HEADER LIGASE 12-FEB-03 1OD2
TITLE ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL-COENZYME A CARBOXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CARBOXYLTRANSFERASE DOMAIN, RESIDUES 1429-2233;
COMPND 5 SYNONYM: ACC;
COMPND 6 EC: 6.4.1.2;
COMPND 7 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIGASE, ACC, ACETYL-COA, ACETYL-COA CARBOXYLASE, OBESITY
EXPDTA X-RAY DIFFRACTION
AUTHOR H.ZHANG,Z.YANG,Y.SHEN,L.TONG
REVDAT 4 13-JUN-18 1OD2 1 JRNL REMARK
REVDAT 3 05-JUL-17 1OD2 1 REMARK
REVDAT 2 24-FEB-09 1OD2 1 VERSN
REVDAT 1 03-APR-03 1OD2 0
JRNL AUTH H.ZHANG,Z.YANG,Y.SHEN,L.TONG
JRNL TITL CRYSTAL STRUCTURE OF THE CARBOXYLTRANSFERASE DOMAIN OF
JRNL TITL 2 ACETYL-COENZYME A CARBOXYLASE.
JRNL REF SCIENCE V. 299 2064 2003
JRNL REFN ESSN 1095-9203
JRNL PMID 12663926
JRNL DOI 10.1126/SCIENCE.1081366
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.2
REMARK 3 NUMBER OF REFLECTIONS : 59546
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6032
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8456
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 958
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11286
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 89
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.55000
REMARK 3 B22 (A**2) : -7.30000
REMARK 3 B33 (A**2) : 9.84000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.49000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.36
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.43
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.44
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.890
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 : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 27.50
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ACO.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OD2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1290012163.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
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 : 168936
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.11600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SNB, SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 69.06500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ILE A 1429
REMARK 465 LYS A 1430
REMARK 465 ASP A 1431
REMARK 465 PRO A 1432
REMARK 465 GLN A 1433
REMARK 465 THR A 1434
REMARK 465 GLY A 1435
REMARK 465 ALA A 1436
REMARK 465 PRO A 1437
REMARK 465 VAL A 1438
REMARK 465 PRO A 1439
REMARK 465 LEU A 1440
REMARK 465 ARG A 1441
REMARK 465 ALA A 1442
REMARK 465 LEU A 1443
REMARK 465 ILE A 1444
REMARK 465 ASN A 1445
REMARK 465 ASN A 1446
REMARK 465 VAL A 1447
REMARK 465 SER A 1448
REMARK 465 GLY A 1449
REMARK 465 TYR A 1450
REMARK 465 VAL A 1451
REMARK 465 ILE A 1452
REMARK 465 LYS A 1453
REMARK 465 THR A 1454
REMARK 465 GLU A 1455
REMARK 465 MSE A 1456
REMARK 465 TYR A 1457
REMARK 465 THR A 1458
REMARK 465 GLU A 1459
REMARK 465 VAL A 1460
REMARK 465 LYS A 1461
REMARK 465 ASN A 1462
REMARK 465 ALA A 1463
REMARK 465 LYS A 1464
REMARK 465 GLY A 1465
REMARK 465 GLU A 1466
REMARK 465 TRP A 1467
REMARK 465 VAL A 1468
REMARK 465 PHE A 1469
REMARK 465 LYS A 1470
REMARK 465 SER A 1471
REMARK 465 LEU A 1472
REMARK 465 GLY A 1473
REMARK 465 LYS A 1474
REMARK 465 PRO A 1475
REMARK 465 GLY A 1476
REMARK 465 SER A 1477
REMARK 465 MSE A 1478
REMARK 465 HIS A 1479
REMARK 465 LEU A 1480
REMARK 465 ARG A 1481
REMARK 465 PRO A 1482
REMARK 465 ILE A 1483
REMARK 465 SER A 2204
REMARK 465 ASP A 2205
REMARK 465 HIS A 2206
REMARK 465 ASP A 2207
REMARK 465 ASN A 2208
REMARK 465 ALA A 2209
REMARK 465 ILE A 2210
REMARK 465 ASP A 2211
REMARK 465 GLY A 2212
REMARK 465 LEU A 2213
REMARK 465 SER A 2214
REMARK 465 GLU A 2215
REMARK 465 VAL A 2216
REMARK 465 ILE A 2217
REMARK 465 LYS A 2218
REMARK 465 MSE A 2219
REMARK 465 LEU A 2220
REMARK 465 SER A 2221
REMARK 465 THR A 2222
REMARK 465 ASP A 2223
REMARK 465 ASP A 2224
REMARK 465 LYS A 2225
REMARK 465 GLU A 2226
REMARK 465 LYS A 2227
REMARK 465 LEU A 2228
REMARK 465 LEU A 2229
REMARK 465 LYS A 2230
REMARK 465 THR A 2231
REMARK 465 LEU A 2232
REMARK 465 LYS A 2233
REMARK 465 ILE B 1429
REMARK 465 LYS B 1430
REMARK 465 ASP B 1431
REMARK 465 PRO B 1432
REMARK 465 GLN B 1433
REMARK 465 THR B 1434
REMARK 465 GLY B 1435
REMARK 465 ALA B 1436
REMARK 465 PRO B 1437
