HEADER PROTEIN BINDING/ACTIVATOR 03-DEC-16 5U3T
TITLE HUMAN PPARDELTA LIGAND-BINDING DOMAIN IN COMPLEXED WITH SPECIFIC
TITLE 2 AGONIST 4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR DELTA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PPAR-DELTA,NUCI,NUCLEAR HORMONE RECEPTOR 1,NUC1,NUCLEAR
COMPND 5 RECEPTOR SUBFAMILY 1 GROUP C MEMBER 2,PEROXISOME PROLIFERATOR-
COMPND 6 ACTIVATED RECEPTOR BETA,PPAR-BETA;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: LIGAND-BINDING DOMAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PPARD, NR1C2, PPARB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A(+)
KEYWDS PPARDELTA, LIGAND-BINDING DOMAIN, AGONIST, PROTEIN BINDING-ACTIVATOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.-C.WU,T.J.BAIGA,M.DOWNES,J.J.LA CLAIR,A.R.ATKINS,S.B.RICHARD,
AUTHOR 2 T.A.STOCKLEY-NOEL,M.E.BOWMAN,R.M.EVANS,J.P.NOEL
REVDAT 5 04-OCT-23 5U3T 1 HETSYN
REVDAT 4 29-JUL-20 5U3T 1 COMPND REMARK HETNAM SITE
REVDAT 4 2 1 ATOM
REVDAT 3 05-APR-17 5U3T 1 JRNL
REVDAT 2 29-MAR-17 5U3T 1 JRNL
REVDAT 1 22-MAR-17 5U3T 0
JRNL AUTH C.C.WU,T.J.BAIGA,M.DOWNES,J.J.LA CLAIR,A.R.ATKINS,
JRNL AUTH 2 S.B.RICHARD,W.FAN,T.A.STOCKLEY-NOEL,M.E.BOWMAN,J.P.NOEL,
JRNL AUTH 3 R.M.EVANS
JRNL TITL STRUCTURAL BASIS FOR SPECIFIC LIGATION OF THE PEROXISOME
JRNL TITL 2 PROLIFERATOR-ACTIVATED RECEPTOR DELTA.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 E2563 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28320959
JRNL DOI 10.1073/PNAS.1621513114
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9PRE_1665
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 72343
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.670
REMARK 3 FREE R VALUE TEST SET COUNT : 1929
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 47.7658 - 4.0965 0.98 5409 137 0.1403 0.1596
REMARK 3 2 4.0965 - 3.2517 1.00 5370 171 0.1471 0.1700
REMARK 3 3 3.2517 - 2.8407 1.00 5383 122 0.1756 0.2535
REMARK 3 4 2.8407 - 2.5810 1.00 5385 156 0.1752 0.2055
REMARK 3 5 2.5810 - 2.3960 1.00 5383 148 0.1681 0.2394
REMARK 3 6 2.3960 - 2.2548 0.99 5328 144 0.1675 0.2117
REMARK 3 7 2.2548 - 2.1419 0.99 5341 141 0.1874 0.2388
REMARK 3 8 2.1419 - 2.0486 0.99 5339 141 0.1942 0.2228
REMARK 3 9 2.0486 - 1.9698 0.98 5249 157 0.2207 0.2917
REMARK 3 10 1.9698 - 1.9018 0.97 5169 146 0.2639 0.2954
REMARK 3 11 1.9018 - 1.8423 0.97 5268 133 0.2947 0.3655
REMARK 3 12 1.8423 - 1.7896 0.95 5013 151 0.3226 0.3635
REMARK 3 13 1.7896 - 1.7425 0.77 4163 104 0.3496 0.3902
REMARK 3 14 1.7425 - 1.7000 0.49 2614 78 0.3616 0.3361
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.530
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.012 4944
REMARK 3 ANGLE : 1.448 6669
REMARK 3 CHIRALITY : 0.054 742
REMARK 3 PLANARITY : 0.006 841
REMARK 3 DIHEDRAL : 14.196 1847
