HEADER TRANSCRIPTION 19-OCT-01 1K7L
TITLE THE 2.5 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE HUMAN PPARALPHA
TITLE 2 LIGAND BINDING DOMAIN BOUND WITH GW409544 AND A CO-ACTIVATOR PEPTIDE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR ALPHA;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN - RESIDUES 192 - 468;
COMPND 5 SYNONYM: PPARALPHA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: STEROID RECEPTOR COACTIVATOR;
COMPND 9 CHAIN: B, D, F, H;
COMPND 10 FRAGMENT: SRC-1 PEPTIDE;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) E.COLI;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PRSETA;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: T7 PROMOTER CONTROL PLASMID;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: CHEMICALLY SYNTHESIZED 21MER PORTION OF THE THE HUMAN
SOURCE 13 SRC-1 COACTIVATOR PEPTIDE.
KEYWDS THE 2.5 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE HUMAN PPARALPHA
KEYWDS 2 LIGAND BINDING DOMAIN BOUND WITH GW409544 AND A COACTIVATOR PEPTIDE,
KEYWDS 3 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR H.E.XU,M.H.LAMBERT,V.G.MONTANA,L.B.MOORE,J.L.COLLINS,J.A.OPLINGER,
AUTHOR 2 S.A.KLIEWER,R.T.GAMPE JR.,D.D.MCKEE,J.T.MOORE,T.M.WILLSON
REVDAT 3 07-FEB-24 1K7L 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1K7L 1 VERSN
REVDAT 1 05-DEC-01 1K7L 0
JRNL AUTH H.E.XU,M.H.LAMBERT,V.G.MONTANA,K.D.PLUNKET,L.B.MOORE,
JRNL AUTH 2 J.L.COLLINS,J.A.OPLINGER,S.A.KLIEWER,R.T.GAMPE JR.,
JRNL AUTH 3 D.D.MCKEE,J.T.MOORE,T.M.WILLSON
JRNL TITL STRUCTURAL DETERMINANTS OF LIGAND BINDING SELECTIVITY
JRNL TITL 2 BETWEEN THE PEROXISOME PROLIFERATOR-ACTIVATED RECEPTORS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 98 13919 2001
JRNL REFN ISSN 0027-8424
JRNL PMID 11698662
JRNL DOI 10.1073/PNAS.241410198
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2000.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,MOLECULAR
REMARK 3 : SIMULATIONS (BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 318526.640
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 48912
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 + TEST SET) : 0.247
REMARK 3 R VALUE (WORKING SET) : 0.247
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.200
REMARK 3 FREE R VALUE TEST SET COUNT : 4018
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7106
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE : 0.3650
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 663
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8912
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 154
REMARK 3 SOLVENT ATOMS : 242
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.29000
REMARK 3 B22 (A**2) : -4.61000
REMARK 3 B33 (A**2) : -2.67000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.33
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) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.43
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.890
