HEADER TRANSCRIPTION 30-JUN-04 1TWH
TITLE RNA POLYMERASE II COMPLEXED WITH 2'DATP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE II LARGEST SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: B220;
COMPND 5 EC: 2.7.7.6;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA-DIRECTED RNA POLYMERASE II 140 KDA POLYPEPTIDE;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: B150, RNA POLYMERASE II SUBUNIT 2;
COMPND 10 EC: 2.7.7.6;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: DNA-DIRECTED RNA POLYMERASE II 45 KDA POLYPEPTIDE;
COMPND 13 CHAIN: C;
COMPND 14 SYNONYM: B44.5;
COMPND 15 EC: 2.7.7.6;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 27 KDA
COMPND 18 POLYPEPTIDE;
COMPND 19 CHAIN: E;
COMPND 20 SYNONYM: ABC27;
COMPND 21 EC: 2.7.7.6;
COMPND 22 MOL_ID: 5;
COMPND 23 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 23 KDA
COMPND 24 POLYPEPTIDE;
COMPND 25 CHAIN: F;
COMPND 26 SYNONYM: ABC23;
COMPND 27 EC: 2.7.7.6;
COMPND 28 MOL_ID: 6;
COMPND 29 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 14.5 KDA
COMPND 30 POLYPEPTIDE;
COMPND 31 CHAIN: H;
COMPND 32 SYNONYM: ABC14.4;
COMPND 33 EC: 2.7.7.6;
COMPND 34 MOL_ID: 7;
COMPND 35 MOLECULE: DNA-DIRECTED RNA POLYMERASE II 14.2 KDA POLYPEPTIDE;
COMPND 36 CHAIN: I;
COMPND 37 SYNONYM: B12.6;
COMPND 38 EC: 2.7.7.6;
COMPND 39 MOL_ID: 8;
COMPND 40 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 8.3 KDA
COMPND 41 POLYPEPTIDE;
COMPND 42 CHAIN: J;
COMPND 43 SYNONYM: ABC10-BETA, ABC8;
COMPND 44 EC: 2.7.7.6;
COMPND 45 MOL_ID: 9;
COMPND 46 MOLECULE: DNA-DIRECTED RNA POLYMERASE II 13.6 KDA POLYPEPTIDE;
COMPND 47 CHAIN: K;
COMPND 48 SYNONYM: B13.6;
COMPND 49 EC: 2.7.7.6;
COMPND 50 MOL_ID: 10;
COMPND 51 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 7.7 KDA
COMPND 52 POLYPEPTIDE;
COMPND 53 CHAIN: L;
COMPND 54 SYNONYM: ABC10-ALPHA;
COMPND 55 EC: 2.7.7.6
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 STRAIN: DELTA-RPB4;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 8 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 9 ORGANISM_TAXID: 4932;
SOURCE 10 STRAIN: DELTA-RPB4;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 4932;
SOURCE 15 STRAIN: DELTA-RPB4;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 18 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 19 ORGANISM_TAXID: 4932;
SOURCE 20 STRAIN: DELTA-RPB4;
SOURCE 21 MOL_ID: 5;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 23 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 24 ORGANISM_TAXID: 4932;
SOURCE 25 STRAIN: DELTA-RPB4;
SOURCE 26 MOL_ID: 6;
SOURCE 27 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 28 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 29 ORGANISM_TAXID: 4932;
SOURCE 30 STRAIN: DELTA-RPB4;
SOURCE 31 MOL_ID: 7;
SOURCE 32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 33 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 34 ORGANISM_TAXID: 4932;
SOURCE 35 STRAIN: DELTA-RPB4;
SOURCE 36 MOL_ID: 8;
SOURCE 37 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 38 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 39 ORGANISM_TAXID: 4932;
SOURCE 40 STRAIN: DELTA-RPB4;
SOURCE 41 MOL_ID: 9;
SOURCE 42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 43 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 44 ORGANISM_TAXID: 4932;
SOURCE 45 STRAIN: DELTA-RPB4;
SOURCE 46 MOL_ID: 10;
SOURCE 47 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 48 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 49 ORGANISM_TAXID: 4932;
SOURCE 50 STRAIN: DELTA-RPB4
KEYWDS TRANSCRIPTION, MRNA, MULTIPROTEIN COMPLEX, MOLECULAR MACHINE, ZINC
KEYWDS 2 MOTIFS
EXPDTA X-RAY DIFFRACTION
AUTHOR K.D.WESTOVER,D.A.BUSHNELL,R.D.KORNBERG
REVDAT 4 23-AUG-23 1TWH 1 REMARK LINK
REVDAT 3 24-FEB-09 1TWH 1 VERSN
REVDAT 2 14-DEC-04 1TWH 1 JRNL
REVDAT 1 16-NOV-04 1TWH 0
JRNL AUTH K.D.WESTOVER,D.A.BUSHNELL,R.D.KORNBERG
JRNL TITL STRUCTURAL BASIS OF TRANSCRIPTION: NUCLEOTIDE SELECTION BY
JRNL TITL 2 ROTATION IN THE RNA POLYMERASE II ACTIVE CENTER.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 119 481 2004
JRNL REFN ISSN 0092-8674
JRNL PMID 15537538
JRNL DOI 10.1016/J.CELL.2004.10.016
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 77646
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 27687
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TWH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000022970.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-AUG-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77646
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PDB ENTRY 1I50
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, AMMONIUM HYDROGEN PHOSPHATE,
REMARK 280 SODIUM DIHYDROGEN PHOSPHATE, DIOXANE, DTT, PH 6.00, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 61.50000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 111.50000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 187.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 61.50000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 111.50000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 187.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 61.50000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 111.50000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 187.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 61.50000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 111.50000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 187.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, F, H, I, J, K, L
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 VAL A 2
REMARK 465 SER A 249
REMARK 465 ILE A 250
REMARK 465 SER A 251
REMARK 465 PHE A 252
REMARK 465 ASN A 253
REMARK 465 GLU A 254
REMARK 465 SER A 255
REMARK 465 GLN A 256
REMARK 465 ARG A 257
REMARK 465 GLY A 258
REMARK 465 GLU A 259
REMARK 465 ASP A 260
REMARK 465 ASN A 306
REMARK 465 ASP A 307
REMARK 465 ILE A 308
REMARK 465 ALA A 309
REMARK 465 GLY A 310
REMARK 465 GLN A 311
REMARK 465 PRO A 312
REMARK 465 GLN A 313
REMARK 465 ALA A 314
REMARK 465 LEU A 315
REMARK 465 GLN A 316
REMARK 465 LYS A 317
REMARK 465 SER A 318
REMARK 465 GLY A 319
REMARK 465 ARG A 320
REMARK 465 PRO A 321
REMARK 465 VAL A 322
REMARK 465 LYS A 323
REMARK 465 ARG A 328
REMARK 465 LEU A 329
REMARK 465 LYS A 330
REMARK 465 GLY A 331
REMARK 465 LYS A 332
REMARK 465 GLU A 333
REMARK 465 GLY A 334
REMARK 465 ARG A 335
REMARK 465 ILE A 336
REMARK 465 ARG A 337
REMARK 465 GLY A 338
REMARK 465 ASN A 339
REMARK 465 LEU A 340
REMARK 465 MET A 341
REMARK 465 GLY A 342
REMARK 465 LYS A 343
REMARK 465 ARG A 344
REMARK 465 VAL A 345
REMARK 465 ASN A 1082
REMARK 465 THR A 1083
REMARK 465 PHE A 1084
REMARK 465 HIS A 1085
REMARK 465 PHE A 1086
REMARK 465 ALA A 1087
REMARK 465 GLY A 1088
REMARK 465 VAL A 1089
REMARK 465 ALA A 1090
REMARK 465 SER A 1091
REMARK 465 PHE A 1174
REMARK 465 SER A 1175
REMARK 465 LEU A 1177
REMARK 465 ASP A 1178
REMARK 465 GLU A 1179
REMARK 465 GLU A 1180
REMARK 465 ALA A 1181
REMARK 465 GLU A 1182
REMARK 465 GLN A 1183
REMARK 465 SER A 1184
REMARK 465 PHE A 1185
REMARK 465 ASP A 1186
REMARK 465 ARG A 1244
REMARK 465 PRO A 1245
REMARK 465 LYS A 1246
REMARK 465 SER A 1247
REMARK 465 LEU A 1248
REMARK 465 ASP A 1249
REMARK 465 ALA A 1250
REMARK 465 GLU A 1251
REMARK 465 THR A 1252
REMARK 465 GLU A 1253
REMARK 465 ARG A 1386
REMARK 465 HIS A 1387
REMARK 465 GLY A 1388
REMARK 465 PHE A 1389
REMARK 465 ASN A 1390
REMARK 465 ARG A 1391
REMARK 465 SER A 1392
REMARK 465 ASN A 1393
REMARK 465 THR A 1394
REMARK 465 GLY A 1395
REMARK 465 ALA A 1396
REMARK 465 LEU A 1397
REMARK 465 MET A 1398
REMARK 465 ARG A 1399
REMARK 465 CYS A 1400
REMARK 465 SER A 1401
REMARK 465 PHE A 1402
REMARK 465 GLU A 1403
REMARK 465 GLU A 1404
REMARK 465 VAL A 1451
REMARK 465 LYS A 1452
REMARK 465 TYR A 1453
REMARK 465 MET A 1454
REMARK 465 PRO A 1455
REMARK 465 GLU A 1456
REMARK 465 GLN A 1457
REMARK 465 LYS A 1458
REMARK 465 ILE A 1459
REMARK 465 THR A 1460
REMARK 465 GLU A 1461
REMARK 465 ILE A 1462
REMARK 465 GLU A 1463
REMARK 465 ASP A 1464
REMARK 465 GLY A 1465
REMARK 465 GLN A 1466
REMARK 465 ASP A 1467
REMARK 465 GLY A 1468
REMARK 465 GLY A 1469
REMARK 465 VAL A 1470
REMARK 465 THR A 1471
REMARK 465 PRO A 1472
REMARK 465 TYR A 1473
REMARK 465 SER A 1474
REMARK 465 ASN A 1475
REMARK 465 GLU A 1476
REMARK 465 SER A 1477
REMARK 465 GLY A 1478
REMARK 465 LEU A 1479
REMARK 465 VAL A 1480
REMARK 465 ASN A 1481
REMARK 465 ALA A 1482
REMARK 465 ASP A 1483
REMARK 465 LEU A 1484
REMARK 465 ASP A 1485
REMARK 465 VAL A 1486
REMARK 465 LYS A 1487
REMARK 465 ASP A 1488
REMARK 465 GLU A 1489
REMARK 465 LEU A 1490
REMARK 465 MET A 1491
REMARK 465 PHE A 1492
REMARK 465 SER A 1493
REMARK 465 PRO A 1494
REMARK 465 LEU A 1495
REMARK 465 VAL A 1496
REMARK 465 ASP A 1497
REMARK 465 SER A 1498
REMARK 465 GLY A 1499
REMARK 465 SER A 1500
REMARK 465 ASN A 1501
REMARK 465 ASP A 1502
REMARK 465 ALA A 1503
REMARK 465 MET A 1504
REMARK 465 ALA A 1505
REMARK 465 GLY A 1506
REMARK 465 GLY A 1507
REMARK 465 PHE A 1508
REMARK 465 THR A 1509
REMARK 465 ALA A 1510
REMARK 465 TYR A 1511
REMARK 465 GLY A 1512
REMARK 465 GLY A 1513
REMARK 465 ALA A 1514
REMARK 465 ASP A 1515
REMARK 465 TYR A 1516
REMARK 465 GLY A 1517
REMARK 465 GLU A 1518
REMARK 465 ALA A 1519
REMARK 465 THR A 1520
REMARK 465 SER A 1521
REMARK 465 PRO A 1522
REMARK 465 PHE A 1523
REMARK 465 GLY A 1524
REMARK 465 ALA A 1525
REMARK 465 TYR A 1526
REMARK 465 GLY A 1527
REMARK 465 GLU A 1528
REMARK 465 ALA A 1529
REMARK 465 PRO A 1530
REMARK 465 THR A 1531
REMARK 465 SER A 1532
REMARK 465 PRO A 1533
REMARK 465 GLY A 1534
