HEADER TRANSCRIPTION 11-OCT-18 6IJR
TITLE HUMAN PPARGAMMA LIGAND BINDING DOMAIN COMPLEXED WITH SB1495
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: PPAR-GAMMA,NUCLEAR RECEPTOR SUBFAMILY 1 GROUP C MEMBER 3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: 16 MER PEPTIDE FROM NUCLEAR RECEPTOR COACTIVATOR 1;
COMPND 8 CHAIN: B, D;
COMPND 9 EC: 2.3.1.48;
COMPND 10 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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3);
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS TYPE 2 DIABETES, NUCLEAR RECEPTOR, INHIBITOR, LIGAND BINDING DOMAIN,
KEYWDS 2 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.Y.JANG,B.W.HAN
REVDAT 2 22-NOV-23 6IJR 1 REMARK
REVDAT 1 16-OCT-19 6IJR 0
JRNL AUTH J.Y.JANG,H.KIM,H.J.KIM,S.W.SUH,S.B.PARK,B.W.HAN
JRNL TITL STRUCTURAL BASIS FOR THE INHIBITORY EFFECTS OF A NOVEL
JRNL TITL 2 REVERSIBLE COVALENT LIGAND ON PPAR GAMMA PHOSPHORYLATION.
JRNL REF SCI REP V. 9 11168 2019
JRNL REFN ESSN 2045-2322
JRNL PMID 31371757
JRNL DOI 10.1038/S41598-019-47672-W
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 14528
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) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 777
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.92
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1034
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3460
REMARK 3 BIN FREE R VALUE SET COUNT : 49
REMARK 3 BIN FREE R VALUE : 0.4080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4691
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
REMARK 3 SOLVENT ATOMS : 24
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 87.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.25000
REMARK 3 B22 (A**2) : 3.36000
REMARK 3 B33 (A**2) : -6.60000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.444
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.382
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.764
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4863 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4729 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6557 ; 1.468 ; 2.007
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11021 ; 0.987 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 579 ; 5.533 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 214 ;36.215 ;25.421
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 936 ;13.687 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;16.915 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 757 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5179 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 895 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2328 ; 4.812 ; 8.665
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2327 ; 4.812 ; 8.662
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2903 ; 7.677 ;12.982
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2904 ; 7.676 ;12.985
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2535 ; 4.920 ; 9.192
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2533 ; 4.919 ; 9.188
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3654 ; 8.017 ;13.599
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5607 ;12.291 ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5605 ;12.293 ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6IJR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1300009324.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAY-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15503