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND ( RESID 170:440 OR RESID 501:508 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.0022 5.1883 125.5684
REMARK 3 T TENSOR
REMARK 3 T11: 0.0987 T22: 0.1098
REMARK 3 T33: 0.1379 T12: 0.0109
REMARK 3 T13: -0.0236 T23: 0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 1.2165 L22: 1.2663
REMARK 3 L33: 2.3953 L12: 0.0836
REMARK 3 L13: -0.4176 L23: -0.6234
REMARK 3 S TENSOR
REMARK 3 S11: -0.0002 S12: -0.0670 S13: -0.0429
REMARK 3 S21: -0.0759 S22: -0.0400 S23: -0.0709
REMARK 3 S31: 0.0058 S32: 0.1741 S33: 0.0072
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN B AND ( RESID 173:441 OR RESID 501:512 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.9911 43.2492 113.4946
REMARK 3 T TENSOR
REMARK 3 T11: 0.1934 T22: 0.1673
REMARK 3 T33: 0.1586 T12: -0.0150
REMARK 3 T13: 0.0049 T23: -0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.9708 L22: 0.8627
REMARK 3 L33: 4.0101 L12: 0.1156
REMARK 3 L13: -0.2997 L23: -0.8200
REMARK 3 S TENSOR
REMARK 3 S11: 0.0579 S12: 0.0280 S13: 0.0829
REMARK 3 S21: -0.0379 S22: 0.0345 S23: -0.0047
REMARK 3 S31: -0.2044 S32: 0.3069 S33: -0.0731
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5U3T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1000225263.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5 - 8.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72951
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 94.690
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 48.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1GWZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BIS-TRIS PROPANE, POTASSIUM CHLORIDE,
REMARK 280 PEG 8000, 1,2-PROPANDIOL, EDTA, DTT, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277.15K
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 47.34500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 TYR A 441
REMARK 465 PRO B 170
REMARK 465 GLN B 171
REMARK 465 VAL B 172
REMARK 465 ALA B 205
REMARK 465 SER B 206
REMARK 465 HIS B 207
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 HE2 HIS A 413 O2 7UY A 501 1.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 424 68.18 -118.28
REMARK 500 ASN B 366 77.83 -101.48
REMARK 500 GLU B 424 63.10 -101.58
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 807 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH B 744 DISTANCE = 5.94 ANGSTROMS
DBREF 5U3T A 170 441 UNP Q03181 PPARD_HUMAN 72 343
DBREF 5U3T B 170 441 UNP Q03181 PPARD_HUMAN 72 343
SEQRES 1 A 272 PRO GLN VAL ALA ASP LEU LYS ALA PHE SER LYS HIS ILE
SEQRES 2 A 272 TYR ASN ALA TYR LEU LYS ASN PHE ASN MET THR LYS LYS
SEQRES 3 A 272 LYS ALA ARG SER ILE LEU THR GLY LYS ALA SER HIS THR
SEQRES 4 A 272 ALA PRO PHE VAL ILE HIS ASP ILE GLU THR LEU TRP GLN