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) : 1.480 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.630 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.750 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.780 ; 2.500
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : BSXPI3.XPL
REMARK 3 PARAMETER FILE 4 : Y.PARA
REMARK 3 PARAMETER FILE 5 : 544.XPL
REMARK 3 PARAMETER FILE 6 : 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 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K7L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014660.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49991
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05400
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: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, NANO3, HEXANEDIOL, YCL3, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 47.78050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.99700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.79850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.99700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.78050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.79850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 181
REMARK 465 LYS A 182
REMARK 465 LYS A 183
REMARK 465 GLY A 184
REMARK 465 HIS A 185
REMARK 465 HIS A 186
REMARK 465 HIS A 187
REMARK 465 HIS A 188
REMARK 465 HIS A 189
REMARK 465 HIS A 190
REMARK 465 GLY A 191
REMARK 465 GLU A 192
REMARK 465 HIS A 193
REMARK 465 ASP A 194
REMARK 465 ILE A 195
REMARK 465 GLU A 196
REMARK 465 ASP A 197
REMARK 465 SER A 198
REMARK 465 GLU A 199
REMARK 465 THR A 200
REMARK 465 ALA A 201
REMARK 465 HIS B 680
REMARK 465 SER B 681
REMARK 465 SER B 682
REMARK 465 LEU B 683
REMARK 465 THR B 684
REMARK 465 SER B 698
REMARK 465 PRO B 699
REMARK 465 SER B 700
REMARK 465 MET C 181
REMARK 465 LYS C 182
REMARK 465 LYS C 183
REMARK 465 GLY C 184
REMARK 465 HIS C 185
REMARK 465 HIS C 186
REMARK 465 HIS C 187
REMARK 465 HIS C 188
REMARK 465 HIS C 189
REMARK 465 HIS C 190
REMARK 465 GLY C 191
REMARK 465 GLU C 192
REMARK 465 HIS C 193
REMARK 465 ASP C 194
REMARK 465 ILE C 195
REMARK 465 GLU C 196
REMARK 465 ASP C 197
REMARK 465 SER C 198
REMARK 465 GLU C 199
REMARK 465 THR C 200
REMARK 465 ALA C 201
REMARK 465 HIS D 680
REMARK 465 SER D 681
REMARK 465 SER D 682
REMARK 465 LEU D 683
REMARK 465 THR D 684
REMARK 465 SER D 698
REMARK 465 PRO D 699
REMARK 465 SER D 700
REMARK 465 MET E 181
REMARK 465 LYS E 182
REMARK 465 LYS E 183
REMARK 465 GLY E 184
REMARK 465 HIS E 185
REMARK 465 HIS E 186
REMARK 465 HIS E 187
REMARK 465 HIS E 188
REMARK 465 HIS E 189
REMARK 465 HIS E 190
REMARK 465 GLY E 191
REMARK 465 GLU E 192
REMARK 465 HIS E 193
REMARK 465 ASP E 194
REMARK 465 ILE E 195
REMARK 465 GLU E 196
REMARK 465 ASP E 197
REMARK 465 SER E 198
REMARK 465 GLU E 199
REMARK 465 THR E 200
REMARK 465 ALA E 201
REMARK 465 HIS F 680
REMARK 465 SER F 681
REMARK 465 SER F 682
REMARK 465 LEU F 683
REMARK 465 THR F 684
