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HEADER HYDROLASE 13-MAR-18 5ZHT
TITLE CRYSTAL STRUCTURE OF OSD14 IN COMPLEX WITH COVALENTLY BOUND KK073
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STRIGOLACTONE ESTERASE D14;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROTEIN DWARF 14,PROTEIN DWARF 88,PROTEIN HIGH-TILLERING
COMPND 5 DWARF 2;
COMPND 6 EC: 3.1.-.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYZA SATIVA SUBSP. JAPONICA;
SOURCE 3 ORGANISM_COMMON: RICE;
SOURCE 4 ORGANISM_TAXID: 39947;
SOURCE 5 GENE: D14, D88, HTD2, OS03G0203200, LOC_OS03G10620;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PLANT HORMONES, PLANT SIGNALLING, STRIGOLACTONES, RECEPTOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.HIRABAYASHI,T.MIYAKAWA,M.TANOKURA
REVDAT 1 21-NOV-18 5ZHT 0
JRNL AUTH H.NAKAMURA,K.HIRABAYASHI,T.MIYAKAWA,K.KIKUZATO,W.HU,Y.XU,
JRNL AUTH 2 K.JIANG,I.TAKAHASHI,R.NIIYAMA,N.DOHMAE,M.TANOKURA,T.ASAMI
JRNL TITL TRIAZOLE UREAS COVALENTLY BIND TO STRIGOLACTONE RECEPTOR AND
JRNL TITL 2 ANTAGONIZE STRIGOLACTONE RESPONSES.
JRNL REF MOL PLANT 2018
JRNL REFN ESSN 1752-9867
JRNL PMID 30391752
JRNL DOI 10.1016/J.MOLP.2018.10.006
REMARK 2
REMARK 2 RESOLUTION. 1.53 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 78145
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) : 0.195
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.760
REMARK 3 FREE R VALUE TEST SET COUNT : 3717
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 41.7368 - 4.5931 1.00 2786 143 0.1610 0.1891
REMARK 3 2 4.5931 - 3.6464 1.00 2788 144 0.1473 0.1715
REMARK 3 3 3.6464 - 3.1856 1.00 2767 138 0.1766 0.2048
REMARK 3 4 3.1856 - 2.8944 1.00 2769 144 0.1915 0.2292
REMARK 3 5 2.8944 - 2.6870 1.00 2826 142 0.1978 0.2024
REMARK 3 6 2.6870 - 2.5286 1.00 2775 134 0.1910 0.2159
REMARK 3 7 2.5286 - 2.4020 1.00 2778 135 0.1987 0.2222
REMARK 3 8 2.4020 - 2.2974 1.00 2774 134 0.1984 0.2046
REMARK 3 9 2.2974 - 2.2090 1.00 2772 138 0.2037 0.2376
REMARK 3 10 2.2090 - 2.1328 1.00 2766 140 0.2091 0.2445
REMARK 3 11 2.1328 - 2.0661 1.00 2783 142 0.2100 0.2648
REMARK 3 12 2.0661 - 2.0070 1.00 2787 138 0.2147 0.2789
REMARK 3 13 2.0070 - 1.9542 1.00 2763 138 0.2177 0.2547
REMARK 3 14 1.9542 - 1.9065 1.00 2762 142 0.2241 0.2465
REMARK 3 15 1.9065 - 1.8632 1.00 2819 138 0.2264 0.2380
REMARK 3 16 1.8632 - 1.8235 1.00 2744 136 0.2287 0.2340
REMARK 3 17 1.8235 - 1.7871 1.00 2842 148 0.2241 0.2418
REMARK 3 18 1.7871 - 1.7533 1.00 2766 138 0.2324 0.2707
REMARK 3 19 1.7533 - 1.7220 1.00 2777 136 0.2344 0.2479
REMARK 3 20 1.7220 - 1.6928 1.00 2775 134 0.2315 0.2551
REMARK 3 21 1.6928 - 1.6655 1.00 2802 143 0.2455 0.2500
REMARK 3 22 1.6655 - 1.6399 1.00 2725 136 0.2366 0.2717
REMARK 3 23 1.6399 - 1.6158 1.00 2834 140 0.2534 0.2753
REMARK 3 24 1.6158 - 1.5930 1.00 2712 131 0.2610 0.2832
REMARK 3 25 1.5930 - 1.5715 0.97 2762 135 0.2812 0.2983
REMARK 3 26 1.5715 - 1.5511 0.94 2559 123 0.3075 0.3321
REMARK 3 27 1.5511 - 1.5317 0.86 2415 127 0.3250 0.3920
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.960
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 : 0.004 2116
REMARK 3 ANGLE : 0.887 2885
REMARK 3 CHIRALITY : 0.033 331
REMARK 3 PLANARITY : 0.004 372
REMARK 3 DIHEDRAL : 16.134 758
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 5ZHT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1300007105.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-16
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 : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : CRYO-COOLED CHANNEL-CUT SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78145
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.532
REMARK 200 RESOLUTION RANGE LOW (A) : 41.721
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 9.000
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.39600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.100
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: 3VXK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, MES, PH 6.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 128.31267
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 64.15633
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 64.15633
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 128.31267
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 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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 679 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 857 LIES ON A SPECIAL POSITION.