REMARK 465 PHE A 1535
REMARK 465 GLY A 1536
REMARK 465 VAL A 1537
REMARK 465 SER A 1538
REMARK 465 SER A 1539
REMARK 465 PRO A 1540
REMARK 465 GLY A 1541
REMARK 465 PHE A 1542
REMARK 465 SER A 1543
REMARK 465 PRO A 1544
REMARK 465 THR A 1545
REMARK 465 SER A 1546
REMARK 465 PRO A 1547
REMARK 465 THR A 1548
REMARK 465 TYR A 1549
REMARK 465 SER A 1550
REMARK 465 PRO A 1551
REMARK 465 THR A 1552
REMARK 465 SER A 1553
REMARK 465 PRO A 1554
REMARK 465 ALA A 1555
REMARK 465 TYR A 1556
REMARK 465 SER A 1557
REMARK 465 PRO A 1558
REMARK 465 THR A 1559
REMARK 465 SER A 1560
REMARK 465 PRO A 1561
REMARK 465 SER A 1562
REMARK 465 TYR A 1563
REMARK 465 SER A 1564
REMARK 465 PRO A 1565
REMARK 465 THR A 1566
REMARK 465 SER A 1567
REMARK 465 PRO A 1568
REMARK 465 SER A 1569
REMARK 465 TYR A 1570
REMARK 465 SER A 1571
REMARK 465 PRO A 1572
REMARK 465 THR A 1573
REMARK 465 SER A 1574
REMARK 465 PRO A 1575
REMARK 465 SER A 1576
REMARK 465 TYR A 1577
REMARK 465 SER A 1578
REMARK 465 PRO A 1579
REMARK 465 THR A 1580
REMARK 465 SER A 1581
REMARK 465 PRO A 1582
REMARK 465 SER A 1583
REMARK 465 TYR A 1584
REMARK 465 SER A 1585
REMARK 465 PRO A 1586
REMARK 465 THR A 1587
REMARK 465 SER A 1588
REMARK 465 PRO A 1589
REMARK 465 SER A 1590
REMARK 465 TYR A 1591
REMARK 465 SER A 1592
REMARK 465 PRO A 1593
REMARK 465 THR A 1594
REMARK 465 SER A 1595
REMARK 465 PRO A 1596
REMARK 465 SER A 1597
REMARK 465 TYR A 1598
REMARK 465 SER A 1599
REMARK 465 PRO A 1600
REMARK 465 THR A 1601
REMARK 465 SER A 1602
REMARK 465 PRO A 1603
REMARK 465 SER A 1604
REMARK 465 TYR A 1605
REMARK 465 SER A 1606
REMARK 465 PRO A 1607
REMARK 465 THR A 1608
REMARK 465 SER A 1609
REMARK 465 PRO A 1610
REMARK 465 SER A 1611
REMARK 465 TYR A 1612
REMARK 465 SER A 1613
REMARK 465 PRO A 1614
REMARK 465 THR A 1615
REMARK 465 SER A 1616
REMARK 465 PRO A 1617
REMARK 465 SER A 1618
REMARK 465 TYR A 1619
REMARK 465 SER A 1620
REMARK 465 PRO A 1621
REMARK 465 THR A 1622
REMARK 465 SER A 1623
REMARK 465 PRO A 1624
REMARK 465 SER A 1625
REMARK 465 TYR A 1626
REMARK 465 SER A 1627
REMARK 465 PRO A 1628
REMARK 465 THR A 1629
REMARK 465 SER A 1630
REMARK 465 PRO A 1631
REMARK 465 SER A 1632
REMARK 465 TYR A 1633
REMARK 465 SER A 1634
REMARK 465 PRO A 1635
REMARK 465 THR A 1636
REMARK 465 SER A 1637
REMARK 465 PRO A 1638
REMARK 465 SER A 1639
REMARK 465 TYR A 1640
REMARK 465 SER A 1641
REMARK 465 PRO A 1642
REMARK 465 THR A 1643
REMARK 465 SER A 1644
REMARK 465 PRO A 1645
REMARK 465 SER A 1646
REMARK 465 TYR A 1647
REMARK 465 SER A 1648
REMARK 465 PRO A 1649
REMARK 465 THR A 1650
REMARK 465 SER A 1651
REMARK 465 PRO A 1652
REMARK 465 SER A 1653
REMARK 465 TYR A 1654
REMARK 465 SER A 1655
REMARK 465 PRO A 1656
REMARK 465 THR A 1657
REMARK 465 SER A 1658
REMARK 465 PRO A 1659
REMARK 465 ALA A 1660
REMARK 465 TYR A 1661
REMARK 465 SER A 1662
REMARK 465 PRO A 1663
REMARK 465 THR A 1664
REMARK 465 SER A 1665
REMARK 465 PRO A 1666
REMARK 465 SER A 1667
REMARK 465 TYR A 1668
REMARK 465 SER A 1669
REMARK 465 PRO A 1670
REMARK 465 THR A 1671
REMARK 465 SER A 1672
REMARK 465 PRO A 1673
REMARK 465 SER A 1674
REMARK 465 TYR A 1675
REMARK 465 SER A 1676
REMARK 465 PRO A 1677
REMARK 465 THR A 1678
REMARK 465 SER A 1679
REMARK 465 PRO A 1680
REMARK 465 SER A 1681
REMARK 465 TYR A 1682
REMARK 465 SER A 1683
REMARK 465 PRO A 1684
REMARK 465 THR A 1685
REMARK 465 SER A 1686
REMARK 465 PRO A 1687
REMARK 465 SER A 1688
REMARK 465 TYR A 1689
REMARK 465 SER A 1690
REMARK 465 PRO A 1691
REMARK 465 THR A 1692
REMARK 465 SER A 1693
REMARK 465 PRO A 1694
REMARK 465 ASN A 1695
REMARK 465 TYR A 1696
REMARK 465 SER A 1697
REMARK 465 PRO A 1698
REMARK 465 THR A 1699
REMARK 465 SER A 1700
REMARK 465 PRO A 1701
REMARK 465 SER A 1702
REMARK 465 TYR A 1703
REMARK 465 SER A 1704
REMARK 465 PRO A 1705
REMARK 465 THR A 1706
REMARK 465 SER A 1707
REMARK 465 PRO A 1708
REMARK 465 GLY A 1709
REMARK 465 TYR A 1710
REMARK 465 SER A 1711
REMARK 465 PRO A 1712
REMARK 465 GLY A 1713
REMARK 465 SER A 1714
REMARK 465 PRO A 1715
REMARK 465 ALA A 1716
REMARK 465 TYR A 1717
REMARK 465 SER A 1718
REMARK 465 PRO A 1719
REMARK 465 LYS A 1720
REMARK 465 GLN A 1721
REMARK 465 ASP A 1722
REMARK 465 GLU A 1723
REMARK 465 GLN A 1724
REMARK 465 LYS A 1725
REMARK 465 HIS A 1726
REMARK 465 ASN A 1727
REMARK 465 GLU A 1728
REMARK 465 ASN A 1729
REMARK 465 GLU A 1730
REMARK 465 ASN A 1731
REMARK 465 SER A 1732
REMARK 465 ARG A 1733
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ASP B 3
REMARK 465 LEU B 4
REMARK 465 ALA B 5
REMARK 465 ASN B 6
REMARK 465 SER B 7
REMARK 465 GLU B 8
REMARK 465 LYS B 9
REMARK 465 TYR B 10
REMARK 465 TYR B 11
REMARK 465 ASP B 12
REMARK 465 GLU B 13
REMARK 465 ASP B 14
REMARK 465 PRO B 15
REMARK 465 TYR B 16
REMARK 465 GLY B 17
REMARK 465 LEU B 71
REMARK 465 GLU B 72
REMARK 465 GLN B 73
REMARK 465 LEU B 74
REMARK 465 ALA B 75
REMARK 465 GLN B 76
REMARK 465 HIS B 77
REMARK 465 THR B 78
REMARK 465 THR B 79
REMARK 465 GLU B 80
REMARK 465 SER B 81
REMARK 465 ASP B 82
REMARK 465 ASN B 83
REMARK 465 ILE B 84
REMARK 465 SER B 85
REMARK 465 ARG B 86
REMARK 465 LYS B 87
REMARK 465 TYR B 88
REMARK 465 ALA B 139
REMARK 465 ILE B 140
REMARK 465 ASP B 141
REMARK 465 VAL B 142
REMARK 465 PRO B 143
REMARK 465 GLY B 144
REMARK 465 ARG B 145
REMARK 465 GLU B 146
REMARK 465 LEU B 147
REMARK 465 LYS B 148
REMARK 465 TYR B 149
REMARK 465 GLU B 150
REMARK 465 LEU B 151
REMARK 465 ILE B 152
REMARK 465 ALA B 153
REMARK 465 GLU B 154
REMARK 465 GLU B 155
REMARK 465 SER B 156
REMARK 465 GLU B 157
REMARK 465 ASP B 158
REMARK 465 ASP B 159
REMARK 465 SER B 160
REMARK 465 GLU B 161
REMARK 465 SER B 162
REMARK 465 GLY B 163
REMARK 465 GLU B 438
REMARK 465 ALA B 439
REMARK 465 HIS B 440
REMARK 465 ASP B 441
REMARK 465 PHE B 442
REMARK 465 ASN B 443
REMARK 465 MET B 444
REMARK 465 LYS B 445
REMARK 465 GLU B 468
REMARK 465 GLN B 469
REMARK 465 LYS B 470
REMARK 465 LYS B 471
REMARK 465 ALA B 472
REMARK 465 MET B 473
REMARK 465 SER B 474
REMARK 465 SER B 475
REMARK 465 ARG B 476
REMARK 465 GLY B 503
REMARK 465 ARG B 504
REMARK 465 ASP B 505
REMARK 465 GLY B 506
REMARK 465 LYS B 507
REMARK 465 LEU B 508
REMARK 465 ILE B 669
REMARK 465 GLU B 670
REMARK 465 GLY B 671
REMARK 465 GLY B 672
REMARK 465 PHE B 673
REMARK 465 GLU B 674
REMARK 465 ASP B 675
REMARK 465 VAL B 676
REMARK 465 GLU B 677
REMARK 465 ALA B 713
REMARK 465 GLU B 714
REMARK 465 ALA B 715
REMARK 465 ASN B 716
REMARK 465 GLU B 717
REMARK 465 GLU B 718
REMARK 465 ASN B 719
REMARK 465 ASP B 720
REMARK 465 LEU B 721
REMARK 465 PRO B 917
REMARK 465 ILE B 918
REMARK 465 SER B 919
REMARK 465 PRO B 920
REMARK 465 ASP B 921
REMARK 465 GLU B 922
REMARK 465 GLU B 923
REMARK 465 GLU B 924
REMARK 465 LEU B 925
REMARK 465 GLY B 926
REMARK 465 GLN B 927
REMARK 465 ARG B 928
REMARK 465 THR B 929
REMARK 465 ALA B 930
REMARK 465 TYR B 931
REMARK 465 HIS B 932
REMARK 465 MET B 1111
REMARK 465 GLN B 1112
REMARK 465 VAL B 1113
REMARK 465 LEU B 1114
REMARK 465 THR B 1115
REMARK 465 ARG B 1116
REMARK 465 GLN B 1117
REMARK 465 PRO B 1118
REMARK 465 VAL B 1119
REMARK 465 GLU B 1120
REMARK 465 GLY B 1121
REMARK 465 ARG B 1122
REMARK 465 SER B 1123
REMARK 465 ARG B 1124
REMARK 465 ASP B 1125
REMARK 465 GLY B 1126
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 LYS C 269
REMARK 465 VAL C 270
REMARK 465 ASN C 271
REMARK 465 PHE C 272
REMARK 465 ALA C 273
REMARK 465 SER C 274
REMARK 465 GLY C 275
REMARK 465 ASP C 276
REMARK 465 ASN C 277
REMARK 465 ASN C 278
REMARK 465 THR C 279
REMARK 465 ALA C 280
REMARK 465 SER C 281
REMARK 465 ASN C 282
REMARK 465 MET C 283
REMARK 465 LEU C 284
REMARK 465 GLY C 285
REMARK 465 SER C 286
REMARK 465 ASN C 287
REMARK 465 GLU C 288
REMARK 465 ASP C 289
REMARK 465 VAL C 290
REMARK 465 MET C 291
REMARK 465 MET C 292
REMARK 465 THR C 293
REMARK 465 GLY C 294
REMARK 465 ALA C 295
REMARK 465 GLU C 296
REMARK 465 GLN C 297
REMARK 465 ASP C 298
REMARK 465 PRO C 299
REMARK 465 TYR C 300
REMARK 465 SER C 301
REMARK 465 ASN C 302
REMARK 465 ALA C 303
REMARK 465 SER C 304
REMARK 465 GLN C 305
REMARK 465 MET C 306
REMARK 465 GLY C 307
REMARK 465 ASN C 308
REMARK 465 THR C 309
REMARK 465 GLY C 310
REMARK 465 SER C 311
REMARK 465 GLY C 312
REMARK 465 GLY C 313
REMARK 465 TYR C 314
REMARK 465 ASP C 315
REMARK 465 ASN C 316
REMARK 465 ALA C 317
REMARK 465 TRP C 318
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 ASP F 3
REMARK 465 TYR F 4
REMARK 465 GLU F 5
REMARK 465 GLU F 6
REMARK 465 ALA F 7
REMARK 465 PHE F 8
REMARK 465 ASN F 9
REMARK 465 ASP F 10
REMARK 465 GLY F 11
REMARK 465 ASN F 12
REMARK 465 GLU F 13
REMARK 465 ASN F 14
REMARK 465 PHE F 15
REMARK 465 GLU F 16
REMARK 465 ASP F 17
REMARK 465 PHE F 18
REMARK 465 ASP F 19
REMARK 465 VAL F 20
REMARK 465 GLU F 21
REMARK 465 HIS F 22
REMARK 465 PHE F 23
REMARK 465 SER F 24
REMARK 465 ASP F 25
REMARK 465 GLU F 26
REMARK 465 GLU F 27
REMARK 465 THR F 28
REMARK 465 TYR F 29
REMARK 465 GLU F 30
REMARK 465 GLU F 31
REMARK 465 LYS F 32
REMARK 465 PRO F 33
REMARK 465 GLN F 34
REMARK 465 PHE F 35
REMARK 465 LYS F 36
REMARK 465 ASP F 37
REMARK 465 GLY F 38
REMARK 465 GLU F 39
REMARK 465 THR F 40
REMARK 465 THR F 41
REMARK 465 ASP F 42
REMARK 465 ALA F 43
REMARK 465 ASN F 44
REMARK 465 GLY F 45
REMARK 465 LYS F 46
REMARK 465 THR F 47
REMARK 465 ILE F 48
REMARK 465 VAL F 49
REMARK 465 THR F 50
REMARK 465 GLY F 51
REMARK 465 GLY F 52
REMARK 465 ASN F 53
REMARK 465 GLY F 54
REMARK 465 PRO F 55
REMARK 465 GLU F 56
REMARK 465 ASP F 57
REMARK 465 PHE F 58
REMARK 465 GLN F 59
REMARK 465 GLN F 60
REMARK 465 HIS F 61
REMARK 465 GLU F 62
REMARK 465 GLN F 63
REMARK 465 ILE F 64
REMARK 465 ARG F 65
