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HEADER HYDROLASE 07-FEB-24 8Y9O
TITLE CRYSTAL STRUCTURE OF ATKAI2 IN COMPLEX WITH KK181N1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE ESTERASE KAI2;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: PROTEIN DWARF-14-LIKE,PROTEIN D14-LIKE,PROTEIN HYPOSENSITIVE
COMPND 5 TO LIGHT,PROTEIN KARRIKIN INSENSITIVE 2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: KAI2, D14L, HTL, AT4G37470, F6G17.120;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ATKAI2, KK181N1, KARRIKIN-INSENSITIVE2, PLANT HORMONE RECEPTOR,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.W.WANG,T.MIYAKAWA,T.ASAMI
REVDAT 1 04-DEC-24 8Y9O 0
JRNL AUTH J.W.WANG,T.MIYAKAWA,T.ASAMI
JRNL TITL CRYSTAL STRUCTURE OF ATKAI2 IN COMPLEX WITH KK181N1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.GUO,Z.ZHENG,J.J.LA CLAIR,J.CHORY,J.P.NOEL
REMARK 1 TITL SMOKE-DERIVED KARRIKIN PERCEPTION BY THE A/B-HYDROLASE KAI2
REMARK 1 TITL 2 FROM ARABIDOPSIS
REMARK 1 REF PROC NATL ACAD SCI U S A V. 110 8284 2013
REMARK 1 REFN ESSN 1091-6490
REMARK 1 DOI 10.1073/PNAS.1306265110
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21.5419
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 94154
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 4659
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 42.3500 - 5.9000 0.97 3024 171 0.2367 0.2480
REMARK 3 2 5.9000 - 4.6800 0.98 2988 138 0.2205 0.2375
REMARK 3 3 4.6800 - 4.0900 0.97 2925 160 0.2004 0.2298
REMARK 3 4 4.0900 - 3.7200 0.97 2974 136 0.2079 0.2497
REMARK 3 5 3.7200 - 3.4500 0.99 2977 159 0.2205 0.2318
REMARK 3 6 3.4500 - 3.2500 0.99 2982 143 0.2325 0.2920
REMARK 3 7 3.2500 - 3.0900 1.00 3013 161 0.2304 0.2660
REMARK 3 8 3.0900 - 2.9500 0.99 2931 195 0.2279 0.2611
REMARK 3 9 2.9500 - 2.8400 0.99 2972 168 0.2492 0.2825
REMARK 3 10 2.8400 - 2.7400 1.00 2981 149 0.2480 0.2857
REMARK 3 11 2.7400 - 2.6500 1.00 2976 176 0.2480 0.2811
REMARK 3 12 2.6500 - 2.5800 1.00 2995 161 0.2467 0.3178
REMARK 3 13 2.5800 - 2.5100 1.00 3013 150 0.2361 0.2815
REMARK 3 14 2.5100 - 2.4500 1.00 2971 146 0.2356 0.2868
REMARK 3 15 2.4500 - 2.3900 1.00 3006 153 0.2367 0.2708
REMARK 3 16 2.3900 - 2.3400 1.00 3017 151 0.2495 0.3007
REMARK 3 17 2.3400 - 2.3000 1.00 2973 133 0.2517 0.3170
REMARK 3 18 2.3000 - 2.2500 1.00 2954 178 0.2566 0.2956
REMARK 3 19 2.2500 - 2.2100 1.00 3014 139 0.2674 0.2932
REMARK 3 20 2.2100 - 2.1700 1.00 2986 149 0.2590 0.3161
REMARK 3 21 2.1700 - 2.1400 1.00 2977 151 0.2615 0.3064
REMARK 3 22 2.1400 - 2.1100 1.00 3042 166 0.2547 0.3211
REMARK 3 23 2.1100 - 2.0800 1.00 2930 160 0.2654 0.2832
REMARK 3 24 2.0800 - 2.0500 1.00 2959 156 0.2730 0.3411
REMARK 3 25 2.0500 - 2.0200 1.00 2997 157 0.2710 0.3122
REMARK 3 26 2.0200 - 1.9900 1.00 3021 140 0.2744 0.3086
REMARK 3 27 1.9900 - 1.9700 1.00 3003 137 0.3035 0.3089
REMARK 3 28 1.9700 - 1.9400 1.00 2939 148 0.3024 0.3507
REMARK 3 29 1.9400 - 1.9200 1.00 3043 146 0.3330 0.3428
REMARK 3 30 1.9200 - 1.9000 1.00 2912 182 0.3300 0.3822
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.272
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.719
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.01
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 : 0.007 6369
REMARK 3 ANGLE : 0.814 8673
REMARK 3 CHIRALITY : 0.053 984
REMARK 3 PLANARITY : 0.006 1129
REMARK 3 DIHEDRAL : 16.025 2279
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 8Y9O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-FEB-24.
