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HEADER HYDROLASE 18-DEC-12 4IH4
TITLE CRYSTAL STRUCTURE OF ARABIDOPSIS DWARF14 ORTHOLOGUE, ATD14
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AT3G03990/T11I18_10;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ALPHA/BETA-HYDROLASE DOMAIN-CONTAINING PROTEIN, T11I18.10
COMPND 5 PROTEIN;
COMPND 6 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: AT3G03990, ATD14, T11I18.10;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETDUET1
KEYWDS STRIGOLACTONE RECEPTOR, ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.E.ZHOU,L.-H.ZHAO,Z.-S.WU,W.YI,S.LI,Y.LI,Y.XU,T.-H.XU,Y.LIU,R.-
AUTHOR 2 Z.CHEN,A.KOVACH,Y.KANG,L.HOU,Y.HE,C.ZHANG,K.MELCHER,H.E.XU
REVDAT 1 30-JAN-13 4IH4 0
JRNL AUTH L.-H.ZHAO,X.E.ZHOU,Z.-S.WU,L.WANG,W.YI,S.LI,Y.LI,Y.XU,
JRNL AUTH 2 T.-H.XU,Y.LIU,R.-Z.CHEN,X.YANG,A.KOVACH,Y.KANG,L.HOU,Y.HE,
JRNL AUTH 3 C.XIE,D.ZHONG,L.JIANG,X.LIU,Y.XU,X.SHEN,C.ZHANG,Y.WANG,J.LI,
JRNL AUTH 4 K.MELCHER,H.E.XU
JRNL TITL CRYSTAL STRUCTURES OF TWO PHYTOHORMONE SIGNAL-TRANSDUCING
JRNL TITL 2 ALPHA/BETA HYDROLASES: KARRIKIN-SIGNALING KAI2 AND
JRNL TITL 3 STRIGOLACTONE-SIGNALING DWARF 14
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1984.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 64.3
REMARK 3 NUMBER OF REFLECTIONS : 9439
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.279
REMARK 3 FREE R VALUE : 0.336
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 686
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 8160
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.64400
REMARK 3 B22 (A**2) : -1.04500
REMARK 3 B33 (A**2) : -6.59900
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 14.48600
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.952 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.716 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 0.926 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.533 ; 2.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : -7.12
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4IH4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-12.
REMARK 100 THE RCSB ID CODE IS RCSB076744.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12471
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.8
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.20400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.55700
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: NULL
REMARK 200 STARTING MODEL: 4IH1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, MGCL2, PH 8.5, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 92.42800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.31450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 92.42800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.31450
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, 3, 4
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 4
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: 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 MET A 1
REMARK 465 SER A 2
REMARK 465 GLN A 3
REMARK 465 HIS A 4
REMARK 465 ASN A 5
REMARK 465 ARG A 267
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLN B 3