REMARK 465 ARG F 66
REMARK 465 LYS F 67
REMARK 465 THR F 68
REMARK 465 LEU F 69
REMARK 465 LYS F 70
REMARK 465 GLU F 71
REMARK 465 LEU F 155
REMARK 465 MET H 1
REMARK 465 ASN H 64
REMARK 465 LEU H 65
REMARK 465 GLU H 66
REMARK 465 ASP H 67
REMARK 465 THR H 68
REMARK 465 PRO H 69
REMARK 465 ALA H 70
REMARK 465 ASN H 71
REMARK 465 ASP H 72
REMARK 465 SER H 73
REMARK 465 SER H 74
REMARK 465 ALA H 75
REMARK 465 SER I 122
REMARK 465 PRO J 65
REMARK 465 LEU J 66
REMARK 465 GLU J 67
REMARK 465 LYS J 68
REMARK 465 ARG J 69
REMARK 465 ASP J 70
REMARK 465 ALA K 115
REMARK 465 ALA K 116
REMARK 465 ASP K 117
REMARK 465 ASP K 118
REMARK 465 ALA K 119
REMARK 465 PHE K 120
REMARK 465 MET L 1
REMARK 465 SER L 2
REMARK 465 ARG L 3
REMARK 465 GLU L 4
REMARK 465 GLY L 5
REMARK 465 PHE L 6
REMARK 465 GLN L 7
REMARK 465 ILE L 8
REMARK 465 PRO L 9
REMARK 465 THR L 10
REMARK 465 ASN L 11
REMARK 465 LEU L 12
REMARK 465 ASP L 13
REMARK 465 ALA L 14
REMARK 465 ALA L 15
REMARK 465 ALA L 16
REMARK 465 ALA L 17
REMARK 465 GLY L 18
REMARK 465 THR L 19
REMARK 465 SER L 20
REMARK 465 GLN L 21
REMARK 465 ALA L 22
REMARK 465 ARG L 23
REMARK 465 THR L 24
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 PRO A 56 CD ARG A 57 1.35
REMARK 500 NZ LYS A 567 CE1 TYR H 95 1.38
REMARK 500 O GLU H 106 O VAL H 107 1.45
REMARK 500 O PHE H 104 N GLU H 106 1.52
REMARK 500 O PRO A 464 N TYR A 465 1.61
REMARK 500 OD2 ASP A 42 N ARG A 47 1.70
REMARK 500 O PHE H 104 C GLU H 105 1.77
REMARK 500 O GLY A 73 N ASN A 75 1.78
REMARK 500 O GLU H 138 C ASN H 139 1.78
REMARK 500 OE1 GLU B 104 NE ARG L 54 1.80
REMARK 500 O ASN K 110 N GLN K 112 1.84
REMARK 500 O GLU H 138 N ALA H 140 1.84
REMARK 500 O LEU H 5 ND2 ASN H 133 1.86
REMARK 500 O PRO F 75 O ASP F 77 1.89
REMARK 500 NZ LYS A 567 CZ TYR H 95 1.89
REMARK 500 C VAL A 1064 N VAL A 1066 1.90
REMARK 500 O ASN H 128 ND2 ASN H 131 1.91
REMARK 500 SG CYS A 70 NE2 HIS A 80 1.92
REMARK 500 OG SER A 369 ND2 ASN K 2 1.93
REMARK 500 NZ LYS H 103 OE2 GLU H 105 1.95
REMARK 500 OH TYR B 1198 NZ LYS B 1201 2.00
REMARK 500 OD1 ASP A 909 N SER A 911 2.01
REMARK 500 O LEU F 111 N GLY F 113 2.02
REMARK 500 O ASP A 55 N ARG A 57 2.04
REMARK 500 OD1 ASP A 909 OG SER A 911 2.05
REMARK 500 O THR E 117 N SER E 119 2.05
REMARK 500 N THR B 916 O ARG B 935 2.06
REMARK 500 ND2 ASN A 517 OD1 ASN A 1364 2.08
REMARK 500 O ALA H 84 OG SER H 88 2.09
REMARK 500 SG CYS I 78 SG CYS I 103 2.09
REMARK 500 O TYR H 115 O MET H 123 2.10
REMARK 500 OH TYR B 890 OD1 ASP B 936 2.11
REMARK 500 NZ LYS B 393 OE2 GLU B 621 2.12
REMARK 500 OG1 THR B 98 O GLY B 127 2.12
REMARK 500 NH2 ARG H 25 OD2 ASP H 41 2.13
REMARK 500 OD2 ASP A 42 C THR A 46 2.13
REMARK 500 OD1 ASP K 24 NH1 ARG K 74 2.15
REMARK 500 CG2 THR B 955 O ARG L 54 2.17
REMARK 500 NZ LYS A 176 O GLY A 178 2.17
REMARK 500 O ASP B 724 N ALA B 726 2.17
REMARK 500 OD1 ASP B 998 NH2 ARG C 35 2.18
REMARK 500 NE2 GLN A 503 NH2 ARG F 90 2.19
REMARK 500 N SER H 13 O GLU H 27 2.19
REMARK 500 O PHE H 104 CA GLU H 106 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLY A 3 N GLY A 3 CA 0.160
REMARK 500 GLN A 4 CB GLN A 4 CG 0.277
REMARK 500 GLN A 4 CG GLN A 4 CD 0.219
REMARK 500 GLN A 4 CA GLN A 4 C 0.169
REMARK 500 GLN A 5 CB GLN A 5 CG 0.348
REMARK 500 SER A 8 CA SER A 8 CB 0.091
REMARK 500 ALA A 9 CA ALA A 9 CB 0.200
REMARK 500 ALA A 9 CA ALA A 9 C -0.171
REMARK 500 PRO A 10 CG PRO A 10 CD 0.208
REMARK 500 ARG A 12 NE ARG A 12 CZ 0.090
REMARK 500 ARG A 12 CZ ARG A 12 NH1 0.166
REMARK 500 VAL A 14 C VAL A 14 O -0.184
REMARK 500 LYS A 15 CD LYS A 15 CE 0.162
REMARK 500 LYS A 15 C LYS A 15 O -0.140
REMARK 500 GLU A 16 N GLU A 16 CA 0.137
REMARK 500 GLU A 16 CG GLU A 16 CD 0.121
REMARK 500 GLU A 16 CD GLU A 16 OE1 0.186
REMARK 500 GLU A 16 CD GLU A 16 OE2 0.165
REMARK 500 GLU A 16 C GLU A 16 O 0.115
REMARK 500 VAL A 17 CA VAL A 17 CB -0.182
REMARK 500 PHE A 19 CA PHE A 19 CB -0.134
REMARK 500 PHE A 19 CD1 PHE A 19 CE1 -0.210
REMARK 500 GLY A 20 C GLY A 20 O 0.117
REMARK 500 PHE A 22 CD1 PHE A 22 CE1 -0.141
REMARK 500 PHE A 22 CE1 PHE A 22 CZ 0.142
REMARK 500 PHE A 22 CZ PHE A 22 CE2 -0.132
REMARK 500 PHE A 22 C PHE A 22 O 0.123
REMARK 500 SER A 23 CA SER A 23 CB -0.097
REMARK 500 SER A 23 C SER A 23 O 0.173
REMARK 500 PRO A 24 C PRO A 24 O 0.189
REMARK 500 GLU A 25 CB GLU A 25 CG 0.128
REMARK 500 GLU A 25 CG GLU A 25 CD 0.157
REMARK 500 GLU A 25 CD GLU A 25 OE1 0.139
REMARK 500 GLU A 25 CD GLU A 25 OE2 0.118
REMARK 500 GLU A 26 CG GLU A 26 CD 0.106
REMARK 500 GLU A 26 CA GLU A 26 C -0.160
REMARK 500 VAL A 27 CB VAL A 27 CG1 0.183
REMARK 500 ARG A 28 CG ARG A 28 CD 0.313
REMARK 500 ARG A 28 NE ARG A 28 CZ 0.112
REMARK 500 ARG A 28 CZ ARG A 28 NH1 0.097
REMARK 500 ARG A 28 CZ ARG A 28 NH2 0.148
REMARK 500 ARG A 28 C ARG A 28 O 0.146
REMARK 500 SER A 31 C SER A 31 O 0.164
REMARK 500 VAL A 32 C VAL A 32 O 0.204
REMARK 500 LYS A 34 CB LYS A 34 CG 0.185
REMARK 500 LYS A 34 CG LYS A 34 CD 0.277
REMARK 500 LYS A 34 CD LYS A 34 CE 0.186
REMARK 500 LYS A 34 C LYS A 34 O -0.130
REMARK 500 ILE A 35 CA ILE A 35 C 0.181
REMARK 500 ARG A 36 CB ARG A 36 CG 0.195
REMARK 500
REMARK 500 THIS ENTRY HAS 4336 BOND DEVIATIONS.
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 GLN A 4 CB - CA - C ANGL. DEV. = 13.3 DEGREES
REMARK 500 ALA A 9 N - CA - C ANGL. DEV. = -18.2 DEGREES
REMARK 500 LEU A 11 CD1 - CG - CD2 ANGL. DEV. = -21.6 DEGREES
REMARK 500 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 THR A 13 CA - CB - CG2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 ARG A 28 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 VAL A 32 CG1 - CB - CG2 ANGL. DEV. = -14.3 DEGREES
REMARK 500 LYS A 34 CD - CE - NZ ANGL. DEV. = 15.9 DEGREES
REMARK 500 LYS A 34 O - C - N ANGL. DEV. = -10.7 DEGREES
REMARK 500 ARG A 36 CG - CD - NE ANGL. DEV. = 17.0 DEGREES
REMARK 500 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 PHE A 37 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ASP A 42 CB - CG - OD2 ANGL. DEV. = 11.9 DEGREES
REMARK 500 THR A 44 CA - CB - CG2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 LYS A 49 CD - CE - NZ ANGL. DEV. = 14.4 DEGREES
REMARK 500 ILE A 50 CB - CA - C ANGL. DEV. = -17.2 DEGREES
REMARK 500 LEU A 53 CA - CB - CG ANGL. DEV. = 28.9 DEGREES
REMARK 500 LEU A 53 CB - CG - CD1 ANGL. DEV. = 15.0 DEGREES
REMARK 500 ARG A 57 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 GLY A 59 N - CA - C ANGL. DEV. = 25.0 DEGREES
REMARK 500 ILE A 61 N - CA - C ANGL. DEV. = -19.2 DEGREES
REMARK 500 ASP A 62 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 LEU A 65 CA - CB - CG ANGL. DEV. = 16.3 DEGREES
REMARK 500 LEU A 65 CB - CG - CD2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 CYS A 67 CB - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 CYS A 70 N - CA - CB ANGL. DEV. = 10.1 DEGREES
REMARK 500 CYS A 70 CA - CB - SG ANGL. DEV. = 23.1 DEGREES
REMARK 500 GLU A 72 N - CA - C ANGL. DEV. = 18.2 DEGREES
REMARK 500 GLY A 79 N - CA - C ANGL. DEV. = -19.9 DEGREES
REMARK 500 PHE A 81 CB - CG - CD2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ILE A 84 CG1 - CB - CG2 ANGL. DEV. = -17.9 DEGREES
REMARK 500 ASP A 85 CB - CG - OD1 ANGL. DEV. = -18.3 DEGREES
REMARK 500 ASP A 85 CB - CG - OD2 ANGL. DEV. = 9.3 DEGREES
REMARK 500 LEU A 86 CB - CG - CD1 ANGL. DEV. = -10.6 DEGREES
REMARK 500 LEU A 86 CB - CG - CD2 ANGL. DEV. = 11.0 DEGREES
REMARK 500 VAL A 90 N - CA - CB ANGL. DEV. = -15.2 DEGREES
REMARK 500 VAL A 93 CB - CA - C ANGL. DEV. = -22.1 DEGREES
REMARK 500 ILE A 96 CG1 - CB - CG2 ANGL. DEV. = -22.3 DEGREES
REMARK 500 ILE A 96 CA - CB - CG1 ANGL. DEV. = 13.8 DEGREES
REMARK 500 LYS A 98 CG - CD - CE ANGL. DEV. = -19.8 DEGREES
REMARK 500 LYS A 100 CD - CE - NZ ANGL. DEV. = 14.3 DEGREES
REMARK 500 VAL A 102 CG1 - CB - CG2 ANGL. DEV. = -11.8 DEGREES
REMARK 500 VAL A 106 CG1 - CB - CG2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 CYS A 107 CA - CB - SG ANGL. DEV. = 21.8 DEGREES
REMARK 500 CYS A 107 N - CA - C ANGL. DEV. = -16.8 DEGREES
REMARK 500 CYS A 110 CA - CB - SG ANGL. DEV. = 17.9 DEGREES
REMARK 500 GLY A 111 CA - C - N ANGL. DEV. = -16.3 DEGREES
REMARK 500 LYS A 112 CD - CE - NZ ANGL. DEV. = -17.1 DEGREES
REMARK 500 GLU A 117 OE1 - CD - OE2 ANGL. DEV. = 12.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 1821 ANGLE DEVIATIONS.
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 ALA A 29 -26.11 -39.63
REMARK 500 VAL A 32 -82.55 -80.69
REMARK 500 ILE A 35 106.73 11.16
REMARK 500 ARG A 36 -45.36 -145.64
REMARK 500 PRO A 38 57.27 -113.60
REMARK 500 MET A 41 175.98 76.11
REMARK 500 ASP A 42 84.98 65.08
REMARK 500 THR A 44 -55.53 80.25
REMARK 500 GLN A 45 21.98 157.67
REMARK 500 ARG A 47 58.27 -54.54
REMARK 500 ALA A 48 -69.43 -129.53
REMARK 500 ASN A 54 -61.42 65.71
REMARK 500 PRO A 56 23.70 -50.86
REMARK 500 ARG A 57 -15.22 122.26
REMARK 500 SER A 60 121.68 154.17
REMARK 500 ASP A 62 2.17 123.11
REMARK 500 ARG A 63 -28.61 60.21
REMARK 500 ASN A 64 97.26 -51.16
REMARK 500 LEU A 65 63.39 -52.23
REMARK 500 CYS A 67 -92.67 -122.02
REMARK 500 THR A 69 10.65 36.66
REMARK 500 GLN A 71 -103.39 63.31
REMARK 500 GLU A 72 161.59 -1.67
REMARK 500 MET A 74 37.91 -55.91
REMARK 500 ASN A 75 -29.22 -170.18
REMARK 500 PRO A 78 -74.06 -33.42
REMARK 500 HIS A 109 -68.48 -90.06
REMARK 500 ASP A 116 -162.68 -175.11
REMARK 500 GLU A 120 -70.40 100.85
REMARK 500 ILE A 128 147.00 -36.52
REMARK 500 ALA A 136 -79.38 -42.41
REMARK 500 ASP A 151 143.52 -172.20
REMARK 500 GLU A 155 -123.93 -41.30
REMARK 500 ASP A 156 -145.06 28.63
REMARK 500 PRO A 158 22.80 -71.00
REMARK 500 CYS A 167 -62.60 87.34
REMARK 500 ASP A 177 67.46 -156.42