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5GTO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 60% (V/V) TACSIMATE, PH 6.5, VAPOR
REMARK 280 DIFFUSION, SITTING 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 31.17950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.08050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.22550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.08050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.17950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.22550
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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: 1090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 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 ALA A 195
REMARK 465 GLU A 196
REMARK 465 GLU B 685
REMARK 465 ARG B 686
REMARK 465 GLU B 696
REMARK 465 GLY B 697
REMARK 465 SER B 698
REMARK 465 PRO B 699
REMARK 465 SER B 700
REMARK 465 GLU D 685
REMARK 465 ARG D 686
REMARK 465 GLY D 697
REMARK 465 SER D 698
REMARK 465 PRO D 699
REMARK 465 SER D 700
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 ASP A 251 -163.61 -166.85
REMARK 500 THR C 241 144.40 -172.52
REMARK 500 ASP C 260 -61.17 -99.69
REMARK 500 LEU D 694 0.09 -69.07
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 A9C A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide A9C C 501 and CYS C
REMARK 800 285
DBREF 6IJR A 195 477 UNP P37231 PPARG_HUMAN 223 505
DBREF 6IJR B 685 700 UNP Q15788 NCOA1_HUMAN 685 700
DBREF 6IJR C 195 477 UNP P37231 PPARG_HUMAN 223 505
DBREF 6IJR D 685 700 UNP Q15788 NCOA1_HUMAN 685 700
SEQRES 1 A 283 ALA GLU ILE SER SER ASP ILE ASP GLN LEU ASN PRO GLU
SEQRES 2 A 283 SER ALA ASP LEU ARG ALA LEU ALA LYS HIS LEU TYR ASP
SEQRES 3 A 283 SER TYR ILE LYS SER PHE PRO LEU THR LYS ALA LYS ALA
SEQRES 4 A 283 ARG ALA ILE LEU THR GLY LYS THR THR ASP LYS SER PRO
SEQRES 5 A 283 PHE VAL ILE TYR ASP MET ASN SER LEU MET MET GLY GLU
SEQRES 6 A 283 ASP LYS ILE LYS PHE LYS HIS ILE THR PRO LEU GLN GLU
SEQRES 7 A 283 GLN SER LYS GLU VAL ALA ILE ARG ILE PHE GLN GLY CYS
SEQRES 8 A 283 GLN PHE ARG SER VAL GLU ALA VAL GLN GLU ILE THR GLU
SEQRES 9 A 283 TYR ALA LYS SER ILE PRO GLY PHE VAL ASN LEU ASP LEU
SEQRES 10 A 283 ASN ASP GLN VAL THR LEU LEU LYS TYR GLY VAL HIS GLU
SEQRES 11 A 283 ILE ILE TYR THR MET LEU ALA SER LEU MET ASN LYS ASP
SEQRES 12 A 283 GLY VAL LEU ILE SER GLU GLY GLN GLY PHE MET THR ARG
SEQRES 13 A 283 GLU PHE LEU LYS SER LEU ARG LYS PRO PHE GLY ASP PHE
SEQRES 14 A 283 MET GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE ASN ALA
SEQRES 15 A 283 LEU GLU LEU ASP ASP SER ASP LEU ALA ILE PHE ILE ALA
SEQRES 16 A 283 VAL ILE ILE LEU SER GLY ASP ARG PRO GLY LEU LEU ASN
SEQRES 17 A 283 VAL LYS PRO ILE GLU ASP ILE GLN ASP ASN LEU LEU GLN
SEQRES 18 A 283 ALA LEU GLU LEU GLN LEU LYS LEU ASN HIS PRO GLU SER
SEQRES 19 A 283 SER GLN LEU PHE ALA LYS LEU LEU GLN LYS MET THR ASP
SEQRES 20 A 283 LEU ARG GLN ILE VAL THR GLU HIS VAL GLN LEU LEU GLN
SEQRES 21 A 283 VAL ILE LYS LYS THR GLU THR ASP MET SER LEU HIS PRO
SEQRES 22 A 283 LEU LEU GLN GLU ILE TYR LYS ASP LEU TYR
SEQRES 1 B 16 GLU ARG HIS LYS ILE LEU HIS ARG LEU LEU GLN GLU GLY
SEQRES 2 B 16 SER PRO SER
SEQRES 1 C 283 ALA GLU ILE SER SER ASP ILE ASP GLN LEU ASN PRO GLU
SEQRES 2 C 283 SER ALA ASP LEU ARG ALA LEU ALA LYS HIS LEU TYR ASP
SEQRES 3 C 283 SER TYR ILE LYS SER PHE PRO LEU THR LYS ALA LYS ALA
SEQRES 4 C 283 ARG ALA ILE LEU THR GLY LYS THR THR ASP LYS SER PRO
SEQRES 5 C 283 PHE VAL ILE TYR ASP MET ASN SER LEU MET MET GLY GLU
SEQRES 6 C 283 ASP LYS ILE LYS PHE LYS HIS ILE THR PRO LEU GLN GLU