REMARK 100 THE DEPOSITION ID IS D_1300045233.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0-7.2
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) : 1.08
REMARK 200 MONOCHROMATOR : NULL
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94191
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 43.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10800
REMARK 200 FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.79700
REMARK 200 FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 1.19.2
REMARK 200 STARTING MODEL: 4JYP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7 M SODIUM PHOSPHATE, PH 7.0, AND 1%
REMARK 280 1,2-BUTANEDIOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 32.02100
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, 3
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 -6
REMARK 465 PRO A -5
REMARK 465 GLY A -4
REMARK 465 TYR A -3
REMARK 465 GLN A -2
REMARK 465 ASP A -1
REMARK 465 PRO A 0
REMARK 465 MET A 1
REMARK 465 ALA A 269
REMARK 465 MET A 270
REMARK 465 GLY B -6
REMARK 465 PRO B -5
REMARK 465 GLY B -4
REMARK 465 TYR B -3
REMARK 465 GLN B -2
REMARK 465 ASP B -1
REMARK 465 PRO B 0
REMARK 465 MET B 1
REMARK 465 ALA B 269
REMARK 465 MET B 270
REMARK 465 GLY C -6
REMARK 465 PRO C -5
REMARK 465 GLY C -4
REMARK 465 TYR C -3
REMARK 465 GLN C -2
REMARK 465 ASP C -1
REMARK 465 PRO C 0
REMARK 465 MET C 1
REMARK 465 GLY C 2
REMARK 465 VAL C 3
REMARK 465 VAL C 4
REMARK 465 ALA C 7
REMARK 465 PHE C 75
REMARK 465 ILE C 78
REMARK 465 ALA C 79
REMARK 465 ALA C 269
REMARK 465 MET C 270
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 THR A 28 -165.42 -129.21
REMARK 500 SER A 95 -118.40 51.40
REMARK 500 LYS A 114 140.09 -173.52
REMARK 500 ASN A 149 96.37 -163.30
REMARK 500 THR B 28 -167.69 -129.92
REMARK 500 SER B 95 -121.61 49.94
REMARK 500 LYS B 114 139.40 -176.04
REMARK 500 ASP B 127 -165.49 -114.27
REMARK 500 PRO B 242 80.30 -69.96
REMARK 500 ILE C 13 -162.92 -125.01
REMARK 500 THR C 28 -165.20 -125.91
REMARK 500 SER C 95 -119.67 57.43
REMARK 500 ASN C 107 -74.56 -51.82
REMARK 500 ASN C 149 112.33 -167.00
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 660 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH A 661 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH A 662 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH A 663 DISTANCE = 6.76 ANGSTROMS
REMARK 525 HOH A 664 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH A 665 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH A 666 DISTANCE = 7.17 ANGSTROMS
REMARK 525 HOH A 667 DISTANCE = 7.40 ANGSTROMS
REMARK 525 HOH A 668 DISTANCE = 7.77 ANGSTROMS
REMARK 525 HOH A 669 DISTANCE = 7.90 ANGSTROMS
REMARK 525 HOH A 670 DISTANCE = 8.13 ANGSTROMS
REMARK 525 HOH A 671 DISTANCE = 8.45 ANGSTROMS
