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HEADER HYDROLASE 13-MAR-18 5ZHR
TITLE CRYSTAL STRUCTURE OF OSD14 IN COMPLEX WITH COVALENTLY BOUND KK094
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STRIGOLACTONE ESTERASE D14;
COMPND 3 CHAIN: A, B;
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 5ZHR 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. 1.45 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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 173170
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.200
REMARK 3 FREE R VALUE TEST SET COUNT : 3809
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 49.5396 - 4.3490 1.00 6328 141 0.1547 0.1783
REMARK 3 2 4.3490 - 3.4522 1.00 6353 142 0.1492 0.2026
REMARK 3 3 3.4522 - 3.0159 1.00 6354 143 0.1636 0.1873
REMARK 3 4 3.0159 - 2.7402 1.00 6349 143 0.1700 0.1827
REMARK 3 5 2.7402 - 2.5438 1.00 6367 145 0.1669 0.1896
REMARK 3 6 2.5438 - 2.3938 1.00 6335 136 0.1673 0.2006
REMARK 3 7 2.3938 - 2.2739 1.00 6370 149 0.1636 0.1966
REMARK 3 8 2.2739 - 2.1749 1.00 6372 139 0.1668 0.2230
REMARK 3 9 2.1749 - 2.0912 1.00 6347 147 0.1636 0.1870
REMARK 3 10 2.0912 - 2.0190 1.00 6319 137 0.1659 0.2062
REMARK 3 11 2.0190 - 1.9559 1.00 6370 140 0.1654 0.2085
REMARK 3 12 1.9559 - 1.9000 1.00 6386 147 0.1666 0.1937
REMARK 3 13 1.9000 - 1.8500 1.00 6317 144 0.1687 0.2187
REMARK 3 14 1.8500 - 1.8048 1.00 6336 142 0.1713 0.1950
REMARK 3 15 1.8048 - 1.7638 1.00 6414 149 0.1754 0.2067
REMARK 3 16 1.7638 - 1.7263 1.00 6305 144 0.1734 0.2213
REMARK 3 17 1.7263 - 1.6917 1.00 6387 143 0.1684 0.2106
REMARK 3 18 1.6917 - 1.6598 1.00 6304 143 0.1689 0.2138
REMARK 3 19 1.6598 - 1.6302 1.00 6385 141 0.1731 0.2180
REMARK 3 20 1.6302 - 1.6025 1.00 6314 146 0.1675 0.1682
REMARK 3 21 1.6025 - 1.5767 1.00 6414 146 0.1697 0.2145
REMARK 3 22 1.5767 - 1.5524 1.00 6250 143 0.1755 0.2309
REMARK 3 23 1.5524 - 1.5296 1.00 6402 142 0.1825 0.1897
REMARK 3 24 1.5296 - 1.5080 1.00 6324 139 0.1905 0.2160
REMARK 3 25 1.5080 - 1.4877 0.98 6267 142 0.1965 0.2287
REMARK 3 26 1.4877 - 1.4683 0.88 5609 127 0.2157 0.2221
REMARK 3 27 1.4683 - 1.4500 0.80 5083 109 0.2280 0.2750
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.220
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 : 0.009 4218
REMARK 3 ANGLE : 1.215 5748
REMARK 3 CHIRALITY : 0.051 662
REMARK 3 PLANARITY : 0.007 744
REMARK 3 DIHEDRAL : 11.996 1508
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 5ZHR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1300007101.
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 : 173170
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 49.511
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 9.300
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 26.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.27400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.900
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 (%): 42.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
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 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 24.12500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.69000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.32000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.69000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.12500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.32000
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 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 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 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 465 GLY B 45
REMARK 465 PRO B 46
REMARK 465 GLY B 47
REMARK 465 TYR B 48
REMARK 465 GLN B 49
REMARK 465 ASP B 50
REMARK 465 PRO B 51
REMARK 465 ASN B 52
REMARK 465 SER B 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 SER A 147 -119.63 58.33
REMARK 500 ARG A 175 121.40 -170.86
REMARK 500 ASN A 201 78.97 -162.73
REMARK 500 GLN A 293 31.82 -88.02
REMARK 500 ALA A 303 55.79 -145.72
REMARK 500 ASP B 81 -167.83 -126.77
REMARK 500 SER B 147 -118.92 57.56
REMARK 500 ARG B 175 120.98 -171.57
REMARK 500 ASP B 181 -8.01 61.50
REMARK 500 ASN B 201 85.26 -154.24
REMARK 500 ALA B 303 57.21 -141.75
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 = 6.11 ANGSTROMS
REMARK 525 HOH B 843 DISTANCE = 6.63 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KOK A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide KOK B 500 and SER B
REMARK 800 147
REMARK 900
REMARK 900 RELATED ENTRIES
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 5ZHR A 54 318 UNP Q10QA5 D14_ORYSJ 54 318
DBREF 5ZHR B 54 318 UNP Q10QA5 D14_ORYSJ 54 318