REMARK 465 SER F 698
REMARK 465 PRO F 699
REMARK 465 SER F 700
REMARK 465 MET G 181
REMARK 465 LYS G 182
REMARK 465 LYS G 183
REMARK 465 GLY G 184
REMARK 465 HIS G 185
REMARK 465 HIS G 186
REMARK 465 HIS G 187
REMARK 465 HIS G 188
REMARK 465 HIS G 189
REMARK 465 HIS G 190
REMARK 465 GLY G 191
REMARK 465 GLU G 192
REMARK 465 HIS G 193
REMARK 465 ASP G 194
REMARK 465 ILE G 195
REMARK 465 GLU G 196
REMARK 465 ASP G 197
REMARK 465 SER G 198
REMARK 465 GLU G 199
REMARK 465 THR G 200
REMARK 465 ALA G 201
REMARK 465 HIS H 680
REMARK 465 SER H 681
REMARK 465 SER H 682
REMARK 465 LEU H 683
REMARK 465 THR H 684
REMARK 465 SER H 698
REMARK 465 PRO H 699
REMARK 465 SER H 700
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 LYS B 688 CG CD CE NZ
REMARK 470 LYS D 688 CG CD CE NZ
REMARK 470 LYS F 688 CG CD CE NZ
REMARK 470 LYS H 688 CG CD CE 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 ASP E 202 N LYS E 204 1.93
REMARK 500 OE1 GLN A 277 N HIS A 457 2.08
REMARK 500 O GLY G 231 N ALA G 233 2.15
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 LEU A 229 23.55 -59.89
REMARK 500 SER A 230 110.29 148.74
REMARK 500 LYS A 232 -76.12 9.15
REMARK 500 ALA A 233 -106.29 70.56
REMARK 500 SER A 234 -75.26 -71.64
REMARK 500 ASN A 235 170.80 177.32
REMARK 500 ASN A 236 64.48 110.16
REMARK 500 VAL A 255 -63.64 -161.02
REMARK 500 ALA A 260 47.43 -145.87
REMARK 500 ASN A 261 40.34 -149.56
REMARK 500 GLU A 267 130.85 -29.56
REMARK 500 PRO A 295 109.74 -53.43
REMARK 500 VAL A 306 5.35 -66.61
REMARK 500 LEU A 392 -75.61 -72.68
REMARK 500 ILE A 420 -75.55 32.74
REMARK 500 PHE A 421 36.82 -91.21
REMARK 500 ILE A 446 -73.35 -56.81
REMARK 500 GLU A 451 57.44 -174.47
REMARK 500 SER A 452 -12.25 -47.00
REMARK 500 MET A 467 -71.56 -87.04
REMARK 500 ARG B 686 -76.35 74.92
REMARK 500 GLU B 696 -25.48 -160.60
REMARK 500 LEU C 229 7.10 -63.80
REMARK 500 SER C 230 -72.30 -153.28
REMARK 500 LYS C 232 -65.30 -1.99
REMARK 500 ALA C 233 -93.51 22.57
REMARK 500 ASN C 235 -157.28 78.85
REMARK 500 ASN C 236 50.31 84.55
REMARK 500 PRO C 238 136.73 -31.39
REMARK 500 LEU C 254 49.70 -96.99
REMARK 500 VAL C 255 -36.86 157.31
REMARK 500 VAL C 259 -2.50 -155.26
REMARK 500 ALA C 260 9.40 -159.88
REMARK 500 ILE C 263 14.20 -64.47
REMARK 500 PRO C 295 114.85 -33.78
REMARK 500 ILE C 420 -111.25 -27.44
REMARK 500 PHE C 421 58.52 -102.80
REMARK 500 THR C 450 -9.20 -173.31
REMARK 500 SER C 452 -8.50 -50.76
REMARK 500 ARG D 686 -61.25 60.30
REMARK 500 GLU D 696 -61.22 -146.85
REMARK 500 LEU E 203 13.86 9.01
REMARK 500 SER E 230 87.06 -161.06
REMARK 500 LYS E 232 -41.37 44.46
REMARK 500 ASN E 235 -119.26 9.93
REMARK 500 PRO E 237 131.53 -28.77
REMARK 500 THR E 253 -92.07 -97.76
REMARK 500 LEU E 254 -0.46 -55.74
REMARK 500 ALA E 256 -11.15 -46.67
REMARK 500 ASN E 261 24.70 -140.68
REMARK 500
REMARK 500 THIS ENTRY HAS 79 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 C 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 E 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 544 A 469