REMARK 525 HOH A 672 DISTANCE = 8.64 ANGSTROMS
REMARK 525 HOH A 673 DISTANCE = 8.75 ANGSTROMS
REMARK 525 HOH B 629 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH B 630 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH B 631 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH B 632 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH B 633 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B 634 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH B 635 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH B 636 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH B 637 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH B 638 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH B 639 DISTANCE = 7.23 ANGSTROMS
REMARK 525 HOH B 640 DISTANCE = 7.34 ANGSTROMS
REMARK 525 HOH B 641 DISTANCE = 7.66 ANGSTROMS
REMARK 525 HOH B 642 DISTANCE = 7.88 ANGSTROMS
REMARK 525 HOH B 643 DISTANCE = 7.88 ANGSTROMS
REMARK 525 HOH B 644 DISTANCE = 8.23 ANGSTROMS
REMARK 525 HOH B 645 DISTANCE = 8.29 ANGSTROMS
REMARK 525 HOH B 646 DISTANCE = 8.32 ANGSTROMS
REMARK 525 HOH B 647 DISTANCE = 8.68 ANGSTROMS
REMARK 525 HOH B 648 DISTANCE = 8.77 ANGSTROMS
REMARK 525 HOH B 649 DISTANCE = 8.91 ANGSTROMS
REMARK 525 HOH B 650 DISTANCE = 9.43 ANGSTROMS
REMARK 525 HOH B 651 DISTANCE = 9.75 ANGSTROMS
REMARK 525 HOH B 652 DISTANCE = 10.39 ANGSTROMS
REMARK 525 HOH B 653 DISTANCE = 10.45 ANGSTROMS
REMARK 525 HOH B 654 DISTANCE = 10.59 ANGSTROMS
REMARK 525 HOH B 655 DISTANCE = 10.74 ANGSTROMS
REMARK 525 HOH B 656 DISTANCE = 10.97 ANGSTROMS
REMARK 525 HOH B 657 DISTANCE = 10.99 ANGSTROMS
REMARK 525 HOH B 658 DISTANCE = 11.05 ANGSTROMS
REMARK 525 HOH B 659 DISTANCE = 11.14 ANGSTROMS
REMARK 525 HOH B 660 DISTANCE = 11.28 ANGSTROMS
REMARK 525 HOH B 661 DISTANCE = 11.52 ANGSTROMS
REMARK 525 HOH B 662 DISTANCE = 12.30 ANGSTROMS
REMARK 525 HOH B 663 DISTANCE = 12.72 ANGSTROMS
REMARK 525 HOH B 664 DISTANCE = 13.06 ANGSTROMS
REMARK 525 HOH B 665 DISTANCE = 13.91 ANGSTROMS
REMARK 525 HOH C 487 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH C 488 DISTANCE = 7.46 ANGSTROMS
DBREF 8Y9O A 1 270 UNP Q9SZU7 KAI2_ARATH 1 270
DBREF 8Y9O B 1 270 UNP Q9SZU7 KAI2_ARATH 1 270
DBREF 8Y9O C 1 270 UNP Q9SZU7 KAI2_ARATH 1 270
SEQADV 8Y9O GLY A -6 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O PRO A -5 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O GLY A -4 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O TYR A -3 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O GLN A -2 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O ASP A -1 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O PRO A 0 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O GLY B -6 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O PRO B -5 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O