REMARK 465 HIS B 4
REMARK 465 ASN B 5
REMARK 465 ARG B 267
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLN C 3
REMARK 465 HIS C 4
REMARK 465 ASN C 5
REMARK 465 ARG C 267
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 GLN D 3
REMARK 465 HIS D 4
REMARK 465 ASN D 5
REMARK 465 ARG D 267
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP C 218 ND1 HIS C 247 2.05
REMARK 500 OD1 ASP A 218 ND1 HIS A 247 2.07
REMARK 500 OD1 ASP D 218 ND1 HIS D 247 2.14
REMARK 500 OD1 ASP B 218 ND1 HIS B 247 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 55 CB CYS B 55 SG -0.099
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 LEU A 10 76.85 -110.73
REMARK 500 ASN A 11 82.84 -28.26
REMARK 500 PHE A 28 154.37 -49.18
REMARK 500 THR A 30 -179.00 -43.90
REMARK 500 HIS A 36 -68.90 -27.89
REMARK 500 LEU A 37 7.81 -53.32
REMARK 500 ILE A 38 11.61 -150.05
REMARK 500 ASN A 45 -32.71 -148.37
REMARK 500 LEU A 53 154.95 -46.83
REMARK 500 ALA A 56 155.63 -37.61
REMARK 500 SER A 58 26.76 -74.53
REMARK 500 ASP A 62 -6.24 -55.60
REMARK 500 ARG A 68 -74.92 -107.47
REMARK 500 TYR A 69 59.07 -66.95
REMARK 500 THR A 71 -153.27 -141.26
REMARK 500 SER A 97 -109.01 46.59
REMARK 500 SER A 99 -5.54 -58.68
REMARK 500 SER A 107 -18.57 -45.11
REMARK 500 ARG A 110 61.20 -155.86
REMARK 500 LEU A 113 22.25 -69.16
REMARK 500 PRO A 124 -75.09 -81.34
REMARK 500 GLU A 138 -39.70 -38.01
REMARK 500 GLU A 140 -39.82 -38.99
REMARK 500 SER A 146 -79.74 -51.36
REMARK 500 ALA A 150 -104.58 -69.83
REMARK 500 ALA A 166 155.86 -40.86
REMARK 500 PHE A 189 -70.44 -65.59
REMARK 500 VAL A 190 -33.05 -35.12
REMARK 500 SER A 191 -70.65 -63.21
REMARK 500 LEU A 199 53.24 -144.29
REMARK 500 ARG A 200 -85.02 -67.68
REMARK 500 THR A 210 -164.03 -75.02
REMARK 500 CYS A 211 88.69 -177.07
REMARK 500 PRO A 222 158.23 -49.61
REMARK 500 HIS A 232 64.27 -106.38
REMARK 500 ASP A 236 93.30 -48.40
REMARK 500 GLN A 250 -19.98 -46.54
REMARK 500 ALA A 253 68.30 -166.78
REMARK 500 ALA A 255 -72.76 -44.01
REMARK 500 ALA A 258 -75.05 -45.47
REMARK 500 ALA A 264 -72.56 -115.97
REMARK 500 LEU B 10 74.79 -108.80
REMARK 500 ASN B 11 85.92 -26.29
REMARK 500 PHE B 28 157.40 -47.58
REMARK 500 THR B 30 176.73 -43.81
REMARK 500 HIS B 36 -66.24 -27.77
REMARK 500 LEU B 37 7.10 -54.84
REMARK 500 ILE B 38 11.23 -150.20
REMARK 500 ASN B 45 -34.24 -147.69
REMARK 500 LEU B 53 157.38 -46.66
REMARK 500
REMARK 500 THIS ENTRY HAS 157 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IH1 RELATED DB: PDB
REMARK 900 RELATED ID: 4IH9 RELATED DB: PDB
REMARK 900 RELATED ID: 4IHA RELATED DB: PDB
DBREF 4IH4 A 1 267 UNP Q9SQR3 Q9SQR3_ARATH 1 267
DBREF 4IH4 B 1 267 UNP Q9SQR3 Q9SQR3_ARATH 1 267
DBREF 4IH4 C 1 267 UNP Q9SQR3 Q9SQR3_ARATH 1 267
DBREF 4IH4 D 1 267 UNP Q9SQR3 Q9SQR3_ARATH 1 267
SEQRES 1 A 267 MET SER GLN HIS ASN ILE LEU GLU ALA LEU ASN VAL ARG
SEQRES 2 A 267 VAL VAL GLY THR GLY ASP ARG ILE LEU PHE LEU ALA HIS
SEQRES 3 A 267 GLY PHE GLY THR ASP GLN SER ALA TRP HIS LEU ILE LEU
SEQRES 4 A 267 PRO TYR PHE THR GLN ASN TYR ARG VAL VAL LEU TYR ASP
SEQRES 5 A 267 LEU VAL CYS ALA GLY SER VAL ASN PRO ASP TYR PHE ASP
SEQRES 6 A 267 PHE ASN ARG TYR THR THR LEU ASP PRO TYR VAL ASP ASP
SEQRES 7 A 267 LEU LEU ASN ILE VAL ASP SER LEU GLY ILE GLN ASN CYS
