HEADER TRANSFERASE 02-MAR-04 1UYR
TITLE ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE DOMAIN IN
TITLE 2 COMPLEX WITH INHIBITOR DICLOFOP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL-COA CARBOXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CARBOXYLTRANSFERASE, RESIDUES 1482-2218;
COMPND 5 SYNONYM: ACC;
COMPND 6 EC: 6.4.1.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: BOUND TO DICLOFOP
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 CARBOXYLASE, CARBOXYLTRANSFERASE, HERBICIDE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.ZHANG,B.TWEEL,L.TONG
REVDAT 3 24-FEB-09 1UYR 1 VERSN
REVDAT 2 09-SEP-04 1UYR 1 JRNL
REVDAT 1 29-MAR-04 1UYR 0
JRNL AUTH H.ZHANG,B.TWEEL,L.TONG
JRNL TITL MOLECULAR BASIS FOR THE INHIBITION OF THE
JRNL TITL 2 CARBOXYLTRANSFERASE DOMAIN OF ACETYL-COENZYME-A
JRNL TITL 3 CARBOXYLASE BY HALOXYFOP AND DICLOFOP
JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 5910 2004
JRNL REFN ISSN 0027-8424
JRNL PMID 15079078
JRNL DOI 10.1073/PNAS.0400891101
REMARK 2
REMARK 2 RESOLUTION. 2.5 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) : 2.5
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 88661
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) : 0.217
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.0
REMARK 3 FREE R VALUE TEST SET COUNT : 8859
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.1
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7287
REMARK 3 BIN R VALUE (WORKING SET) : 0.261
REMARK 3 BIN FREE R VALUE : 0.295
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.9
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 798
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11010
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 177
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.2
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.1
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02
REMARK 3 B22 (A**2) : 0.02
REMARK 3 B33 (A**2) : -0.04
REMARK 3 B12 (A**2) : 6.27
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.27
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) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.33
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.2
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.3
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.79
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UYR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAR-04.
REMARK 100 THE PDBE ID CODE IS EBI-14705.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.50
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) : 0.90193
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88661
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 96.0