GLY B -4 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O TYR B -3 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O GLN B -2 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O ASP B -1 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O PRO B 0 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O GLY C -6 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O PRO C -5 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O GLY C -4 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O TYR C -3 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O GLN C -2 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O ASP C -1 UNP Q9SZU7 EXPRESSION TAG
SEQADV 8Y9O PRO C 0 UNP Q9SZU7 EXPRESSION TAG
SEQRES 1 A 277 GLY PRO GLY TYR GLN ASP PRO MET GLY VAL VAL GLU GLU
SEQRES 2 A 277 ALA HIS ASN VAL LYS VAL ILE GLY SER GLY GLU ALA THR
SEQRES 3 A 277 ILE VAL LEU GLY HIS GLY PHE GLY THR ASP GLN SER VAL
SEQRES 4 A 277 TRP LYS HIS LEU VAL PRO HIS LEU VAL ASP ASP TYR ARG
SEQRES 5 A 277 VAL VAL LEU TYR ASP ASN MET GLY ALA GLY THR THR ASN
SEQRES 6 A 277 PRO ASP TYR PHE ASP PHE ASP ARG TYR SER ASN LEU GLU
SEQRES 7 A 277 GLY TYR SER PHE ASP LEU ILE ALA ILE LEU GLU ASP LEU
SEQRES 8 A 277 LYS ILE GLU SER CYS ILE PHE VAL GLY HIS SER VAL SER
SEQRES 9 A 277 ALA MET ILE GLY VAL LEU ALA SER LEU ASN ARG PRO ASP
SEQRES 10 A 277 LEU PHE SER LYS ILE VAL MET ILE SER ALA SER PRO ARG
SEQRES 11 A 277 TYR VAL ASN ASP VAL ASP TYR GLN GLY GLY PHE GLU GLN
SEQRES 12 A 277 GLU ASP LEU ASN GLN LEU PHE GLU ALA ILE ARG SER ASN
SEQRES 13 A 277 TYR LYS ALA TRP CYS LEU GLY PHE ALA PRO LEU ALA VAL
SEQRES 14 A 277 GLY GLY ASP MET ASP SER ILE ALA VAL GLN GLU PHE SER
SEQRES 15 A 277 ARG THR LEU PHE ASN MET ARG PRO ASP ILE ALA LEU SER
SEQRES 16 A 277 VAL GLY GLN THR ILE PHE GLN SER ASP MET ARG GLN ILE
SEQRES 17 A 277 LEU PRO PHE VAL THR VAL PRO CYS HIS ILE LEU GLN SER
SEQRES 18 A 277 VAL LYS ASP LEU ALA VAL PRO VAL VAL VAL SER GLU TYR
SEQRES 19 A 277 LEU HIS ALA ASN LEU GLY CYS GLU SER VAL VAL GLU VAL
SEQRES 20 A 277 ILE PRO SER ASP GLY HIS LEU PRO GLN LEU SER SER PRO
SEQRES 21 A 277 ASP SER VAL ILE PRO VAL ILE LEU ARG HIS ILE ARG ASN
SEQRES 22 A 277 ASP ILE ALA MET
SEQRES 1 B 277 GLY PRO GLY TYR GLN ASP PRO MET GLY VAL VAL GLU GLU
SEQRES 2 B 277 ALA HIS ASN VAL LYS VAL ILE GLY SER GLY GLU ALA THR
SEQRES 3 B 277 ILE VAL LEU GLY HIS GLY PHE GLY THR ASP GLN SER VAL
SEQRES 4 B 277 TRP LYS HIS LEU VAL PRO HIS LEU VAL ASP ASP TYR ARG
SEQRES 5 B 277 VAL VAL LEU TYR ASP ASN MET GLY ALA GLY THR THR ASN
SEQRES 6 B 277 PRO ASP TYR PHE ASP PHE ASP ARG TYR SER ASN LEU GLU
SEQRES 7 B 277 GLY TYR SER PHE ASP LEU ILE ALA ILE LEU GLU ASP LEU
SEQRES 8 B 277 LYS ILE GLU SER CYS ILE PHE VAL GLY HIS SER VAL SER
SEQRES 9 B 277 ALA MET ILE GLY VAL LEU ALA SER LEU ASN ARG PRO ASP