REMARK 465 VAL B 1438
REMARK 465 PRO B 1439
REMARK 465 LEU B 1440
REMARK 465 ARG B 1441
REMARK 465 ALA B 1442
REMARK 465 LEU B 1443
REMARK 465 ILE B 1444
REMARK 465 ASN B 1445
REMARK 465 ASN B 1446
REMARK 465 VAL B 1447
REMARK 465 SER B 1448
REMARK 465 GLY B 1449
REMARK 465 TYR B 1450
REMARK 465 VAL B 1451
REMARK 465 ILE B 1452
REMARK 465 LYS B 1453
REMARK 465 THR B 1454
REMARK 465 GLU B 1455
REMARK 465 MSE B 1456
REMARK 465 TYR B 1457
REMARK 465 THR B 1458
REMARK 465 GLU B 1459
REMARK 465 VAL B 1460
REMARK 465 LYS B 1461
REMARK 465 ASN B 1462
REMARK 465 ALA B 1463
REMARK 465 LYS B 1464
REMARK 465 GLY B 1465
REMARK 465 GLU B 1466
REMARK 465 TRP B 1467
REMARK 465 VAL B 1468
REMARK 465 PHE B 1469
REMARK 465 LYS B 1470
REMARK 465 SER B 1471
REMARK 465 LEU B 1472
REMARK 465 GLY B 1473
REMARK 465 LYS B 1474
REMARK 465 PRO B 1475
REMARK 465 GLY B 1476
REMARK 465 SER B 1477
REMARK 465 MSE B 1478
REMARK 465 HIS B 1479
REMARK 465 LEU B 1480
REMARK 465 ARG B 1481
REMARK 465 PRO B 1482
REMARK 465 ILE B 1483
REMARK 465 ALA B 1484
REMARK 465 THR B 1485
REMARK 465 PRO B 1486
REMARK 465 TYR B 1487
REMARK 465 PRO B 1488
REMARK 465 VAL B 1489
REMARK 465 LYS B 1490
REMARK 465 GLU B 1491
REMARK 465 TRP B 1492
REMARK 465 LEU B 1493
REMARK 465 GLN B 1494
REMARK 465 LEU B 2191
REMARK 465 GLU B 2192
REMARK 465 SER B 2193
REMARK 465 PHE B 2194
REMARK 465 ALA B 2195
REMARK 465 GLN B 2196
REMARK 465 ASP B 2197
REMARK 465 LEU B 2198
REMARK 465 ALA B 2199
REMARK 465 LYS B 2200
REMARK 465 LYS B 2201
REMARK 465 ILE B 2202
REMARK 465 ARG B 2203
REMARK 465 SER B 2204
REMARK 465 ASP B 2205
REMARK 465 HIS B 2206
REMARK 465 ASP B 2207
REMARK 465 ASN B 2208
REMARK 465 ALA B 2209
REMARK 465 ILE B 2210
REMARK 465 ASP B 2211
REMARK 465 GLY B 2212
REMARK 465 LEU B 2213
REMARK 465 SER B 2214
REMARK 465 GLU B 2215
REMARK 465 VAL B 2216
REMARK 465 ILE B 2217
REMARK 465 LYS B 2218
REMARK 465 MSE B 2219
REMARK 465 LEU B 2220
REMARK 465 SER B 2221
REMARK 465 THR B 2222
REMARK 465 ASP B 2223
REMARK 465 ASP B 2224
REMARK 465 LYS B 2225
REMARK 465 GLU B 2226
REMARK 465 LYS B 2227
REMARK 465 LEU B 2228
REMARK 465 LEU B 2229
REMARK 465 LYS B 2230
REMARK 465 THR B 2231
REMARK 465 LEU B 2232
REMARK 465 LYS B 2233
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A2203 CA C O CB CG CD NE
REMARK 470 ARG A2203 CZ NH1 NH2
REMARK 470 LYS B2190 CA C O CB CG CD CE
REMARK 470 LYS B2190 NZ
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 B 1991 N GLY B 1993 2.09
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 THR A1485 112.03 54.37
REMARK 500 SER A1527 81.55 -174.41
REMARK 500 THR A1533 -153.97 -81.14
REMARK 500 ASP A1545 -147.82 -92.56
REMARK 500 LEU A1638 32.38 -142.03
REMARK 500 ALA A1642 81.53 -69.82
REMARK 500 ASN A1648 70.19 -167.37
REMARK 500 TYR A1655 158.81 170.30
REMARK 500 LYS A1668 16.15 -64.86
REMARK 500 PHE A1669 -2.41 -157.18
REMARK 500 ASP A1670 73.81 63.88
REMARK 500 LYS A1671 49.10 -149.30
REMARK 500 SER A1674 -16.64 -49.99
REMARK 500 THR A1677 -168.95 -105.00
REMARK 500 GLU A1678 106.78 -161.79
REMARK 500 ARG A1679 161.65 -40.50
REMARK 500 THR A1680 155.25 172.64
REMARK 500 ILE A1682 -146.39 -140.40
REMARK 500 ASN A1683 21.15 -55.25
REMARK 500 THR A1692 119.77 -164.89
REMARK 500 ILE A1725 135.86 -171.79
REMARK 500 CYS A1730 -43.20 -139.63
REMARK 500 ARG A1731 160.80 168.08
REMARK 500 GLN A1744 -83.91 63.01
REMARK 500 LEU A1756 -112.90 -104.66
REMARK 500 ILE A1782 -71.49 -104.25
REMARK 500 PRO A1819 98.47 -64.45
REMARK 500 THR A1826 157.36 -42.84
REMARK 500 ASP A1832 -79.43 -74.97
REMARK 500 ASN A1837 48.94 -68.26
REMARK 500 ASP A1838 -83.55 -144.90
REMARK 500 GLU A1853 5.48 -66.56
REMARK 500 ALA A1874 63.37 39.12
REMARK 500 PRO A1910 -32.22 -39.49
REMARK 500 ASN A1952 68.04 -156.43
REMARK 500 PRO A1991 -95.24 -24.29
REMARK 500 THR A1992 6.78 -63.37
REMARK 500 ALA A2022 135.91 -171.12
REMARK 500 PHE A2035 59.08 -152.80
REMARK 500 ARG A2037 -72.22 -52.90
REMARK 500 GLU A2038 -39.44 -35.48
REMARK 500 ARG A2080 30.54 -77.91
REMARK 500 GLU A2081 -28.80 -150.68
REMARK 500 ASP A2098 39.95 -76.10
REMARK 500 LEU A2139 23.08 -71.32
REMARK 500 SER A2140 16.74 -141.98
REMARK 500 GLN A2142 -135.00 -76.06
REMARK 500 VAL A2143 -99.64 -96.98
REMARK 500 GLU A2145 130.16 -34.40
REMARK 500 ALA A2161 -30.13 -38.14
REMARK 500
REMARK 500 THIS ENTRY HAS 107 RAMACHANDRAN OUTLIERS.