REMARK 500 LYS A 186 -163.25 -112.54
REMARK 500 ASP A 188 -164.77 174.11
REMARK 500 ALA A 190 41.72 120.49
REMARK 500 THR A 191 -123.89 -87.89
REMARK 500 ASP A 193 -58.99 112.50
REMARK 500 ALA A 194 88.23 -165.39
REMARK 500 GLU A 196 125.76 96.99
REMARK 500 ARG A 200 127.12 -173.56
REMARK 500 SER A 221 -36.75 -39.64
REMARK 500 GLU A 226 -26.51 -38.41
REMARK 500 THR A 237 -43.97 -148.62
REMARK 500 THR A 278 43.38 -73.79
REMARK 500 LEU A 279 -44.25 -161.86
REMARK 500
REMARK 500 THIS ENTRY HAS 315 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 31 VAL A 32 148.77
REMARK 500 THR A 44 GLN A 45 -128.69
REMARK 500 GLY A 52 LEU A 53 145.89
REMARK 500 SER A 60 ILE A 61 146.78
REMARK 500 MET A 74 ASN A 75 -140.30
REMARK 500 GLU A 120 LEU A 121 144.35
REMARK 500 SER A 154 GLU A 155 141.60
REMARK 500 PRO A 158 THR A 159 141.85
REMARK 500 GLY A 165 GLY A 166 145.67
REMARK 500 LYS A 187 ASP A 188 -149.71
REMARK 500 THR A 191 GLY A 192 115.20
REMARK 500 ILE A 325 ARG A 326 148.52
REMARK 500 HIS A 399 PRO A 400 -41.79
REMARK 500 PRO A 464 TYR A 465 -121.98
REMARK 500 ASP A 555 TRP A 556 148.36
REMARK 500 LYS A 705 HIS A 706 144.82
REMARK 500 HIS A 706 GLY A 707 -140.71
REMARK 500 GLY A 707 MET A 708 149.10
REMARK 500 VAL A 1064 GLY A 1065 -147.50
REMARK 500 LYS A 1093 VAL A 1094 140.03
REMARK 500 ASP A 1155 PRO A 1156 -148.66
REMARK 500 ASN A 1232 ASP A 1233 -131.37
REMARK 500 ALA A 1254 GLU A 1255 -146.62
REMARK 500 MET A 1267 LEU A 1268 -147.94
REMARK 500 VAL A 1384 THR A 1385 139.20
REMARK 500 GLU B 104 SER B 105 142.02
REMARK 500 GLY B 107 VAL B 108 145.79
REMARK 500 THR B 123 TYR B 124 -149.22
REMARK 500 SER B 248 ARG B 249 148.16
REMARK 500 GLU B 262 GLY B 263 -148.38
REMARK 500 ILE B 276 LYS B 277 -148.15
REMARK 500 GLY B 369 PHE B 370 -129.27
REMARK 500 ARG B 434 THR B 435 145.49
REMARK 500 PRO B 501 ILE B 502 143.57
REMARK 500 ASP B 642 ASP B 643 43.91
REMARK 500 ASP B 643 GLU B 644 -125.09
REMARK 500 GLU B 644 SER B 645 97.12
REMARK 500 LEU B 646 GLY B 647 148.36
REMARK 500 SER B 732 HIS B 733 123.81
REMARK 500 MET B 868 SER B 869 -148.59
REMARK 500 ILE B 870 THR B 871 -137.94
REMARK 500 GLN B 878 ARG B 879 -143.66
REMARK 500 THR B 882 LEU B 883 140.75
REMARK 500 THR B 915 THR B 916 148.80
REMARK 500 ASP B 1101 LYS B 1102 -142.88
REMARK 500 LYS B 1102 ILE B 1103 140.64
REMARK 500 ILE B 1103 HIS B 1104 143.79
REMARK 500 GLY B 1109 PRO B 1110 139.93
REMARK 500 MET B 1152 GLU B 1153 130.23
REMARK 500 SER B 1155 ASP B 1156 -142.89
REMARK 500
REMARK 500 THIS ENTRY HAS 84 NON CIS, NON-TRANS OMEGA OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 434 0.09 SIDE CHAIN
REMARK 500 PHE A 444 0.10 SIDE CHAIN
REMARK 500 ARG A 469 0.08 SIDE CHAIN
REMARK 500 PHE A 591 0.08 SIDE CHAIN
REMARK 500 HIS A 631 0.11 SIDE CHAIN
REMARK 500 HIS A 659 0.16 SIDE CHAIN
REMARK 500 PHE A 787 0.07 SIDE CHAIN
REMARK 500 TYR A 852 0.08 SIDE CHAIN
REMARK 500 HIS A 877 0.08 SIDE CHAIN
REMARK 500 PHE A 893 0.07 SIDE CHAIN
REMARK 500 TYR A1035 0.10 SIDE CHAIN
REMARK 500 TYR A1119 0.08 SIDE CHAIN
REMARK 500 TYR A1298 0.09 SIDE CHAIN
REMARK 500 PHE B 51 0.09 SIDE CHAIN
REMARK 500 HIS B 515 0.10 SIDE CHAIN
REMARK 500 HIS B 518 0.17 SIDE CHAIN
REMARK 500 PHE B 627 0.08 SIDE CHAIN
REMARK 500 HIS B 984 0.14 SIDE CHAIN
REMARK 500 ARG B 995 0.08 SIDE CHAIN
REMARK 500 HIS B1025 0.18 SIDE CHAIN
REMARK 500 TYR B1092 0.07 SIDE CHAIN
REMARK 500 HIS B1097 0.12 SIDE CHAIN
REMARK 500 HIS B1141 0.07 SIDE CHAIN
REMARK 500 HIS B1177 0.08 SIDE CHAIN
REMARK 500 HIS E 147 0.27 SIDE CHAIN
REMARK 500 HIS E 153 0.14 SIDE CHAIN
REMARK 500 TYR E 211 0.08 SIDE CHAIN
REMARK 500 ARG E 212 0.16 SIDE CHAIN
REMARK 500 PHE I 27 0.07 SIDE CHAIN
REMARK 500 HIS I 79 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 TYR A 417 -12.85
REMARK 500 PRO A 464 10.73
REMARK 500 ARG A 469 -12.41
REMARK 500 GLY A 484 11.62
REMARK 500 ASP A 538 10.16
REMARK 500 HIS A 631 -10.99
REMARK 500 SER A 751 10.18
REMARK 500 ALA A 759 10.45
REMARK 500 ASP A 790 -11.53
REMARK 500 LEU A 936 -12.62
REMARK 500 LYS A 938 10.53
REMARK 500 LYS A 941 13.09
REMARK 500 ALA A1027 -10.89
REMARK 500 VAL A1064 67.23
REMARK 500 MET A1111 -11.21
REMARK 500 ASP A1155 10.40
REMARK 500 GLU A1301 -15.59
REMARK 500 SER A1361 10.77
REMARK 500 MET A1375 -12.33
REMARK 500 LYS B 277 10.45
REMARK 500 VAL B 479 -11.97
REMARK 500 THR B 517 -12.25
REMARK 500 LEU B 535 11.63
REMARK 500 SER B 543 -10.51
REMARK 500 TRP B 586 12.42
REMARK 500 VAL B 589 11.56
REMARK 500 GLU B 641 13.15
REMARK 500 GLU B 742 -10.09
REMARK 500 PRO B 745 -11.32
REMARK 500 GLY B 832 -10.18
REMARK 500 CYS B1166 11.73
REMARK 500 CYS C 92 -11.53
REMARK 500 ALA C 103 10.25
REMARK 500 LEU C 124 10.67
REMARK 500 LEU C 155 -10.12
REMARK 500 THR C 156 -12.05
REMARK 500 CYS C 157 -10.28
REMARK 500 GLY C 171 11.79
REMARK 500 ASN C 184 11.80
REMARK 500 VAL C 240 11.84
REMARK 500 VAL E 195 11.11
REMARK 500 ARG F 135 -11.42
REMARK 500 LEU I 42 -10.21
REMARK 500 VAL I 43 12.78
REMARK 500 ARG K 70 10.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 ATP A 3011
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 ZN A3008 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 67 SG
REMARK 620 2 CYS A 70 SG 98.6
REMARK 620 3 CYS A 77 SG 76.1 149.6
REMARK 620 4 HIS A 80 NE2 120.9 81.6 127.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A3006 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 107 SG
REMARK 620 2 CYS A 110 SG 71.3
REMARK 620 3 CYS A 148 SG 113.6 149.2
REMARK 620 4 CYS A 167 SG 96.1 100.3 109.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A3009 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 481 OD1
REMARK 620 2 ASP A 483 OD2 80.4
REMARK 620 3 ASP A 485 OD2 82.8 80.8
REMARK 620 4 ATP A3011 O2G 170.1 108.6 102.4
REMARK 620 5 ATP A3011 O1B 92.8 92.8 172.7 82.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A3010 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 481 OD2
REMARK 620 2 ASP A 483 OD1 92.5
REMARK 620 3 ATP A3011 O1B 89.2 78.4
REMARK 620 4 ATP A3011 O1A 161.4 104.8 87.9
REMARK 620 5 ASP B 837 OD2 81.9 105.6 170.4 99.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B3007 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1163 SG
REMARK 620 2 CYS B1166 SG 98.2
REMARK 620 3 CYS B1182 SG 111.8 97.0
REMARK 620 4 CYS B1185 SG 87.3 116.1 139.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C3002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 86 SG
REMARK 620 2 CYS C 88 SG 123.1
REMARK 620 3 CYS C 92 SG 111.4 102.8
REMARK 620 4 CYS C 95 SG 117.3 96.4 103.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I3003 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 7 SG
REMARK 620 2 CYS I 10 SG 98.4
REMARK 620 3 CYS I 29 SG 119.5 108.0
REMARK 620 4 CYS I 32 SG 111.9 99.6 115.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I3004 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 75 SG
REMARK 620 2 CYS I 78 SG 112.9
REMARK 620 3 CYS I 103 SG 101.5 60.5
REMARK 620 4 CYS I 106 SG 161.4 85.4 84.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J3001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 7 SG
REMARK 620 2 CYS J 10 SG 110.8
REMARK 620 3 CYS J 45 SG 108.6 122.7
REMARK 620 4 CYS J 46 SG 93.8 96.2 120.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN L3005 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 31 SG
REMARK 620 2 CYS L 34 SG 116.5
REMARK 620 3 CYS L 48 SG 75.2 149.0
REMARK 620 4 CYS L 51 SG 85.9 124.5 83.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 3009
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 3010
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 3004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 3005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 3007
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3008
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 3011
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TWA RELATED DB: PDB
REMARK 900 RELATED ID: 1TWC RELATED DB: PDB
REMARK 900 RELATED ID: 1TWF RELATED DB: PDB
REMARK 900 RELATED ID: 1TWG RELATED DB: PDB
DBREF 1TWH A 1 1733 UNP P04050 RPB1_YEAST 1 1733
DBREF 1TWH B 1 1224 UNP P08518 RPB2_YEAST 1 1224
DBREF 1TWH C 1 318 UNP P16370 RPB3_YEAST 1 318
DBREF 1TWH E 1 215 UNP P20434 RPB5_YEAST 1 215
DBREF 1TWH F 1 155 UNP P20435 RPB6_YEAST 1 155
DBREF 1TWH H 1 146 UNP P20436 RPB8_YEAST 1 146
DBREF 1TWH I 1 122 UNP P27999 RPB9_YEAST 1 122
DBREF 1TWH J 1 70 UNP P22139 RPB10_YEAST 1 70
DBREF 1TWH K 1 120 UNP P38902 RPB11_YEAST 1 120
DBREF 1TWH L 1 70 UNP P40422 RPC10_YEAST 1 70
SEQRES 1 A 1733 MET VAL GLY GLN GLN TYR SER SER ALA PRO LEU ARG THR
SEQRES 2 A 1733 VAL LYS GLU VAL GLN PHE GLY LEU PHE SER PRO GLU GLU
SEQRES 3 A 1733 VAL ARG ALA ILE SER VAL ALA LYS ILE ARG PHE PRO GLU
SEQRES 4 A 1733 THR MET ASP GLU THR GLN THR ARG ALA LYS ILE GLY GLY
SEQRES 5 A 1733 LEU ASN ASP PRO ARG LEU GLY SER ILE ASP ARG ASN LEU
SEQRES 6 A 1733 LYS CYS GLN THR CYS GLN GLU GLY MET ASN GLU CYS PRO
SEQRES 7 A 1733 GLY HIS PHE GLY HIS ILE ASP LEU ALA LYS PRO VAL PHE
SEQRES 8 A 1733 HIS VAL GLY PHE ILE ALA LYS ILE LYS LYS VAL CYS GLU
SEQRES 9 A 1733 CYS VAL CYS MET HIS CYS GLY LYS LEU LEU LEU ASP GLU
SEQRES 10 A 1733 HIS ASN GLU LEU MET ARG GLN ALA LEU ALA ILE LYS ASP
SEQRES 11 A 1733 SER LYS LYS ARG PHE ALA ALA ILE TRP THR LEU CYS LYS
SEQRES 12 A 1733 THR LYS MET VAL CYS GLU THR ASP VAL PRO SER GLU ASP
SEQRES 13 A 1733 ASP PRO THR GLN LEU VAL SER ARG GLY GLY CYS GLY ASN
SEQRES 14 A 1733 THR GLN PRO THR ILE ARG LYS ASP GLY LEU LYS LEU VAL
SEQRES 15 A 1733 GLY SER TRP LYS LYS ASP ARG ALA THR GLY ASP ALA ASP
SEQRES 16 A 1733 GLU PRO GLU LEU ARG VAL LEU SER THR GLU GLU ILE LEU
