HEADER TRANSCRIPTION/TRANSCRIPTION INHIBITOR 17-MAY-18 6DGQ
TITLE CRYSTAL STRUCTURE OF HUMAN PPARGAMMA LIGAND BINDING DOMAIN IN COMPLEX
TITLE 2 WITH CAY10506
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PPAR-GAMMA,NUCLEAR RECEPTOR SUBFAMILY 1 GROUP C MEMBER 3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PPARG, NR1C3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET46
KEYWDS NUCLEAR RECEPTORS, TZDS, DRUG DESIGN, THERAPEUTIC TARGETS,
KEYWDS 2 TRANSCRIPTION, TRANSCRIPTION-TRANSCRIPTION INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SHANG,D.J.KOJETIN
REVDAT 4 11-OCT-23 6DGQ 1 REMARK
REVDAT 3 25-DEC-19 6DGQ 1 REMARK
REVDAT 2 06-NOV-19 6DGQ 1 JRNL
REVDAT 1 22-MAY-19 6DGQ 0
JRNL AUTH J.SHANG,R.BRUST,P.R.GRIFFIN,T.M.KAMENECKA,D.J.KOJETIN
JRNL TITL QUANTITATIVE STRUCTURAL ASSESSMENT OF GRADED RECEPTOR
JRNL TITL 2 AGONISM.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 116 22179 2019
JRNL REFN ESSN 1091-6490
JRNL PMID 31611383
JRNL DOI 10.1073/PNAS.1909016116
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 22237
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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 47.7575 - 5.9018 0.98 1510 149 0.1842 0.1721
REMARK 3 2 5.9018 - 4.6857 0.98 1483 145 0.1801 0.2563
REMARK 3 3 4.6857 - 4.0938 0.98 1472 146 0.1569 0.1991
REMARK 3 4 4.0938 - 3.7196 0.98 1436 142 0.1712 0.2198
REMARK 3 5 3.7196 - 3.4531 0.97 1441 143 0.1801 0.2526
REMARK 3 6 3.4531 - 3.2496 0.97 1447 143 0.1866 0.2498
REMARK 3 7 3.2496 - 3.0869 0.97 1438 142 0.2099 0.2821
REMARK 3 8 3.0869 - 2.9525 0.97 1443 142 0.2279 0.3324
REMARK 3 9 2.9525 - 2.8389 0.97 1428 141 0.2134 0.2702
REMARK 3 10 2.8389 - 2.7409 0.97 1420 141 0.2148 0.2932
REMARK 3 11 2.7409 - 2.6552 0.97 1450 143 0.2086 0.2866
REMARK 3 12 2.6552 - 2.5793 0.97 1410 139 0.2114 0.3307
REMARK 3 13 2.5793 - 2.5114 0.97 1421 141 0.2232 0.2661
REMARK 3 14 2.5114 - 2.4501 0.97 1439 142 0.2083 0.2580
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.510
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 : 0.008 4187
REMARK 3 ANGLE : 1.046 5637
REMARK 3 CHIRALITY : 0.052 653
REMARK 3 PLANARITY : 0.005 712
REMARK 3 DIHEDRAL : 5.572 2590
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6DGQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1000234573.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-AUG-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97741
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22240
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
REMARK 200 RESOLUTION RANGE LOW (A) : 45.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.890
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: 1PRG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M SODIUM CITRATE, 100MM TRIS, PH
REMARK 280 7.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 46.10000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.74500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.10000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.74500
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
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 GLY A 202
REMARK 465 GLN A 203
REMARK 465 LEU A 204
REMARK 465 ASN A 205
REMARK 465 PRO A 206
REMARK 465 LYS A 263
REMARK 465 PHE A 264
REMARK 465 LYS A 265
REMARK 465 HIS A 266
REMARK 465 ILE A 267