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 ACO A 3203
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACO A3203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADE B3190
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OD4 RELATED DB: PDB
REMARK 900 ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN
DBREF 1OD2 A 1429 2233 UNP Q00955 COAC_YEAST 1429 2233
DBREF 1OD2 B 1429 2233 UNP Q00955 COAC_YEAST 1429 2233
SEQRES 1 A 805 ILE LYS ASP PRO GLN THR GLY ALA PRO VAL PRO LEU ARG
SEQRES 2 A 805 ALA LEU ILE ASN ASN VAL SER GLY TYR VAL ILE LYS THR
SEQRES 3 A 805 GLU MSE TYR THR GLU VAL LYS ASN ALA LYS GLY GLU TRP
SEQRES 4 A 805 VAL PHE LYS SER LEU GLY LYS PRO GLY SER MSE HIS LEU
SEQRES 5 A 805 ARG PRO ILE ALA THR PRO TYR PRO VAL LYS GLU TRP LEU
SEQRES 6 A 805 GLN PRO LYS ARG TYR LYS ALA HIS LEU MSE GLY THR THR
SEQRES 7 A 805 TYR VAL TYR ASP PHE PRO GLU LEU PHE ARG GLN ALA SER
SEQRES 8 A 805 SER SER GLN TRP LYS ASN PHE SER ALA ASP VAL LYS LEU
SEQRES 9 A 805 THR ASP ASP PHE PHE ILE SER ASN GLU LEU ILE GLU ASP
SEQRES 10 A 805 GLU ASN GLY GLU LEU THR GLU VAL GLU ARG GLU PRO GLY
SEQRES 11 A 805 ALA ASN ALA ILE GLY MSE VAL ALA PHE LYS ILE THR VAL
SEQRES 12 A 805 LYS THR PRO GLU TYR PRO ARG GLY ARG GLN PHE VAL VAL
SEQRES 13 A 805 VAL ALA ASN ASP ILE THR PHE LYS ILE GLY SER PHE GLY
SEQRES 14 A 805 PRO GLN GLU ASP GLU PHE PHE ASN LYS VAL THR GLU TYR
SEQRES 15 A 805 ALA ARG LYS ARG GLY ILE PRO ARG ILE TYR LEU ALA ALA
SEQRES 16 A 805 ASN SER GLY ALA ARG ILE GLY MSE ALA GLU GLU ILE VAL
SEQRES 17 A 805 PRO LEU PHE GLN VAL ALA TRP ASN ASP ALA ALA ASN PRO
SEQRES 18 A 805 ASP LYS GLY PHE GLN TYR LEU TYR LEU THR SER GLU GLY
SEQRES 19 A 805 MSE GLU THR LEU LYS LYS PHE ASP LYS GLU ASN SER VAL
SEQRES 20 A 805 LEU THR GLU ARG THR VAL ILE ASN GLY GLU GLU ARG PHE
SEQRES 21 A 805 VAL ILE LYS THR ILE ILE GLY SER GLU ASP GLY LEU GLY
SEQRES 22 A 805 VAL GLU CYS LEU ARG GLY SER GLY LEU ILE ALA GLY ALA
SEQRES 23 A 805 THR SER ARG ALA TYR HIS ASP ILE PHE THR ILE THR LEU
SEQRES 24 A 805 VAL THR CYS ARG SER VAL GLY ILE GLY ALA TYR LEU VAL
SEQRES 25 A 805 ARG LEU GLY GLN ARG ALA ILE GLN VAL GLU GLY GLN PRO
SEQRES 26 A 805 ILE ILE LEU THR GLY ALA PRO ALA ILE ASN LYS MSE LEU
SEQRES 27 A 805 GLY ARG GLU VAL TYR THR SER ASN LEU GLN LEU GLY GLY
SEQRES 28 A 805 THR GLN ILE MSE TYR ASN ASN GLY VAL SER HIS LEU THR
SEQRES 29 A 805 ALA VAL ASP ASP LEU ALA GLY VAL GLU LYS ILE VAL GLU
SEQRES 30 A 805 TRP MSE SER TYR VAL PRO ALA LYS ARG ASN MSE PRO VAL
SEQRES 31 A 805 PRO ILE LEU GLU THR LYS ASP THR TRP ASP ARG PRO VAL
SEQRES 32 A 805 ASP PHE THR PRO THR ASN ASP GLU THR TYR ASP VAL ARG
SEQRES 33 A 805 TRP MSE ILE GLU GLY ARG GLU THR GLU SER GLY PHE GLU
SEQRES 34 A 805 TYR GLY LEU PHE ASP LYS GLY SER PHE PHE GLU THR LEU
SEQRES 35 A 805 SER GLY TRP ALA LYS GLY VAL VAL VAL GLY ARG ALA ARG
SEQRES 36 A 805 LEU GLY GLY ILE PRO LEU GLY VAL ILE GLY VAL GLU THR
SEQRES 37 A 805 ARG THR VAL GLU ASN LEU ILE PRO ALA ASP PRO ALA ASN
SEQRES 38 A 805 PRO ASN SER ALA GLU THR LEU ILE GLN GLU PRO GLY GLN
SEQRES 39 A 805 VAL TRP HIS PRO ASN SER ALA PHE LYS THR ALA GLN ALA
SEQRES 40 A 805 ILE ASN ASP PHE ASN ASN GLY GLU GLN LEU PRO MSE MSE
SEQRES 41 A 805 ILE LEU ALA ASN TRP ARG GLY PHE SER GLY GLY GLN ARG
SEQRES 42 A 805 ASP MSE PHE ASN GLU VAL LEU LYS TYR GLY SER PHE ILE
SEQRES 43 A 805 VAL ASP ALA LEU VAL ASP TYR LYS GLN PRO ILE ILE ILE
SEQRES 44 A 805 TYR ILE PRO PRO THR GLY GLU LEU ARG GLY GLY SER TRP