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.31700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: COMO
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 162.94000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 81.47000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 81.47000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 162.94000
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 GENERATING THE BIOMOLECULE
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 GLY A 1959
REMARK 465 GLN A 1960
REMARK 465 ARG A 1961
REMARK 465 ASP A 1962
REMARK 465 MET A 1963
REMARK 465 PHE A 1964
REMARK 465 ASP A 2048
REMARK 465 ASP A 2049
REMARK 465 LYS A 2050
REMARK 465 TYR A 2051
REMARK 465 ARG A 2052
REMARK 465 GLU A 2053
REMARK 465 LEU A 2054
REMARK 465 ARG A 2055
REMARK 465 SER A 2056
REMARK 465 GLN A 2057
REMARK 465 LEU A 2058
REMARK 465 SER A 2059
REMARK 465 ASN A 2060
REMARK 465 LYS A 2061
REMARK 465 SER A 2062
REMARK 465 LEU A 2063
REMARK 465 ALA A 2064
REMARK 465 PRO A 2065
REMARK 465 GLU A 2066
REMARK 465 VAL A 2067
REMARK 465 HIS A 2068
REMARK 465 GLN A 2069
REMARK 465 GLN A 2070
REMARK 465 ILE A 2071
REMARK 465 SER A 2072
REMARK 465 LYS A 2073
REMARK 465 GLN A 2074
REMARK 465 LEU A 2075
REMARK 465 ALA A 2076
REMARK 465 ASP A 2077
REMARK 465 ARG A 2078
REMARK 465 GLU A 2079
REMARK 465 ARG A 2080
REMARK 465 PRO B 1482
REMARK 465 ILE B 1483
REMARK 465 GLY B 1959
REMARK 465 GLN B 1960
REMARK 465 ARG B 1961
REMARK 465 ASP B 1962
REMARK 465 MET B 1963
REMARK 465 PHE B 1964
REMARK 465 LEU B 2047
REMARK 465 ASP B 2048
REMARK 465 ASP B 2049
REMARK 465 LYS B 2050
REMARK 465 TYR B 2051
REMARK 465 ARG B 2052
REMARK 465 GLU B 2053
REMARK 465 LEU B 2054
REMARK 465 ARG B 2055
REMARK 465 SER B 2056
REMARK 465 GLN B 2057
REMARK 465 LEU B 2058
REMARK 465 SER B 2059
REMARK 465 ASN B 2060
REMARK 465 LYS B 2061
REMARK 465 SER B 2062
REMARK 465 LEU B 2063
REMARK 465 ALA B 2064
REMARK 465 PRO B 2065
REMARK 465 GLU B 2066
REMARK 465 VAL B 2067
REMARK 465 HIS B 2068
REMARK 465 GLN B 2069
REMARK 465 GLN B 2070
REMARK 465 ILE B 2071
REMARK 465 SER B 2072
REMARK 465 LYS B 2073
REMARK 465 GLN B 2074
REMARK 465 LEU B 2075
REMARK 465 ALA B 2076
REMARK 465 ASP B 2077
REMARK 465 ARG B 2078
REMARK 465 GLU B 2079
REMARK 465 ARG B 2080
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 SER A2204 OG
REMARK 470 ASP A2205 CG OD1 OD2
REMARK 470 HIS A2206 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A2207 CG OD1 OD2
REMARK 470 ASN A2208 CG OD1 ND2
REMARK 470 ILE A2210 CG1 CG2 CD1
REMARK 470 ASP A2211 CG OD1 OD2
REMARK 470 LEU A2213 CG CD1 CD2
REMARK 470 SER A2214 OG
REMARK 470 GLU A2215 CG CD OE1 OE2
REMARK 470 VAL A2216 CG1 CG2
REMARK 470 ILE A2217 CG1 CG2 CD1
REMARK 470 LYS A2218 CG CD CE NZ