SEQRES 8 A 267 ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE
SEQRES 9 A 267 ILE ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS LEU
SEQRES 10 A 267 ILE LEU ILE GLY PHE SER PRO ARG PHE LEU ASN ASP GLU
SEQRES 11 A 267 ASP TYR HIS GLY GLY PHE GLU GLU GLY GLU ILE GLU LYS
SEQRES 12 A 267 VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP VAL
SEQRES 13 A 267 HIS GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO
SEQRES 14 A 267 ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN MET
SEQRES 15 A 267 ARG PRO ASP ILE SER LEU PHE VAL SER ARG THR VAL PHE
SEQRES 16 A 267 ASN SER ASP LEU ARG GLY VAL LEU GLY LEU VAL ARG VAL
SEQRES 17 A 267 PRO THR CYS VAL ILE GLN THR ALA LYS ASP VAL SER VAL
SEQRES 18 A 267 PRO ALA SER VAL ALA GLU TYR LEU ARG SER HIS LEU GLY
SEQRES 19 A 267 GLY ASP THR THR VAL GLU THR LEU LYS THR GLU GLY HIS
SEQRES 20 A 267 LEU PRO GLN LEU SER ALA PRO ALA GLN LEU ALA GLN PHE
SEQRES 21 A 267 LEU ARG ARG ALA LEU PRO ARG
SEQRES 1 B 267 MET SER GLN HIS ASN ILE LEU GLU ALA LEU ASN VAL ARG
SEQRES 2 B 267 VAL VAL GLY THR GLY ASP ARG ILE LEU PHE LEU ALA HIS
SEQRES 3 B 267 GLY PHE GLY THR ASP GLN SER ALA TRP HIS LEU ILE LEU
SEQRES 4 B 267 PRO TYR PHE THR GLN ASN TYR ARG VAL VAL LEU TYR ASP
SEQRES 5 B 267 LEU VAL CYS ALA GLY SER VAL ASN PRO ASP TYR PHE ASP
SEQRES 6 B 267 PHE ASN ARG TYR THR THR LEU ASP PRO TYR VAL ASP ASP
SEQRES 7 B 267 LEU LEU ASN ILE VAL ASP SER LEU GLY ILE GLN ASN CYS
SEQRES 8 B 267 ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE
SEQRES 9 B 267 ILE ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS LEU
SEQRES 10 B 267 ILE LEU ILE GLY PHE SER PRO ARG PHE LEU ASN ASP GLU
SEQRES 11 B 267 ASP TYR HIS GLY GLY PHE GLU GLU GLY GLU ILE GLU LYS
SEQRES 12 B 267 VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP VAL
SEQRES 13 B 267 HIS GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO
SEQRES 14 B 267 ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN MET
SEQRES 15 B 267 ARG PRO ASP ILE SER LEU PHE VAL SER ARG THR VAL PHE
SEQRES 16 B 267 ASN SER ASP LEU ARG GLY VAL LEU GLY LEU VAL ARG VAL
SEQRES 17 B 267 PRO THR CYS VAL ILE GLN THR ALA LYS ASP VAL SER VAL
SEQRES 18 B 267 PRO ALA SER VAL ALA GLU TYR LEU ARG SER HIS LEU GLY
SEQRES 19 B 267 GLY ASP THR THR VAL GLU THR LEU LYS THR GLU GLY HIS
SEQRES 20 B 267 LEU PRO GLN LEU SER ALA PRO ALA GLN LEU ALA GLN PHE
SEQRES 21 B 267 LEU ARG ARG ALA LEU PRO ARG
SEQRES 1 C 267 MET SER GLN HIS ASN ILE LEU GLU ALA LEU ASN VAL ARG
SEQRES 2 C 267 VAL VAL GLY THR GLY ASP ARG ILE LEU PHE LEU ALA HIS
SEQRES 3 C 267 GLY PHE GLY THR ASP GLN SER ALA TRP HIS LEU ILE LEU
SEQRES 4 C 267 PRO TYR PHE THR GLN ASN TYR ARG VAL VAL LEU TYR ASP
SEQRES 5 C 267 LEU VAL CYS ALA GLY SER VAL ASN PRO ASP TYR PHE ASP
SEQRES 6 C 267 PHE ASN ARG TYR THR THR LEU ASP PRO TYR VAL ASP ASP
SEQRES 7 C 267 LEU LEU ASN ILE VAL ASP SER LEU GLY ILE GLN ASN CYS
SEQRES 8 C 267 ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE
SEQRES 9 C 267 ILE ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS LEU
SEQRES 10 C 267 ILE LEU ILE GLY PHE SER PRO ARG PHE LEU ASN ASP GLU
SEQRES 11 C 267 ASP TYR HIS GLY GLY PHE GLU GLU GLY GLU ILE GLU LYS