SEQRES 17 A 1733 ASN ILE PHE LYS HIS ILE SER VAL LYS ASP PHE THR SER
SEQRES 18 A 1733 LEU GLY PHE ASN GLU VAL PHE SER ARG PRO GLU TRP MET
SEQRES 19 A 1733 ILE LEU THR CYS LEU PRO VAL PRO PRO PRO PRO VAL ARG
SEQRES 20 A 1733 PRO SER ILE SER PHE ASN GLU SER GLN ARG GLY GLU ASP
SEQRES 21 A 1733 ASP LEU THR PHE LYS LEU ALA ASP ILE LEU LYS ALA ASN
SEQRES 22 A 1733 ILE SER LEU GLU THR LEU GLU HIS ASN GLY ALA PRO HIS
SEQRES 23 A 1733 HIS ALA ILE GLU GLU ALA GLU SER LEU LEU GLN PHE HIS
SEQRES 24 A 1733 VAL ALA THR TYR MET ASP ASN ASP ILE ALA GLY GLN PRO
SEQRES 25 A 1733 GLN ALA LEU GLN LYS SER GLY ARG PRO VAL LYS SER ILE
SEQRES 26 A 1733 ARG ALA ARG LEU LYS GLY LYS GLU GLY ARG ILE ARG GLY
SEQRES 27 A 1733 ASN LEU MET GLY LYS ARG VAL ASP PHE SER ALA ARG THR
SEQRES 28 A 1733 VAL ILE SER GLY ASP PRO ASN LEU GLU LEU ASP GLN VAL
SEQRES 29 A 1733 GLY VAL PRO LYS SER ILE ALA LYS THR LEU THR TYR PRO
SEQRES 30 A 1733 GLU VAL VAL THR PRO TYR ASN ILE ASP ARG LEU THR GLN
SEQRES 31 A 1733 LEU VAL ARG ASN GLY PRO ASN GLU HIS PRO GLY ALA LYS
SEQRES 32 A 1733 TYR VAL ILE ARG ASP SER GLY ASP ARG ILE ASP LEU ARG
SEQRES 33 A 1733 TYR SER LYS ARG ALA GLY ASP ILE GLN LEU GLN TYR GLY
SEQRES 34 A 1733 TRP LYS VAL GLU ARG HIS ILE MET ASP ASN ASP PRO VAL
SEQRES 35 A 1733 LEU PHE ASN ARG GLN PRO SER LEU HIS LYS MET SER MET
SEQRES 36 A 1733 MET ALA HIS ARG VAL LYS VAL ILE PRO TYR SER THR PHE
SEQRES 37 A 1733 ARG LEU ASN LEU SER VAL THR SER PRO TYR ASN ALA ASP
SEQRES 38 A 1733 PHE ASP GLY ASP GLU MET ASN LEU HIS VAL PRO GLN SER
SEQRES 39 A 1733 GLU GLU THR ARG ALA GLU LEU SER GLN LEU CYS ALA VAL
SEQRES 40 A 1733 PRO LEU GLN ILE VAL SER PRO GLN SER ASN LYS PRO CYS
SEQRES 41 A 1733 MET GLY ILE VAL GLN ASP THR LEU CYS GLY ILE ARG LYS
SEQRES 42 A 1733 LEU THR LEU ARG ASP THR PHE ILE GLU LEU ASP GLN VAL
SEQRES 43 A 1733 LEU ASN MET LEU TYR TRP VAL PRO ASP TRP ASP GLY VAL
SEQRES 44 A 1733 ILE PRO THR PRO ALA ILE ILE LYS PRO LYS PRO LEU TRP
SEQRES 45 A 1733 SER GLY LYS GLN ILE LEU SER VAL ALA ILE PRO ASN GLY
SEQRES 46 A 1733 ILE HIS LEU GLN ARG PHE ASP GLU GLY THR THR LEU LEU
SEQRES 47 A 1733 SER PRO LYS ASP ASN GLY MET LEU ILE ILE ASP GLY GLN
SEQRES 48 A 1733 ILE ILE PHE GLY VAL VAL GLU LYS LYS THR VAL GLY SER
SEQRES 49 A 1733 SER ASN GLY GLY LEU ILE HIS VAL VAL THR ARG GLU LYS
SEQRES 50 A 1733 GLY PRO GLN VAL CYS ALA LYS LEU PHE GLY ASN ILE GLN
SEQRES 51 A 1733 LYS VAL VAL ASN PHE TRP LEU LEU HIS ASN GLY PHE SER
SEQRES 52 A 1733 THR GLY ILE GLY ASP THR ILE ALA ASP GLY PRO THR MET
SEQRES 53 A 1733 ARG GLU ILE THR GLU THR ILE ALA GLU ALA LYS LYS LYS
SEQRES 54 A 1733 VAL LEU ASP VAL THR LYS GLU ALA GLN ALA ASN LEU LEU
SEQRES 55 A 1733 THR ALA LYS HIS GLY MET THR LEU ARG GLU SER PHE GLU
SEQRES 56 A 1733 ASP ASN VAL VAL ARG PHE LEU ASN GLU ALA ARG ASP LYS
SEQRES 57 A 1733 ALA GLY ARG LEU ALA GLU VAL ASN LEU LYS ASP LEU ASN
SEQRES 58 A 1733 ASN VAL LYS GLN MET VAL MET ALA GLY SER LYS GLY SER
SEQRES 59 A 1733 PHE ILE ASN ILE ALA GLN MET SER ALA CYS VAL GLY GLN
SEQRES 60 A 1733 GLN SER VAL GLU GLY LYS ARG ILE ALA PHE GLY PHE VAL
SEQRES 61 A 1733 ASP ARG THR LEU PRO HIS PHE SER LYS ASP ASP TYR SER
SEQRES 62 A 1733 PRO GLU SER LYS GLY PHE VAL GLU ASN SER TYR LEU ARG
SEQRES 63 A 1733 GLY LEU THR PRO GLN GLU PHE PHE PHE HIS ALA MET GLY
SEQRES 64 A 1733 GLY ARG GLU GLY LEU ILE ASP THR ALA VAL LYS THR ALA
SEQRES 65 A 1733 GLU THR GLY TYR ILE GLN ARG ARG LEU VAL LYS ALA LEU
SEQRES 66 A 1733 GLU ASP ILE MET VAL HIS TYR ASP ASN THR THR ARG ASN
SEQRES 67 A 1733 SER LEU GLY ASN VAL ILE GLN PHE ILE TYR GLY GLU ASP
SEQRES 68 A 1733 GLY MET ASP ALA ALA HIS ILE GLU LYS GLN SER LEU ASP
SEQRES 69 A 1733 THR ILE GLY GLY SER ASP ALA ALA PHE GLU LYS ARG TYR
SEQRES 70 A 1733 ARG VAL ASP LEU LEU ASN THR ASP HIS THR LEU ASP PRO
SEQRES 71 A 1733 SER LEU LEU GLU SER GLY SER GLU ILE LEU GLY ASP LEU
SEQRES 72 A 1733 LYS LEU GLN VAL LEU LEU ASP GLU GLU TYR LYS GLN LEU
SEQRES 73 A 1733 VAL LYS ASP ARG LYS PHE LEU ARG GLU VAL PHE VAL ASP
SEQRES 74 A 1733 GLY GLU ALA ASN TRP PRO LEU PRO VAL ASN ILE ARG ARG
SEQRES 75 A 1733 ILE ILE GLN ASN ALA GLN GLN THR PHE HIS ILE ASP HIS
SEQRES 76 A 1733 THR LYS PRO SER ASP LEU THR ILE LYS ASP ILE VAL LEU
SEQRES 77 A 1733 GLY VAL LYS ASP LEU GLN GLU ASN LEU LEU VAL LEU ARG
SEQRES 78 A 1733 GLY LYS ASN GLU ILE ILE GLN ASN ALA GLN ARG ASP ALA
SEQRES 79 A 1733 VAL THR LEU PHE CYS CYS LEU LEU ARG SER ARG LEU ALA
SEQRES 80 A 1733 THR ARG ARG VAL LEU GLN GLU TYR ARG LEU THR LYS GLN
SEQRES 81 A 1733 ALA PHE ASP TRP VAL LEU SER ASN ILE GLU ALA GLN PHE
SEQRES 82 A 1733 LEU ARG SER VAL VAL HIS PRO GLY GLU MET VAL GLY VAL
SEQRES 83 A 1733 LEU ALA ALA GLN SER ILE GLY GLU PRO ALA THR GLN MET
SEQRES 84 A 1733 THR LEU ASN THR PHE HIS PHE ALA GLY VAL ALA SER LYS
SEQRES 85 A 1733 LYS VAL THR SER GLY VAL PRO ARG LEU LYS GLU ILE LEU
SEQRES 86 A 1733 ASN VAL ALA LYS ASN MET LYS THR PRO SER LEU THR VAL
SEQRES 87 A 1733 TYR LEU GLU PRO GLY HIS ALA ALA ASP GLN GLU GLN ALA
SEQRES 88 A 1733 LYS LEU ILE ARG SER ALA ILE GLU HIS THR THR LEU LYS
SEQRES 89 A 1733 SER VAL THR ILE ALA SER GLU ILE TYR TYR ASP PRO ASP
SEQRES 90 A 1733 PRO ARG SER THR VAL ILE PRO GLU ASP GLU GLU ILE ILE
SEQRES 91 A 1733 GLN LEU HIS PHE SER LEU LEU ASP GLU GLU ALA GLU GLN
SEQRES 92 A 1733 SER PHE ASP GLN GLN SER PRO TRP LEU LEU ARG LEU GLU
SEQRES 93 A 1733 LEU ASP ARG ALA ALA MET ASN ASP LYS ASP LEU THR MET
SEQRES 94 A 1733 GLY GLN VAL GLY GLU ARG ILE LYS GLN THR PHE LYS ASN
SEQRES 95 A 1733 ASP LEU PHE VAL ILE TRP SER GLU ASP ASN ASP GLU LYS
SEQRES 96 A 1733 LEU ILE ILE ARG CYS ARG VAL VAL ARG PRO LYS SER LEU
SEQRES 97 A 1733 ASP ALA GLU THR GLU ALA GLU GLU ASP HIS MET LEU LYS
SEQRES 98 A 1733 LYS ILE GLU ASN THR MET LEU GLU ASN ILE THR LEU ARG
SEQRES 99 A 1733 GLY VAL GLU ASN ILE GLU ARG VAL VAL MET MET LYS TYR
SEQRES 100 A 1733 ASP ARG LYS VAL PRO SER PRO THR GLY GLU TYR VAL LYS
SEQRES 101 A 1733 GLU PRO GLU TRP VAL LEU GLU THR ASP GLY VAL ASN LEU
SEQRES 102 A 1733 SER GLU VAL MET THR VAL PRO GLY ILE ASP PRO THR ARG
SEQRES 103 A 1733 ILE TYR THR ASN SER PHE ILE ASP ILE MET GLU VAL LEU
SEQRES 104 A 1733 GLY ILE GLU ALA GLY ARG ALA ALA LEU TYR LYS GLU VAL
SEQRES 105 A 1733 TYR ASN VAL ILE ALA SER ASP GLY SER TYR VAL ASN TYR
SEQRES 106 A 1733 ARG HIS MET ALA LEU LEU VAL ASP VAL MET THR THR GLN
SEQRES 107 A 1733 GLY GLY LEU THR SER VAL THR ARG HIS GLY PHE ASN ARG
SEQRES 108 A 1733 SER ASN THR GLY ALA LEU MET ARG CYS SER PHE GLU GLU
SEQRES 109 A 1733 THR VAL GLU ILE LEU PHE GLU ALA GLY ALA SER ALA GLU
SEQRES 110 A 1733 LEU ASP ASP CYS ARG GLY VAL SER GLU ASN VAL ILE LEU
SEQRES 111 A 1733 GLY GLN MET ALA PRO ILE GLY THR GLY ALA PHE ASP VAL
SEQRES 112 A 1733 MET ILE ASP GLU GLU SER LEU VAL LYS TYR MET PRO GLU
SEQRES 113 A 1733 GLN LYS ILE THR GLU ILE GLU ASP GLY GLN ASP GLY GLY
SEQRES 114 A 1733 VAL THR PRO TYR SER ASN GLU SER GLY LEU VAL ASN ALA
SEQRES 115 A 1733 ASP LEU ASP VAL LYS ASP GLU LEU MET PHE SER PRO LEU
SEQRES 116 A 1733 VAL ASP SER GLY SER ASN ASP ALA MET ALA GLY GLY PHE
SEQRES 117 A 1733 THR ALA TYR GLY GLY ALA ASP TYR GLY GLU ALA THR SER
SEQRES 118 A 1733 PRO PHE GLY ALA TYR GLY GLU ALA PRO THR SER PRO GLY
SEQRES 119 A 1733 PHE GLY VAL SER SER PRO GLY PHE SER PRO THR SER PRO
SEQRES 120 A 1733 THR TYR SER PRO THR SER PRO ALA TYR SER PRO THR SER
SEQRES 121 A 1733 PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO THR
SEQRES 122 A 1733 SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO
SEQRES 123 A 1733 THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER
SEQRES 124 A 1733 PRO THR SER PRO SER TYR SER PRO THR SER PRO SER TYR
SEQRES 125 A 1733 SER PRO THR SER PRO SER TYR SER PRO THR SER PRO SER
SEQRES 126 A 1733 TYR SER PRO THR SER PRO SER TYR SER PRO THR SER PRO
SEQRES 127 A 1733 SER TYR SER PRO THR SER PRO SER TYR SER PRO THR SER
SEQRES 128 A 1733 PRO SER TYR SER PRO THR SER PRO ALA TYR SER PRO THR
SEQRES 129 A 1733 SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO
SEQRES 130 A 1733 THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER
SEQRES 131 A 1733 PRO THR SER PRO ASN TYR SER PRO THR SER PRO SER TYR
SEQRES 132 A 1733 SER PRO THR SER PRO GLY TYR SER PRO GLY SER PRO ALA
SEQRES 133 A 1733 TYR SER PRO LYS GLN ASP GLU GLN LYS HIS ASN GLU ASN
SEQRES 134 A 1733 GLU ASN SER ARG
SEQRES 1 B 1224 MET SER ASP LEU ALA ASN SER GLU LYS TYR TYR ASP GLU
SEQRES 2 B 1224 ASP PRO TYR GLY PHE GLU ASP GLU SER ALA PRO ILE THR
SEQRES 3 B 1224 ALA GLU ASP SER TRP ALA VAL ILE SER ALA PHE PHE ARG
SEQRES 4 B 1224 GLU LYS GLY LEU VAL SER GLN GLN LEU ASP SER PHE ASN
SEQRES 5 B 1224 GLN PHE VAL ASP TYR THR LEU GLN ASP ILE ILE CYS GLU
SEQRES 6 B 1224 ASP SER THR LEU ILE LEU GLU GLN LEU ALA GLN HIS THR
SEQRES 7 B 1224 THR GLU SER ASP ASN ILE SER ARG LYS TYR GLU ILE SER
SEQRES 8 B 1224 PHE GLY LYS ILE TYR VAL THR LYS PRO MET VAL ASN GLU
SEQRES 9 B 1224 SER ASP GLY VAL THR HIS ALA LEU TYR PRO GLN GLU ALA
SEQRES 10 B 1224 ARG LEU ARG ASN LEU THR TYR SER SER GLY LEU PHE VAL
SEQRES 11 B 1224 ASP VAL LYS LYS ARG THR TYR GLU ALA ILE ASP VAL PRO
SEQRES 12 B 1224 GLY ARG GLU LEU LYS TYR GLU LEU ILE ALA GLU GLU SER
SEQRES 13 B 1224 GLU ASP ASP SER GLU SER GLY LYS VAL PHE ILE GLY ARG
SEQRES 14 B 1224 LEU PRO ILE MET LEU ARG SER LYS ASN CYS TYR LEU SER
SEQRES 15 B 1224 GLU ALA THR GLU SER ASP LEU TYR LYS LEU LYS GLU CYS
SEQRES 16 B 1224 PRO PHE ASP MET GLY GLY TYR PHE ILE ILE ASN GLY SER
SEQRES 17 B 1224 GLU LYS VAL LEU ILE ALA GLN GLU ARG SER ALA GLY ASN
SEQRES 18 B 1224 ILE VAL GLN VAL PHE LYS LYS ALA ALA PRO SER PRO ILE
SEQRES 19 B 1224 SER HIS VAL ALA GLU ILE ARG SER ALA LEU GLU LYS GLY
SEQRES 20 B 1224 SER ARG PHE ILE SER THR LEU GLN VAL LYS LEU TYR GLY