REMARK 470 SER B2204 OG
REMARK 470 ASP B2205 CG OD1 OD2
REMARK 470 HIS B2206 CG ND1 CD2 CE1 NE2
REMARK 470 ASP B2207 CG OD1 OD2
REMARK 470 ILE B2210 CG1 CG2 CD1
REMARK 470 ASP B2211 CG OD1 OD2
REMARK 470 LEU B2213 CG CD1 CD2
REMARK 470 SER B2214 OG
REMARK 470 GLU B2215 CG CD OE1 OE2
REMARK 470 VAL B2216 CG1 CG2
REMARK 470 ILE B2217 CG1 CG2 CD1
REMARK 470 LYS B2218 CG CD CE NZ
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 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 A1484 88.44 49.91
REMARK 500 LEU A1638 -45.45 -133.42
REMARK 500 GLN A1654 -60.44 -97.96
REMARK 500 ASP A1670 -2.88 64.09
REMARK 500 LYS A1671 47.81 -82.90
REMARK 500 ASN A1673 48.40 -76.12
REMARK 500 ARG A1731 153.15 -36.96
REMARK 500 GLN A1744 -71.49 66.08
REMARK 500 MET A1765 -75.17 -63.74
REMARK 500 ASP A1838 -93.95 -78.10
REMARK 500 GLU A1900 69.90 -115.78
REMARK 500 ASN A1909 99.88 -164.01
REMARK 500 SER A1912 134.09 -170.48
REMARK 500 ASN A1952 60.69 -154.53
REMARK 500 ILE A2033 -34.08 -136.78
REMARK 500 GLU A2038 -71.15 -53.67
REMARK 500 ARG A2046 -12.43 -49.92
REMARK 500 HIS A2141 30.12 -85.49
REMARK 500 ARG A2203 33.06 -88.89
REMARK 500 SER A2204 2.41 -154.07
REMARK 500 ASP A2205 42.21 -178.71
REMARK 500 HIS A2206 -35.45 -39.17
REMARK 500 ASP A2207 -83.32 -58.57
REMARK 500 GLU A2215 -9.68 -55.95
REMARK 500 ILE A2217 -65.42 -99.69
REMARK 500 SER B1527 89.72 -151.60
REMARK 500 ASP B1529 48.65 -76.53
REMARK 500 ASP B1534 -30.77 -36.75
REMARK 500 GLU B1554 74.23 -109.64
REMARK 500 MET B1631 146.20 -173.76
REMARK 500 ALA B1632 96.19 -66.44
REMARK 500 LEU B1638 55.35 -110.58
REMARK 500 ASN B1644 -137.62 -74.91
REMARK 500 ASP B1645 48.58 -76.54
REMARK 500 PRO B1649 -33.67 -33.16
REMARK 500 ASP B1650 -36.74 -29.39
REMARK 500 TYR B1655 -173.75 -175.33
REMARK 500 LYS B1671 37.92 -96.29
REMARK 500 THR B1680 81.83 -153.65
REMARK 500 GLN B1744 -71.05 66.61
REMARK 500 MET B1765 30.42 -140.20
REMARK 500 THR B1823 -164.28 -123.67
REMARK 500 ASP B1832 -72.88 -76.30
REMARK 500 GLU B1839 132.10 168.34
REMARK 500 ASN B1952 61.21 -154.35
REMARK 500 ILE B2033 -37.91 -147.83
REMARK 500 PHE B2035 57.51 -166.49
REMARK 500 ARG B2037 -49.68 -29.75
REMARK 500 ASP B2098 30.49 -73.73
REMARK 500 LYS B2111 162.33 170.21
REMARK 500 ARG B2203 32.28 -81.38
REMARK 500 SER B2204 -11.35 -159.38
REMARK 500 ASP B2205 47.35 -168.00
REMARK 500 ILE B2217 66.24 -69.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D1L A3219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D1L B3219
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OD2 RELATED DB: PDB
REMARK 900 ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERAS
REMARK 900 DOMAINE
REMARK 900 RELATED ID: 1OD4 RELATED DB: PDB
REMARK 900 ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE