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 544 C 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 544 E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 544 G 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K74 RELATED DB: PDB
REMARK 900 RELATED ID: 1FM6 RELATED DB: PDB
REMARK 900 RELATED ID: 1FM9 RELATED DB: PDB
DBREF 1K7L A 192 468 UNP Q07869 PPAR_HUMAN 192 468
DBREF 1K7L C 192 468 UNP Q07869 PPAR_HUMAN 192 468
DBREF 1K7L E 192 468 UNP Q07869 PPAR_HUMAN 192 468
DBREF 1K7L G 192 468 UNP Q07869 PPAR_HUMAN 192 468
DBREF 1K7L B 680 700 UNP O43792 O43792 680 700
DBREF 1K7L D 680 700 UNP O43792 O43792 680 700
DBREF 1K7L F 680 700 UNP O43792 O43792 680 700
DBREF 1K7L H 680 700 UNP O43792 O43792 680 700
SEQADV 1K7L MET A 181 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L LYS A 182 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L LYS A 183 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L GLY A 184 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS A 185 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS A 186 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS A 187 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS A 188 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS A 189 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS A 190 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L GLY A 191 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L MET C 181 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L LYS C 182 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L LYS C 183 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L GLY C 184 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS C 185 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS C 186 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS C 187 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS C 188 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS C 189 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS C 190 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L GLY C 191 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L MET E 181 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L LYS E 182 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L LYS E 183 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L GLY E 184 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS E 185 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS E 186 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS E 187 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS E 188 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS E 189 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS E 190 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L GLY E 191 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L MET G 181 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L LYS G 182 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L