SEQRES 21 B 1224 ARG GLU GLY SER SER ALA ARG THR ILE LYS ALA THR LEU
SEQRES 22 B 1224 PRO TYR ILE LYS GLN ASP ILE PRO ILE VAL ILE ILE PHE
SEQRES 23 B 1224 ARG ALA LEU GLY ILE ILE PRO ASP GLY GLU ILE LEU GLU
SEQRES 24 B 1224 HIS ILE CYS TYR ASP VAL ASN ASP TRP GLN MET LEU GLU
SEQRES 25 B 1224 MET LEU LYS PRO CYS VAL GLU ASP GLY PHE VAL ILE GLN
SEQRES 26 B 1224 ASP ARG GLU THR ALA LEU ASP PHE ILE GLY ARG ARG GLY
SEQRES 27 B 1224 THR ALA LEU GLY ILE LYS LYS GLU LYS ARG ILE GLN TYR
SEQRES 28 B 1224 ALA LYS ASP ILE LEU GLN LYS GLU PHE LEU PRO HIS ILE
SEQRES 29 B 1224 THR GLN LEU GLU GLY PHE GLU SER ARG LYS ALA PHE PHE
SEQRES 30 B 1224 LEU GLY TYR MET ILE ASN ARG LEU LEU LEU CYS ALA LEU
SEQRES 31 B 1224 ASP ARG LYS ASP GLN ASP ASP ARG ASP HIS PHE GLY LYS
SEQRES 32 B 1224 LYS ARG LEU ASP LEU ALA GLY PRO LEU LEU ALA GLN LEU
SEQRES 33 B 1224 PHE LYS THR LEU PHE LYS LYS LEU THR LYS ASP ILE PHE
SEQRES 34 B 1224 ARG TYR MET GLN ARG THR VAL GLU GLU ALA HIS ASP PHE
SEQRES 35 B 1224 ASN MET LYS LEU ALA ILE ASN ALA LYS THR ILE THR SER
SEQRES 36 B 1224 GLY LEU LYS TYR ALA LEU ALA THR GLY ASN TRP GLY GLU
SEQRES 37 B 1224 GLN LYS LYS ALA MET SER SER ARG ALA GLY VAL SER GLN
SEQRES 38 B 1224 VAL LEU ASN ARG TYR THR TYR SER SER THR LEU SER HIS
SEQRES 39 B 1224 LEU ARG ARG THR ASN THR PRO ILE GLY ARG ASP GLY LYS
SEQRES 40 B 1224 LEU ALA LYS PRO ARG GLN LEU HIS ASN THR HIS TRP GLY
SEQRES 41 B 1224 LEU VAL CYS PRO ALA GLU THR PRO GLU GLY GLN ALA CYS
SEQRES 42 B 1224 GLY LEU VAL LYS ASN LEU SER LEU MET SER CYS ILE SER
SEQRES 43 B 1224 VAL GLY THR ASP PRO MET PRO ILE ILE THR PHE LEU SER
SEQRES 44 B 1224 GLU TRP GLY MET GLU PRO LEU GLU ASP TYR VAL PRO HIS
SEQRES 45 B 1224 GLN SER PRO ASP ALA THR ARG VAL PHE VAL ASN GLY VAL
SEQRES 46 B 1224 TRP HIS GLY VAL HIS ARG ASN PRO ALA ARG LEU MET GLU
SEQRES 47 B 1224 THR LEU ARG THR LEU ARG ARG LYS GLY ASP ILE ASN PRO
SEQRES 48 B 1224 GLU VAL SER MET ILE ARG ASP ILE ARG GLU LYS GLU LEU
SEQRES 49 B 1224 LYS ILE PHE THR ASP ALA GLY ARG VAL TYR ARG PRO LEU
SEQRES 50 B 1224 PHE ILE VAL GLU ASP ASP GLU SER LEU GLY HIS LYS GLU
SEQRES 51 B 1224 LEU LYS VAL ARG LYS GLY HIS ILE ALA LYS LEU MET ALA
SEQRES 52 B 1224 THR GLU TYR GLN ASP ILE GLU GLY GLY PHE GLU ASP VAL
SEQRES 53 B 1224 GLU GLU TYR THR TRP SER SER LEU LEU ASN GLU GLY LEU
SEQRES 54 B 1224 VAL GLU TYR ILE ASP ALA GLU GLU GLU GLU SER ILE LEU
SEQRES 55 B 1224 ILE ALA MET GLN PRO GLU ASP LEU GLU PRO ALA GLU ALA
SEQRES 56 B 1224 ASN GLU GLU ASN ASP LEU ASP VAL ASP PRO ALA LYS ARG
SEQRES 57 B 1224 ILE ARG VAL SER HIS HIS ALA THR THR PHE THR HIS CYS
SEQRES 58 B 1224 GLU ILE HIS PRO SER MET ILE LEU GLY VAL ALA ALA SER
SEQRES 59 B 1224 ILE ILE PRO PHE PRO ASP HIS ASN GLN SER PRO ARG ASN
SEQRES 60 B 1224 THR TYR GLN SER ALA MET GLY LYS GLN ALA MET GLY VAL
SEQRES 61 B 1224 PHE LEU THR ASN TYR ASN VAL ARG MET ASP THR MET ALA
SEQRES 62 B 1224 ASN ILE LEU TYR TYR PRO GLN LYS PRO LEU GLY THR THR
SEQRES 63 B 1224 ARG ALA MET GLU TYR LEU LYS PHE ARG GLU LEU PRO ALA
SEQRES 64 B 1224 GLY GLN ASN ALA ILE VAL ALA ILE ALA CYS TYR SER GLY
SEQRES 65 B 1224 TYR ASN GLN GLU ASP SER MET ILE MET ASN GLN SER SER
SEQRES 66 B 1224 ILE ASP ARG GLY LEU PHE ARG SER LEU PHE PHE ARG SER
SEQRES 67 B 1224 TYR MET ASP GLN GLU LYS LYS TYR GLY MET SER ILE THR
SEQRES 68 B 1224 GLU THR PHE GLU LYS PRO GLN ARG THR ASN THR LEU ARG
SEQRES 69 B 1224 MET LYS HIS GLY THR TYR ASP LYS LEU ASP ASP ASP GLY
SEQRES 70 B 1224 LEU ILE ALA PRO GLY VAL ARG VAL SER GLY GLU ASP VAL
SEQRES 71 B 1224 ILE ILE GLY LYS THR THR PRO ILE SER PRO ASP GLU GLU
SEQRES 72 B 1224 GLU LEU GLY GLN ARG THR ALA TYR HIS SER LYS ARG ASP
SEQRES 73 B 1224 ALA SER THR PRO LEU ARG SER THR GLU ASN GLY ILE VAL
SEQRES 74 B 1224 ASP GLN VAL LEU VAL THR THR ASN GLN ASP GLY LEU LYS
SEQRES 75 B 1224 PHE VAL LYS VAL ARG VAL ARG THR THR LYS ILE PRO GLN
SEQRES 76 B 1224 ILE GLY ASP LYS PHE ALA SER ARG HIS GLY GLN LYS GLY
SEQRES 77 B 1224 THR ILE GLY ILE THR TYR ARG ARG GLU ASP MET PRO PHE
SEQRES 78 B 1224 THR ALA GLU GLY ILE VAL PRO ASP LEU ILE ILE ASN PRO
SEQRES 79 B 1224 HIS ALA ILE PRO SER ARG MET THR VAL ALA HIS LEU ILE
SEQRES 80 B 1224 GLU CYS LEU LEU SER LYS VAL ALA ALA LEU SER GLY ASN
SEQRES 81 B 1224 GLU GLY ASP ALA SER PRO PHE THR ASP ILE THR VAL GLU
SEQRES 82 B 1224 GLY ILE SER LYS LEU LEU ARG GLU HIS GLY TYR GLN SER
SEQRES 83 B 1224 ARG GLY PHE GLU VAL MET TYR ASN GLY HIS THR GLY LYS
SEQRES 84 B 1224 LYS LEU MET ALA GLN ILE PHE PHE GLY PRO THR TYR TYR
SEQRES 85 B 1224 GLN ARG LEU ARG HIS MET VAL ASP ASP LYS ILE HIS ALA
SEQRES 86 B 1224 ARG ALA ARG GLY PRO MET GLN VAL LEU THR ARG GLN PRO
SEQRES 87 B 1224 VAL GLU GLY ARG SER ARG ASP GLY GLY LEU ARG PHE GLY
SEQRES 88 B 1224 GLU MET GLU ARG ASP CYS MET ILE ALA HIS GLY ALA ALA
SEQRES 89 B 1224 SER PHE LEU LYS GLU ARG LEU MET GLU ALA SER ASP ALA
SEQRES 90 B 1224 PHE ARG VAL HIS ILE CYS GLY ILE CYS GLY LEU MET THR
SEQRES 91 B 1224 VAL ILE ALA LYS LEU ASN HIS ASN GLN PHE GLU CYS LYS
SEQRES 92 B 1224 GLY CYS ASP ASN LYS ILE ASP ILE TYR GLN ILE HIS ILE
SEQRES 93 B 1224 PRO TYR ALA ALA LYS LEU LEU PHE GLN GLU LEU MET ALA
SEQRES 94 B 1224 MET ASN ILE THR PRO ARG LEU TYR THR ASP ARG SER ARG
SEQRES 95 B 1224 ASP PHE
SEQRES 1 C 318 MET SER GLU GLU GLY PRO GLN VAL LYS ILE ARG GLU ALA
SEQRES 2 C 318 SER LYS ASP ASN VAL ASP PHE ILE LEU SER ASN VAL ASP
SEQRES 3 C 318 LEU ALA MET ALA ASN SER LEU ARG ARG VAL MET ILE ALA
SEQRES 4 C 318 GLU ILE PRO THR LEU ALA ILE ASP SER VAL GLU VAL GLU
SEQRES 5 C 318 THR ASN THR THR VAL LEU ALA ASP GLU PHE ILE ALA HIS
SEQRES 6 C 318 ARG LEU GLY LEU ILE PRO LEU GLN SER MET ASP ILE GLU
SEQRES 7 C 318 GLN LEU GLU TYR SER ARG ASP CYS PHE CYS GLU ASP HIS
SEQRES 8 C 318 CYS ASP LYS CYS SER VAL VAL LEU THR LEU GLN ALA PHE
SEQRES 9 C 318 GLY GLU SER GLU SER THR THR ASN VAL TYR SER LYS ASP
SEQRES 10 C 318 LEU VAL ILE VAL SER ASN LEU MET GLY ARG ASN ILE GLY
SEQRES 11 C 318 HIS PRO ILE ILE GLN ASP LYS GLU GLY ASN GLY VAL LEU
SEQRES 12 C 318 ILE CYS LYS LEU ARG LYS GLY GLN GLU LEU LYS LEU THR
SEQRES 13 C 318 CYS VAL ALA LYS LYS GLY ILE ALA LYS GLU HIS ALA LYS
SEQRES 14 C 318 TRP GLY PRO ALA ALA ALA ILE GLU PHE GLU TYR ASP PRO
SEQRES 15 C 318 TRP ASN LYS LEU LYS HIS THR ASP TYR TRP TYR GLU GLN
SEQRES 16 C 318 ASP SER ALA LYS GLU TRP PRO GLN SER LYS ASN CYS GLU
SEQRES 17 C 318 TYR GLU ASP PRO PRO ASN GLU GLY ASP PRO PHE ASP TYR
SEQRES 18 C 318 LYS ALA GLN ALA ASP THR PHE TYR MET ASN VAL GLU SER
SEQRES 19 C 318 VAL GLY SER ILE PRO VAL ASP GLN VAL VAL VAL ARG GLY
SEQRES 20 C 318 ILE ASP THR LEU GLN LYS LYS VAL ALA SER ILE LEU LEU
SEQRES 21 C 318 ALA LEU THR GLN MET ASP GLN ASP LYS VAL ASN PHE ALA
SEQRES 22 C 318 SER GLY ASP ASN ASN THR ALA SER ASN MET LEU GLY SER
SEQRES 23 C 318 ASN GLU ASP VAL MET MET THR GLY ALA GLU GLN ASP PRO
SEQRES 24 C 318 TYR SER ASN ALA SER GLN MET GLY ASN THR GLY SER GLY
SEQRES 25 C 318 GLY TYR ASP ASN ALA TRP
SEQRES 1 E 215 MET ASP GLN GLU ASN GLU ARG ASN ILE SER ARG LEU TRP
SEQRES 2 E 215 ARG ALA PHE ARG THR VAL LYS GLU MET VAL LYS ASP ARG
SEQRES 3 E 215 GLY TYR PHE ILE THR GLN GLU GLU VAL GLU LEU PRO LEU
SEQRES 4 E 215 GLU ASP PHE LYS ALA LYS TYR CYS ASP SER MET GLY ARG
SEQRES 5 E 215 PRO GLN ARG LYS MET MET SER PHE GLN ALA ASN PRO THR
SEQRES 6 E 215 GLU GLU SER ILE SER LYS PHE PRO ASP MET GLY SER LEU
SEQRES 7 E 215 TRP VAL GLU PHE CYS ASP GLU PRO SER VAL GLY VAL LYS
SEQRES 8 E 215 THR MET LYS THR PHE VAL ILE HIS ILE GLN GLU LYS ASN
SEQRES 9 E 215 PHE GLN THR GLY ILE PHE VAL TYR GLN ASN ASN ILE THR
SEQRES 10 E 215 PRO SER ALA MET LYS LEU VAL PRO SER ILE PRO PRO ALA
SEQRES 11 E 215 THR ILE GLU THR PHE ASN GLU ALA ALA LEU VAL VAL ASN
SEQRES 12 E 215 ILE THR HIS HIS GLU LEU VAL PRO LYS HIS ILE ARG LEU
SEQRES 13 E 215 SER SER ASP GLU LYS ARG GLU LEU LEU LYS ARG TYR ARG
SEQRES 14 E 215 LEU LYS GLU SER GLN LEU PRO ARG ILE GLN ARG ALA ASP
SEQRES 15 E 215 PRO VAL ALA LEU TYR LEU GLY LEU LYS ARG GLY GLU VAL
SEQRES 16 E 215 VAL LYS ILE ILE ARG LYS SER GLU THR SER GLY ARG TYR
SEQRES 17 E 215 ALA SER TYR ARG ILE CYS MET
SEQRES 1 F 155 MET SER ASP TYR GLU GLU ALA PHE ASN ASP GLY ASN GLU
SEQRES 2 F 155 ASN PHE GLU ASP PHE ASP VAL GLU HIS PHE SER ASP GLU
SEQRES 3 F 155 GLU THR TYR GLU GLU LYS PRO GLN PHE LYS ASP GLY GLU
SEQRES 4 F 155 THR THR ASP ALA ASN GLY LYS THR ILE VAL THR GLY GLY
SEQRES 5 F 155 ASN GLY PRO GLU ASP PHE GLN GLN HIS GLU GLN ILE ARG
SEQRES 6 F 155 ARG LYS THR LEU LYS GLU LYS ALA ILE PRO LYS ASP GLN
SEQRES 7 F 155 ARG ALA THR THR PRO TYR MET THR LYS TYR GLU ARG ALA
SEQRES 8 F 155 ARG ILE LEU GLY THR ARG ALA LEU GLN ILE SER MET ASN
SEQRES 9 F 155 ALA PRO VAL PHE VAL ASP LEU GLU GLY GLU THR ASP PRO
SEQRES 10 F 155 LEU ARG ILE ALA MET LYS GLU LEU ALA GLU LYS LYS ILE
SEQRES 11 F 155 PRO LEU VAL ILE ARG ARG TYR LEU PRO ASP GLY SER PHE
SEQRES 12 F 155 GLU ASP TRP SER VAL GLU GLU LEU ILE VAL ASP LEU
SEQRES 1 H 146 MET SER ASN THR LEU PHE ASP ASP ILE PHE GLN VAL SER
SEQRES 2 H 146 GLU VAL ASP PRO GLY ARG TYR ASN LYS VAL CYS ARG ILE
SEQRES 3 H 146 GLU ALA ALA SER THR THR GLN ASP GLN CYS LYS LEU THR
SEQRES 4 H 146 LEU ASP ILE ASN VAL GLU LEU PHE PRO VAL ALA ALA GLN
SEQRES 5 H 146 ASP SER LEU THR VAL THR ILE ALA SER SER LEU ASN LEU
SEQRES 6 H 146 GLU ASP THR PRO ALA ASN ASP SER SER ALA THR ARG SER
SEQRES 7 H 146 TRP ARG PRO PRO GLN ALA GLY ASP ARG SER LEU ALA ASP
SEQRES 8 H 146 ASP TYR ASP TYR VAL MET TYR GLY THR ALA TYR LYS PHE
SEQRES 9 H 146 GLU GLU VAL SER LYS ASP LEU ILE ALA VAL TYR TYR SER
SEQRES 10 H 146 PHE GLY GLY LEU LEU MET ARG LEU GLU GLY ASN TYR ARG
SEQRES 11 H 146 ASN LEU ASN ASN LEU LYS GLN GLU ASN ALA TYR LEU LEU
SEQRES 12 H 146 ILE ARG ARG
SEQRES 1 I 122 MET THR THR PHE ARG PHE CYS ARG ASP CYS ASN ASN MET