REMARK 900 DOMAIN
REMARK 900 RELATED ID: 1UYS RELATED DB: PDB
REMARK 900 ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE
REMARK 900 DOMAIN
REMARK 900 RELATED ID: 1UYT RELATED DB: PDB
REMARK 900 ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE
REMARK 900 DOMAIN
REMARK 900 RELATED ID: 1UYV RELATED DB: PDB
REMARK 900 ACETYL-COA CARBOXYLASE CARBOXYLTRANSFERASE
REMARK 900 DOMAIN
DBREF 1UYR A 1482 2218 UNP Q00955 COAC_YEAST 1482 2218
DBREF 1UYR B 1482 2218 UNP Q00955 COAC_YEAST 1482 2218
SEQRES 1 A 737 PRO ILE ALA THR PRO TYR PRO VAL LYS GLU TRP LEU GLN
SEQRES 2 A 737 PRO LYS ARG TYR LYS ALA HIS LEU MET GLY THR THR TYR
SEQRES 3 A 737 VAL TYR ASP PHE PRO GLU LEU PHE ARG GLN ALA SER SER
SEQRES 4 A 737 SER GLN TRP LYS ASN PHE SER ALA ASP VAL LYS LEU THR
SEQRES 5 A 737 ASP ASP PHE PHE ILE SER ASN GLU LEU ILE GLU ASP GLU
SEQRES 6 A 737 ASN GLY GLU LEU THR GLU VAL GLU ARG GLU PRO GLY ALA
SEQRES 7 A 737 ASN ALA ILE GLY MET VAL ALA PHE LYS ILE THR VAL LYS
SEQRES 8 A 737 THR PRO GLU TYR PRO ARG GLY ARG GLN PHE VAL VAL VAL
SEQRES 9 A 737 ALA ASN ASP ILE THR PHE LYS ILE GLY SER PHE GLY PRO
SEQRES 10 A 737 GLN GLU ASP GLU PHE PHE ASN LYS VAL THR GLU TYR ALA
SEQRES 11 A 737 ARG LYS ARG GLY ILE PRO ARG ILE TYR LEU ALA ALA ASN
SEQRES 12 A 737 SER GLY ALA ARG ILE GLY MET ALA GLU GLU ILE VAL PRO
SEQRES 13 A 737 LEU PHE GLN VAL ALA TRP ASN ASP ALA ALA ASN PRO ASP
SEQRES 14 A 737 LYS GLY PHE GLN TYR LEU TYR LEU THR SER GLU GLY MET
SEQRES 15 A 737 GLU THR LEU LYS LYS PHE ASP LYS GLU ASN SER VAL LEU
SEQRES 16 A 737 THR GLU ARG THR VAL ILE ASN GLY GLU GLU ARG PHE VAL
SEQRES 17 A 737 ILE LYS THR ILE ILE GLY SER GLU ASP GLY LEU GLY VAL
SEQRES 18 A 737 GLU CYS LEU ARG GLY SER GLY LEU ILE ALA GLY ALA THR
SEQRES 19 A 737 SER ARG ALA TYR HIS ASP ILE PHE THR ILE THR LEU VAL
SEQRES 20 A 737 THR CYS ARG SER VAL GLY ILE GLY ALA TYR LEU VAL ARG
SEQRES 21 A 737 LEU GLY GLN ARG ALA ILE GLN VAL GLU GLY GLN PRO ILE
SEQRES 22 A 737 ILE LEU THR GLY ALA PRO ALA ILE ASN LYS MET LEU GLY
SEQRES 23 A 737 ARG GLU VAL TYR THR SER ASN LEU GLN LEU GLY GLY THR
SEQRES 24 A 737 GLN ILE MET TYR ASN ASN GLY VAL SER HIS LEU THR ALA
SEQRES 25 A 737 VAL ASP ASP LEU ALA GLY VAL GLU LYS ILE VAL GLU TRP
SEQRES 26 A 737 MET SER TYR VAL PRO ALA LYS ARG ASN MET PRO VAL PRO
SEQRES 27 A 737 ILE LEU GLU THR LYS ASP THR TRP ASP ARG PRO VAL ASP
SEQRES 28 A 737 PHE THR PRO THR ASN ASP GLU THR TYR ASP VAL ARG TRP
SEQRES 29 A 737 MET ILE GLU GLY ARG GLU THR GLU SER GLY PHE GLU TYR
SEQRES 30 A 737 GLY LEU PHE ASP LYS GLY SER PHE PHE GLU THR LEU SER
SEQRES 31 A 737 GLY TRP ALA LYS GLY VAL VAL VAL GLY ARG ALA ARG LEU
SEQRES 32 A 737 GLY GLY ILE PRO LEU GLY VAL ILE GLY VAL GLU THR ARG
SEQRES 33 A 737 THR VAL GLU ASN LEU ILE PRO ALA ASP PRO ALA ASN PRO
