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HEADER HYDROLASE 01-NOV-12 4HTA
TITLE THE STRUCTURE OF THE KARRIKIN INSENSITIVE (KAI2) PROTEIN IN
TITLE 2 ARABIDOPSIS THALIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE, ALPHA/BETA FOLD FAMILY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: KARRIKIN-INSENSITIVE 2, KAI2, PUTATIVE UNCHARACTERIZED
COMPND 5 PROTEIN AT4G37470, PUTATIVE UNCHARACTERIZED PROTEIN AT4G37470,
COMPND 6 PUTATIVE UNCHARACTERIZED PROTEIN F6G17.120;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS, THALE-CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: F6G17.120, AT4G37470;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ALPHA/BETA HYDROLASE, SIGNALING PROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.BYTHELL-DOUGLAS,M.T.WATERS,A.SCAFFIDI,G.R.FLEMATTI,S.M.SMITH,
AUTHOR 2 C.S.BOND
REVDAT 1 27-FEB-13 4HTA 0
JRNL AUTH R.BYTHELL-DOUGLAS,M.T.WATERS,A.SCAFFIDI,G.R.FLEMATTI,
JRNL AUTH 2 S.M.SMITH,C.S.BOND
JRNL TITL THE STRUCTURE OF THE KARRIKIN-INSENSITIVE PROTEIN (KAI2) IN
JRNL TITL 2 ARABIDOPSIS THALIANA
JRNL REF PLOS ONE V. 8 54758 2013
JRNL REFN ESSN 1932-6203
JRNL PMID 23349965
JRNL DOI 10.1371/JOURNAL.PONE.0054758
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 26093
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) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1324
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 13
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.11
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2677
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1846
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2552
REMARK 3 BIN R VALUE (WORKING SET) : 0.1827
REMARK 3 BIN FREE R VALUE : 0.2233
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.67
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 125
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2106
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 266
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.58
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.37960
REMARK 3 B22 (A**2) : 2.85960
REMARK 3 B33 (A**2) : -3.23920
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.16
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.12
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.10
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.11
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.10
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2187 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2968 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 736 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 56 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 313 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2187 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 277 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2788 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.96
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.32
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.45
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4HTA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-NOV-12.
REMARK 100 THE RCSB ID CODE IS RCSB075893.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95390
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26147
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.901
REMARK 200 RESOLUTION RANGE LOW (A) : 77.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
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) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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 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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M SODIUM POTASSIUM PHOSPHATE, PH
REMARK 280 7.2, VAPOR 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 31.69250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.81000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.03200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.81000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.69250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.03200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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 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 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 LEU A -12
REMARK 465 GLU A -11
REMARK 465 SER A -10
REMARK 465 THR A -9
REMARK 465 LYS A -3
REMARK 465 ALA A -2
REMARK 465 GLY A -1
REMARK 465 PHE A 0
REMARK 465 MET A 1
REMARK 465 ALA A 269
REMARK 465 MET A 270
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A -8 N CB OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG A 182 O HOH A 665 3555 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 -164.81 -120.11
REMARK 500 SER A 95 -122.15 52.63
REMARK 500 ARG A 123 127.11 -171.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 TYR A -6 24.6 L L OUTSIDE RANGE
REMARK 500 VAL A 41 24.7 L L OUTSIDE RANGE