SEQADV 5ZHR GLY A 45 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR PRO A 46 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR GLY A 47 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR TYR A 48 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR GLN A 49 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR ASP A 50 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR PRO A 51 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR ASN A 52 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR SER A 53 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR GLY B 45 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR PRO B 46 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR GLY B 47 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR TYR B 48 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR GLN B 49 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR ASP B 50 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR PRO B 51 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR ASN B 52 UNP Q10QA5 EXPRESSION TAG
SEQADV 5ZHR SER B 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
SEQRES 1 B 274 GLY PRO GLY TYR GLN ASP PRO ASN SER ALA LYS LEU LEU
SEQRES 2 B 274 GLN ILE LEU ASN VAL ARG VAL VAL GLY SER GLY GLU ARG
SEQRES 3 B 274 VAL VAL VAL LEU SER HIS GLY PHE GLY THR ASP GLN SER
SEQRES 4 B 274 ALA TRP SER ARG VAL LEU PRO TYR LEU THR ARG ASP HIS
SEQRES 5 B 274 ARG VAL VAL LEU TYR ASP LEU VAL CYS ALA GLY SER VAL
SEQRES 6 B 274 ASN PRO ASP HIS PHE ASP PHE ARG ARG TYR ASP ASN LEU
SEQRES 7 B 274 ASP ALA TYR VAL ASP ASP LEU LEU ALA ILE LEU ASP ALA
SEQRES 8 B 274 LEU ARG ILE PRO ARG CYS ALA PHE VAL GLY HIS SER VAL
SEQRES 9 B 274 SER ALA MET ILE GLY ILE LEU ALA SER ILE ARG ARG PRO
SEQRES 10 B 274 ASP LEU PHE ALA LYS LEU VAL LEU ILE GLY ALA SER PRO
SEQRES 11 B 274 ARG PHE LEU ASN ASP SER ASP TYR HIS GLY GLY PHE GLU
SEQRES 12 B 274 LEU GLU GLU ILE GLN GLN VAL PHE ASP ALA MET GLY ALA
SEQRES 13 B 274 ASN TYR SER ALA TRP ALA THR GLY TYR ALA PRO LEU ALA
SEQRES 14 B 274 VAL GLY ALA ASP VAL PRO ALA ALA VAL GLN GLU PHE SER
SEQRES 15 B 274 ARG THR LEU PHE ASN MET ARG PRO ASP ILE SER LEU HIS
SEQRES 16 B 274 VAL CYS GLN THR VAL PHE LYS THR ASP LEU ARG GLY VAL
SEQRES 17 B 274 LEU GLY MET VAL ARG ALA PRO CYS VAL VAL VAL GLN THR
SEQRES 18 B 274 THR ARG ASP VAL SER VAL PRO ALA SER VAL ALA ALA TYR
SEQRES 19 B 274 LEU LYS ALA HIS LEU GLY GLY ARG THR THR VAL GLU PHE
SEQRES 20 B 274 LEU GLN THR GLU GLY HIS LEU PRO HIS LEU SER ALA PRO
SEQRES 21 B 274 SER LEU LEU ALA GLN VAL LEU ARG ARG ALA LEU ALA ARG
SEQRES 22 B 274 TYR
HET KOK A 500 11
HET KOK B 500 11
HETNAM KOK (2,3-DIHYDRO-1H-INDOL-1-YL)(1H-1,2,3-TRIAZOL-1-YL)
HETNAM 2 KOK METHANONE
FORMUL 3 KOK 2(C11 H10 N4 O)
FORMUL 5 HOH *526(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 MET A 232 1 15
HELIX 11 AB2 ARG A 233 THR A 247 1 15
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
HELIX 16 AB7 LYS B 55 LEU B 60 1 6
HELIX 17 AB8 ASP B 81 SER B 86 5 6
HELIX 18 AB9 VAL B 88 LEU B 92 5 5
HELIX 19 AC1 ASN B 110 PHE B 114 5 5
HELIX 20 AC2 ARG B 117 ASP B 120 5 4
HELIX 21 AC3 ASN B 121 LEU B 136 1 16
HELIX 22 AC4 SER B 147 ARG B 160 1 14
HELIX 23 AC5 GLU B 187 ASN B 201 1 15
HELIX 24 AC6 ASN B 201 GLY B 215 1 15
HELIX 25 AC7 VAL B 218 MET B 232 1 15
HELIX 26 AC8 ARG B 233 LYS B 246 1 14
HELIX 27 AC9 LEU B 249 VAL B 256 5 8
HELIX 28 AD1 ALA B 273 LEU B 283 1 11
HELIX 29 AD2 LEU B 298 ALA B 303 1 6
HELIX 30 AD3 ALA B 303 LEU B 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 ARG A 97
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 ALA A 165 N CYS A 141
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 THR A 288 N VAL A 262
SHEET 1 AA2 7 ARG B 63 GLY B 66 0
SHEET 2 AA2 7 ARG B 97 LEU B 100 -1 O VAL B 98 N VAL B 65
SHEET 3 AA2 7 VAL B 71 SER B 75 1 N VAL B 72 O VAL B 99
SHEET 4 AA2 7 CYS B 141 HIS B 146 1 O VAL B 144 N VAL B 73
SHEET 5 AA2 7 PHE B 164 ILE B 170 1 O ALA B 165 N CYS B 141
SHEET 6 AA2 7 CYS B 260 GLN B 264 1 O VAL B 263 N LEU B 169
SHEET 7 AA2 7 THR B 287 PHE B 291 1 O GLU B 290 N GLN B 264
LINK OG SER A 147 CAA KOK A 500 1555 1555 1.40
LINK OG SER B 147 CAA KOK B 500 1555 1555 1.37
SITE 1 AC1 8 PHE A 78 SER A 147 VAL A 148 PHE A 176
SITE 2 AC1 8 VAL A 244 PHE A 245 SER A 270 HOH A 723
SITE 1 AC2 15 PHE B 78 HIS B 146 VAL B 148 SER B 149
SITE 2 AC2 15 ALA B 150 MET B 151 ILE B 170 GLY B 171
SITE 3 AC2 15 PHE B 176 VAL B 244 PHE B 245 SER B 270
SITE 4 AC2 15 HIS B 297 HOH B 689 HOH B 738
CRYST1 48.250 88.640 119.380 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 0.020725 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011282 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008377 0.00000
TER 2052 TYR A 318
TER 4104 TYR B 318
MASTER 305 0 2 30 14 0 6 6 4650 2 24 44
END |