SEQRES 34 A 737 ASN SER ALA GLU THR LEU ILE GLN GLU PRO GLY GLN VAL
SEQRES 35 A 737 TRP HIS PRO ASN SER ALA PHE LYS THR ALA GLN ALA ILE
SEQRES 36 A 737 ASN ASP PHE ASN ASN GLY GLU GLN LEU PRO MET MET ILE
SEQRES 37 A 737 LEU ALA ASN TRP ARG GLY PHE SER GLY GLY GLN ARG ASP
SEQRES 38 A 737 MET PHE ASN GLU VAL LEU LYS TYR GLY SER PHE ILE VAL
SEQRES 39 A 737 ASP ALA LEU VAL ASP TYR LYS GLN PRO ILE ILE ILE TYR
SEQRES 40 A 737 ILE PRO PRO THR GLY GLU LEU ARG GLY GLY SER TRP VAL
SEQRES 41 A 737 VAL VAL ASP PRO THR ILE ASN ALA ASP GLN MET GLU MET
SEQRES 42 A 737 TYR ALA ASP VAL ASN ALA ARG ALA GLY VAL LEU GLU PRO
SEQRES 43 A 737 GLN GLY MET VAL GLY ILE LYS PHE ARG ARG GLU LYS LEU
SEQRES 44 A 737 LEU ASP THR MET ASN ARG LEU ASP ASP LYS TYR ARG GLU
SEQRES 45 A 737 LEU ARG SER GLN LEU SER ASN LYS SER LEU ALA PRO GLU
SEQRES 46 A 737 VAL HIS GLN GLN ILE SER LYS GLN LEU ALA ASP ARG GLU
SEQRES 47 A 737 ARG GLU LEU LEU PRO ILE TYR GLY GLN ILE SER LEU GLN
SEQRES 48 A 737 PHE ALA ASP LEU HIS ASP ARG SER SER ARG MET VAL ALA
SEQRES 49 A 737 LYS GLY VAL ILE SER LYS GLU LEU GLU TRP THR GLU ALA
SEQRES 50 A 737 ARG ARG PHE PHE PHE TRP ARG LEU ARG ARG ARG LEU ASN
SEQRES 51 A 737 GLU GLU TYR LEU ILE LYS ARG LEU SER HIS GLN VAL GLY
SEQRES 52 A 737 GLU ALA SER ARG LEU GLU LYS ILE ALA ARG ILE ARG SER
SEQRES 53 A 737 TRP TYR PRO ALA SER VAL ASP HIS GLU ASP ASP ARG GLN
SEQRES 54 A 737 VAL ALA THR TRP ILE GLU GLU ASN TYR LYS THR LEU ASP
SEQRES 55 A 737 ASP LYS LEU LYS GLY LEU LYS LEU GLU SER PHE ALA GLN
SEQRES 56 A 737 ASP LEU ALA LYS LYS ILE ARG SER ASP HIS ASP ASN ALA
SEQRES 57 A 737 ILE ASP GLY LEU SER GLU VAL ILE LYS
SEQRES 1 B 737 PRO ILE ALA THR PRO TYR PRO VAL LYS GLU TRP LEU GLN
SEQRES 2 B 737 PRO LYS ARG TYR LYS ALA HIS LEU MET GLY THR THR TYR
SEQRES 3 B 737 VAL TYR ASP PHE PRO GLU LEU PHE ARG GLN ALA SER SER
SEQRES 4 B 737 SER GLN TRP LYS ASN PHE SER ALA ASP VAL LYS LEU THR
SEQRES 5 B 737 ASP ASP PHE PHE ILE SER ASN GLU LEU ILE GLU ASP GLU
SEQRES 6 B 737 ASN GLY GLU LEU THR GLU VAL GLU ARG GLU PRO GLY ALA
SEQRES 7 B 737 ASN ALA ILE GLY MET VAL ALA PHE LYS ILE THR VAL LYS
SEQRES 8 B 737 THR PRO GLU TYR PRO ARG GLY ARG GLN PHE VAL VAL VAL
SEQRES 9 B 737 ALA ASN ASP ILE THR PHE LYS ILE GLY SER PHE GLY PRO
SEQRES 10 B 737 GLN GLU ASP GLU PHE PHE ASN LYS VAL THR GLU TYR ALA
SEQRES 11 B 737 ARG LYS ARG GLY ILE PRO ARG ILE TYR LEU ALA ALA ASN
SEQRES 12 B 737 SER GLY ALA ARG ILE GLY MET ALA GLU GLU ILE VAL PRO
SEQRES 13 B 737 LEU PHE GLN VAL ALA TRP ASN ASP ALA ALA ASN PRO ASP
SEQRES 14 B 737 LYS GLY PHE GLN TYR LEU TYR LEU THR SER GLU GLY MET
SEQRES 15 B 737 GLU THR LEU LYS LYS PHE ASP LYS GLU ASN SER VAL LEU
SEQRES 16 B 737 THR GLU ARG THR VAL ILE ASN GLY GLU GLU ARG PHE VAL
SEQRES 17 B 737 ILE LYS THR ILE ILE GLY SER GLU ASP GLY LEU GLY VAL
