLY GLY ASP PHE LEU ASP PHE GLN VAL HIS
SEQRES 16 A 490 GLU ARG LEU ALA PRO LEU ILE LYS GLU GLU ASN ASP MET
SEQRES 17 A 490 GLU ASN MET ALA ASP GLU GLN LYS ARG SER THR ASP VAL
SEQRES 18 A 490 TRP TYR GLU ALA SER THR TRP ILE GLN GLN PHE LYS SER
SEQRES 19 A 490 THR MET LEU GLN VAL SER GLU LYS ASP LEU PHE GLU LEU
SEQRES 20 A 490 GLU ARG TYR TYR LYS GLU GLN ALA ASP ILE TYR ALA LYS
SEQRES 21 A 490 GLN GLN GLU GLN LEU LYS GLN MET ASP GLN GLN LEU GLN
SEQRES 22 A 490 TYR THR ALA LEU THR GLY SER PRO ASN ASN PRO LEU VAL
SEQRES 23 A 490 GLN LYS LYS ASN PHE LEU PHE LYS PRO LEU ASN LYS THR
SEQRES 24 A 490 LEU THR LEU ASP LEU LYS GLU CYS TYR GLN PHE ALA GLU
SEQRES 25 A 490 TYR LEU PHE LYS PRO GLN LEU ILE SER ASP LYS PHE SER
SEQRES 26 A 490 PRO GLU ASP GLY LEU GLY PRO LEU MET ALA LYS SER VAL
SEQRES 27 A 490 LYS LYS ALA GLY ALA SER ILE ASN SER MET LYS ALA ASN
SEQRES 28 A 490 THR SER THR ASN PRO ASN GLY LEU GLY THR SER HIS ILE
SEQRES 29 A 490 ASN THR ASN VAL GLY ASP ASN ASN SER THR ALA SER SER
SEQRES 30 A 490 SER ASN ILE SER PRO GLU GLN VAL TYR SER LEU LEU LEU
SEQRES 31 A 490 THR ASN VAL ILE ILE THR GLY SER THR SER LEU ILE GLU
SEQRES 32 A 490 GLY MET GLU GLN ARG ILE ILE LYS GLU LEU SER ILE ARG
SEQRES 33 A 490 PHE PRO GLN TYR LYS LEU THR THR PHE ALA ASN GLN VAL
SEQRES 34 A 490 MET MET ASP ARG LYS ILE GLN GLY TRP LEU GLY ALA LEU
SEQRES 35 A 490 THR MET ALA ASN LEU PRO SER TRP SER LEU GLY LYS TRP
SEQRES 36 A 490 TYR SER LYS GLU ASP TYR GLU THR LEU LYS ARG ASP ARG
SEQRES 37 A 490 LYS GLN SER GLN ALA THR ASN ALA THR ASN LEU VAL PRO
SEQRES 38 A 490 ARG GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 467 MET ALA PRO PHE ARG GLN ASP SER ILE LEU ILE ILE TYR
SEQRES 2 B 467 PRO ARG SER GLN THR THR LEU VAL GLN PHE GLY LEU ASN
SEQRES 3 B 467 GLU GLU THR PHE THR VAL PRO GLU LEU GLU ILE PRO THR
SEQRES 4 B 467 GLN ILE TYR ARG THR THR ARG GLN ASP GLY SER TYR THR
SEQRES 5 B 467 TYR HIS SER THR ASN LYS ASP ASN LYS ALA GLU LEU ILE
SEQRES 6 B 467 LYS PRO ILE GLN ASN GLY GLU ILE ILE ASP ILE SER ALA
SEQRES 7 B 467 PHE THR GLN PHE LEU ARG LEU ILE PHE VAL SER ILE LEU
SEQRES 8 B 467 SER ASP ARG ALA ASN LYS ASN GLN ASP ALA PHE GLU ALA
SEQRES 9 B 467 GLU LEU SER ASN ILE PRO LEU LEU LEU ILE THR HIS HIS
SEQRES 10 B 467 SER TRP SER GLN SER ASP LEU GLU ILE ILE THR GLN TYR
SEQRES 11 B 467 VAL PHE GLU SER LEU GLU ILE ASN ASN LEU ILE GLN LEU
SEQRES 12 B 467 PRO ALA SER LEU ALA ALA THR TYR SER MET ILE SER LEU