SEQRES 7 C 283 GLN SER LYS GLU VAL ALA ILE ARG ILE PHE GLN GLY CYS
SEQRES 8 C 283 GLN PHE ARG SER VAL GLU ALA VAL GLN GLU ILE THR GLU
SEQRES 9 C 283 TYR ALA LYS SER ILE PRO GLY PHE VAL ASN LEU ASP LEU
SEQRES 10 C 283 ASN ASP GLN VAL THR LEU LEU LYS TYR GLY VAL HIS GLU
SEQRES 11 C 283 ILE ILE TYR THR MET LEU ALA SER LEU MET ASN LYS ASP
SEQRES 12 C 283 GLY VAL LEU ILE SER GLU GLY GLN GLY PHE MET THR ARG
SEQRES 13 C 283 GLU PHE LEU LYS SER LEU ARG LYS PRO PHE GLY ASP PHE
SEQRES 14 C 283 MET GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE ASN ALA
SEQRES 15 C 283 LEU GLU LEU ASP ASP SER ASP LEU ALA ILE PHE ILE ALA
SEQRES 16 C 283 VAL ILE ILE LEU SER GLY ASP ARG PRO GLY LEU LEU ASN
SEQRES 17 C 283 VAL LYS PRO ILE GLU ASP ILE GLN ASP ASN LEU LEU GLN
SEQRES 18 C 283 ALA LEU GLU LEU GLN LEU LYS LEU ASN HIS PRO GLU SER
SEQRES 19 C 283 SER GLN LEU PHE ALA LYS LEU LEU GLN LYS MET THR ASP
SEQRES 20 C 283 LEU ARG GLN ILE VAL THR GLU HIS VAL GLN LEU LEU GLN
SEQRES 21 C 283 VAL ILE LYS LYS THR GLU THR ASP MET SER LEU HIS PRO
SEQRES 22 C 283 LEU LEU GLN GLU ILE TYR LYS ASP LEU TYR
SEQRES 1 D 16 GLU ARG HIS LYS ILE LEU HIS ARG LEU LEU GLN GLU GLY
SEQRES 2 D 16 SER PRO SER
HET A9C A 501 42
HET A9C C 501 42
HETNAM A9C N-{[3-({[(1S,2R)-2-{[(2E)-2-CYANO-4,4-DIMETHYLPENT-2-
HETNAM 2 A9C ENOYL]AMINO}CYCLOPENTYL]OXY}METHYL)PHENYL]METHYL}-4-
HETNAM 3 A9C [(4-METHYLPIPERAZIN-1-YL)METHYL]BENZAMIDE
FORMUL 5 A9C 2(C34 H45 N5 O3)
FORMUL 7 HOH *24(H2 O)
HELIX 1 AA1 GLU A 207 PHE A 226 1 20
HELIX 2 AA2 THR A 229 GLY A 239 1 11
HELIX 3 AA3 ASP A 251 LYS A 261 1 11
HELIX 4 AA4 LEU A 270 LYS A 275 5 6
HELIX 5 AA5 GLU A 276 SER A 302 1 27
HELIX 6 AA6 ASP A 310 ALA A 331 1 22
HELIX 7 AA7 SER A 332 MET A 334 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 LYS A 474 1 9
HELIX 14 AB5 LYS B 688 LEU B 694 1 7
HELIX 15 AB6 GLU C 196 ILE C 201 1 6
HELIX 16 AB7 GLU C 207 PHE C 226 1 20
HELIX 17 AB8 THR C 229 GLY C 239 1 11
HELIX 18 AB9 ASP C 251 LYS C 261 1 11
HELIX 19 AC1 PRO C 269 SER C 274 1 6
HELIX 20 AC2 GLU C 276 ILE C 303 1 28
HELIX 21 AC3 ASP C 310 LEU C 333 1 24
HELIX 22 AC4 ARG C 350 SER C 355 1 6
HELIX 23 AC5 MET C 364 ALA C 376 1 13
HELIX 24 AC6 ASP C 380 LEU C 393 1 14
HELIX 25 AC7 ASN C 402 HIS C 425 1 24
HELIX 26 AC8 GLN C 430 GLU C 460 1 31
HELIX 27 AC9 HIS C 466 LYS C 474 1 9
HELIX 28 AD1 LYS D 688 LEU D 694 1 7
SHEET 1 AA1 3 PHE A 247 ILE A 249 0
SHEET 2 AA1 3 GLY A 346 THR A 349 1 O PHE A 347 N ILE A 249
SHEET 3 AA1 3 GLY A 338 ILE A 341 -1 N ILE A 341 O GLY A 346
SHEET 1 AA2 4 PHE C 247 ILE C 249 0
SHEET 2 AA2 4 GLY C 346 THR C 349 1 O PHE C 347 N ILE C 249
SHEET 3 AA2 4 GLY C 338 ILE C 341 -1 N ILE C 341 O GLY C 346
SHEET 4 AA2 4 MET C 334 ASN C 335 -1 N ASN C 335 O GLY C 338
LINK SG CYS A 285 CBA A9C A 501 1555 1555 1.78
LINK SG CYS C 285 CBA A9C C 501 1555 1555 1.79
CISPEP 1 LYS A 358 PRO A 359 0 9.89
CISPEP 2 LYS C 358 PRO C 359 0 15.50
SITE 1 AC1 13 HIS A 266 THR A 268 ILE A 281 PHE A 282
SITE 2 AC1 13 CYS A 285 ARG A 288 SER A 289 TYR A 327
SITE 3 AC1 13 LEU A 330 ILE A 341 SER A 342 LEU A 353
SITE 4 AC1 13 MET A 364
SITE 1 AC2 17 HIS C 266 THR C 268 ILE C 281 PHE C 282
SITE 2 AC2 17 GLN C 283 GLY C 284 GLN C 286 PHE C 287
SITE 3 AC2 17 ARG C 288 SER C 289 TYR C 327 LEU C 330
SITE 4 AC2 17 ILE C 341 SER C 342 LEU C 353 PHE C 363
SITE 5 AC2 17 MET C 364
CRYST1 62.359 62.451 162.161 90.00 90.00 90.00 P 21 21 21 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 0.016036 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016013 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006167 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