SEQRES 5 A 272 ALA GLU LYS GLY LEU VAL TRP LYS GLN LEU VAL ASN GLY
SEQRES 6 A 272 LEU PRO PRO TYR LYS GLU ILE SER VAL HIS VAL PHE TYR
SEQRES 7 A 272 ARG CYS GLN CME THR THR VAL GLU THR VAL ARG GLU LEU
SEQRES 8 A 272 THR GLU PHE ALA LYS SER ILE PRO SER PHE SER SER LEU
SEQRES 9 A 272 PHE LEU ASN ASP GLN VAL THR LEU LEU LYS TYR GLY VAL
SEQRES 10 A 272 HIS GLU ALA ILE PHE ALA MET LEU ALA SER ILE VAL ASN
SEQRES 11 A 272 LYS ASP GLY LEU LEU VAL ALA ASN GLY SER GLY PHE VAL
SEQRES 12 A 272 THR ARG GLU PHE LEU ARG SER LEU ARG LYS PRO PHE SER
SEQRES 13 A 272 ASP ILE ILE GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE
SEQRES 14 A 272 ASN ALA LEU GLU LEU ASP ASP SER ASP LEU ALA LEU PHE
SEQRES 15 A 272 ILE ALA ALA ILE ILE LEU CYS GLY ASP ARG PRO GLY LEU
SEQRES 16 A 272 MET ASN VAL PRO ARG VAL GLU ALA ILE GLN ASP THR ILE
SEQRES 17 A 272 LEU ARG ALA LEU GLU PHE HIS LEU GLN ALA ASN HIS PRO
SEQRES 18 A 272 ASP ALA GLN TYR LEU PHE PRO LYS LEU LEU GLN LYS MET
SEQRES 19 A 272 ALA ASP LEU ARG GLN LEU VAL THR GLU HIS ALA GLN MET
SEQRES 20 A 272 MET GLN ARG ILE LYS LYS THR GLU THR GLU THR SER LEU
SEQRES 21 A 272 HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP MET TYR
SEQRES 1 B 272 PRO GLN VAL ALA ASP LEU LYS ALA PHE SER LYS HIS ILE
SEQRES 2 B 272 TYR ASN ALA TYR LEU LYS ASN PHE ASN MET THR LYS LYS
SEQRES 3 B 272 LYS ALA ARG SER ILE LEU THR GLY LYS ALA SER HIS THR
SEQRES 4 B 272 ALA PRO PHE VAL ILE HIS ASP ILE GLU THR LEU TRP GLN
SEQRES 5 B 272 ALA GLU LYS GLY LEU VAL TRP LYS GLN LEU VAL ASN GLY
SEQRES 6 B 272 LEU PRO PRO TYR LYS GLU ILE SER VAL HIS VAL PHE TYR
SEQRES 7 B 272 ARG CYS GLN CME THR THR VAL GLU THR VAL ARG GLU LEU
SEQRES 8 B 272 THR GLU PHE ALA LYS SER ILE PRO SER PHE SER SER LEU
SEQRES 9 B 272 PHE LEU ASN ASP GLN VAL THR LEU LEU LYS TYR GLY VAL
SEQRES 10 B 272 HIS GLU ALA ILE PHE ALA MET LEU ALA SER ILE VAL ASN
SEQRES 11 B 272 LYS ASP GLY LEU LEU VAL ALA ASN GLY SER GLY PHE VAL
SEQRES 12 B 272 THR ARG GLU PHE LEU ARG SER LEU ARG LYS PRO PHE SER
SEQRES 13 B 272 ASP ILE ILE GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE
SEQRES 14 B 272 ASN ALA LEU GLU LEU ASP ASP SER ASP LEU ALA LEU PHE
SEQRES 15 B 272 ILE ALA ALA ILE ILE LEU CYS GLY ASP ARG PRO GLY LEU
SEQRES 16 B 272 MET ASN VAL PRO ARG VAL GLU ALA ILE GLN ASP THR ILE
SEQRES 17 B 272 LEU ARG ALA LEU GLU PHE HIS LEU GLN ALA ASN HIS PRO
SEQRES 18 B 272 ASP ALA GLN TYR LEU PHE PRO LYS LEU LEU GLN LYS MET
SEQRES 19 B 272 ALA ASP LEU ARG GLN LEU VAL THR GLU HIS ALA GLN MET
SEQRES 20 B 272 MET GLN ARG ILE LYS LYS THR GLU THR GLU THR SER LEU
SEQRES 21 B 272 HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP MET TYR
MODRES 5U3T CME A 251 CYS MODIFIED RESIDUE
MODRES 5U3T CME B 251 CYS MODIFIED RESIDUE
HET CME A 251 18
HET CME B 251 18
HET 7UY A 501 126
HET B7G A 502 45
HET PGO A 503 26