SEQRES 13 B 467 GLN ASN CYS CYS ILE ILE ASP VAL GLY THR HIS HIS THR
SEQRES 14 B 467 ASP ILE ILE PRO ILE VAL ASP TYR ALA GLN LEU ASP HIS
SEQRES 15 B 467 LEU VAL SER SER ILE PRO MET GLY GLY GLN SER ILE ASN
SEQRES 16 B 467 ASP SER LEU LYS LYS LEU LEU PRO GLN TRP ASP ASP ASP
SEQRES 17 B 467 GLN ILE GLU SER LEU LYS LYS SER PRO ILE PHE GLU VAL
SEQRES 18 B 467 LEU SER ASP ASP ALA LYS LYS LEU SER SER PHE ASP PHE
SEQRES 19 B 467 GLY ASN GLU ASN GLU ASP GLU ASP GLU GLY THR LEU ASN
SEQRES 20 B 467 VAL ALA GLU ILE ILE THR SER GLY ARG ASP THR ARG GLU
SEQRES 21 B 467 VAL LEU GLU GLU ARG GLU ARG GLY GLN LYS VAL LYS ASN
SEQRES 22 B 467 VAL LYS ASN SER ASP LEU GLU PHE ASN THR PHE TRP ASP
SEQRES 23 B 467 GLU LYS GLY ASN GLU ILE LYS VAL GLY LYS GLN ARG PHE
SEQRES 24 B 467 GLN GLY CYS ASN ASN LEU ILE LYS ASN ILE SER ASN ARG
SEQRES 25 B 467 VAL GLY LEU THR LEU ASP ASN ILE ASP ASP ILE ASN LYS
SEQRES 26 B 467 ALA LYS ALA VAL TRP GLU ASN ILE ILE ILE VAL GLY GLY
SEQRES 27 B 467 THR THR SER ILE SER GLY PHE LYS GLU ALA LEU LEU GLY
SEQRES 28 B 467 GLN LEU LEU LYS ASP HIS LEU ILE ILE GLU PRO GLU GLU
SEQRES 29 B 467 GLU LYS SER LYS ARG GLU GLU GLU ALA LYS SER VAL LEU
SEQRES 30 B 467 PRO ALA ALA THR LYS LYS LYS SER LYS PHE MET THR ASN
SEQRES 31 B 467 SER THR ALA PHE VAL PRO THR ILE GLU TYR VAL GLN CYS
SEQRES 32 B 467 PRO THR VAL ILE LYS LEU ALA LYS TYR PRO ASP TYR PHE
SEQRES 33 B 467 PRO GLU TRP LYS LYS SER GLY TYR SER GLU ILE ILE PHE
SEQRES 34 B 467 LEU GLY ALA GLN ILE VAL SER LYS GLN ILE PHE THR HIS
SEQRES 35 B 467 PRO LYS ASP THR PHE TYR ILE THR ARG GLU LYS TYR ASN
SEQRES 36 B 467 MET LYS GLY PRO ALA ALA LEU TRP ASP VAL GLN PHE
SEQRES 1 C 158 SER MET ASP PRO GLN THR LEU ILE THR LYS ALA ASN LYS
SEQRES 2 C 158 VAL SER TYR TYR GLY ASN PRO THR SER LYS GLU SER TRP
SEQRES 3 C 158 ARG TYR ASP TRP TYR GLN PRO SER LYS VAL SER SER ASN
SEQRES 4 C 158 VAL GLN GLN PRO GLN GLN GLN LEU GLY ASP MET GLU ASN
SEQRES 5 C 158 ASN LEU GLU LYS TYR PRO PHE ARG TYR LYS THR TRP LEU
SEQRES 6 C 158 ARG ASN GLN GLU ASP GLU LYS ASN LEU GLN ARG GLU SER
SEQRES 7 C 158 CYS GLU ASP ILE LEU ASP LEU LYS GLU PHE ASP ARG ARG
SEQRES 8 C 158 ILE LEU LYS LYS SER LEU MET THR SER HIS THR LYS GLY
SEQRES 9 C 158 ASP THR SER LYS ALA THR GLY ALA PRO SER ALA ASN GLN
SEQRES 10 C 158 GLY ASP GLU ALA LEU SER VAL ASP ASP ILE ARG GLY ALA
SEQRES 11 C 158 VAL GLY ASN SER GLU ALA ILE PRO GLY LEU SER ALA GLY