SEQRES 45 A 805 VAL VAL VAL ASP PRO THR ILE ASN ALA ASP GLN MSE GLU
SEQRES 46 A 805 MSE TYR ALA ASP VAL ASN ALA ARG ALA GLY VAL LEU GLU
SEQRES 47 A 805 PRO GLN GLY MSE VAL GLY ILE LYS PHE ARG ARG GLU LYS
SEQRES 48 A 805 LEU LEU ASP THR MSE ASN ARG LEU ASP ASP LYS TYR ARG
SEQRES 49 A 805 GLU LEU ARG SER GLN LEU SER ASN LYS SER LEU ALA PRO
SEQRES 50 A 805 GLU VAL HIS GLN GLN ILE SER LYS GLN LEU ALA ASP ARG
SEQRES 51 A 805 GLU ARG GLU LEU LEU PRO ILE TYR GLY GLN ILE SER LEU
SEQRES 52 A 805 GLN PHE ALA ASP LEU HIS ASP ARG SER SER ARG MSE VAL
SEQRES 53 A 805 ALA LYS GLY VAL ILE SER LYS GLU LEU GLU TRP THR GLU
SEQRES 54 A 805 ALA ARG ARG PHE PHE PHE TRP ARG LEU ARG ARG ARG LEU
SEQRES 55 A 805 ASN GLU GLU TYR LEU ILE LYS ARG LEU SER HIS GLN VAL
SEQRES 56 A 805 GLY GLU ALA SER ARG LEU GLU LYS ILE ALA ARG ILE ARG
SEQRES 57 A 805 SER TRP TYR PRO ALA SER VAL ASP HIS GLU ASP ASP ARG
SEQRES 58 A 805 GLN VAL ALA THR TRP ILE GLU GLU ASN TYR LYS THR LEU
SEQRES 59 A 805 ASP ASP LYS LEU LYS GLY LEU LYS LEU GLU SER PHE ALA
SEQRES 60 A 805 GLN ASP LEU ALA LYS LYS ILE ARG SER ASP HIS ASP ASN
SEQRES 61 A 805 ALA ILE ASP GLY LEU SER GLU VAL ILE LYS MSE LEU SER
SEQRES 62 A 805 THR ASP ASP LYS GLU LYS LEU LEU LYS THR LEU LYS
SEQRES 1 B 805 ILE LYS ASP PRO GLN THR GLY ALA PRO VAL PRO LEU ARG
SEQRES 2 B 805 ALA LEU ILE ASN ASN VAL SER GLY TYR VAL ILE LYS THR
SEQRES 3 B 805 GLU MSE TYR THR GLU VAL LYS ASN ALA LYS GLY GLU TRP
SEQRES 4 B 805 VAL PHE LYS SER LEU GLY LYS PRO GLY SER MSE HIS LEU
SEQRES 5 B 805 ARG PRO ILE ALA THR PRO TYR PRO VAL LYS GLU TRP LEU
SEQRES 6 B 805 GLN PRO LYS ARG TYR LYS ALA HIS LEU MSE GLY THR THR
SEQRES 7 B 805 TYR VAL TYR ASP PHE PRO GLU LEU PHE ARG GLN ALA SER
SEQRES 8 B 805 SER SER GLN TRP LYS ASN PHE SER ALA ASP VAL LYS LEU
SEQRES 9 B 805 THR ASP ASP PHE PHE ILE SER ASN GLU LEU ILE GLU ASP
SEQRES 10 B 805 GLU ASN GLY GLU LEU THR GLU VAL GLU ARG GLU PRO GLY
SEQRES 11 B 805 ALA ASN ALA ILE GLY MSE VAL ALA PHE LYS ILE THR VAL
SEQRES 12 B 805 LYS THR PRO GLU TYR PRO ARG GLY ARG GLN PHE VAL VAL
SEQRES 13 B 805 VAL ALA ASN ASP ILE THR PHE LYS ILE GLY SER PHE GLY
SEQRES 14 B 805 PRO GLN GLU ASP GLU PHE PHE ASN LYS VAL THR GLU TYR
SEQRES 15 B 805 ALA ARG LYS ARG GLY ILE PRO ARG ILE TYR LEU ALA ALA
SEQRES 16 B 805 ASN SER GLY ALA ARG ILE GLY MSE ALA GLU GLU ILE VAL
SEQRES 17 B 805 PRO LEU PHE GLN VAL ALA TRP ASN ASP ALA ALA ASN PRO
SEQRES 18 B 805 ASP LYS GLY PHE GLN TYR LEU TYR LEU THR SER GLU GLY
SEQRES 19 B 805 MSE GLU THR LEU LYS LYS PHE ASP LYS GLU ASN SER VAL
SEQRES 20 B 805 LEU THR GLU ARG THR VAL ILE ASN GLY GLU GLU ARG PHE
SEQRES 21 B 805 VAL ILE LYS THR ILE ILE GLY SER GLU ASP GLY LEU GLY
SEQRES 22 B 805 VAL GLU CYS LEU ARG GLY SER GLY LEU ILE ALA GLY ALA
SEQRES 23 B 805 THR SER ARG ALA TYR HIS ASP ILE PHE THR ILE THR LEU
SEQRES 24 B 805 VAL THR CYS ARG SER VAL GLY ILE GLY ALA TYR LEU VAL
SEQRES 25 B 805 ARG LEU GLY GLN ARG ALA ILE GLN VAL GLU GLY GLN PRO
SEQRES 26 B 805 ILE ILE LEU THR GLY ALA PRO ALA ILE ASN LYS MSE LEU
SEQRES 27 B 805 GLY ARG GLU VAL TYR THR SER ASN LEU GLN LEU GLY GLY
SEQRES 28 B 805 THR GLN ILE MSE TYR ASN ASN GLY VAL SER HIS LEU THR
SEQRES 29 B 805 ALA VAL ASP ASP LEU ALA GLY VAL GLU LYS ILE VAL GLU
SEQRES 30 B 805 TRP MSE SER TYR VAL PRO ALA LYS ARG ASN MSE PRO VAL
SEQRES 31 B 805 PRO ILE LEU GLU THR LYS ASP THR TRP ASP ARG PRO VAL
SEQRES 32 B 805 ASP PHE THR PRO THR ASN ASP GLU THR TYR ASP VAL ARG
SEQRES 33 B 805 TRP MSE ILE GLU GLY ARG GLU THR GLU SER GLY PHE GLU