HET PGO A 504 26
HET PGO A 505 13
HET PEG A 506 17
HET PGO A 507 13
HET PEG A 508 17
HET 7UY B 501 126
HET B7G B 502 45
HET PGE B 503 24
HET PGO B 504 26
HET PEG B 505 17
HET PEG B 506 17
HET PEG B 507 17
HET PGO B 508 13
HET PGO B 509 13
HET PEG B 510 17
HET PGO B 511 13
HET PGO B 512 13
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM 7UY 6-[2-({(PROPAN-2-YL)[4-(THIOPHEN-3-YL)BENZENE-1-
HETNAM 2 7UY CARBONYL]AMINO}METHYL)PHENOXY]HEXANOIC ACID
HETNAM B7G HEPTYL BETA-D-GLUCOPYRANOSIDE
HETNAM PGO S-1,2-PROPANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN B7G HEPTYL-BETA-D-GLUCOPYRANOSIDE; HEPTYL BETA-D-GLUCOSIDE;
HETSYN 2 B7G HEPTYL D-GLUCOSIDE; HEPTYL GLUCOSIDE
FORMUL 1 CME 2(C5 H11 N O3 S2)
FORMUL 3 7UY 2(C27 H31 N O4 S)
FORMUL 4 B7G 2(C13 H26 O6)
FORMUL 5 PGO 9(C3 H8 O2)
FORMUL 8 PEG 6(C4 H10 O3)
FORMUL 13 PGE C6 H14 O4
FORMUL 23 HOH *351(H2 O)
HELIX 1 AA1 PRO A 170 PHE A 190 1 21
HELIX 2 AA2 THR A 193 THR A 202 1 10
HELIX 3 AA3 ASP A 215 LEU A 226 1 12
HELIX 4 AA4 LEU A 231 LEU A 235 5 5
HELIX 5 AA5 GLU A 240 SER A 266 1 27
HELIX 6 AA6 ILE A 267 SER A 272 1 6
HELIX 7 AA7 PHE A 274 ALA A 295 1 22
HELIX 8 AA8 ARG A 314 SER A 319 1 6
HELIX 9 AA9 PRO A 323 ALA A 340 1 18
HELIX 10 AB1 ASP A 344 LEU A 357 1 14
HELIX 11 AB2 ASN A 366 HIS A 389 1 24
HELIX 12 AB3 TYR A 394 GLU A 424 1 31
HELIX 13 AB4 HIS A 430 LYS A 438 1 9
HELIX 14 AB5 ASP B 174 PHE B 190 1 17
HELIX 15 AB6 THR B 193 THR B 202 1 10
HELIX 16 AB7 ASP B 215 LEU B 226 1 12
HELIX 17 AB8 LEU B 231 LEU B 235 5 5
HELIX 18 AB9 GLU B 240 SER B 266 1 27
HELIX 19 AC1 ILE B 267 SER B 272 1 6
HELIX 20 AC2 PHE B 274 ALA B 295 1 22
HELIX 21 AC3 ARG B 314 SER B 319 1 6
HELIX 22 AC4 PRO B 323 ALA B 340 1 18
HELIX 23 AC5 ASP B 344 LEU B 357 1 14
HELIX 24 AC6 ASN B 366 HIS B 389 1 24
HELIX 25 AC7 TYR B 394 GLU B 424 1 31
HELIX 26 AC8 HIS B 430 LYS B 438 1 9
SHEET 1 AA1 4 PHE A 211 ILE A 213 0
SHEET 2 AA1 4 GLY A 310 THR A 313 1 O PHE A 311 N ILE A 213
SHEET 3 AA1 4 GLY A 302 VAL A 305 -1 N LEU A 303 O VAL A 312
SHEET 4 AA1 4 VAL A 298 ASN A 299 -1 N ASN A 299 O GLY A 302
SHEET 1 AA2 4 PHE B 211 ILE B 213 0
SHEET 2 AA2 4 GLY B 310 THR B 313 1 O PHE B 311 N ILE B 213
SHEET 3 AA2 4 GLY B 302 VAL B 305 -1 N LEU B 303 O VAL B 312
SHEET 4 AA2 4 VAL B 298 ASN B 299 -1 N ASN B 299 O GLY B 302
LINK C GLN A 250 N CME A 251 1555 1555 1.33
LINK C CME A 251 N THR A 252 1555 1555 1.33
LINK C GLN B 250 N CME B 251 1555 1555 1.34
LINK C CME B 251 N THR B 252 1555 1555 1.32
CISPEP 1 LYS A 322 PRO A 323 0 5.33
CISPEP 2 LYS B 322 PRO B 323 0 4.47
CRYST1 39.640 94.690 96.430 90.00 97.99 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 0.025227 0.000000 0.003541 0.00000
SCALE2 0.000000 0.010561 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010472 0.00000
(ATOM LINES ARE NOT SHOWN.)
END