REMARK 465 THR A 268
REMARK 465 PRO A 269
REMARK 465 LEU A 270
REMARK 465 GLN A 271
REMARK 465 GLU A 272
REMARK 465 GLN A 273
REMARK 465 SER A 274
REMARK 465 ARG A 357
REMARK 465 TYR A 477
REMARK 465 GLY B 202
REMARK 465 GLN B 203
REMARK 465 LEU B 204
REMARK 465 ASN B 205
REMARK 465 PRO B 206
REMARK 465 LYS B 263
REMARK 465 PHE B 264
REMARK 465 LYS B 265
REMARK 465 HIS B 266
REMARK 465 ILE B 267
REMARK 465 THR B 268
REMARK 465 PRO B 269
REMARK 465 LEU B 270
REMARK 465 GLN B 271
REMARK 465 GLU B 272
REMARK 465 GLN B 273
REMARK 465 SER B 274
REMARK 465 THR B 461
REMARK 465 ASP B 462
REMARK 465 MET B 463
REMARK 465 SER B 464
REMARK 465 LEU B 465
REMARK 465 TYR B 477
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 LYS A 244 -176.20 -69.00
REMARK 500 ASP A 475 104.64 -51.42
REMARK 500 SER B 208 1.78 -63.58
REMARK 500 LEU B 237 -96.84 -64.10
REMARK 500 LYS B 240 -71.12 -82.72
REMARK 500 THR B 241 72.83 36.90
REMARK 500 THR B 242 37.07 -82.92
REMARK 500 SER B 355 2.42 -68.82
REMARK 500 ARG B 357 -127.21 -73.35
REMARK 500 LYS B 358 -86.89 -59.50
REMARK 500 LYS B 458 34.21 -91.28
REMARK 500 TYR B 473 76.35 -102.07
REMARK 500 ASP B 475 -38.92 -171.50
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 B 586 DISTANCE = 6.59 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GBV A 501
DBREF 6DGQ A 203 477 UNP P37231 PPARG_HUMAN 231 505
DBREF 6DGQ B 203 477 UNP P37231 PPARG_HUMAN 231 505
SEQADV 6DGQ GLY A 202 UNP P37231 EXPRESSION TAG
SEQADV 6DGQ GLY B 202 UNP P37231 EXPRESSION TAG
SEQRES 1 A 276 GLY GLN LEU ASN PRO GLU SER ALA ASP LEU ARG ALA LEU
SEQRES 2 A 276 ALA LYS HIS LEU TYR ASP SER TYR ILE LYS SER PHE PRO
SEQRES 3 A 276 LEU THR LYS ALA LYS ALA ARG ALA ILE LEU THR GLY LYS
SEQRES 4 A 276 THR THR ASP LYS SER PRO PHE VAL ILE TYR ASP MET ASN
SEQRES 5 A 276 SER LEU MET MET GLY GLU ASP LYS ILE LYS PHE LYS HIS
SEQRES 6 A 276 ILE THR PRO LEU GLN GLU GLN SER LYS GLU VAL ALA ILE
SEQRES 7 A 276 ARG ILE PHE GLN GLY CYS GLN PHE ARG SER VAL GLU ALA
SEQRES 8 A 276 VAL GLN GLU ILE THR GLU TYR ALA LYS SER ILE PRO GLY
SEQRES 9 A 276 PHE VAL ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU
SEQRES 10 A 276 LYS TYR GLY VAL HIS GLU ILE ILE TYR THR MET LEU ALA
SEQRES 11 A 276 SER LEU MET ASN LYS ASP GLY VAL LEU ILE SER GLU GLY
SEQRES 12 A 276 GLN GLY PHE MET THR ARG GLU PHE LEU LYS SER LEU ARG
SEQRES 13 A 276 LYS PRO PHE GLY ASP PHE MET GLU PRO LYS PHE GLU PHE
SEQRES 14 A 276 ALA VAL LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP
SEQRES 15 A 276 LEU ALA ILE PHE ILE ALA VAL ILE ILE LEU SER GLY ASP
SEQRES 16 A 276 ARG PRO GLY LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE
SEQRES 17 A 276 GLN ASP ASN LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS
SEQRES 18 A 276 LEU ASN HIS PRO GLU SER SER GLN LEU PHE ALA LYS LEU
SEQRES 19 A 276 LEU GLN LYS MET THR ASP LEU ARG GLN ILE VAL THR GLU
SEQRES 20 A 276 HIS VAL GLN LEU LEU GLN VAL ILE LYS LYS THR GLU THR
SEQRES 21 A 276 ASP MET SER LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS
SEQRES 22 A 276 ASP LEU TYR
SEQRES 1 B 276 GLY GLN LEU ASN PRO GLU SER ALA ASP LEU ARG ALA LEU
SEQRES 2 B 276 ALA LYS HIS LEU TYR ASP SER TYR ILE LYS SER PHE PRO
SEQRES 3 B 276 LEU THR LYS ALA LYS ALA ARG ALA ILE LEU THR GLY LYS
SEQRES 4 B 276 THR THR ASP LYS SER PRO PHE VAL ILE TYR ASP MET ASN
SEQRES 5 B 276 SER LEU MET MET GLY GLU ASP LYS ILE LYS PHE LYS HIS