LYS G 183 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L GLY G 184 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS G 185 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS G 186 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS G 187 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS G 188 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS G 189 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L HIS G 190 UNP Q07869 EXPRESSION TAG
SEQADV 1K7L GLY G 191 UNP Q07869 EXPRESSION TAG
SEQRES 1 A 288 MET LYS LYS GLY HIS HIS HIS HIS HIS HIS GLY GLU HIS
SEQRES 2 A 288 ASP ILE GLU ASP SER GLU THR ALA ASP LEU LYS SER LEU
SEQRES 3 A 288 ALA LYS ARG ILE TYR GLU ALA TYR LEU LYS ASN PHE ASN
SEQRES 4 A 288 MET ASN LYS VAL LYS ALA ARG VAL ILE LEU SER GLY LYS
SEQRES 5 A 288 ALA SER ASN ASN PRO PRO PHE VAL ILE HIS ASP MET GLU
SEQRES 6 A 288 THR LEU CYS MET ALA GLU LYS THR LEU VAL ALA LYS LEU
SEQRES 7 A 288 VAL ALA ASN GLY ILE GLN ASN LYS GLU ALA GLU VAL ARG
SEQRES 8 A 288 ILE PHE HIS CYS CYS GLN CYS THR SER VAL GLU THR VAL
SEQRES 9 A 288 THR GLU LEU THR GLU PHE ALA LYS ALA ILE PRO GLY PHE
SEQRES 10 A 288 ALA ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS
SEQRES 11 A 288 TYR GLY VAL TYR GLU ALA ILE PHE ALA MET LEU SER SER
SEQRES 12 A 288 VAL MET ASN LYS ASP GLY MET LEU VAL ALA TYR GLY ASN
SEQRES 13 A 288 GLY PHE ILE THR ARG GLU PHE LEU LYS SER LEU ARG LYS
SEQRES 14 A 288 PRO PHE CYS ASP ILE MET GLU PRO LYS PHE ASP PHE ALA
SEQRES 15 A 288 MET LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP ILE
SEQRES 16 A 288 SER LEU PHE VAL ALA ALA ILE ILE CYS CYS GLY ASP ARG
SEQRES 17 A 288 PRO GLY LEU LEU ASN VAL GLY HIS ILE GLU LYS MET GLN
SEQRES 18 A 288 GLU GLY ILE VAL HIS VAL LEU ARG LEU HIS LEU GLN SER
SEQRES 19 A 288 ASN HIS PRO ASP ASP ILE PHE LEU PHE PRO LYS LEU LEU
SEQRES 20 A 288 GLN LYS MET ALA ASP LEU ARG GLN LEU VAL THR GLU HIS
SEQRES 21 A 288 ALA GLN LEU VAL GLN ILE ILE LYS LYS THR GLU SER ASP
SEQRES 22 A 288 ALA ALA LEU HIS PRO LEU LEU GLN GLU ILE TYR ARG ASP
SEQRES 23 A 288 MET TYR
SEQRES 1 B 21 HIS SER SER LEU THR GLU ARG HIS LYS ILE LEU HIS ARG
SEQRES 2 B 21 LEU LEU GLN GLU GLY SER PRO SER
SEQRES 1 C 288 MET LYS LYS GLY HIS HIS HIS HIS HIS HIS GLY GLU HIS
SEQRES 2 C 288 ASP ILE GLU ASP SER GLU THR ALA ASP LEU LYS SER LEU
SEQRES 3 C 288 ALA LYS ARG ILE TYR GLU ALA TYR LEU LYS ASN PHE ASN
SEQRES 4 C 288 MET ASN LYS VAL LYS ALA ARG VAL ILE LEU SER GLY LYS
SEQRES 5 C 288 ALA SER ASN ASN PRO PRO PHE VAL ILE HIS ASP MET GLU
SEQRES 6 C 288 THR LEU CYS MET ALA GLU LYS THR LEU VAL ALA LYS LEU
SEQRES 7 C 288 VAL ALA ASN GLY ILE GLN ASN LYS GLU ALA GLU VAL ARG
SEQRES 8 C 288 ILE PHE HIS CYS CYS GLN CYS THR SER VAL GLU THR VAL
SEQRES 9 C 288 THR GLU LEU THR GLU PHE ALA LYS ALA ILE PRO GLY PHE
SEQRES 10 C 288 ALA ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS
SEQRES 11 C 288 TYR GLY VAL TYR GLU ALA ILE PHE ALA MET LEU SER SER