SEQRES 12 C 158 VAL ASN ASN ASP ASN THR LYS GLU SER LYS ASP VAL LYS
SEQRES 13 C 158 MET ASN
SEQRES 1 D 490 MET MET THR LEU ASN ARG LYS CYS VAL VAL ILE HIS ASN
SEQRES 2 D 490 GLY SER HIS ARG THR VAL ALA GLY PHE SER ASN VAL GLU
SEQRES 3 D 490 LEU PRO GLN CYS ILE ILE PRO SER SER TYR ILE LYS ARG
SEQRES 4 D 490 THR ASP GLU GLY GLY GLU ALA GLU PHE ILE PHE GLY THR
SEQRES 5 D 490 TYR ASN MET ILE ASP ALA ALA ALA GLU LYS ARG ASN GLY
SEQRES 6 D 490 ASP GLU VAL TYR THR LEU VAL ASP SER GLN GLY LEU PRO
SEQRES 7 D 490 TYR ASN TRP ASP ALA LEU GLU MET GLN TRP ARG TYR LEU
SEQRES 8 D 490 TYR ASP THR GLN LEU LYS VAL SER PRO GLU GLU LEU PRO
SEQRES 9 D 490 LEU VAL ILE THR MET PRO ALA THR ASN GLY LYS PRO ASP
SEQRES 10 D 490 MET ALA ILE LEU GLU ARG TYR TYR GLU LEU ALA PHE ASP
SEQRES 11 D 490 LYS LEU ASN VAL PRO VAL PHE GLN ILE VAL ILE GLU PRO
SEQRES 12 D 490 LEU ALA ILE ALA LEU SER MET GLY LYS SER SER ALA PHE
SEQRES 13 D 490 VAL ILE ASP ILE GLY ALA SER GLY CYS ASN VAL THR PRO
SEQRES 14 D 490 ILE ILE ASP GLY ILE VAL VAL LYS ASN ALA VAL VAL ARG
SEQRES 15 D 490 SER LYS PHE GLY GLY ASP PHE LEU ASP PHE GLN VAL HIS
SEQRES 16 D 490 GLU ARG LEU ALA PRO LEU ILE LYS GLU GLU ASN ASP MET
SEQRES 17 D 490 GLU ASN MET ALA ASP GLU GLN LYS ARG SER THR ASP VAL
SEQRES 18 D 490 TRP TYR GLU ALA SER THR TRP ILE GLN GLN PHE LYS SER
SEQRES 19 D 490 THR MET LEU GLN VAL SER GLU LYS ASP LEU PHE GLU LEU
SEQRES 20 D 490 GLU ARG TYR TYR LYS GLU GLN ALA ASP ILE TYR ALA LYS
SEQRES 21 D 490 GLN GLN GLU GLN LEU LYS GLN MET ASP GLN GLN LEU GLN
SEQRES 22 D 490 TYR THR ALA LEU THR GLY SER PRO ASN ASN PRO LEU VAL
SEQRES 23 D 490 GLN LYS LYS ASN PHE LEU PHE LYS PRO LEU ASN LYS THR
SEQRES 24 D 490 LEU THR LEU ASP LEU LYS GLU CYS TYR GLN PHE ALA GLU
SEQRES 25 D 490 TYR LEU PHE LYS PRO GLN LEU ILE SER ASP LYS PHE SER
SEQRES 26 D 490 PRO GLU ASP GLY LEU GLY PRO LEU MET ALA LYS SER VAL
SEQRES 27 D 490 LYS LYS ALA GLY ALA SER ILE ASN SER MET LYS ALA ASN
SEQRES 28 D 490 THR SER THR ASN PRO ASN GLY LEU GLY THR SER HIS ILE
SEQRES 29 D 490 ASN THR ASN VAL GLY ASP ASN ASN SER THR ALA SER SER
SEQRES 30 D 490 SER ASN ILE SER PRO GLU GLN VAL TYR SER LEU LEU LEU
SEQRES 31 D 490 THR ASN VAL ILE ILE THR GLY SER THR SER LEU ILE GLU
SEQRES 32 D 490 GLY MET GLU GLN ARG ILE ILE LYS GLU LEU SER ILE ARG
SEQRES 33 D 490 PHE PRO GLN TYR LYS LEU THR THR PHE ALA ASN GLN VAL