SEQRES 10 B 277 LEU PHE SER LYS ILE VAL MET ILE SER ALA SER PRO ARG
SEQRES 11 B 277 TYR VAL ASN ASP VAL ASP TYR GLN GLY GLY PHE GLU GLN
SEQRES 12 B 277 GLU ASP LEU ASN GLN LEU PHE GLU ALA ILE ARG SER ASN
SEQRES 13 B 277 TYR LYS ALA TRP CYS LEU GLY PHE ALA PRO LEU ALA VAL
SEQRES 14 B 277 GLY GLY ASP MET ASP SER ILE ALA VAL GLN GLU PHE SER
SEQRES 15 B 277 ARG THR LEU PHE ASN MET ARG PRO ASP ILE ALA LEU SER
SEQRES 16 B 277 VAL GLY GLN THR ILE PHE GLN SER ASP MET ARG GLN ILE
SEQRES 17 B 277 LEU PRO PHE VAL THR VAL PRO CYS HIS ILE LEU GLN SER
SEQRES 18 B 277 VAL LYS ASP LEU ALA VAL PRO VAL VAL VAL SER GLU TYR
SEQRES 19 B 277 LEU HIS ALA ASN LEU GLY CYS GLU SER VAL VAL GLU VAL
SEQRES 20 B 277 ILE PRO SER ASP GLY HIS LEU PRO GLN LEU SER SER PRO
SEQRES 21 B 277 ASP SER VAL ILE PRO VAL ILE LEU ARG HIS ILE ARG ASN
SEQRES 22 B 277 ASP ILE ALA MET
SEQRES 1 C 277 GLY PRO GLY TYR GLN ASP PRO MET GLY VAL VAL GLU GLU
SEQRES 2 C 277 ALA HIS ASN VAL LYS VAL ILE GLY SER GLY GLU ALA THR
SEQRES 3 C 277 ILE VAL LEU GLY HIS GLY PHE GLY THR ASP GLN SER VAL
SEQRES 4 C 277 TRP LYS HIS LEU VAL PRO HIS LEU VAL ASP ASP TYR ARG
SEQRES 5 C 277 VAL VAL LEU TYR ASP ASN MET GLY ALA GLY THR THR ASN
SEQRES 6 C 277 PRO ASP TYR PHE ASP PHE ASP ARG TYR SER ASN LEU GLU
SEQRES 7 C 277 GLY TYR SER PHE ASP LEU ILE ALA ILE LEU GLU ASP LEU
SEQRES 8 C 277 LYS ILE GLU SER CYS ILE PHE VAL GLY HIS SER VAL SER
SEQRES 9 C 277 ALA MET ILE GLY VAL LEU ALA SER LEU ASN ARG PRO ASP
SEQRES 10 C 277 LEU PHE SER LYS ILE VAL MET ILE SER ALA SER PRO ARG
SEQRES 11 C 277 TYR VAL ASN ASP VAL ASP TYR GLN GLY GLY PHE GLU GLN
SEQRES 12 C 277 GLU ASP LEU ASN GLN LEU PHE GLU ALA ILE ARG SER ASN
SEQRES 13 C 277 TYR LYS ALA TRP CYS LEU GLY PHE ALA PRO LEU ALA VAL
SEQRES 14 C 277 GLY GLY ASP MET ASP SER ILE ALA VAL GLN GLU PHE SER
SEQRES 15 C 277 ARG THR LEU PHE ASN MET ARG PRO ASP ILE ALA LEU SER
SEQRES 16 C 277 VAL GLY GLN THR ILE PHE GLN SER ASP MET ARG GLN ILE
SEQRES 17 C 277 LEU PRO PHE VAL THR VAL PRO CYS HIS ILE LEU GLN SER
SEQRES 18 C 277 VAL LYS ASP LEU ALA VAL PRO VAL VAL VAL SER GLU TYR
SEQRES 19 C 277 LEU HIS ALA ASN LEU GLY CYS GLU SER VAL VAL GLU VAL
SEQRES 20 C 277 ILE PRO SER ASP GLY HIS LEU PRO GLN LEU SER SER PRO
SEQRES 21 C 277 ASP SER VAL ILE PRO VAL ILE LEU ARG HIS ILE ARG ASN
SEQRES 22 C 277 ASP ILE ALA MET
HET IB0 A 301 17
HET IB0 B 301 17
HET IB0 C 301 17
HETNAM IB0 (7-METHYL-2,3-DIHYDROINDOL-1-YL)-(1,2,3-TRIAZOL-1-YL)
HETNAM 2 IB0 METHANONE
FORMUL 4 IB0 3(C12 H12 N4 O)
FORMUL 7 HOH *626(H2 O)
HELIX 1 AA1 GLY A 2 HIS A 8 1 7
HELIX 2 AA2 ASP A 29 LYS A 34 5 6
HELIX 3 AA3 LEU A 36 LEU A 40 5 5
HELIX 4 AA4 ASN A 58 PHE A 62 5 5
HELIX 5 AA5 ASN A 69 LEU A 84 1 16
HELIX 6 AA6 SER A 95 ARG A 108 1 14
HELIX 7 AA7 GLU A 135 ASN A 149 1 15
HELIX 8 AA8 ASN A 149 GLY A 163 1 15