SEQRES 2 I 122 LEU TYR PRO ARG GLU ASP LYS GLU ASN ASN ARG LEU LEU
SEQRES 3 I 122 PHE GLU CYS ARG THR CYS SER TYR VAL GLU GLU ALA GLY
SEQRES 4 I 122 SER PRO LEU VAL TYR ARG HIS GLU LEU ILE THR ASN ILE
SEQRES 5 I 122 GLY GLU THR ALA GLY VAL VAL GLN ASP ILE GLY SER ASP
SEQRES 6 I 122 PRO THR LEU PRO ARG SER ASP ARG GLU CYS PRO LYS CYS
SEQRES 7 I 122 HIS SER ARG GLU ASN VAL PHE PHE GLN SER GLN GLN ARG
SEQRES 8 I 122 ARG LYS ASP THR SER MET VAL LEU PHE PHE VAL CYS LEU
SEQRES 9 I 122 SER CYS SER HIS ILE PHE THR SER ASP GLN LYS ASN LYS
SEQRES 10 I 122 ARG THR GLN PHE SER
SEQRES 1 J 70 MET ILE VAL PRO VAL ARG CYS PHE SER CYS GLY LYS VAL
SEQRES 2 J 70 VAL GLY ASP LYS TRP GLU SER TYR LEU ASN LEU LEU GLN
SEQRES 3 J 70 GLU ASP GLU LEU ASP GLU GLY THR ALA LEU SER ARG LEU
SEQRES 4 J 70 GLY LEU LYS ARG TYR CYS CYS ARG ARG MET ILE LEU THR
SEQRES 5 J 70 HIS VAL ASP LEU ILE GLU LYS PHE LEU ARG TYR ASN PRO
SEQRES 6 J 70 LEU GLU LYS ARG ASP
SEQRES 1 K 120 MET ASN ALA PRO ASP ARG PHE GLU LEU PHE LEU LEU GLY
SEQRES 2 K 120 GLU GLY GLU SER LYS LEU LYS ILE ASP PRO ASP THR LYS
SEQRES 3 K 120 ALA PRO ASN ALA VAL VAL ILE THR PHE GLU LYS GLU ASP
SEQRES 4 K 120 HIS THR LEU GLY ASN LEU ILE ARG ALA GLU LEU LEU ASN
SEQRES 5 K 120 ASP ARG LYS VAL LEU PHE ALA ALA TYR LYS VAL GLU HIS
SEQRES 6 K 120 PRO PHE PHE ALA ARG PHE LYS LEU ARG ILE GLN THR THR
SEQRES 7 K 120 GLU GLY TYR ASP PRO LYS ASP ALA LEU LYS ASN ALA CYS
SEQRES 8 K 120 ASN SER ILE ILE ASN LYS LEU GLY ALA LEU LYS THR ASN
SEQRES 9 K 120 PHE GLU THR GLU TRP ASN LEU GLN THR LEU ALA ALA ASP
SEQRES 10 K 120 ASP ALA PHE
SEQRES 1 L 70 MET SER ARG GLU GLY PHE GLN ILE PRO THR ASN LEU ASP
SEQRES 2 L 70 ALA ALA ALA ALA GLY THR SER GLN ALA ARG THR ALA THR
SEQRES 3 L 70 LEU LYS TYR ILE CYS ALA GLU CYS SER SER LYS LEU SER
SEQRES 4 L 70 LEU SER ARG THR ASP ALA VAL ARG CYS LYS ASP CYS GLY
SEQRES 5 L 70 HIS ARG ILE LEU LEU LYS ALA ARG THR LYS ARG LEU VAL
SEQRES 6 L 70 GLN PHE GLU ALA ARG
HET MN A3009 1
HET MN A3010 1
HET ZN A3006 1
HET ZN A3008 1
HET ATP A3011 30
HET ZN B3007 1
HET ZN C3002 1
HET ZN I3003 1
HET ZN I3004 1
HET ZN J3001 1
HET ZN L3005 1
HETNAM MN MANGANESE (II) ION
HETNAM ZN ZINC ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 11 MN 2(MN 2+)
FORMUL 13 ZN 8(ZN 2+)
FORMUL 15 ATP C10 H16 N5 O13 P3
FORMUL 22 HOH *(H2 O)
HELIX 1 1 SER A 23 ILE A 30 1 8
HELIX 2 2 PHE A 95 GLU A 104 1 10
HELIX 3 3 ASP A 116 ASN A 119 5 4
HELIX 4 4 GLU A 120 ILE A 128 1 9
HELIX 5 5 ASP A 130 LYS A 143 1 14
HELIX 6 6 SER A 203 LYS A 212 1 10
HELIX 7 7 SER A 215 LEU A 222 1 8
HELIX 8 8 ARG A 230 TRP A 233 5 4
HELIX 9 9 LEU A 262 HIS A 281 1 20
HELIX 10 10 PRO A 285 ASP A 305 1 21
HELIX 11 11 LYS A 368 LEU A 374 1 7
HELIX 12 12 ASN A 384 GLY A 395 1 12
HELIX 13 13 HIS A 451 MET A 453 5 3
HELIX 14 14 ASN A 471 SER A 473 5 3
HELIX 15 15 VAL A 474 ASN A 479 1 6
HELIX 16 16 SER A 494 CYS A 505 1 12
HELIX 17 17 VAL A 507 GLN A 510 5 4
HELIX 18 18 VAL A 524 THR A 535 1 12
HELIX 19 19 GLU A 542 VAL A 553 1 12
HELIX 20 20 GLY A 574 SER A 579 1 6
HELIX 21 21 GLU A 618 GLY A 623 1 6
HELIX 22 22 GLY A 628 GLY A 638 1 11
HELIX 23 23 GLY A 638 HIS A 659 1 22
HELIX 24 24 GLY A 665 ILE A 670 5 6
HELIX 25 25 ASP A 672 ALA A 699 1 28
HELIX 26 26 THR A 709 LEU A 737 1 29
HELIX 27 27 ASN A 741 GLY A 750 1 10
HELIX 28 28 SER A 754 ALA A 763 1 10
HELIX 29 29 THR A 809 GLU A 846 1 38
HELIX 30 30 ILE A 867 ASP A 871 5 5
HELIX 31 31 ASP A 874 ALA A 876 5 3
HELIX 32 32 ASP A 884 GLY A 887 5 4
HELIX 33 33 SER A 889 ARG A 898 1 10
HELIX 34 34 LEU A 913 SER A 917 5 5
HELIX 35 35 ASP A 922 PHE A 947 1 26
HELIX 36 36 ASN A 959 PHE A 971 1 13
HELIX 37 37 THR A 982 GLU A 995 1 14
HELIX 38 38 ASN A 1004 VAL A 1015 1 12
HELIX 39 39 VAL A 1015 LEU A 1026 1 12
HELIX 40 40 ALA A 1027 GLU A 1034 1 8
HELIX 41 41 THR A 1038 SER A 1056 1 19
HELIX 42 42 MET A 1063 THR A 1077 1 15
HELIX 43 43 SER A 1096 ASN A 1106 1 11
HELIX 44 44 ASP A 1127 GLU A 1139 1 13
HELIX 45 45 LEU A 1143 VAL A 1146 1 4
HELIX 46 46 ILE A 1163 GLU A 1165 5 3
HELIX 47 47 ASP A 1166 LEU A 1172 1 7
HELIX 48 48 ASP A 1198 ASP A 1204 1 7
HELIX 49 49 THR A 1208 LYS A 1221 1 14
HELIX 50 50 ASN A 1222 LEU A 1224 5 3
HELIX 51 51 GLU A 1230 GLU A 1234 5 5
HELIX 52 52 ASP A 1257 ASN A 1270 1 14
HELIX 53 53 ASN A 1312 MET A 1317 1 6
HELIX 54 54 SER A 1331 GLY A 1340 1 10
HELIX 55 55 GLY A 1340 ASP A 1359 1 20
HELIX 56 56 ASN A 1364 THR A 1377 1 14
HELIX 57 57 THR A 1405 ALA A 1416 1 12
HELIX 58 58 GLY A 1423 LEU A 1430 1 8
HELIX 59 59 ILE A 1436 GLY A 1439 5 4
HELIX 60 60 THR B 26 GLU B 28 5 3
HELIX 61 61 ASP B 29 GLY B 42 1 14
HELIX 62 62 VAL B 44 TYR B 57 1 14
HELIX 63 63 TYR B 57 ILE B 63 1 7
HELIX 64 64 TYR B 113 ARG B 120 1 8
HELIX 65 65 THR B 185 LEU B 192 1 8
HELIX 66 66 ILE B 282 LEU B 289 1 8
HELIX 67 67 PRO B 293 CYS B 302 1 10
HELIX 68 68 ASP B 307 PHE B 322 1 16
HELIX 69 69 ASP B 326 ARG B 336 1 11
HELIX 70 70 LYS B 344 GLU B 359 1 16
HELIX 71 71 PHE B 370 LEU B 390 1 21
HELIX 72 72 HIS B 400 GLY B 402 5 3
HELIX 73 73 LEU B 408 LEU B 420 1 13
HELIX 74 74 LEU B 420 THR B 425 1 6
HELIX 75 75 ALA B 450 GLY B 464 1 15
HELIX 76 76 THR B 487 LEU B 495 1 9
HELIX 77 77 HIS B 515 TRP B 519 5 5
HELIX 78 78 PRO B 551 TRP B 561 1 11
HELIX 79 79 VAL B 570 SER B 574 5 5
HELIX 80 80 ASN B 592 ARG B 605 1 14
HELIX 81 81 ILE B 619 GLU B 621 5 3
HELIX 82 82 ARG B 654 GLN B 667 1 14
HELIX 83 83 THR B 680 GLU B 687 1 8
HELIX 84 84 GLU B 696 ILE B 701 5 6
HELIX 85 85 GLN B 706 LEU B 710 5 5
HELIX 86 86 HIS B 744 LEU B 749 5 6
HELIX 87 87 ALA B 752 ILE B 756 5 5
HELIX 88 88 PHE B 758 ASN B 762 5 5
HELIX 89 89 GLN B 763 GLY B 774 1 12
HELIX 90 90 LYS B 775 ALA B 777 5 3
HELIX 91 91 ASN B 784 ARG B 788 5 5
HELIX 92 92 ALA B 808 LYS B 813 1 6
HELIX 93 93 GLN B 843 GLY B 849 1 7
HELIX 94 94 ASN B 1013 ILE B 1017 5 5
HELIX 95 95 THR B 1022 GLY B 1039 1 18
HELIX 96 96 THR B 1051 HIS B 1062 1 12
HELIX 97 97 MET B 1098 ILE B 1103 1 6
HELIX 98 98 GLY B 1131 GLY B 1142 1 12
HELIX 99 99 ALA B 1143 LEU B 1151 1 9
HELIX 100 100 TYR B 1198 MET B 1210 1 13
HELIX 101 101 ASP C 26 GLU C 40 1 15
HELIX 102 102 ALA C 59 ILE C 70 1 12
HELIX 103 103 ASP C 76 LEU C 80 5 5
HELIX 104 104 TYR C 82 CYS C 86 5 5
HELIX 105 105 LYS C 116 LEU C 118 5 3
HELIX 106 106 HIS C 167 GLY C 171 5 5
HELIX 107 107 ASP C 196 TRP C 201 1 6
HELIX 108 108 SER C 204 GLU C 208 5 5
HELIX 109 109 VAL C 240 GLN C 264 1 25
HELIX 110 110 GLU E 4 GLY E 27 1 24
HELIX 111 111 THR E 31 LEU E 37 1 7
HELIX 112 112 PRO E 38 TYR E 46 1 9
HELIX 113 113 GLN E 54 SER E 59 1 6
HELIX 114 114 THR E 65 PHE E 72 1 8
HELIX 115 115 GLY E 89 LYS E 103 1 15
HELIX 116 116 ALA E 120 VAL E 124 5 5
HELIX 117 117 ALA E 138 VAL E 141 5 4
HELIX 118 118 ASN E 143 HIS E 147 5 5
HELIX 119 119 SER E 157 TYR E 168 1 12
HELIX 120 120 LYS E 171 LEU E 175 5 5
HELIX 121 121 ASP E 182 LEU E 188 1 7
HELIX 122 122 THR F 86 MET F 103 1 18
HELIX 123 123 ASP F 116 GLU F 127 1 12
HELIX 124 124 GLU F 149 LEU F 151 5 3
HELIX 125 125 ARG H 130 ASN H 134 5 5
HELIX 126 126 ASP I 61 ASP I 65 5 5
HELIX 127 127 LYS J 17 GLU J 27 1 11
HELIX 128 128 ASP J 31 LEU J 39 1 9
HELIX 129 129 ARG J 43 HIS J 53 1 11
HELIX 130 130 LEU J 56 LEU J 61 1 6
HELIX 131 131 ASP K 5 PHE K 10 5 6
HELIX 132 132 ASP K 39 LEU K 51 1 13
HELIX 133 133 PRO K 83 TRP K 109 1 27
SHEET 1 A 3 LEU A1418 ASP A1419 0
SHEET 2 A 3 GLU A 16 LEU A 21 -1 N VAL A 17 O ASP A1419
SHEET 3 A 3 ILE B1212 TYR B1217 -1 O ARG B1215 N GLN A 18
SHEET 1 B 2 ASP A 85 PHE A 91 0
SHEET 2 B 2 ILE A 235 CYS A 238 -1 O LEU A 236 N VAL A 90
SHEET 1 C 2 ASP A 151 PRO A 153 0
SHEET 2 C 2 LEU A 161 SER A 163 -1 O VAL A 162 N VAL A 152
SHEET 1 D 3 THR A 173 ASP A 177 0
SHEET 2 D 3 LYS A 180 TRP A 185 -1 O VAL A 182 N ARG A 175
SHEET 3 D 3 GLU A 198 LEU A 202 -1 O ARG A 200 N GLY A 183
SHEET 1 E 7 SER A 348 GLY A 355 0
SHEET 2 E 7 PHE A 468 LEU A 470 1 O PHE A 468 N VAL A 352
SHEET 3 E 7 GLN A 363 PRO A 367 -1 N GLY A 365 O ARG A 469
SHEET 4 E 7 MET A 455 ILE A 463 1 O ILE A 463 N VAL A 366
SHEET 5 E 7 PRO A 441 ASN A 445 -1 N VAL A 442 O HIS A 458
SHEET 6 E 7 GLU A 486 HIS A 490 -1 O ASN A 488 N ASN A 445
SHEET 7 E 7 SER A 348 GLY A 355 -1 N ALA A 349 O LEU A 489
SHEET 1 F 4 THR A 375 VAL A 379 0
SHEET 2 F 4 LYS A 431 HIS A 435 -1 O VAL A 432 N GLU A 378
SHEET 3 F 4 ALA A 402 ILE A 406 -1 N LYS A 403 O GLU A 433
SHEET 4 F 4 ARG A 412 ASP A 414 -1 O ILE A 413 N VAL A 405
SHEET 1 G 2 VAL A 512 SER A 513 0
SHEET 2 G 2 LYS A 518 PRO A 519 -1 O LYS A 518 N SER A 513
SHEET 1 H 2 PHE A 540 ILE A 541 0
SHEET 2 H 2 TRP A 572 SER A 573 -1 O TRP A 572 N ILE A 541
SHEET 1 I 3 LEU A 588 ARG A 590 0
SHEET 2 I 3 MET A 605 ILE A 608 -1 O MET A 605 N ARG A 590
SHEET 3 I 3 GLN A 611 PHE A 614 -1 O ILE A 613 N LEU A 606
SHEET 1 J 2 GLY A 766 GLN A 767 0
SHEET 2 J 2 PHE A 799 VAL A 800 -1 O VAL A 800 N GLY A 766
SHEET 1 K 3 MET A 849 VAL A 850 0
SHEET 2 K 3 THR A 856 ARG A 857 -1 O ARG A 857 N MET A 849
SHEET 3 K 3 VAL A 863 GLN A 865 -1 O ILE A 864 N THR A 856
SHEET 1 L 2 ILE A 878 SER A 882 0
SHEET 2 L 2 ASN A 953 PRO A 957 -1 O TRP A 954 N GLN A 881
SHEET 1 M 4 VAL A1282 TYR A1287 0
SHEET 2 M 4 GLU A1303 THR A1308 -1 O GLU A1303 N TYR A1287
SHEET 3 M 4 LEU A1116 TYR A1119 -1 N VAL A1118 O LEU A1306
SHEET 4 M 4 TYR A1328 THR A1329 -1 O TYR A1328 N THR A1117
SHEET 1 N 2 THR A1141 THR A1142 0
SHEET 2 N 2 THR A1272 ARG A1274 -1 O LEU A1273 N THR A1141
SHEET 1 O 5 PHE A1225 TRP A1228 0
SHEET 2 O 5 LEU A1236 ARG A1241 -1 O ARG A1241 N PHE A1225
SHEET 3 O 5 TRP A1191 LEU A1197 -1 N LEU A1193 O CYS A1240
SHEET 4 O 5 THR A1147 TYR A1154 -1 N ILE A1148 O GLU A1196
SHEET 5 O 5 LEU I 42 GLU I 47 -1 O HIS I 46 N SER A1150