SEQRES 34 B 805 TYR GLY LEU PHE ASP LYS GLY SER PHE PHE GLU THR LEU
SEQRES 35 B 805 SER GLY TRP ALA LYS GLY VAL VAL VAL GLY ARG ALA ARG
SEQRES 36 B 805 LEU GLY GLY ILE PRO LEU GLY VAL ILE GLY VAL GLU THR
SEQRES 37 B 805 ARG THR VAL GLU ASN LEU ILE PRO ALA ASP PRO ALA ASN
SEQRES 38 B 805 PRO ASN SER ALA GLU THR LEU ILE GLN GLU PRO GLY GLN
SEQRES 39 B 805 VAL TRP HIS PRO ASN SER ALA PHE LYS THR ALA GLN ALA
SEQRES 40 B 805 ILE ASN ASP PHE ASN ASN GLY GLU GLN LEU PRO MSE MSE
SEQRES 41 B 805 ILE LEU ALA ASN TRP ARG GLY PHE SER GLY GLY GLN ARG
SEQRES 42 B 805 ASP MSE PHE ASN GLU VAL LEU LYS TYR GLY SER PHE ILE
SEQRES 43 B 805 VAL ASP ALA LEU VAL ASP TYR LYS GLN PRO ILE ILE ILE
SEQRES 44 B 805 TYR ILE PRO PRO THR GLY GLU LEU ARG GLY GLY SER TRP
SEQRES 45 B 805 VAL VAL VAL ASP PRO THR ILE ASN ALA ASP GLN MSE GLU
SEQRES 46 B 805 MSE TYR ALA ASP VAL ASN ALA ARG ALA GLY VAL LEU GLU
SEQRES 47 B 805 PRO GLN GLY MSE VAL GLY ILE LYS PHE ARG ARG GLU LYS
SEQRES 48 B 805 LEU LEU ASP THR MSE ASN ARG LEU ASP ASP LYS TYR ARG
SEQRES 49 B 805 GLU LEU ARG SER GLN LEU SER ASN LYS SER LEU ALA PRO
SEQRES 50 B 805 GLU VAL HIS GLN GLN ILE SER LYS GLN LEU ALA ASP ARG
SEQRES 51 B 805 GLU ARG GLU LEU LEU PRO ILE TYR GLY GLN ILE SER LEU
SEQRES 52 B 805 GLN PHE ALA ASP LEU HIS ASP ARG SER SER ARG MSE VAL
SEQRES 53 B 805 ALA LYS GLY VAL ILE SER LYS GLU LEU GLU TRP THR GLU
SEQRES 54 B 805 ALA ARG ARG PHE PHE PHE TRP ARG LEU ARG ARG ARG LEU
SEQRES 55 B 805 ASN GLU GLU TYR LEU ILE LYS ARG LEU SER HIS GLN VAL
SEQRES 56 B 805 GLY GLU ALA SER ARG LEU GLU LYS ILE ALA ARG ILE ARG
SEQRES 57 B 805 SER TRP TYR PRO ALA SER VAL ASP HIS GLU ASP ASP ARG
SEQRES 58 B 805 GLN VAL ALA THR TRP ILE GLU GLU ASN TYR LYS THR LEU
SEQRES 59 B 805 ASP ASP LYS LEU LYS GLY LEU LYS LEU GLU SER PHE ALA
SEQRES 60 B 805 GLN ASP LEU ALA LYS LYS ILE ARG SER ASP HIS ASP ASN
SEQRES 61 B 805 ALA ILE ASP GLY LEU SER GLU VAL ILE LYS MSE LEU SER
SEQRES 62 B 805 THR ASP ASP LYS GLU LYS LEU LEU LYS THR LEU LYS
MODRES 1OD2 MSE A 1503 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 1564 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 1631 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 1663 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 1765 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 1783 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 1807 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 1816 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 1846 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 1947 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 1948 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 1963 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 2012 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 2014 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 2030 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 2044 MET SELENOMETHIONINE
MODRES 1OD2 MSE A 2103 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 1503 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 1564 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 1631 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 1663 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 1765 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 1783 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 1807 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 1816 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 1846 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 1947 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 1948 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 1963 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 2012 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 2014 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 2030 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 2044 MET SELENOMETHIONINE