HELIX 9 AA9 SER A 168 MET A 181 1 14
HELIX 10 AB1 ARG A 182 GLN A 195 1 14
HELIX 11 AB2 MET A 198 VAL A 205 5 8
HELIX 12 AB3 PRO A 221 LEU A 232 1 12
HELIX 13 AB4 LEU A 247 SER A 252 1 6
HELIX 14 AB5 SER A 252 ASN A 266 1 15
HELIX 15 AB6 VAL B 3 HIS B 8 1 6
HELIX 16 AB7 ASP B 29 LYS B 34 5 6
HELIX 17 AB8 LEU B 36 LEU B 40 5 5
HELIX 18 AB9 ASN B 58 PHE B 62 5 5
HELIX 19 AC1 ASP B 65 SER B 68 5 4
HELIX 20 AC2 ASN B 69 LEU B 84 1 16
HELIX 21 AC3 SER B 95 ARG B 108 1 14
HELIX 22 AC4 GLU B 135 ASN B 149 1 15
HELIX 23 AC5 ASN B 149 GLY B 163 1 15
HELIX 24 AC6 SER B 168 MET B 181 1 14
HELIX 25 AC7 ARG B 182 GLN B 195 1 14
HELIX 26 AC8 MET B 198 VAL B 205 5 8
HELIX 27 AC9 PRO B 221 LEU B 232 1 12
HELIX 28 AD1 LEU B 247 SER B 252 1 6
HELIX 29 AD2 SER B 252 ASN B 266 1 15
HELIX 30 AD3 ASP C 29 LYS C 34 5 6
HELIX 31 AD4 LEU C 36 LEU C 40 5 5
HELIX 32 AD5 ASN C 58 PHE C 62 5 5
HELIX 33 AD6 ASP C 65 ASN C 69 5 5
HELIX 34 AD7 SER C 95 ARG C 108 1 14
HELIX 35 AD8 GLU C 135 ASN C 149 1 15
HELIX 36 AD9 ASN C 149 GLY C 163 1 15
HELIX 37 AE1 SER C 168 ASN C 180 1 13
HELIX 38 AE2 ARG C 182 GLN C 195 1 14
HELIX 39 AE3 ILE C 201 VAL C 205 5 5
HELIX 40 AE4 PRO C 221 LEU C 232 1 12
HELIX 41 AE5 LEU C 247 SER C 252 1 6
HELIX 42 AE6 SER C 252 ASN C 266 1 15
SHEET 1 AA1 7 LYS A 11 GLY A 14 0
SHEET 2 AA1 7 ARG A 45 LEU A 48 -1 O VAL A 46 N ILE A 13
SHEET 3 AA1 7 THR A 19 GLY A 23 1 N ILE A 20 O VAL A 47
SHEET 4 AA1 7 CYS A 89 HIS A 94 1 O VAL A 92 N VAL A 21
SHEET 5 AA1 7 PHE A 112 ILE A 118 1 O VAL A 116 N PHE A 91
SHEET 6 AA1 7 CYS A 209 LYS A 216 1 O HIS A 210 N MET A 117
SHEET 7 AA1 7 SER A 236 ASP A 244 1 O VAL A 237 N ILE A 211
SHEET 1 AA2 7 LYS B 11 ILE B 13 0
SHEET 2 AA2 7 ARG B 45 LEU B 48 -1 O VAL B 46 N ILE B 13
SHEET 3 AA2 7 THR B 19 GLY B 23 1 N ILE B 20 O ARG B 45
SHEET 4 AA2 7 CYS B 89 HIS B 94 1 O ILE B 90 N VAL B 21
SHEET 5 AA2 7 PHE B 112 ILE B 118 1 O VAL B 116 N PHE B 91
SHEET 6 AA2 7 CYS B 209 LYS B 216 1 O HIS B 210 N MET B 117
SHEET 7 AA2 7 SER B 236 ASP B 244 1 O VAL B 237 N ILE B 211
SHEET 1 AA3 7 LYS C 11 GLY C 14 0
SHEET 2 AA3 7 ARG C 45 LEU C 48 -1 O LEU C 48 N LYS C 11
SHEET 3 AA3 7 THR C 19 GLY C 23 1 N ILE C 20 O VAL C 47
SHEET 4 AA3 7 CYS C 89 HIS C 94 1 O VAL C 92 N VAL C 21
SHEET 5 AA3 7 PHE C 112 ILE C 118 1 O VAL C 116 N GLY C 93
SHEET 6 AA3 7 CYS C 209 LYS C 216 1 O HIS C 210 N MET C 117
SHEET 7 AA3 7 SER C 236 ASP C 244 1 O VAL C 237 N ILE C 211
CRYST1 85.314 64.042 114.958 90.00 104.79 90.00 P 1 21 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 0.011721 0.000000 0.003095 0.00000
SCALE2 0.000000 0.015615 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008997 0.00000
TER 2075 ILE A 268
TER 4150 ILE B 268
TER 6178 ILE C 268
MASTER 370 0 3 42 21 0 0 6 6852 3 51 66
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