SEQRES 18 B 737 GLU CYS LEU ARG GLY SER GLY LEU ILE ALA GLY ALA THR
SEQRES 19 B 737 SER ARG ALA TYR HIS ASP ILE PHE THR ILE THR LEU VAL
SEQRES 20 B 737 THR CYS ARG SER VAL GLY ILE GLY ALA TYR LEU VAL ARG
SEQRES 21 B 737 LEU GLY GLN ARG ALA ILE GLN VAL GLU GLY GLN PRO ILE
SEQRES 22 B 737 ILE LEU THR GLY ALA PRO ALA ILE ASN LYS MET LEU GLY
SEQRES 23 B 737 ARG GLU VAL TYR THR SER ASN LEU GLN LEU GLY GLY THR
SEQRES 24 B 737 GLN ILE MET TYR ASN ASN GLY VAL SER HIS LEU THR ALA
SEQRES 25 B 737 VAL ASP ASP LEU ALA GLY VAL GLU LYS ILE VAL GLU TRP
SEQRES 26 B 737 MET SER TYR VAL PRO ALA LYS ARG ASN MET PRO VAL PRO
SEQRES 27 B 737 ILE LEU GLU THR LYS ASP THR TRP ASP ARG PRO VAL ASP
SEQRES 28 B 737 PHE THR PRO THR ASN ASP GLU THR TYR ASP VAL ARG TRP
SEQRES 29 B 737 MET ILE GLU GLY ARG GLU THR GLU SER GLY PHE GLU TYR
SEQRES 30 B 737 GLY LEU PHE ASP LYS GLY SER PHE PHE GLU THR LEU SER
SEQRES 31 B 737 GLY TRP ALA LYS GLY VAL VAL VAL GLY ARG ALA ARG LEU
SEQRES 32 B 737 GLY GLY ILE PRO LEU GLY VAL ILE GLY VAL GLU THR ARG
SEQRES 33 B 737 THR VAL GLU ASN LEU ILE PRO ALA ASP PRO ALA ASN PRO
SEQRES 34 B 737 ASN SER ALA GLU THR LEU ILE GLN GLU PRO GLY GLN VAL
SEQRES 35 B 737 TRP HIS PRO ASN SER ALA PHE LYS THR ALA GLN ALA ILE
SEQRES 36 B 737 ASN ASP PHE ASN ASN GLY GLU GLN LEU PRO MET MET ILE
SEQRES 37 B 737 LEU ALA ASN TRP ARG GLY PHE SER GLY GLY GLN ARG ASP
SEQRES 38 B 737 MET PHE ASN GLU VAL LEU LYS TYR GLY SER PHE ILE VAL
SEQRES 39 B 737 ASP ALA LEU VAL ASP TYR LYS GLN PRO ILE ILE ILE TYR
SEQRES 40 B 737 ILE PRO PRO THR GLY GLU LEU ARG GLY GLY SER TRP VAL
SEQRES 41 B 737 VAL VAL ASP PRO THR ILE ASN ALA ASP GLN MET GLU MET
SEQRES 42 B 737 TYR ALA ASP VAL ASN ALA ARG ALA GLY VAL LEU GLU PRO
SEQRES 43 B 737 GLN GLY MET VAL GLY ILE LYS PHE ARG ARG GLU LYS LEU
SEQRES 44 B 737 LEU ASP THR MET ASN ARG LEU ASP ASP LYS TYR ARG GLU
SEQRES 45 B 737 LEU ARG SER GLN LEU SER ASN LYS SER LEU ALA PRO GLU
SEQRES 46 B 737 VAL HIS GLN GLN ILE SER LYS GLN LEU ALA ASP ARG GLU
SEQRES 47 B 737 ARG GLU LEU LEU PRO ILE TYR GLY GLN ILE SER LEU GLN
SEQRES 48 B 737 PHE ALA ASP LEU HIS ASP ARG SER SER ARG MET VAL ALA
SEQRES 49 B 737 LYS GLY VAL ILE SER LYS GLU LEU GLU TRP THR GLU ALA
SEQRES 50 B 737 ARG ARG PHE PHE PHE TRP ARG LEU ARG ARG ARG LEU ASN
SEQRES 51 B 737 GLU GLU TYR LEU ILE LYS ARG LEU SER HIS GLN VAL GLY
SEQRES 52 B 737 GLU ALA SER ARG LEU GLU LYS ILE ALA ARG ILE ARG SER
SEQRES 53 B 737 TRP TYR PRO ALA SER VAL ASP HIS GLU ASP ASP ARG GLN
SEQRES 54 B 737 VAL ALA THR TRP ILE GLU GLU ASN TYR LYS THR LEU ASP
SEQRES 55 B 737 ASP LYS LEU LYS GLY LEU LYS LEU GLU SER PHE ALA GLN
SEQRES 56 B 737 ASP LEU ALA LYS LYS ILE ARG SER ASP HIS ASP ASN ALA
SEQRES 57 B 737 ILE ASP GLY LEU SER GLU VAL ILE LYS