SEQRES 12 C 288 VAL MET ASN LYS ASP GLY MET LEU VAL ALA TYR GLY ASN
SEQRES 13 C 288 GLY PHE ILE THR ARG GLU PHE LEU LYS SER LEU ARG LYS
SEQRES 14 C 288 PRO PHE CYS ASP ILE MET GLU PRO LYS PHE ASP PHE ALA
SEQRES 15 C 288 MET LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP ILE
SEQRES 16 C 288 SER LEU PHE VAL ALA ALA ILE ILE CYS CYS GLY ASP ARG
SEQRES 17 C 288 PRO GLY LEU LEU ASN VAL GLY HIS ILE GLU LYS MET GLN
SEQRES 18 C 288 GLU GLY ILE VAL HIS VAL LEU ARG LEU HIS LEU GLN SER
SEQRES 19 C 288 ASN HIS PRO ASP ASP ILE PHE LEU PHE PRO LYS LEU LEU
SEQRES 20 C 288 GLN LYS MET ALA ASP LEU ARG GLN LEU VAL THR GLU HIS
SEQRES 21 C 288 ALA GLN LEU VAL GLN ILE ILE LYS LYS THR GLU SER ASP
SEQRES 22 C 288 ALA ALA LEU HIS PRO LEU LEU GLN GLU ILE TYR ARG ASP
SEQRES 23 C 288 MET TYR
SEQRES 1 D 21 HIS SER SER LEU THR GLU ARG HIS LYS ILE LEU HIS ARG
SEQRES 2 D 21 LEU LEU GLN GLU GLY SER PRO SER
SEQRES 1 E 288 MET LYS LYS GLY HIS HIS HIS HIS HIS HIS GLY GLU HIS
SEQRES 2 E 288 ASP ILE GLU ASP SER GLU THR ALA ASP LEU LYS SER LEU
SEQRES 3 E 288 ALA LYS ARG ILE TYR GLU ALA TYR LEU LYS ASN PHE ASN
SEQRES 4 E 288 MET ASN LYS VAL LYS ALA ARG VAL ILE LEU SER GLY LYS
SEQRES 5 E 288 ALA SER ASN ASN PRO PRO PHE VAL ILE HIS ASP MET GLU
SEQRES 6 E 288 THR LEU CYS MET ALA GLU LYS THR LEU VAL ALA LYS LEU
SEQRES 7 E 288 VAL ALA ASN GLY ILE GLN ASN LYS GLU ALA GLU VAL ARG
SEQRES 8 E 288 ILE PHE HIS CYS CYS GLN CYS THR SER VAL GLU THR VAL
SEQRES 9 E 288 THR GLU LEU THR GLU PHE ALA LYS ALA ILE PRO GLY PHE
SEQRES 10 E 288 ALA ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS
SEQRES 11 E 288 TYR GLY VAL TYR GLU ALA ILE PHE ALA MET LEU SER SER
SEQRES 12 E 288 VAL MET ASN LYS ASP GLY MET LEU VAL ALA TYR GLY ASN
SEQRES 13 E 288 GLY PHE ILE THR ARG GLU PHE LEU LYS SER LEU ARG LYS
SEQRES 14 E 288 PRO PHE CYS ASP ILE MET GLU PRO LYS PHE ASP PHE ALA
SEQRES 15 E 288 MET LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP ILE
SEQRES 16 E 288 SER LEU PHE VAL ALA ALA ILE ILE CYS CYS GLY ASP ARG
SEQRES 17 E 288 PRO GLY LEU LEU ASN VAL GLY HIS ILE GLU LYS MET GLN
SEQRES 18 E 288 GLU GLY ILE VAL HIS VAL LEU ARG LEU HIS LEU GLN SER
SEQRES 19 E 288 ASN HIS PRO ASP ASP ILE PHE LEU PHE PRO LYS LEU LEU
SEQRES 20 E 288 GLN LYS MET ALA ASP LEU ARG GLN LEU VAL THR GLU HIS
SEQRES 21 E 288 ALA GLN LEU VAL GLN ILE ILE LYS LYS THR GLU SER ASP
SEQRES 22 E 288 ALA ALA LEU HIS PRO LEU LEU GLN GLU ILE TYR ARG ASP
SEQRES 23 E 288 MET TYR
SEQRES 1 F 21 HIS SER SER LEU THR GLU ARG HIS LYS ILE LEU HIS ARG
SEQRES 2 F 21 LEU LEU GLN GLU GLY SER PRO SER
SEQRES 1 G 288 MET LYS LYS GLY HIS HIS HIS HIS HIS HIS GLY GLU HIS
SEQRES 2 G 288 ASP ILE GLU ASP SER GLU THR ALA ASP LEU LYS SER LEU
SEQRES 3 G 288 ALA LYS ARG ILE TYR GLU ALA TYR LEU LYS ASN PHE ASN
SEQRES 4 G 288 MET ASN LYS VAL LYS ALA ARG VAL ILE LEU SER GLY LYS
SEQRES 5 G 288 ALA SER ASN ASN PRO PRO PHE VAL ILE HIS ASP MET GLU
SEQRES 6 G 288 THR LEU CYS MET ALA GLU LYS THR LEU VAL ALA LYS LEU
SEQRES 7 G 288 VAL ALA ASN GLY ILE GLN ASN LYS GLU ALA GLU VAL ARG