SEQRES 34 D 490 MET MET ASP ARG LYS ILE GLN GLY TRP LEU GLY ALA LEU
SEQRES 35 D 490 THR MET ALA ASN LEU PRO SER TRP SER LEU GLY LYS TRP
SEQRES 36 D 490 TYR SER LYS GLU ASP TYR GLU THR LEU LYS ARG ASP ARG
SEQRES 37 D 490 LYS GLN SER GLN ALA THR ASN ALA THR ASN LEU VAL PRO
SEQRES 38 D 490 ARG GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 E 467 MET ALA PRO PHE ARG GLN ASP SER ILE LEU ILE ILE TYR
SEQRES 2 E 467 PRO ARG SER GLN THR THR LEU VAL GLN PHE GLY LEU ASN
SEQRES 3 E 467 GLU GLU THR PHE THR VAL PRO GLU LEU GLU ILE PRO THR
SEQRES 4 E 467 GLN ILE TYR ARG THR THR ARG GLN ASP GLY SER TYR THR
SEQRES 5 E 467 TYR HIS SER THR ASN LYS ASP ASN LYS ALA GLU LEU ILE
SEQRES 6 E 467 LYS PRO ILE GLN ASN GLY GLU ILE ILE ASP ILE SER ALA
SEQRES 7 E 467 PHE THR GLN PHE LEU ARG LEU ILE PHE VAL SER ILE LEU
SEQRES 8 E 467 SER ASP ARG ALA ASN LYS ASN GLN ASP ALA PHE GLU ALA
SEQRES 9 E 467 GLU LEU SER ASN ILE PRO LEU LEU LEU ILE THR HIS HIS
SEQRES 10 E 467 SER TRP SER GLN SER ASP LEU GLU ILE ILE THR GLN TYR
SEQRES 11 E 467 VAL PHE GLU SER LEU GLU ILE ASN ASN LEU ILE GLN LEU
SEQRES 12 E 467 PRO ALA SER LEU ALA ALA THR TYR SER MET ILE SER LEU
SEQRES 13 E 467 GLN ASN CYS CYS ILE ILE ASP VAL GLY THR HIS HIS THR
SEQRES 14 E 467 ASP ILE ILE PRO ILE VAL ASP TYR ALA GLN LEU ASP HIS
SEQRES 15 E 467 LEU VAL SER SER ILE PRO MET GLY GLY GLN SER ILE ASN
SEQRES 16 E 467 ASP SER LEU LYS LYS LEU LEU PRO GLN TRP ASP ASP ASP
SEQRES 17 E 467 GLN ILE GLU SER LEU LYS LYS SER PRO ILE PHE GLU VAL
SEQRES 18 E 467 LEU SER ASP ASP ALA LYS LYS LEU SER SER PHE ASP PHE
SEQRES 19 E 467 GLY ASN GLU ASN GLU ASP GLU ASP GLU GLY THR LEU ASN
SEQRES 20 E 467 VAL ALA GLU ILE ILE THR SER GLY ARG ASP THR ARG GLU
SEQRES 21 E 467 VAL LEU GLU GLU ARG GLU ARG GLY GLN LYS VAL LYS ASN
SEQRES 22 E 467 VAL LYS ASN SER ASP LEU GLU PHE ASN THR PHE TRP ASP
SEQRES 23 E 467 GLU LYS GLY ASN GLU ILE LYS VAL GLY LYS GLN ARG PHE
SEQRES 24 E 467 GLN GLY CYS ASN ASN LEU ILE LYS ASN ILE SER ASN ARG
SEQRES 25 E 467 VAL GLY LEU THR LEU ASP ASN ILE ASP ASP ILE ASN LYS
SEQRES 26 E 467 ALA LYS ALA VAL TRP GLU ASN ILE ILE ILE VAL GLY GLY
SEQRES 27 E 467 THR THR SER ILE SER GLY PHE LYS GLU ALA LEU LEU GLY
SEQRES 28 E 467 GLN LEU LEU LYS ASP HIS LEU ILE ILE GLU PRO GLU GLU
SEQRES 29 E 467 GLU LYS SER LYS ARG GLU GLU GLU ALA LYS SER VAL LEU
SEQRES 30 E 467 PRO ALA ALA THR LYS LYS LYS SER LYS PHE MET THR ASN