MODRES 1OD2 MSE B 2103 MET SELENOMETHIONINE
HET MSE A1503 8
HET MSE A1564 8
HET MSE A1631 8
HET MSE A1663 8
HET MSE A1765 8
HET MSE A1783 8
HET MSE A1807 8
HET MSE A1816 8
HET MSE A1846 8
HET MSE A1947 8
HET MSE A1948 8
HET MSE A1963 8
HET MSE A2012 8
HET MSE A2014 8
HET MSE A2030 8
HET MSE A2044 8
HET MSE A2103 8
HET MSE B1503 8
HET MSE B1564 8
HET MSE B1631 8
HET MSE B1663 8
HET MSE B1765 8
HET MSE B1783 8
HET MSE B1807 8
HET MSE B1816 8
HET MSE B1846 8
HET MSE B1947 8
HET MSE B1948 8
HET MSE B1963 8
HET MSE B2012 8
HET MSE B2014 8
HET MSE B2030 8
HET MSE B2044 8
HET MSE B2103 8
HET ACO A3203 48
HET ADE B3190 10
HETNAM MSE SELENOMETHIONINE
HETNAM ACO ACETYL COENZYME *A
HETNAM ADE ADENINE
FORMUL 1 MSE 34(C5 H11 N O2 SE)
FORMUL 3 ACO C23 H38 N7 O17 P3 S
FORMUL 4 ADE C5 H5 N5
FORMUL 5 HOH *89(H2 O)
HELIX 1 1 VAL A 1489 GLN A 1494 1 6
HELIX 2 2 GLN A 1494 MSE A 1503 1 10
HELIX 3 3 TYR A 1507 TYR A 1509 5 3
HELIX 4 4 ASP A 1510 ASN A 1525 1 16
HELIX 5 5 THR A 1590 SER A 1595 5 6
HELIX 6 6 GLY A 1597 GLY A 1615 1 19
HELIX 7 7 ILE A 1635 PHE A 1639 5 5
HELIX 8 8 ASN A 1648 LYS A 1651 5 4
HELIX 9 9 THR A 1659 LEU A 1666 1 8
HELIX 10 10 LYS A 1667 ASP A 1670 5 4
HELIX 11 11 GLY A 1701 TYR A 1719 1 19
HELIX 12 12 GLY A 1734 GLY A 1743 1 10
HELIX 13 13 GLY A 1758 LEU A 1766 1 9
HELIX 14 14 ASN A 1774 GLY A 1779 1 6
HELIX 15 15 GLY A 1779 TYR A 1784 1 6
HELIX 16 16 ASP A 1795 SER A 1808 1 14
HELIX 17 17 ASP A 1842 GLU A 1848 1 7
HELIX 18 18 HIS A 1925 GLY A 1942 1 18
HELIX 19 19 GLY A 1959 ASN A 1965 1 7
HELIX 20 20 GLU A 1966 TYR A 1981 1 16
HELIX 21 21 GLY A 1997 VAL A 2002 1 6
HELIX 22 22 ASP A 2004 ALA A 2009 5 6
HELIX 23 23 GLU A 2026 PHE A 2035 1 10
HELIX 24 24 ARG A 2036 ASP A 2048 1 13
HELIX 25 25 ASP A 2048 ASN A 2060 1 13
HELIX 26 26 ALA A 2064 ASP A 2095 1 32
HELIX 27 27 ARG A 2099 LYS A 2106 1 8
HELIX 28 28 GLU A 2114 THR A 2116 5 3
HELIX 29 29 GLU A 2117 LEU A 2139 1 23
HELIX 30 30 SER A 2147 SER A 2157 1 11
HELIX 31 31 ASP A 2167 ASN A 2178 1 12
HELIX 32 32 ASN A 2178 PHE A 2194 1 17
HELIX 33 33 ALA A 2195 LYS A 2200 1 6
HELIX 34 34 PRO B 1495 GLY B 1504 1 10
HELIX 35 35 TYR B 1507 TYR B 1509 5 3
HELIX 36 36 ASP B 1510 SER B 1527 1 18
HELIX 37 37 THR B 1533 ASP B 1535 5 3
HELIX 38 38 GLY B 1597 GLY B 1615 1 19
HELIX 39 39 ALA B 1632 VAL B 1636 5 5
HELIX 40 40 ASN B 1648 LYS B 1651 5 4
HELIX 41 41 THR B 1659 PHE B 1669 1 11
HELIX 42 42 GLY B 1701 HIS B 1720 1 20
HELIX 43 43 GLY B 1734 GLY B 1743 1 10
HELIX 44 44 GLY B 1758 LEU B 1766 1 9
HELIX 45 45 ASN B 1774 GLY B 1779 1 6
HELIX 46 46 GLY B 1779 TYR B 1784 1 6
HELIX 47 47 ASP B 1795 SER B 1808 1 14
HELIX 48 48 ASP B 1842 GLY B 1849 1 8
HELIX 49 49 HIS B 1925 GLY B 1942 1 18
HELIX 50 50 GLY B 1959 ASN B 1965 1 7
HELIX 51 51 GLU B 1966 TYR B 1981 1 16
HELIX 52 52 GLY B 1997 VAL B 2002 1 6
HELIX 53 53 VAL B 2003 ALA B 2009 5 7
HELIX 54 54 GLU B 2026 PHE B 2035 1 10
HELIX 55 55 ARG B 2036 ASP B 2048 1 13
HELIX 56 56 ASP B 2048 LEU B 2058 1 11