SEQRES 8 G 288 ILE PHE HIS CYS CYS GLN CYS THR SER VAL GLU THR VAL
SEQRES 9 G 288 THR GLU LEU THR GLU PHE ALA LYS ALA ILE PRO GLY PHE
SEQRES 10 G 288 ALA ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS
SEQRES 11 G 288 TYR GLY VAL TYR GLU ALA ILE PHE ALA MET LEU SER SER
SEQRES 12 G 288 VAL MET ASN LYS ASP GLY MET LEU VAL ALA TYR GLY ASN
SEQRES 13 G 288 GLY PHE ILE THR ARG GLU PHE LEU LYS SER LEU ARG LYS
SEQRES 14 G 288 PRO PHE CYS ASP ILE MET GLU PRO LYS PHE ASP PHE ALA
SEQRES 15 G 288 MET LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP ILE
SEQRES 16 G 288 SER LEU PHE VAL ALA ALA ILE ILE CYS CYS GLY ASP ARG
SEQRES 17 G 288 PRO GLY LEU LEU ASN VAL GLY HIS ILE GLU LYS MET GLN
SEQRES 18 G 288 GLU GLY ILE VAL HIS VAL LEU ARG LEU HIS LEU GLN SER
SEQRES 19 G 288 ASN HIS PRO ASP ASP ILE PHE LEU PHE PRO LYS LEU LEU
SEQRES 20 G 288 GLN LYS MET ALA ASP LEU ARG GLN LEU VAL THR GLU HIS
SEQRES 21 G 288 ALA GLN LEU VAL GLN ILE ILE LYS LYS THR GLU SER ASP
SEQRES 22 G 288 ALA ALA LEU HIS PRO LEU LEU GLN GLU ILE TYR ARG ASP
SEQRES 23 G 288 MET TYR
SEQRES 1 H 21 HIS SER SER LEU THR GLU ARG HIS LYS ILE LEU HIS ARG
SEQRES 2 H 21 LEU LEU GLN GLU GLY SER PRO SER
HET 544 A 469 38
HET YT3 C 469 1
HET 544 C 470 38
HET YT3 E 469 1
HET 544 E 501 38
HET 544 G 601 38
HETNAM 544 2-(1-METHYL-3-OXO-3-PHENYL-PROPYLAMINO)-3-{4-[2-(5-
HETNAM 2 544 METHYL-2-PHENYL-OXAZOL-4-YL)-ETHOXY]-PHENYL}-PROPIONIC
HETNAM 3 544 ACID
HETNAM YT3 YTTRIUM (III) ION
HETSYN 544 GW409544
FORMUL 9 544 4(C31 H30 N2 O5)
FORMUL 10 YT3 2(Y 3+)
FORMUL 15 HOH *242(H2 O)
HELIX 1 1 LEU A 203 PHE A 218 1 16
HELIX 2 2 ASN A 221 LEU A 229 1 9
HELIX 3 3 ASP A 243 LEU A 254 1 12
HELIX 4 4 GLY A 262 LYS A 266 5 5
HELIX 5 5 GLU A 267 ALA A 293 1 27
HELIX 6 6 GLY A 296 LEU A 300 5 5
HELIX 7 7 ASP A 301 SER A 322 1 22
HELIX 8 8 ALA A 333 GLY A 335 5 3
HELIX 9 9 ARG A 341 SER A 346 1 6
HELIX 10 10 PRO A 350 ILE A 354 5 5
HELIX 11 11 MET A 355 LEU A 368 1 14
HELIX 12 12 ASP A 371 CYS A 384 1 14
HELIX 13 13 ASN A 393 HIS A 416 1 24
HELIX 14 14 PHE A 421 GLU A 451 1 31
HELIX 15 15 HIS A 457 ARG A 465 1 9
HELIX 16 16 HIS B 687 GLU B 696 1 10
HELIX 17 17 LYS C 204 PHE C 218 1 15
HELIX 18 18 ASN C 221 LEU C 229 1 9
HELIX 19 19 ASP C 243 LEU C 254 1 12
HELIX 20 20 GLU C 267 ALA C 293 1 27
HELIX 21 21 ASP C 301 SER C 323 1 23
HELIX 22 22 ALA C 333 GLY C 335 5 3
HELIX 23 23 ARG C 341 SER C 346 1 6
HELIX 24 24 PRO C 350 ILE C 354 5 5
HELIX 25 25 MET C 355 ALA C 367 1 13
HELIX 26 26 ASP C 371 CYS C 384 1 14
HELIX 27 27 ASN C 393 HIS C 416 1 24
HELIX 28 28 PHE C 421 LYS C 449 1 29
HELIX 29 29 HIS C 457 ARG C 465 1 9
HELIX 30 30 HIS D 687 LEU D 694 1 8
HELIX 31 31 LYS E 204 PHE E 218 1 15
HELIX 32 32 ASN E 221 LEU E 229 1 9
HELIX 33 33 ASP E 243 THR E 253 1 11
HELIX 34 34 GLU E 267 ALA E 293 1 27
HELIX 35 35 ASP E 301 SER E 322 1 22
HELIX 36 36 ARG E 341 SER E 346 1 6
HELIX 37 37 PRO E 350 ILE E 354 5 5
HELIX 38 38 MET E 355 ALA E 367 1 13
HELIX 39 39 ASP E 371 CYS E 384 1 14