HET D1L A3219 21
HET D1L B3219 21
HETNAM D1L 2-[4-(2,4-DICHLOROPHENOXY)PHENOXY]PROPANOIC
HETNAM 2 D1L ACID
HETSYN D1L DICLOFOP INHIBITOR
FORMUL 3 D1L 2(C15 H12 CL2 O4)
FORMUL 5 HOH *177(H2 O1)
HELIX 1 1 VAL A 1489 GLN A 1494 1 6
HELIX 2 2 GLN A 1494 MET A 1503 1 10
HELIX 3 3 TYR A 1507 TYR A 1509 5 3
HELIX 4 4 ASP A 1510 SER A 1527 1 18
HELIX 5 5 THR A 1533 ASP A 1535 5 3
HELIX 6 6 PHE A 1591 SER A 1595 5 5
HELIX 7 7 GLY A 1597 GLY A 1615 1 19
HELIX 8 8 ALA A 1632 VAL A 1636 5 5
HELIX 9 9 ASN A 1648 LYS A 1651 5 4
HELIX 10 10 THR A 1659 PHE A 1669 1 11
HELIX 11 11 LYS A 1671 ASN A 1673 5 3
HELIX 12 12 GLY A 1701 ILE A 1722 1 22
HELIX 13 13 GLY A 1734 GLY A 1743 1 10
HELIX 14 14 GLY A 1758 LEU A 1766 1 9
HELIX 15 15 ASN A 1774 GLY A 1779 1 6
HELIX 16 16 GLY A 1779 TYR A 1784 1 6
HELIX 17 17 ASP A 1795 SER A 1808 1 14
HELIX 18 18 ASP A 1842 GLY A 1849 1 8
HELIX 19 19 HIS A 1925 ASN A 1941 1 17
HELIX 20 20 GLU A 1966 ASP A 1980 1 15
HELIX 21 21 GLY A 1997 VAL A 2002 1 6
HELIX 22 22 VAL A 2003 ALA A 2009 5 7
HELIX 23 23 GLU A 2026 PHE A 2035 1 10
HELIX 24 24 ARG A 2036 LEU A 2047 1 12
HELIX 25 25 LEU A 2082 LEU A 2096 1 15
HELIX 26 26 ARG A 2099 GLY A 2107 1 9
HELIX 27 27 GLU A 2114 ARG A 2138 1 25
HELIX 28 28 SER A 2147 SER A 2157 1 11
HELIX 29 29 ASP A 2167 ASN A 2178 1 12
HELIX 30 30 ASN A 2178 ARG A 2203 1 26
HELIX 31 31 ASP A 2205 GLU A 2215 1 11
HELIX 32 32 LEU B 1493 MET B 1503 1 11
HELIX 33 33 TYR B 1507 TYR B 1509 5 3
HELIX 34 34 ASP B 1510 SER B 1527 1 18
HELIX 35 35 THR B 1533 ASP B 1535 5 3
HELIX 36 36 PHE B 1591 SER B 1595 5 5
HELIX 37 37 GLY B 1597 GLY B 1615 1 19
HELIX 38 38 THR B 1659 PHE B 1669 1 11
HELIX 39 39 LYS B 1671 ASN B 1673 5 3
HELIX 40 40 GLY B 1701 ILE B 1722 1 22
HELIX 41 41 GLY B 1734 GLY B 1743 1 10
HELIX 42 42 GLY B 1758 LYS B 1764 1 7
HELIX 43 43 ASN B 1774 GLY B 1779 1 6
HELIX 44 44 GLY B 1779 TYR B 1784 1 6
HELIX 45 45 ASP B 1795 SER B 1808 1 14
HELIX 46 46 ASP B 1842 GLU B 1848 1 7
HELIX 47 47 HIS B 1925 ASN B 1941 1 17
HELIX 48 48 ASN B 1965 TYR B 1981 1 17
HELIX 49 49 GLY B 1997 VAL B 2002 1 6
HELIX 50 50 VAL B 2003 ALA B 2009 5 7
HELIX 51 51 GLU B 2026 PHE B 2035 1 10
HELIX 52 52 ARG B 2036 THR B 2043 1 8
HELIX 53 53 LEU B 2082 LEU B 2096 1 15
HELIX 54 54 ARG B 2099 LYS B 2106 1 8
HELIX 55 55 GLU B 2114 ARG B 2138 1 25
HELIX 56 56 SER B 2147 SER B 2157 1 11
HELIX 57 57 ASP B 2167 ILE B 2217 1 51
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 MET A1564 VAL A1571 -1 O ALA A1566 N LEU A1542
SHEET 4 AA 8 ARG A1580 ASN A1587 -1 O ARG A1580 N VAL A1571
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 4 GLN A1640 TRP A1643 0
SHEET 2 AB 4 PHE A1653 LEU A1658 -1 N GLN A1654 O ALA A1642
SHEET 3 AB 4 GLU A1685 ILE A1693 -1 O PHE A1688 N LEU A1658