HELIX 57 57 ALA B 2064 LEU B 2096 1 33
HELIX 58 58 ARG B 2099 LYS B 2106 1 8
HELIX 59 59 GLU B 2114 THR B 2116 5 3
HELIX 60 60 GLU B 2117 HIS B 2141 1 25
HELIX 61 61 SER B 2147 SER B 2157 1 11
HELIX 62 62 ASP B 2167 GLU B 2177 1 11
HELIX 63 63 ASN B 2178 GLY B 2188 1 11
SHEET 1 AA 8 LEU A1550 VAL A1553 0
SHEET 2 AA 8 PHE A1537 GLU A1544 -1 O GLU A1541 N VAL A1553
SHEET 3 AA 8 MSE A1564 THR A1573 -1 O ALA A1566 N LEU A1542
SHEET 4 AA 8 TYR A1576 ASN A1587 -1 N TYR A1576 O THR A1573
SHEET 5 AA 8 ARG A1618 ALA A1622 1 O ILE A1619 N VAL A1585
SHEET 6 AA 8 THR A1724 VAL A1728 1 O ILE A1725 N TYR A1620
SHEET 7 AA 8 ALA A1746 VAL A1749 1 O ILE A1747 N VAL A1728
SHEET 8 AA 8 LEU A1791 ALA A1793 1 O LEU A1791 N GLN A1748
SHEET 1 AB 3 GLN A1640 TRP A1643 0
SHEET 2 AB 3 PHE A1653 LEU A1658 -1 N GLN A1654 O ALA A1642
SHEET 3 AB 3 PHE A1688 VAL A1689 -1 O PHE A1688 N LEU A1658
SHEET 1 AC 2 VAL A1675 LEU A1676 0
SHEET 2 AC 2 THR A1692 ILE A1693 -1 O THR A1692 N LEU A1676
SHEET 1 AD 2 SER A1732 VAL A1733 0
SHEET 2 AD 2 ILE A1754 ILE A1755 1 N ILE A1755 O SER A1732
SHEET 1 AE 2 GLY A1849 THR A1852 0
SHEET 2 AE 2 GLY A1855 TYR A1858 -1 O GLY A1855 N THR A1852
SHEET 1 AF 7 PHE A1867 THR A1869 0
SHEET 2 AF 7 VAL A1877 LEU A1884 -1 O VAL A1879 N THR A1869
SHEET 3 AF 7 ILE A1887 VAL A1894 -1 O ILE A1887 N LEU A1884
SHEET 4 AF 7 MSE A1947 ILE A1949 1 O MSE A1948 N ILE A1892
SHEET 5 AF 7 ILE A1985 ILE A1989 1 O ILE A1986 N ILE A1949
SHEET 6 AF 7 MSE A2012 ASP A2017 1 O GLU A2013 N ILE A1987
SHEET 7 AF 7 LYS A2111 LEU A2113 1 O LYS A2111 N ALA A2016
SHEET 1 AG 2 VAL A1899 ILE A1903 0
SHEET 2 AG 2 THR A1915 GLU A1919 -1 O THR A1915 N ILE A1903
SHEET 1 AH 2 GLU A1994 ARG A1996 0
SHEET 2 AH 2 ARG A2021 GLY A2023 1 O ARG A2021 N LEU A1995
SHEET 1 BA 8 THR B1551 VAL B1553 0
SHEET 2 BA 8 PHE B1537 ILE B1543 -1 O GLU B1541 N VAL B1553
SHEET 3 BA 8 MSE B1564 VAL B1571 -1 O ALA B1566 N LEU B1542
SHEET 4 BA 8 ARG B1580 ASN B1587 -1 O ARG B1580 N VAL B1571
SHEET 5 BA 8 ARG B1618 ALA B1622 1 O ILE B1619 N VAL B1585
SHEET 6 BA 8 THR B1724 VAL B1728 1 O ILE B1725 N TYR B1620
SHEET 7 BA 8 ARG B1745 VAL B1749 1 O ARG B1745 N THR B1726
SHEET 8 BA 8 LEU B1791 ALA B1793 1 O LEU B1791 N GLN B1748
SHEET 1 BB 2 SER B1595 PHE B1596 0
SHEET 2 BB 2 GLY B1626 ALA B1627 1 O GLY B1626 N PHE B1596
SHEET 1 BC 4 PHE B1639 TRP B1643 0
SHEET 2 BC 4 PHE B1653 LEU B1658 -1 N GLN B1654 O ALA B1642
SHEET 3 BC 4 PHE B1688 ILE B1693 -1 O PHE B1688 N LEU B1658
SHEET 4 BC 4 VAL B1675 GLU B1678 -1 O LEU B1676 N LYS B1691
SHEET 1 BD 2 SER B1732 VAL B1733 0
SHEET 2 BD 2 ILE B1754 ILE B1755 1 N ILE B1755 O SER B1732
SHEET 1 BE 2 ARG B1850 THR B1852 0
SHEET 2 BE 2 GLY B1855 GLU B1857 -1 O GLY B1855 N THR B1852
SHEET 1 BF 7 PHE B1867 GLU B1868 0
SHEET 2 BF 7 VAL B1877 LEU B1884 -1 O ARG B1881 N PHE B1867
SHEET 3 BF 7 ILE B1887 VAL B1894 -1 O ILE B1887 N LEU B1884
SHEET 4 BF 7 MSE B1947 ILE B1949 1 O MSE B1948 N ILE B1892
SHEET 5 BF 7 ILE B1985 ILE B1989 1 O ILE B1986 N ILE B1949
SHEET 6 BF 7 MSE B2014 ASP B2017 1 O TYR B2015 N ILE B1989
SHEET 7 BF 7 GLU B2112 LEU B2113 1 N LEU B2113 O ALA B2016
SHEET 1 BG 2 VAL B1899 ILE B1903 0
SHEET 2 BG 2 THR B1915 GLU B1919 -1 O THR B1915 N ILE B1903
SHEET 1 BH 2 GLU B1994 ARG B1996 0
SHEET 2 BH 2 ARG B2021 GLY B2023 1 O ARG B2021 N LEU B1995
LINK C LEU A1502 N MSE A1503 1555 1555 1.33
LINK C MSE A1503 N GLY A1504 1555 1555 1.33
LINK C GLY A1563 N MSE A1564 1555 1555 1.32