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 640 DISTANCE = 5.66 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 306
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HRX RELATED DB: PDB
REMARK 900 HIGH RESOLUTION STRUCTURE IN P212121
REMARK 900 RELATED ID: 4HRY RELATED DB: PDB
REMARK 900 KAI2 CRYSTALLISED IN P21 SPACE GROUP
DBREF 4HTA A 1 270 UNP Q9SZU7 Q9SZU7_ARATH 1 270
SEQADV 4HTA HIS A -18 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA HIS A -17 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA HIS A -16 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA HIS A -15 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA HIS A -14 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA HIS A -13 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA LEU A -12 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA GLU A -11 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA SER A -10 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA THR A -9 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA SER A -8 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA LEU A -7 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA TYR A -6 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA LYS A -5 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA LYS A -3 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA ALA A -2 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA GLY A -1 UNP Q9SZU7 EXPRESSION TAG
SEQADV 4HTA PHE A 0 UNP Q9SZU7 EXPRESSION TAG
SEQRES 1 A 288 HIS HIS HIS HIS HIS HIS LEU GLU SER THR SER LEU TYR
SEQRES 2 A 288 LYS LYS ALA GLY PHE MET GLY VAL VAL GLU GLU ALA HIS
SEQRES 3 A 288 ASN VAL LYS VAL ILE GLY SER GLY GLU ALA THR ILE VAL
SEQRES 4 A 288 LEU GLY HIS GLY PHE GLY THR ASP GLN SER VAL TRP LYS
SEQRES 5 A 288 HIS LEU VAL PRO HIS LEU VAL ASP ASP TYR ARG VAL VAL
SEQRES 6 A 288 LEU TYR ASP ASN MET GLY ALA GLY THR THR ASN PRO ASP
SEQRES 7 A 288 TYR PHE ASP PHE ASP ARG TYR SER ASN LEU GLU GLY TYR
SEQRES 8 A 288 SER PHE ASP LEU ILE ALA ILE LEU GLU ASP LEU LYS ILE
SEQRES 9 A 288 GLU SER CYS ILE PHE VAL GLY HIS SER VAL SER ALA MET
SEQRES 10 A 288 ILE GLY VAL LEU ALA SER LEU ASN ARG PRO ASP LEU PHE
SEQRES 11 A 288 SER LYS ILE VAL MET ILE SER ALA SER PRO ARG TYR VAL
SEQRES 12 A 288 ASN ASP VAL ASP TYR GLN GLY GLY PHE GLU GLN GLU ASP
SEQRES 13 A 288 LEU ASN GLN LEU PHE GLU ALA ILE ARG SER ASN TYR LYS
SEQRES 14 A 288 ALA TRP CYS LEU GLY PHE ALA PRO LEU ALA VAL GLY GLY
SEQRES 15 A 288 ASP MET ASP SER ILE ALA VAL GLN GLU PHE SER ARG THR
SEQRES 16 A 288 LEU PHE ASN MET ARG PRO ASP ILE ALA LEU SER VAL GLY
SEQRES 17 A 288 GLN THR ILE PHE GLN SER ASP MET ARG GLN ILE LEU PRO
SEQRES 18 A 288 PHE VAL THR VAL PRO CYS HIS ILE LEU GLN SER VAL LYS
SEQRES 19 A 288 ASP LEU ALA VAL PRO VAL VAL VAL SER GLU TYR LEU HIS
SEQRES 20 A 288 ALA ASN LEU GLY CYS GLU SER VAL VAL GLU VAL ILE PRO
SEQRES 21 A 288 SER ASP GLY HIS LEU PRO GLN LEU SER SER PRO ASP SER
SEQRES 22 A 288 VAL ILE PRO VAL ILE LEU ARG HIS ILE ARG ASN ASP ILE
SEQRES 23 A 288 ALA MET
HET GOL A 301 6
HET GOL A 302 6
HET GOL A 303 6
HET GOL A 304 6
HET GOL A 305 6
HET PO4 A 306 5
HETNAM GOL GLYCEROL
HETNAM PO4 PHOSPHATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 5(C3 H8 O3)
FORMUL 7 PO4 O4 P 3-
FORMUL 8 HOH *266(H2 O)
HELIX 1 1 VAL A 3 HIS A 8 1 6
HELIX 2 2 ASP A 29 LYS A 34 5 6
HELIX 3 3 LEU A 36 LEU A 40 5 5
HELIX 4 4 ASN A 58 PHE A 62 5 5
HELIX 5 5 ASP A 65 ASN A 69 5 5
HELIX 6 6 LEU A 70 LYS A 85 1 16
HELIX 7 7 SER A 95 ARG A 108 1 14
HELIX 8 8 GLU A 135 ASN A 149 1 15
HELIX 9 9 ASN A 149 GLY A 163 1 15
HELIX 10 10 SER A 168 ASN A 180 1 13
HELIX 11 11 ARG A 182 GLN A 195 1 14
HELIX 12 12 MET A 198 VAL A 205 5 8
HELIX 13 13 PRO A 221 LEU A 232 1 12
HELIX 14 14 LEU A 247 SER A 252 1 6
HELIX 15 15 SER A 252 ASN A 266 1 15
SHEET 1 A 7 LYS A 11 GLY A 14 0
SHEET 2 A 7 ARG A 45 TYR A 49 -1 O LEU A 48 N LYS A 11
SHEET 3 A 7 THR A 19 GLY A 23 1 N ILE A 20 O VAL A 47
SHEET 4 A 7 CYS A 89 HIS A 94 1 O HIS A 94 N GLY A 23
SHEET 5 A 7 PHE A 112 ILE A 118 1 O VAL A 116 N PHE A 91
SHEET 6 A 7 CYS A 209 LYS A 216 1 O HIS A 210 N MET A 117
SHEET 7 A 7 SER A 236 ASP A 244 1 O VAL A 237 N ILE A 211
SITE 1 AC1 8 PHE A 26 SER A 95 TYR A 124 PHE A 157
SITE 2 AC1 8 ILE A 193 HIS A 246 HOH A 426 HOH A 562
SITE 1 AC2 9 PRO A 109 LYS A 216 ASP A 217 PRO A 221
SITE 2 AC2 9 HOH A 425 HOH A 438 HOH A 454 HOH A 458
SITE 3 AC2 9 HOH A 494
SITE 1 AC3 2 HIS A 210 ARG A 262
SITE 1 AC4 5 LEU A 142 TRP A 153 GLY A 156 PHE A 157
SITE 2 AC4 5 LEU A 160
SITE 1 AC5 7 ASN A 69 LEU A 70 GLU A 71 LEU A 103
SITE 2 AC5 7 SER A 196 ASP A 197 HOH A 515
SITE 1 AC6 6 HIS A 39 ARG A 265 HOH A 559 HOH A 570
SITE 2 AC6 6 HOH A 611 HOH A 638
CRYST1 63.385 66.064 77.620 90.00 90.00 90.00 P 21 21 21 4
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 0.015777 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015137 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012883 0.00000
TER 2112 ILE A 268
MASTER 346 0 6 15 7 0 12 6 2407 1 35 23
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