SHEET 4 AB 4 VAL A1675 ILE A1682 -1 O LEU A1676 N LYS A1691
SHEET 1 AC 2 SER A1732 VAL A1733 0
SHEET 2 AC 2 ILE A1754 ILE A1755 1 N ILE A1755 O SER A1732
SHEET 1 AD 2 ARG A1850 THR A1852 0
SHEET 2 AD 2 GLY A1855 GLU A1857 -1 O GLY A1855 N THR A1852
SHEET 1 AE 7 PHE A1867 THR A1869 0
SHEET 2 AE 7 VAL A1877 LEU A1884 -1 O VAL A1879 N THR A1869
SHEET 3 AE 7 ILE A1887 VAL A1894 -1 O ILE A1887 N LEU A1884
SHEET 4 AE 7 MET A1947 ILE A1949 1 O MET A1948 N ILE A1892
SHEET 5 AE 7 ILE A1985 ILE A1989 1 O ILE A1986 N ILE A1949
SHEET 6 AE 7 MET A2012 ASP A2017 1 O GLU A2013 N ILE A1987
SHEET 7 AE 7 LYS A2111 LEU A2113 1 O LYS A2111 N ALA A2016
SHEET 1 AF 2 VAL A1899 ILE A1903 0
SHEET 2 AF 2 THR A1915 GLU A1919 -1 O THR A1915 N ILE A1903
SHEET 1 AG 2 GLU A1994 ARG A1996 0
SHEET 2 AG 2 ARG A2021 GLY A2023 1 O ARG A2021 N LEU A1995
SHEET 1 BA 8 LEU B1550 VAL B1553 0
SHEET 2 BA 8 PHE B1537 GLU B1544 -1 O GLU B1541 N VAL B1553
SHEET 3 BA 8 MET 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 ALA B1746 VAL B1749 1 O ILE B1747 N VAL B1728
SHEET 8 BA 8 LEU B1791 ALA B1793 1 O LEU B1791 N GLN B1748
SHEET 1 BB 4 GLN B1640 TRP B1643 0
SHEET 2 BB 4 PHE B1653 LEU B1658 -1 N GLN B1654 O ALA B1642
SHEET 3 BB 4 GLU B1685 ILE B1693 -1 O PHE B1688 N LEU B1658
SHEET 4 BB 4 VAL B1675 ILE B1682 -1 O LEU B1676 N LYS B1691
SHEET 1 BC 2 SER B1732 VAL B1733 0
SHEET 2 BC 2 ILE B1754 ILE B1755 1 N ILE B1755 O SER B1732
SHEET 1 BD 2 GLY B1849 THR B1852 0
SHEET 2 BD 2 GLY B1855 TYR B1858 -1 O GLY B1855 N THR B1852
SHEET 1 BE 7 PHE B1867 GLU B1868 0
SHEET 2 BE 7 VAL B1877 LEU B1884 -1 O ARG B1881 N PHE B1867
SHEET 3 BE 7 ILE B1887 VAL B1894 -1 O ILE B1887 N LEU B1884
SHEET 4 BE 7 MET B1947 ILE B1949 1 O MET B1948 N ILE B1892
SHEET 5 BE 7 ILE B1985 ILE B1989 1 O ILE B1986 N ILE B1949
SHEET 6 BE 7 MET B2012 ASP B2017 1 O GLU B2013 N ILE B1987
SHEET 7 BE 7 LYS B2111 LEU B2113 1 O LYS B2111 N ALA B2016
SHEET 1 BF 2 VAL B1899 ILE B1903 0
SHEET 2 BF 2 THR B1915 GLU B1919 -1 O THR B1915 N ILE B1903
SHEET 1 BG 2 GLU B1994 ARG B1996 0
SHEET 2 BG 2 ARG B2021 GLY B2023 1 O ARG B2021 N LEU B1995
SITE 1 AC1 14 GLY A1626 ALA A1627 LEU A1705 GLY A1734
SITE 2 AC1 14 ILE A1735 TYR A1738 LEU A1756 TRP B1924
SITE 3 AC1 14 PHE B1956 LEU B1968 GLY B1971 GLY B1997
SITE 4 AC1 14 GLY B1998 VAL B2001
SITE 1 AC2 13 TRP A1924 LEU A1968 GLY A1997 GLY A1998
SITE 2 AC2 13 VAL A2001 VAL A2002 GLY B1626 ALA B1627
SITE 3 AC2 13 LEU B1705 GLY B1734 ILE B1735 TYR B1738
SITE 4 AC2 13 LEU B1756
CRYST1 136.780 136.780 244.410 90.00 90.00 120.00 P 32 2 1 12
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 0.007311 0.004221 0.000000 0.00000
SCALE2 0.000000 0.008442 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004091 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