SEQRES 31 E 467 SER THR ALA PHE VAL PRO THR ILE GLU TYR VAL GLN CYS
SEQRES 32 E 467 PRO THR VAL ILE LYS LEU ALA LYS TYR PRO ASP TYR PHE
SEQRES 33 E 467 PRO GLU TRP LYS LYS SER GLY TYR SER GLU ILE ILE PHE
SEQRES 34 E 467 LEU GLY ALA GLN ILE VAL SER LYS GLN ILE PHE THR HIS
SEQRES 35 E 467 PRO LYS ASP THR PHE TYR ILE THR ARG GLU LYS TYR ASN
SEQRES 36 E 467 MET LYS GLY PRO ALA ALA LEU TRP ASP VAL GLN PHE
SEQRES 1 F 158 SER MET ASP PRO GLN THR LEU ILE THR LYS ALA ASN LYS
SEQRES 2 F 158 VAL SER TYR TYR GLY ASN PRO THR SER LYS GLU SER TRP
SEQRES 3 F 158 ARG TYR ASP TRP TYR GLN PRO SER LYS VAL SER SER ASN
SEQRES 4 F 158 VAL GLN GLN PRO GLN GLN GLN LEU GLY ASP MET GLU ASN
SEQRES 5 F 158 ASN LEU GLU LYS TYR PRO PHE ARG TYR LYS THR TRP LEU
SEQRES 6 F 158 ARG ASN GLN GLU ASP GLU LYS ASN LEU GLN ARG GLU SER
SEQRES 7 F 158 CYS GLU ASP ILE LEU ASP LEU LYS GLU PHE ASP ARG ARG
SEQRES 8 F 158 ILE LEU LYS LYS SER LEU MET THR SER HIS THR LYS GLY
SEQRES 9 F 158 ASP THR SER LYS ALA THR GLY ALA PRO SER ALA ASN GLN
SEQRES 10 F 158 GLY ASP GLU ALA LEU SER VAL ASP ASP ILE ARG GLY ALA
SEQRES 11 F 158 VAL GLY ASN SER GLU ALA ILE PRO GLY LEU SER ALA GLY
SEQRES 12 F 158 VAL ASN ASN ASP ASN THR LYS GLU SER LYS ASP VAL LYS
SEQRES 13 F 158 MET ASN
HET ATP A 501 43
HET SO4 B 501 5
HET SO4 B 502 5
HET ATP D 501 43
HET SO4 E 501 5
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM SO4 SULFATE ION
FORMUL 7 ATP 2(C10 H16 N5 O13 P3)
FORMUL 8 SO4 3(O4 S 2-)
HELIX 1 AA1 GLY A 50 LYS A 61 1 12
HELIX 2 AA2 ASN A 79 THR A 93 1 15
HELIX 3 AA3 PRO A 115 PHE A 128 1 14
HELIX 4 AA4 GLU A 141 MET A 149 1 9
HELIX 5 AA5 GLY A 185 LYS A 202 1 18
HELIX 6 AA6 ARG A 216 THR A 226 1 11
HELIX 7 AA7 THR A 226 MET A 235 1 10
HELIX 8 AA8 ASP A 242 GLN A 269 1 28
HELIX 9 AA9 ASN A 282 VAL A 285 5 4
HELIX 10 AB1 LEU A 303 LYS A 315 1 13
HELIX 11 AB2 PRO A 316 ILE A 319 5 4
HELIX 12 AB3 SER A 324 ASP A 327 5 4
HELIX 13 AB4 GLY A 328 SER A 343 1 16
HELIX 14 AB5 SER A 380 ASN A 391 1 12
HELIX 15 AB6 GLY A 396 ILE A 401 5 6
HELIX 16 AB7 GLY A 403 PHE A 416 1 14
HELIX 17 AB8 VAL A 428 ASN A 445 1 18
HELIX 18 AB9 SER A 448 GLY A 452 5 5
HELIX 19 AC1 ARG B 5 SER B 8 5 4
HELIX 20 AC2 ASP B 75 ASN B 98 1 24
HELIX 21 AC3 ASP B 100 ALA B 104 5 5
HELIX 22 AC4 SER B 120 SER B 134 1 15
HELIX 23 AC5 ALA B 145 MET B 153 1 9
HELIX 24 AC6 ASP B 181 VAL B 184 5 4
HELIX 25 AC7 GLY B 190 LEU B 202 1 13
HELIX 26 AC8 ASP B 206 SER B 216 1 11