SEQRES 6 B 276 ILE THR PRO LEU GLN GLU GLN SER LYS GLU VAL ALA ILE
SEQRES 7 B 276 ARG ILE PHE GLN GLY CYS GLN PHE ARG SER VAL GLU ALA
SEQRES 8 B 276 VAL GLN GLU ILE THR GLU TYR ALA LYS SER ILE PRO GLY
SEQRES 9 B 276 PHE VAL ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU
SEQRES 10 B 276 LYS TYR GLY VAL HIS GLU ILE ILE TYR THR MET LEU ALA
SEQRES 11 B 276 SER LEU MET ASN LYS ASP GLY VAL LEU ILE SER GLU GLY
SEQRES 12 B 276 GLN GLY PHE MET THR ARG GLU PHE LEU LYS SER LEU ARG
SEQRES 13 B 276 LYS PRO PHE GLY ASP PHE MET GLU PRO LYS PHE GLU PHE
SEQRES 14 B 276 ALA VAL LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP
SEQRES 15 B 276 LEU ALA ILE PHE ILE ALA VAL ILE ILE LEU SER GLY ASP
SEQRES 16 B 276 ARG PRO GLY LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE
SEQRES 17 B 276 GLN ASP ASN LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS
SEQRES 18 B 276 LEU ASN HIS PRO GLU SER SER GLN LEU PHE ALA LYS LEU
SEQRES 19 B 276 LEU GLN LYS MET THR ASP LEU ARG GLN ILE VAL THR GLU
SEQRES 20 B 276 HIS VAL GLN LEU LEU GLN VAL ILE LYS LYS THR GLU THR
SEQRES 21 B 276 ASP MET SER LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS
SEQRES 22 B 276 ASP LEU TYR
HET GBV A 501 29
HETNAM GBV N-(2-{4-[(2,4-DIOXO-3,4-DIHYDRO-2H-1LAMBDA~4~,3-
HETNAM 2 GBV THIAZOL-5-YL)METHYL]PHENOXY}ETHYL)-5-[(3R)-1,2-
HETNAM 3 GBV DITHIOLAN-3-YL]PENTANAMIDE
FORMUL 3 GBV C20 H26 N2 O4 S3
FORMUL 4 HOH *185(H2 O)
HELIX 1 AA1 GLU A 207 PHE A 226 1 20
HELIX 2 AA2 THR A 229 THR A 238 1 10
HELIX 3 AA3 ASP A 251 ILE A 262 1 12
HELIX 4 AA4 GLU A 276 SER A 302 1 27
HELIX 5 AA5 GLY A 305 LEU A 309 5 5
HELIX 6 AA6 ASP A 310 LEU A 333 1 24
HELIX 7 AA7 SER A 342 GLY A 344 5 3
HELIX 8 AA8 ARG A 350 SER A 355 1 6
HELIX 9 AA9 MET A 364 ALA A 376 1 13
HELIX 10 AB1 ASP A 380 LEU A 393 1 14
HELIX 11 AB2 ASN A 402 HIS A 425 1 24
HELIX 12 AB3 GLN A 430 GLU A 460 1 31
HELIX 13 AB4 HIS A 466 TYR A 473 1 8
HELIX 14 AB5 SER B 208 PHE B 226 1 19
HELIX 15 AB6 THR B 229 ALA B 235 1 7
HELIX 16 AB7 ASP B 251 ILE B 262 1 12
HELIX 17 AB8 GLU B 276 LYS B 301 1 26
HELIX 18 AB9 GLY B 305 LEU B 309 5 5
HELIX 19 AC1 ASP B 310 TYR B 320 1 11
HELIX 20 AC2 GLY B 321 SER B 332 1 12
HELIX 21 AC3 ARG B 350 SER B 355 1 6
HELIX 22 AC4 MET B 364 ALA B 376 1 13
HELIX 23 AC5 ASP B 380 LEU B 393 1 14
HELIX 24 AC6 ASN B 402 HIS B 425 1 24
HELIX 25 AC7 GLN B 430 ILE B 456 1 27
HELIX 26 AC8 LYS B 457 THR B 459 5 3
HELIX 27 AC9 PRO B 467 TYR B 473 1 7
SHEET 1 AA1 4 PHE A 247 ILE A 249 0
SHEET 2 AA1 4 GLY A 346 THR A 349 1 O PHE A 347 N ILE A 249
SHEET 3 AA1 4 GLY A 338 ILE A 341 -1 N VAL A 339 O MET A 348
SHEET 4 AA1 4 MET A 334 ASN A 335 -1 N ASN A 335 O GLY A 338
SHEET 1 AA2 4 PHE B 247 ILE B 249 0
SHEET 2 AA2 4 GLY B 346 THR B 349 1 O PHE B 347 N ILE B 249
SHEET 3 AA2 4 GLY B 338 ILE B 341 -1 N ILE B 341 O GLY B 346
SHEET 4 AA2 4 MET B 334 ASN B 335 -1 N ASN B 335 O GLY B 338
SITE 1 AC1 13 PHE A 282 GLY A 284 CYS A 285 SER A 289
SITE 2 AC1 13 HIS A 323 LEU A 330 ILE A 341 MET A 364
SITE 3 AC1 13 HIS A 449 LEU A 453 LEU A 469 TYR A 473
SITE 4 AC1 13 HOH A 671
CRYST1 92.200 59.490 116.730 90.00 103.55 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010846 0.000000 0.002614 0.00000
SCALE2 0.000000 0.016810 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008812 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