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 45
REMARK 465 PRO A 46
REMARK 465 GLY A 47
REMARK 465 TYR A 48
REMARK 465 GLN A 49
REMARK 465 ASP A 50
REMARK 465 PRO A 51
REMARK 465 ASN A 52
REMARK 465 SER A 53
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 81 -164.62 -126.76
REMARK 500 TYR A 119 34.91 -89.48
REMARK 500 SER A 147 -114.63 55.53
REMARK 500 ASP A 181 -14.75 73.08
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 883 DISTANCE = 6.29 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9GU A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5ZHS RELATED DB: PDB
REMARK 900 PDB ENTRIES FOR THE SAME CITATION. THE SAME PROTEIN (WITH DIFFERENT
REMARK 900 LIGAND)
REMARK 900 RELATED ID: 5ZHR RELATED DB: PDB
REMARK 900 PDB ENTRIES FOR THE SAME CITATION. THE SAME PROTEIN (WITH DIFFERENT
REMARK 900 LIGAND)
REMARK 900 RELATED ID: 5YZ7 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN (WITH DIFFERENT LIGAND)
REMARK 900 RELATED ID: 3VXK RELATED DB: PDB
REMARK 900 THE SAME PROTEIN (LIGAND-FREE STRUCTURE)
REMARK 900 RELATED ID: 3WIO RELATED DB: PDB
REMARK 900 THE SAME PROTEIN (WITH DIFFERENT LIGAND)
DBREF 5ZHT A 54 318 UNP Q10QA5 D14_ORYSJ 54 318
SEQADV 5ZHT GLY A 45 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHT PRO A 46 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHT GLY A 47 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHT TYR A 48 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHT GLN A 49 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHT ASP A 50 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHT PRO A 51 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHT ASN A 52 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHT SER A 53 UNP Q10QA5 EXPRESSION TAG
SEQRES 1 A 274 GLY PRO GLY TYR GLN ASP PRO ASN SER ALA LYS LEU LEU
SEQRES 2 A 274 GLN ILE LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG
SEQRES 3 A 274 VAL VAL VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER
SEQRES 4 A 274 ALA TRP SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS
SEQRES 5 A 274 ARG VAL VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL
SEQRES 6 A 274 ASN PRO ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU
SEQRES 7 A 274 ASP ALA TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA
SEQRES 8 A 274 LEU ARG ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL
SEQRES 9 A 274 SER ALA MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO
SEQRES 10 A 274 ASP LEU PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO
SEQRES 11 A 274 ARG PHE LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU
SEQRES 12 A 274 LEU GLU GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA
SEQRES 13 A 274 ASN TYR SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA
SEQRES 14 A 274 VAL GLY ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER
SEQRES 15 A 274 ARG THR LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS
SEQRES 16 A 274 VAL CYS GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL
SEQRES 17 A 274 LEU GLY MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR
SEQRES 18 A 274 THR ARG ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR
SEQRES 19 A 274 LEU LYS ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE
SEQRES 20 A 274 LEU GLN THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO
SEQRES 21 A 274 SER LEU LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG
SEQRES 22 A 274 TYR
HET 9GU A 500 18
HETNAM 9GU (1H-1,2,3-TRIAZOL-1-YL){4-[4-(TRIFLUOROMETHYL)
HETNAM 2 9GU PHENYL]PIPERAZIN-1-YL}METHANONE
FORMUL 2 9GU C14 H14 F3 N5 O
FORMUL 3 HOH *283(H2 O)
HELIX 1 AA1 ALA A 54 LEU A 60 1 7
HELIX 2 AA2 ASP A 81 SER A 86 5 6
HELIX 3 AA3 VAL A 88 LEU A 92 5 5
HELIX 4 AA4 ASN A 110 PHE A 114 5 5
HELIX 5 AA5 ARG A 117 ASP A 120 5 4
HELIX 6 AA6 ASN A 121 LEU A 136 1 16
HELIX 7 AA7 SER A 147 ARG A 160 1 14
HELIX 8 AA8 GLU A 187 ASN A 201 1 15
HELIX 9 AA9 ASN A 201 GLY A 215 1 15
HELIX 10 AB1 VAL A 218 PHE A 230 1 13
HELIX 11 AB2 ARG A 233 LYS A 246 1 14
HELIX 12 AB3 LEU A 249 VAL A 256 5 8
HELIX 13 AB4 SER A 274 LEU A 283 1 10
HELIX 14 AB5 LEU A 298 ALA A 303 1 6
HELIX 15 AB6 ALA A 303 LEU A 315 1 13
SHEET 1 AA1 7 ARG A 63 GLY A 66 0
SHEET 2 AA1 7 ARG A 97 LEU A 100 -1 O VAL A 98 N VAL A 65
SHEET 3 AA1 7 VAL A 71 SER A 75 1 N VAL A 72 O VAL A 99
SHEET 4 AA1 7 CYS A 141 HIS A 146 1 O VAL A 144 N VAL A 73
SHEET 5 AA1 7 PHE A 164 ILE A 170 1 O VAL A 168 N PHE A 143
SHEET 6 AA1 7 CYS A 260 GLN A 264 1 O VAL A 261 N LEU A 169
SHEET 7 AA1 7 THR A 287 PHE A 291 1 O GLU A 290 N GLN A 264
LINK OG SER A 147 CAM 9GU A 500 1555 1555 1.40
SITE 1 AC1 11 PHE A 78 SER A 147 VAL A 148 PHE A 176
SITE 2 AC1 11 PHE A 186 VAL A 194 TRP A 205 TYR A 209
SITE 3 AC1 11 PHE A 245 SER A 270 HOH A 737
CRYST1 49.349 49.349 192.469 90.00 90.00 120.00 P 32 2 1 6
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 0.020264 0.011699 0.000000 0.00000
SCALE2 0.000000 0.023399 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005196 0.00000
TER 2052 TYR A 318
MASTER 299 0 1 15 7 0 3 6 2352 1 19 22
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