HELIX 27 AC9 GLY B 295 GLN B 300 5 6
HELIX 28 AD1 CYS B 302 ASN B 319 1 18
HELIX 29 AD2 ASP B 322 ASN B 332 1 11
HELIX 30 AD3 THR B 339 ILE B 342 5 4
HELIX 31 AD4 GLY B 344 LEU B 358 1 15
HELIX 32 AD5 PRO B 362 ALA B 373 1 12
HELIX 33 AD6 GLY B 423 HIS B 442 1 20
HELIX 34 AD7 ARG B 451 LYS B 457 1 7
HELIX 35 AD8 GLY B 458 TRP B 463 5 6
HELIX 36 AD9 ASP C 2 ALA C 10 1 9
HELIX 37 AE1 GLY D 50 GLU D 60 1 11
HELIX 38 AE2 ASN D 79 THR D 93 1 15
HELIX 39 AE3 PRO D 115 PHE D 128 1 14
HELIX 40 AE4 GLU D 141 MET D 149 1 9
HELIX 41 AE5 GLY D 185 GLU D 203 1 19
HELIX 42 AE6 ARG D 216 THR D 226 1 11
HELIX 43 AE7 THR D 226 MET D 235 1 10
HELIX 44 AE8 ASP D 242 LYS D 259 1 18
HELIX 45 AE9 GLN D 260 GLN D 266 5 7
HELIX 46 AF1 ASN D 282 VAL D 285 5 4
HELIX 47 AF2 LEU D 303 LYS D 315 1 13
HELIX 48 AF3 PRO D 316 ILE D 319 5 4
HELIX 49 AF4 SER D 324 ASP D 327 5 4
HELIX 50 AF5 GLY D 328 SER D 343 1 16
HELIX 51 AF6 SER D 380 ASN D 391 1 12
HELIX 52 AF7 GLY D 396 ILE D 401 5 6
HELIX 53 AF8 GLY D 403 PHE D 416 1 14
HELIX 54 AF9 VAL D 428 ASN D 445 1 18
HELIX 55 AG1 SER D 448 GLY D 452 5 5
HELIX 56 AG2 SER D 456 LEU D 463 1 8
HELIX 57 AG3 ARG E 5 SER E 8 5 4
HELIX 58 AG4 ASP E 75 ASN E 98 1 24
HELIX 59 AG5 GLN E 99 ALA E 104 5 6
HELIX 60 AG6 SER E 120 SER E 134 1 15
HELIX 61 AG7 ALA E 145 MET E 153 1 9
HELIX 62 AG8 GLY E 190 LEU E 202 1 13
HELIX 63 AG9 ASP E 206 LYS E 215 1 10
HELIX 64 AH1 LYS E 275 LEU E 279 5 5
HELIX 65 AH2 GLY E 295 GLN E 300 5 6
HELIX 66 AH3 CYS E 302 ASN E 319 1 18
HELIX 67 AH4 ASP E 322 ASN E 332 1 11
HELIX 68 AH5 THR E 339 ILE E 342 5 4
HELIX 69 AH6 GLY E 344 LEU E 358 1 15
HELIX 70 AH7 PRO E 362 ALA E 373 1 12
HELIX 71 AH8 PHE E 416 LYS E 420 5 5
HELIX 72 AH9 TYR E 424 PHE E 440 1 17
HELIX 73 AI1 ARG E 451 GLY E 458 1 8
HELIX 74 AI2 PRO E 459 ASP E 464 5 6
HELIX 75 AI3 ASP F 2 ALA F 10 1 9
HELIX 76 AI4 ASP F 83 ASP F 88 5 6
SHEET 1 AA1 6 CYS A 29 PRO A 32 0
SHEET 2 AA1 6 ARG A 16 PHE A 21 -1 N THR A 17 O ILE A 31
SHEET 3 AA1 6 VAL A 8 ASN A 12 -1 N HIS A 11 O VAL A 18
SHEET 4 AA1 6 LEU A 104 MET A 108 1 O VAL A 105 N VAL A 8
SHEET 5 AA1 6 VAL A 135 ILE A 140 1 O GLN A 137 N LEU A 104
SHEET 6 AA1 6 TRP A 454 SER A 456 -1 O TYR A 455 N PHE A 136
SHEET 1 AA2 2 SER A 34 LYS A 37 0
SHEET 2 AA2 2 GLU A 66 THR A 69 -1 O TYR A 68 N TYR A 35
SHEET 1 AA3 3 ILE A 173 VAL A 174 0
SHEET 2 AA3 3 CYS A 164 ILE A 170 -1 N ILE A 170 O ILE A 173