HELIX 40 40 ASN E 393 HIS E 416 1 24
HELIX 41 41 PHE E 421 GLU E 451 1 31
HELIX 42 42 HIS E 457 ARG E 465 1 9
HELIX 43 43 HIS F 687 GLU F 696 1 10
HELIX 44 44 LEU G 206 PHE G 218 1 13
HELIX 45 45 ASN G 221 LEU G 229 1 9
HELIX 46 46 ASP G 243 VAL G 255 1 13
HELIX 47 47 GLY G 262 LYS G 266 5 5
HELIX 48 48 GLU G 267 LYS G 292 1 26
HELIX 49 49 ASP G 301 SER G 323 1 23
HELIX 50 50 ARG G 341 SER G 346 1 6
HELIX 51 51 PRO G 350 ILE G 354 5 5
HELIX 52 52 MET G 355 ALA G 367 1 13
HELIX 53 53 ASP G 371 CYS G 384 1 14
HELIX 54 54 GLY G 395 HIS G 416 1 22
HELIX 55 55 PHE G 421 LYS G 449 1 29
HELIX 56 56 HIS G 457 ARG G 465 1 9
HELIX 57 57 HIS H 687 GLU H 696 1 10
SHEET 1 A 4 PHE A 239 ILE A 241 0
SHEET 2 A 4 GLY A 337 THR A 340 1 O PHE A 338 N ILE A 241
SHEET 3 A 4 GLY A 329 VAL A 332 -1 N MET A 330 O ILE A 339
SHEET 4 A 4 MET A 325 ASN A 326 -1 N ASN A 326 O GLY A 329
SHEET 1 B 4 PHE C 239 ILE C 241 0
SHEET 2 B 4 GLY C 337 THR C 340 1 O PHE C 338 N ILE C 241
SHEET 3 B 4 GLY C 329 VAL C 332 -1 N VAL C 332 O GLY C 337
SHEET 4 B 4 MET C 325 ASN C 326 -1 N ASN C 326 O GLY C 329
SHEET 1 C 4 PHE E 239 ILE E 241 0
SHEET 2 C 4 GLY E 337 THR E 340 1 O PHE E 338 N ILE E 241
SHEET 3 C 4 GLY E 329 VAL E 332 -1 N MET E 330 O ILE E 339
SHEET 4 C 4 MET E 325 ASN E 326 -1 N ASN E 326 O GLY E 329
SHEET 1 D 4 PHE G 239 ILE G 241 0
SHEET 2 D 4 GLY G 337 THR G 340 1 O PHE G 338 N ILE G 241
SHEET 3 D 4 GLY G 329 VAL G 332 -1 N VAL G 332 O GLY G 337
SHEET 4 D 4 MET G 325 ASN G 326 -1 N ASN G 326 O GLY G 329
CISPEP 1 LYS A 349 PRO A 350 0 -0.45
CISPEP 2 LYS C 349 PRO C 350 0 -0.28
CISPEP 3 LYS E 349 PRO E 350 0 0.01
CISPEP 4 LYS G 349 PRO G 350 0 0.16
SITE 1 AC1 6 GLU A 267 GLU A 451 ASP A 453 GLU C 267
SITE 2 AC1 6 GLU C 451 ASP C 453
SITE 1 AC2 6 GLU E 267 GLU E 451 ASP E 453 GLU G 267
SITE 2 AC2 6 GLU G 451 ASP G 453
SITE 1 AC3 12 PHE A 273 CYS A 275 CYS A 276 SER A 280
SITE 2 AC3 12 TYR A 314 LEU A 321 VAL A 332 PHE A 351
SITE 3 AC3 12 ILE A 354 MET A 355 HIS A 440 TYR A 464
SITE 1 AC4 17 LEU C 247 GLU C 269 PHE C 273 CYS C 275
SITE 2 AC4 17 CYS C 276 GLN C 277 SER C 280 TYR C 314
SITE 3 AC4 17 MET C 330 VAL C 332 LEU C 347 PHE C 351
SITE 4 AC4 17 ILE C 354 HIS C 440 VAL C 444 TYR C 464
SITE 5 AC4 17 HOH C 527
SITE 1 AC5 14 GLU E 269 PHE E 273 CYS E 275 CYS E 276
SITE 2 AC5 14 SER E 280 TYR E 314 MET E 330 VAL E 332
SITE 3 AC5 14 PHE E 351 ILE E 354 MET E 355 HIS E 440
SITE 4 AC5 14 LEU E 460 TYR E 464
SITE 1 AC6 18 LEU G 247 ILE G 272 PHE G 273 CYS G 275
SITE 2 AC6 18 CYS G 276 THR G 279 SER G 280 TYR G 314
SITE 3 AC6 18 LEU G 321 MET G 330 VAL G 332 LEU G 347
SITE 4 AC6 18 PHE G 351 ILE G 354 MET G 355 HIS G 440
SITE 5 AC6 18 LEU G 460 TYR G 464
CRYST1 95.561 121.597 121.994 90.00 90.00 90.00 P 21 21 21 16
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 0.010465 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008224 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008197 0.00000
(ATOM LINES ARE NOT SHOWN.)
END