LINK C MSE A1564 N VAL A1565 1555 1555 1.33
LINK C GLY A1630 N MSE A1631 1555 1555 1.33
LINK C MSE A1631 N ALA A1632 1555 1555 1.33
LINK C GLY A1662 N MSE A1663 1555 1555 1.33
LINK C MSE A1663 N GLU A1664 1555 1555 1.33
LINK C LYS A1764 N MSE A1765 1555 1555 1.33
LINK C MSE A1765 N LEU A1766 1555 1555 1.33
LINK C ILE A1782 N MSE A1783 1555 1555 1.32
LINK C MSE A1783 N TYR A1784 1555 1555 1.33
LINK C TRP A1806 N MSE A1807 1555 1555 1.32
LINK C MSE A1807 N SER A1808 1555 1555 1.33
LINK C ASN A1815 N MSE A1816 1555 1555 1.32
LINK C MSE A1816 N PRO A1817 1555 1555 1.34
LINK C TRP A1845 N MSE A1846 1555 1555 1.33
LINK C MSE A1846 N ILE A1847 1555 1555 1.33
LINK C PRO A1946 N MSE A1947 1555 1555 1.32
LINK C MSE A1947 N MSE A1948 1555 1555 1.32
LINK C MSE A1948 N ILE A1949 1555 1555 1.32
LINK C ASP A1962 N MSE A1963 1555 1555 1.33
LINK C MSE A1963 N PHE A1964 1555 1555 1.32
LINK C GLN A2011 N MSE A2012 1555 1555 1.33
LINK C MSE A2012 N GLU A2013 1555 1555 1.33
LINK C GLU A2013 N MSE A2014 1555 1555 1.33
LINK C MSE A2014 N TYR A2015 1555 1555 1.32
LINK C GLY A2029 N MSE A2030 1555 1555 1.33
LINK C MSE A2030 N VAL A2031 1555 1555 1.33
LINK C THR A2043 N MSE A2044 1555 1555 1.32
LINK C MSE A2044 N ASN A2045 1555 1555 1.33
LINK C ARG A2102 N MSE A2103 1555 1555 1.33
LINK C MSE A2103 N VAL A2104 1555 1555 1.33
LINK C LEU B1502 N MSE B1503 1555 1555 1.33
LINK C MSE B1503 N GLY B1504 1555 1555 1.33
LINK C GLY B1563 N MSE B1564 1555 1555 1.33
LINK C MSE B1564 N VAL B1565 1555 1555 1.33
LINK C GLY B1630 N MSE B1631 1555 1555 1.33
LINK C MSE B1631 N ALA B1632 1555 1555 1.33
LINK C GLY B1662 N MSE B1663 1555 1555 1.33
LINK C MSE B1663 N GLU B1664 1555 1555 1.34
LINK C LYS B1764 N MSE B1765 1555 1555 1.33
LINK C MSE B1765 N LEU B1766 1555 1555 1.33
LINK C ILE B1782 N MSE B1783 1555 1555 1.33
LINK C MSE B1783 N TYR B1784 1555 1555 1.32
LINK C TRP B1806 N MSE B1807 1555 1555 1.33
LINK C MSE B1807 N SER B1808 1555 1555 1.33
LINK C ASN B1815 N MSE B1816 1555 1555 1.33
LINK C MSE B1816 N PRO B1817 1555 1555 1.33
LINK C TRP B1845 N MSE B1846 1555 1555 1.33
LINK C MSE B1846 N ILE B1847 1555 1555 1.33
LINK C PRO B1946 N MSE B1947 1555 1555 1.32
LINK C MSE B1947 N MSE B1948 1555 1555 1.32
LINK C MSE B1948 N ILE B1949 1555 1555 1.32
LINK C ASP B1962 N MSE B1963 1555 1555 1.33
LINK C MSE B1963 N PHE B1964 1555 1555 1.33
LINK C GLN B2011 N MSE B2012 1555 1555 1.33
LINK C MSE B2012 N GLU B2013 1555 1555 1.33
LINK C GLU B2013 N MSE B2014 1555 1555 1.32
LINK C MSE B2014 N TYR B2015 1555 1555 1.33
LINK C GLY B2029 N MSE B2030 1555 1555 1.33
LINK C MSE B2030 N VAL B2031 1555 1555 1.33
LINK C THR B2043 N MSE B2044 1555 1555 1.32
LINK C MSE B2044 N ASN B2045 1555 1555 1.33
LINK C ARG B2102 N MSE B2103 1555 1555 1.33
LINK C MSE B2103 N VAL B2104 1555 1555 1.33
SITE 1 AC1 13 ILE A1593 SER A1595 SER A1625 ALA A1627
SITE 2 AC1 13 ARG A1628 ILE A1629 ARG A1731 GLY A1734
SITE 3 AC1 13 THR A1757 GLY B1998 ILE B2033 LYS B2034
SITE 4 AC1 13 ARG B2036
SITE 1 AC2 5 ILE B1593 SER B1625 ALA B1627 ARG B1628
SITE 2 AC2 5 ILE B1629
CRYST1 92.870 138.130 101.400 90.00 114.42 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010768 0.000000 0.004889 0.00000
SCALE2 0.000000 0.007239 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010831 0.00000
MTRIX1 1 0.221560 -0.714710 -0.663410 23.68200 1
MTRIX2 1 -0.709900 -0.584630 0.392760 7.65045 1
MTRIX3 1 -0.668550 0.383930 -0.636900 35.03892 1
(ATOM LINES ARE NOT SHOWN.)
END