SHEET 3 AA3 3 VAL A 180 ARG A 181 -1 O VAL A 180 N VAL A 166
SHEET 1 AA4 5 ILE A 173 VAL A 174 0
SHEET 2 AA4 5 CYS A 164 ILE A 170 -1 N ILE A 170 O ILE A 173
SHEET 3 AA4 5 ALA A 154 ILE A 159 -1 N ASP A 158 O ASN A 165
SHEET 4 AA4 5 VAL A 392 THR A 395 1 O ILE A 393 N PHE A 155
SHEET 5 AA4 5 THR A 423 ALA A 425 1 O PHE A 424 N VAL A 392
SHEET 1 AA5 2 LYS A 287 PHE A 292 0
SHEET 2 AA5 2 LYS A 297 ASP A 302 -1 O LEU A 301 N LYS A 288
SHEET 1 AA6 6 LEU B 35 PRO B 38 0
SHEET 2 AA6 6 THR B 18 PHE B 23 -1 N THR B 19 O ILE B 37
SHEET 3 AA6 6 LEU B 10 TYR B 13 -1 N ILE B 11 O GLN B 22
SHEET 4 AA6 6 LEU B 111 THR B 115 1 O LEU B 112 N LEU B 10
SHEET 5 AA6 6 ASN B 139 PRO B 144 1 O ILE B 141 N LEU B 113
SHEET 6 AA6 6 TYR B 448 THR B 450 -1 O ILE B 449 N LEU B 140
SHEET 1 AA7 2 TYR B 42 THR B 45 0
SHEET 2 AA7 2 TYR B 51 HIS B 54 -1 O HIS B 54 N TYR B 42
SHEET 1 AA8 2 ILE B 68 GLN B 69 0
SHEET 2 AA8 2 GLU B 72 ILE B 73 -1 O GLU B 72 N GLN B 69
SHEET 1 AA9 3 ALA B 178 GLN B 179 0
SHEET 2 AA9 3 THR B 169 VAL B 175 -1 N VAL B 175 O ALA B 178
SHEET 3 AA9 3 SER B 185 ILE B 187 -1 O SER B 185 N ILE B 171
SHEET 1 AB1 4 ALA B 178 GLN B 179 0
SHEET 2 AB1 4 THR B 169 VAL B 175 -1 N VAL B 175 O ALA B 178
SHEET 3 AB1 4 CYS B 159 VAL B 164 -1 N CYS B 159 O ILE B 174
SHEET 4 AB1 4 ILE B 333 GLY B 337 1 O ILE B 334 N ILE B 162
SHEET 1 AB2 2 ASN B 282 TRP B 285 0
SHEET 2 AB2 2 GLU B 291 VAL B 294 -1 O ILE B 292 N PHE B 284
SHEET 1 AB3 2 TRP C 25 TYR C 30 0
SHEET 2 AB3 2 TYR C 60 ARG C 65 -1 O LEU C 64 N ARG C 26
SHEET 1 AB4 6 CYS D 29 PRO D 32 0
SHEET 2 AB4 6 ARG D 16 PHE D 21 -1 N THR D 17 O ILE D 31
SHEET 3 AB4 6 VAL D 8 ASN D 12 -1 N HIS D 11 O VAL D 18
SHEET 4 AB4 6 LEU D 104 MET D 108 1 O VAL D 105 N ILE D 10
SHEET 5 AB4 6 PHE D 136 ILE D 140 1 O VAL D 139 N MET D 108
SHEET 6 AB4 6 TRP D 454 TYR D 455 -1 O TYR D 455 N PHE D 136
SHEET 1 AB5 3 ALA D 45 ILE D 48 0
SHEET 2 AB5 3 SER D 34 THR D 39 -1 N ARG D 38 O GLU D 46
SHEET 3 AB5 3 ASP D 65 THR D 69 -1 O TYR D 68 N TYR D 35
SHEET 1 AB6 3 ILE D 173 VAL D 174 0
SHEET 2 AB6 3 CYS D 164 ILE D 170 -1 N ILE D 170 O ILE D 173
SHEET 3 AB6 3 VAL D 180 ARG D 181 -1 O VAL D 180 N VAL D 166
SHEET 1 AB7 5 ILE D 173 VAL D 174 0
SHEET 2 AB7 5 CYS D 164 ILE D 170 -1 N ILE D 170 O ILE D 173
SHEET 3 AB7 5 ALA D 154 ILE D 159 -1 N ASP D 158 O ASN D 165
SHEET 4 AB7 5 VAL D 392 THR D 395 1 O ILE D 393 N ILE D 157