SHEET 1 P 2 LYS A1290 PRO A1292 0
SHEET 2 P 2 TYR A1298 LYS A1300 -1 O VAL A1299 N VAL A1291
SHEET 1 Q 3 PHE A1441 ILE A1445 0
SHEET 2 Q 3 LEU F 132 TYR F 137 -1 O ARG F 135 N ASP A1442
SHEET 3 Q 3 PHE F 143 SER F 147 -1 O TRP F 146 N ILE F 134
SHEET 1 R 4 HIS B 110 ALA B 111 0
SHEET 2 R 4 TYR B 96 VAL B 102 -1 N VAL B 102 O HIS B 110
SHEET 3 R 4 SER B 125 PHE B 129 -1 O PHE B 129 N TYR B 96
SHEET 4 R 4 PHE B 166 PRO B 171 -1 O ILE B 167 N LEU B 128
SHEET 1 S 3 PHE B 203 ILE B 205 0
SHEET 2 S 3 SER B 208 LEU B 212 -1 O LYS B 210 N PHE B 203
SHEET 3 S 3 SER B 480 VAL B 482 -1 O GLN B 481 N VAL B 211
SHEET 1 T 4 LYS B 404 ASP B 407 0
SHEET 2 T 4 ALA B 214 SER B 218 -1 N ARG B 217 O ARG B 405
SHEET 3 T 4 ARG B 497 ASN B 499 1 O ASN B 499 N ALA B 214
SHEET 4 T 4 VAL B 536 ASN B 538 -1 O LYS B 537 N THR B 498
SHEET 1 U 5 GLN B 224 LYS B 227 0
SHEET 2 U 5 ILE B 234 ARG B 241 -1 O VAL B 237 N PHE B 226
SHEET 3 U 5 THR B 253 TYR B 259 -1 O LEU B 258 N SER B 235
SHEET 4 U 5 ILE B 269 THR B 272 -1 O LYS B 270 N LYS B 257
SHEET 5 U 5 ILE B 280 PRO B 281 -1 O ILE B 280 N ALA B 271
SHEET 1 V 3 CYS B 544 ILE B 545 0
SHEET 2 V 3 VAL B 633 GLU B 641 -1 O TYR B 634 N CYS B 544
SHEET 3 V 3 VAL B 690 ASP B 694 -1 O ILE B 693 N ARG B 635
SHEET 1 W 4 GLU B 650 LEU B 651 0
SHEET 2 W 4 VAL B 633 GLU B 641 -1 N GLU B 641 O GLU B 650
SHEET 3 W 4 HIS B 740 CYS B 741 -1 O CYS B 741 N PHE B 638
SHEET 4 W 4 ILE B 703 ALA B 704 1 N ALA B 704 O HIS B 740
SHEET 1 X 5 GLU B 564 PRO B 565 0
SHEET 2 X 5 VAL B 585 HIS B 590 -1 O VAL B 589 N GLU B 564
SHEET 3 X 5 THR B 578 VAL B 582 -1 N VAL B 580 O GLY B 588
SHEET 4 X 5 GLU B 623 PHE B 627 1 O ILE B 626 N PHE B 581
SHEET 5 X 5 SER B 614 ASP B 618 -1 N SER B 614 O PHE B 627
SHEET 1 Y 5 MET B 792 LEU B 796 0
SHEET 2 Y 5 SER B 853 ASP B 861 -1 O LEU B 854 N ILE B 795
SHEET 3 Y 5 LYS B 962 LYS B 972 -1 O VAL B 964 N ASP B 861
SHEET 4 Y 5 GLY B 947 THR B 956 -1 N LEU B 953 O LYS B 965
SHEET 5 Y 5 ARG B 904 VAL B 905 -1 N VAL B 905 O GLY B 947
SHEET 1 Z 5 MET B 792 LEU B 796 0
SHEET 2 Z 5 SER B 853 ASP B 861 -1 O LEU B 854 N ILE B 795
SHEET 3 Z 5 LYS B 962 LYS B 972 -1 O VAL B 964 N ASP B 861
SHEET 4 Z 5 GLY B 947 THR B 956 -1 N LEU B 953 O LYS B 965
SHEET 5 Z 5 ILE L 55 LEU L 57 -1 O LEU L 56 N VAL B 954
SHEET 1 AA 2 GLY B 804 THR B 805 0
SHEET 2 AA 2 GLY B1042 ASP B1043 1 O GLY B1042 N THR B 805
SHEET 1 AB 8 PHE B1069 GLU B1070 0
SHEET 2 AB 8 ILE B1085 LEU B1095 -1 O ILE B1085 N GLU B1070
SHEET 3 AB 8 LYS B 979 ALA B 981 -1 N ALA B 981 O GLN B1093
SHEET 4 AB 8 LYS B 987 TYR B 994 -1 O GLY B 988 N PHE B 980
SHEET 5 AB 8 SER B 838 ASN B 842 1 N MET B 839 O GLY B 991
SHEET 6 AB 8 LEU B1010 ILE B1012 -1 O ILE B1011 N ILE B 840
SHEET 7 AB 8 GLN B 821 ILE B 827 1 N ALA B 826 O LEU B1010
SHEET 8 AB 8 ILE B1085 LEU B1095 -1 O GLY B1088 N VAL B 825
SHEET 1 AC 2 VAL B 910 ILE B 912 0
SHEET 2 AC 2 THR B 939 PRO B 940 -1 O THR B 939 N ILE B 912
SHEET 1 AD 2 PHE B1001 THR B1002 0
SHEET 2 AD 2 MET B1072 TYR B1073 -1 O TYR B1073 N PHE B1001
SHEET 1 AE 2 ALA B1157 CYS B1163 0
SHEET 2 AE 2 ILE B1191 PRO B1197 -1 O ILE B1194 N VAL B1160
SHEET 1 AF 2 ILE B1172 LYS B1174 0
SHEET 2 AF 2 GLN B1179 GLU B1181 -1 O GLN B1179 N LYS B1174
SHEET 1 AG 4 GLU C 12 ALA C 13 0
SHEET 2 AG 4 ASN C 17 ASP C 19 -1 O ASP C 19 N GLU C 12
SHEET 3 AG 4 ASN C 231 SER C 234 -1 O VAL C 232 N VAL C 18
SHEET 4 AG 4 ALA C 173 GLU C 177 -1 N GLU C 177 O ASN C 231
SHEET 1 AH 2 LEU C 22 SER C 23 0
SHEET 2 AH 2 THR C 227 PHE C 228 -1 O PHE C 228 N LEU C 22
SHEET 1 AI 5 VAL C 119 ILE C 120 0
SHEET 2 AI 5 VAL C 98 PHE C 104 -1 N THR C 100 O VAL C 119
SHEET 3 AI 5 GLU C 152 GLY C 162 -1 O LEU C 155 N LEU C 101
SHEET 4 AI 5 THR C 43 ASN C 54 -1 N THR C 53 O LYS C 154
SHEET 5 AI 5 GLN L 66 PHE L 67 -1 O PHE L 67 N VAL C 49
SHEET 1 AJ 2 THR C 111 TYR C 114 0
SHEET 2 AJ 2 LEU C 143 LEU C 147 -1 O LEU C 147 N THR C 111
SHEET 1 AK 4 PHE E 60 ALA E 62 0
SHEET 2 AK 4 LEU E 78 PHE E 82 -1 O VAL E 80 N PHE E 60
SHEET 3 AK 4 THR E 107 TYR E 112 1 O VAL E 111 N GLU E 81
SHEET 4 AK 4 THR E 131 ASN E 136 1 O GLU E 133 N GLY E 108
SHEET 1 AL 2 SER E 87 VAL E 88 0
SHEET 2 AL 2 ASN E 115 ILE E 116 1 O ASN E 115 N VAL E 88
SHEET 1 AM 4 LYS E 152 ARG E 155 0
SHEET 2 AM 4 VAL E 195 SER E 202 -1 O ILE E 199 N LYS E 152
SHEET 3 AM 4 GLY E 206 CYS E 214 -1 O TYR E 208 N ARG E 200
SHEET 4 AM 4 ARG E 177 ILE E 178 1 N ILE E 178 O ILE E 213
SHEET 1 AN 8 TYR H 95 GLY H 99 0
SHEET 2 AN 8 ALA H 140 ARG H 145 -1 O LEU H 142 N MET H 97
SHEET 3 AN 8 SER H 54 ALA H 60 -1 N THR H 58 O LEU H 143
SHEET 4 AN 8 ILE H 9 ASP H 16 -1 N PHE H 10 O LEU H 55
SHEET 5 AN 8 VAL H 23 SER H 30 -1 O GLU H 27 N SER H 13
SHEET 6 AN 8 LYS H 37 ASN H 43 -1 O LEU H 40 N ILE H 26
SHEET 7 AN 8 LEU H 121 GLU H 126 -1 O GLU H 126 N LYS H 37
SHEET 8 AN 8 ALA H 113 VAL H 114 -1 N VAL H 114 O LEU H 125
SHEET 1 AO 8 TYR H 95 GLY H 99 0
SHEET 2 AO 8 ALA H 140 ARG H 145 -1 O LEU H 142 N MET H 97
SHEET 3 AO 8 SER H 54 ALA H 60 -1 N THR H 58 O LEU H 143
SHEET 4 AO 8 ILE H 9 ASP H 16 -1 N PHE H 10 O LEU H 55
SHEET 5 AO 8 VAL H 23 SER H 30 -1 O GLU H 27 N SER H 13
SHEET 6 AO 8 LYS H 37 ASN H 43 -1 O LEU H 40 N ILE H 26
SHEET 7 AO 8 LEU H 121 GLU H 126 -1 O GLU H 126 N LYS H 37
SHEET 8 AO 8 SER H 117 PHE H 118 -1 N PHE H 118 O LEU H 121
SHEET 1 AP 3 TYR I 15 ASP I 19 0
SHEET 2 AP 3 ARG I 24 GLU I 28 -1 O ARG I 24 N ASP I 19
SHEET 3 AP 3 VAL I 35 GLU I 37 -1 O GLU I 36 N PHE I 27
SHEET 1 AQ 4 ARG I 70 SER I 71 0
SHEET 2 AQ 4 ASN I 83 GLN I 87 -1 O ASN I 83 N SER I 71
SHEET 3 AQ 4 LEU I 99 CYS I 103 -1 O VAL I 102 N VAL I 84
SHEET 4 AQ 4 ILE I 109 THR I 111 -1 O PHE I 110 N PHE I 101
SHEET 1 AR 4 ILE K 21 PRO K 23 0
SHEET 2 AR 4 ALA K 30 GLU K 36 -1 O VAL K 32 N ASP K 22
SHEET 3 AR 4 ARG K 70 THR K 77 -1 O LEU K 73 N ILE K 33
SHEET 4 AR 4 VAL K 56 LYS K 62 -1 N PHE K 58 O GLN K 76
SSBOND 1 CYS A 70 CYS A 77 1555 1555 2.90
SSBOND 2 CYS A 107 CYS A 110 1555 1555 1.93
SSBOND 3 CYS A 110 CYS A 148 1555 1555 2.48
SSBOND 4 CYS A 148 CYS A 167 1555 1555 2.95
SSBOND 5 CYS B 1163 CYS B 1185 1555 1555 2.18
SSBOND 6 CYS B 1166 CYS B 1185 1555 1555 2.44
SSBOND 7 CYS B 1182 CYS B 1185 1555 1555 2.89
SSBOND 8 CYS C 86 CYS C 95 1555 1555 2.51
SSBOND 9 CYS C 88 CYS C 95 1555 1555 2.60
SSBOND 10 CYS I 7 CYS I 32 1555 1555 2.11
SSBOND 11 CYS I 10 CYS I 32 1555 1555 2.03
SSBOND 12 CYS I 29 CYS I 32 1555 1555 2.58
SSBOND 13 CYS I 75 CYS I 78 1555 1555 2.18
SSBOND 14 CYS I 78 CYS I 106 1555 1555 1.74
SSBOND 15 CYS I 103 CYS I 106 1555 1555 2.68
SSBOND 16 CYS J 7 CYS J 45 1555 1555 2.59
SSBOND 17 CYS J 10 CYS J 46 1555 1555 2.73
SSBOND 18 CYS L 31 CYS L 48 1555 1555 2.32
SSBOND 19 CYS L 48 CYS L 51 1555 1555 2.69
LINK SG CYS A 67 ZN ZN A3008 1555 1555 2.95
LINK SG CYS A 70 ZN ZN A3008 1555 1555 1.18
LINK SG CYS A 77 ZN ZN A3008 1555 1555 1.83
LINK NE2 HIS A 80 ZN ZN A3008 1555 1555 1.69
LINK SG CYS A 107 ZN ZN A3006 1555 1555 1.95
LINK SG CYS A 110 ZN ZN A3006 1555 1555 1.16
LINK SG CYS A 148 ZN ZN A3006 1555 1555 1.41
LINK SG CYS A 167 ZN ZN A3006 1555 1555 2.17
LINK OD1 ASP A 481 MN MN A3009 1555 1555 1.79
LINK OD2 ASP A 481 MN MN A3010 1555 1555 1.90
LINK OD2 ASP A 483 MN MN A3009 1555 1555 1.98
LINK OD1 ASP A 483 MN MN A3010 1555 1555 1.90
LINK OD2 ASP A 485 MN MN A3009 1555 1555 2.06
LINK MN MN A3009 O2G ATP A3011 1555 1555 1.88
LINK MN MN A3009 O1B ATP A3011 1555 1555 2.47
LINK MN MN A3010 O1B ATP A3011 1555 1555 1.84
LINK MN MN A3010 O1A ATP A3011 1555 1555 2.62
LINK MN MN A3010 OD2 ASP B 837 1555 1555 2.42
LINK SG CYS B1163 ZN ZN B3007 1555 1555 1.98
LINK SG CYS B1166 ZN ZN B3007 1555 1555 1.83
LINK SG CYS B1182 ZN ZN B3007 1555 1555 2.06
LINK SG CYS B1185 ZN ZN B3007 1555 1555 1.00
LINK SG CYS C 86 ZN ZN C3002 1555 1555 1.31
LINK SG CYS C 88 ZN ZN C3002 1555 1555 1.86
LINK SG CYS C 92 ZN ZN C3002 1555 1555 2.19
LINK SG CYS C 95 ZN ZN C3002 1555 1555 1.62
LINK SG CYS I 7 ZN ZN I3003 1555 1555 1.56
LINK SG CYS I 10 ZN ZN I3003 1555 1555 1.64
LINK SG CYS I 29 ZN ZN I3003 1555 1555 2.02
LINK SG CYS I 32 ZN ZN I3003 1555 1555 0.95
LINK SG CYS I 75 ZN ZN I3004 1555 1555 1.51
LINK SG CYS I 78 ZN ZN I3004 1555 1555 1.09
LINK SG CYS I 103 ZN ZN I3004 1555 1555 2.40
LINK SG CYS I 106 ZN ZN I3004 1555 1555 1.45
LINK SG CYS J 7 ZN ZN J3001 1555 1555 1.60
LINK SG CYS J 10 ZN ZN J3001 1555 1555 1.59
LINK SG CYS J 45 ZN ZN J3001 1555 1555 1.59
LINK SG CYS J 46 ZN ZN J3001 1555 1555 2.05
LINK SG CYS L 31 ZN ZN L3005 1555 1555 1.81
LINK SG CYS L 34 ZN ZN L3005 1555 1555 1.76
LINK SG CYS L 48 ZN ZN L3005 1555 1555 1.99
LINK SG CYS L 51 ZN ZN L3005 1555 1555 2.07
CISPEP 1 GLN A 447 PRO A 448 0 1.84
SITE 1 AC1 5 ASP A 481 ASP A 483 ASP A 485 MN A3010
SITE 2 AC1 5 ATP A3011
SITE 1 AC2 5 ASP A 481 ASP A 483 MN A3009 ATP A3011
SITE 2 AC2 5 ASP B 837
SITE 1 AC3 4 CYS J 7 CYS J 10 CYS J 45 CYS J 46
SITE 1 AC4 4 CYS C 86 CYS C 88 CYS C 92 CYS C 95
SITE 1 AC5 4 CYS I 7 CYS I 10 CYS I 29 CYS I 32
SITE 1 AC6 4 CYS I 75 CYS I 78 CYS I 103 CYS I 106
SITE 1 AC7 5 CYS L 31 CYS L 34 SER L 36 CYS L 48
SITE 2 AC7 5 CYS L 51
SITE 1 AC8 5 CYS A 107 CYS A 110 CYS A 148 GLY A 166
SITE 2 AC8 5 CYS A 167
SITE 1 AC9 4 CYS B1163 CYS B1166 CYS B1182 CYS B1185
SITE 1 BC1 4 CYS A 67 CYS A 70 CYS A 77 HIS A 80
SITE 1 BC2 9 ASP A 481 ASP A 483 ASP A 485 MN A3009
SITE 2 BC2 9 MN A3010 ARG B 766 GLN B 986 LYS B 987
SITE 3 BC2 9 ARG B1020
CRYST1 123.000 223.000 374.000 90.00 90.00 90.00 I 2 2 2 8
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 0.008130 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004484 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002674 0.00000
(ATOM LINES ARE NOT SHOWN.)
END