SHEET 5 AB7 5 THR D 423 PHE D 424 1 O PHE D 424 N VAL D 392
SHEET 1 AB8 2 LYS D 287 PHE D 292 0
SHEET 2 AB8 2 LYS D 297 ASP D 302 -1 O LEU D 299 N PHE D 290
SHEET 1 AB9 6 LEU E 35 PRO E 38 0
SHEET 2 AB9 6 THR E 18 PHE E 23 -1 N THR E 19 O ILE E 37
SHEET 3 AB9 6 LEU E 10 TYR E 13 -1 N TYR E 13 O LEU E 20
SHEET 4 AB9 6 LEU E 111 THR E 115 1 O LEU E 112 N LEU E 10
SHEET 5 AB9 6 ASN E 139 PRO E 144 1 O ILE E 141 N LEU E 113
SHEET 6 AB9 6 ILE E 449 THR E 450 -1 O ILE E 449 N LEU E 140
SHEET 1 AC1 3 TYR E 51 HIS E 54 0
SHEET 2 AC1 3 ILE E 41 THR E 45 -1 N THR E 44 O THR E 52
SHEET 3 AC1 3 GLU E 63 ILE E 65 -1 O GLU E 63 N ARG E 43
SHEET 1 AC2 2 ILE E 68 GLN E 69 0
SHEET 2 AC2 2 GLU E 72 ILE E 73 -1 O GLU E 72 N GLN E 69
SHEET 1 AC3 3 ALA E 178 GLN E 179 0
SHEET 2 AC3 3 THR E 169 VAL E 175 -1 N VAL E 175 O ALA E 178
SHEET 3 AC3 3 SER E 185 ILE E 187 -1 O SER E 185 N ILE E 171
SHEET 1 AC4 4 ALA E 178 GLN E 179 0
SHEET 2 AC4 4 THR E 169 VAL E 175 -1 N VAL E 175 O ALA E 178
SHEET 3 AC4 4 CYS E 159 VAL E 164 -1 N CYS E 159 O ILE E 174
SHEET 4 AC4 4 ILE E 333 GLY E 337 1 O ILE E 334 N ILE E 162
SHEET 1 AC5 2 ASN E 282 TRP E 285 0
SHEET 2 AC5 2 GLU E 291 VAL E 294 -1 O ILE E 292 N PHE E 284
SHEET 1 AC6 2 TRP F 25 TYR F 30 0
SHEET 2 AC6 2 TYR F 60 ARG F 65 -1 O LEU F 64 N ARG F 26
CISPEP 1 LYS B 374 SER B 375 0 -19.09
CISPEP 2 LEU B 377 PRO B 378 0 7.81
CISPEP 3 CYS B 403 PRO B 404 0 -4.32
CISPEP 4 GLY D 42 GLY D 43 0 -0.59
CISPEP 5 ASP D 268 GLN D 269 0 -11.58
CISPEP 6 CYS E 403 PRO E 404 0 -7.32
CISPEP 7 TYR F 15 TYR F 16 0 -22.42
SITE 1 AC1 13 GLY A 13 SER A 14 HIS A 15 ARG A 16
SITE 2 AC1 13 GLY A 160 ALA A 161 SER A 162 GLY A 186
SITE 3 AC1 13 LYS A 232 SER A 233 SER A 397 THR A 398
SITE 4 AC1 13 LYS A 433
SITE 1 AC2 7 SER B 16 GLN B 17 ASN B 70 GLY B 165
SITE 2 AC2 7 THR B 166 HIS B 167 HIS B 168
SITE 1 AC3 3 GLY B 337 TYR B 424 SER B 425
SITE 1 AC4 13 GLY D 13 SER D 14 HIS D 15 ARG D 16
SITE 2 AC4 13 GLY D 160 SER D 162 GLY D 186 GLN D 229
SITE 3 AC4 13 LYS D 232 SER D 233 SER D 397 THR D 398
SITE 4 AC4 13 LYS D 433
SITE 1 AC5 5 SER E 16 GLN E 17 THR E 166 HIS E 167
SITE 2 AC5 5 HIS E 168
CRYST1 79.387 87.982 105.430 109.03 104.64 96.20 P 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012597 0.001369 0.004079 0.00000
SCALE2 0.000000 0.011433 0.004515 0.00000
SCALE3 0.000000 0.000000 0.010540 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