SEQRES 12 C 267 VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP VAL
SEQRES 13 C 267 HIS GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO
SEQRES 14 C 267 ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN MET
SEQRES 15 C 267 ARG PRO ASP ILE SER LEU PHE VAL SER ARG THR VAL PHE
SEQRES 16 C 267 ASN SER ASP LEU ARG GLY VAL LEU GLY LEU VAL ARG VAL
SEQRES 17 C 267 PRO THR CYS VAL ILE GLN THR ALA LYS ASP VAL SER VAL
SEQRES 18 C 267 PRO ALA SER VAL ALA GLU TYR LEU ARG SER HIS LEU GLY
SEQRES 19 C 267 GLY ASP THR THR VAL GLU THR LEU LYS THR GLU GLY HIS
SEQRES 20 C 267 LEU PRO GLN LEU SER ALA PRO ALA GLN LEU ALA GLN PHE
SEQRES 21 C 267 LEU ARG ARG ALA LEU PRO ARG
SEQRES 1 D 267 MET SER GLN HIS ASN ILE LEU GLU ALA LEU ASN VAL ARG
SEQRES 2 D 267 VAL VAL GLY THR GLY ASP ARG ILE LEU PHE LEU ALA HIS
SEQRES 3 D 267 GLY PHE GLY THR ASP GLN SER ALA TRP HIS LEU ILE LEU
SEQRES 4 D 267 PRO TYR PHE THR GLN ASN TYR ARG VAL VAL LEU TYR ASP
SEQRES 5 D 267 LEU VAL CYS ALA GLY SER VAL ASN PRO ASP TYR PHE ASP
SEQRES 6 D 267 PHE ASN ARG TYR THR THR LEU ASP PRO TYR VAL ASP ASP
SEQRES 7 D 267 LEU LEU ASN ILE VAL ASP SER LEU GLY ILE GLN ASN CYS
SEQRES 8 D 267 ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE
SEQRES 9 D 267 ILE ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS LEU
SEQRES 10 D 267 ILE LEU ILE GLY PHE SER PRO ARG PHE LEU ASN ASP GLU
SEQRES 11 D 267 ASP TYR HIS GLY GLY PHE GLU GLU GLY GLU ILE GLU LYS
SEQRES 12 D 267 VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP VAL
SEQRES 13 D 267 HIS GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO
SEQRES 14 D 267 ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN MET
SEQRES 15 D 267 ARG PRO ASP ILE SER LEU PHE VAL SER ARG THR VAL PHE
SEQRES 16 D 267 ASN SER ASP LEU ARG GLY VAL LEU GLY LEU VAL ARG VAL
SEQRES 17 D 267 PRO THR CYS VAL ILE GLN THR ALA LYS ASP VAL SER VAL
SEQRES 18 D 267 PRO ALA SER VAL ALA GLU TYR LEU ARG SER HIS LEU GLY
SEQRES 19 D 267 GLY ASP THR THR VAL GLU THR LEU LYS THR GLU GLY HIS
SEQRES 20 D 267 LEU PRO GLN LEU SER ALA PRO ALA GLN LEU ALA GLN PHE
SEQRES 21 D 267 LEU ARG ARG ALA LEU PRO ARG
HELIX 1 1 ASP A 31 ILE A 38 5 8
HELIX 2 2 LEU A 39 GLN A 44 1 6
HELIX 3 3 ASN A 60 PHE A 64 5 5
HELIX 4 4 ASP A 73 LEU A 86 1 14
HELIX 5 5 SER A 97 ARG A 110 1 14
HELIX 6 6 GLU A 137 ASN A 151 1 15
HELIX 7 7 ASN A 151 GLY A 165 1 15
HELIX 8 8 PRO A 169 MET A 182 1 14
HELIX 9 9 ARG A 183 ASN A 196 1 14
HELIX 10 10 GLY A 201 VAL A 206 1 6
HELIX 11 11 SER A 224 HIS A 232 1 9
HELIX 12 12 LEU A 248 ALA A 253 1 6
HELIX 13 13 ALA A 253 ARG A 263 1 11
HELIX 14 14 ASP B 31 ILE B 38 5 8
HELIX 15 15 LEU B 39 GLN B 44 1 6
HELIX 16 16 ASN B 60 PHE B 64 5 5
HELIX 17 17 ASP B 73 LEU B 86 1 14
HELIX 18 18 SER B 97 ARG B 110 1 14
HELIX 19 19 GLU B 137 ASN B 151 1 15
HELIX 20 20 ASN B 151 GLY B 165 1 15
HELIX 21 21 ARG B 173 MET B 182 1 10
HELIX 22 22 ARG B 183 SER B 197 1 15
HELIX 23 23 GLY B 201 VAL B 206 1 6
HELIX 24 24 SER B 224 HIS B 232 1 9
HELIX 25 25 LEU B 248 ALA B 253 1 6
HELIX 26 26 ALA B 253 ARG B 263 1 11
HELIX 27 27 ASP C 31 ILE C 38 5 8
HELIX 28 28 LEU C 39 GLN C 44 1 6
HELIX 29 29 ASN C 60 PHE C 64 5 5
HELIX 30 30 ASP C 73 LEU C 86 1 14
HELIX 31 31 SER C 97 ARG C 110 1 14
HELIX 32 32 GLU C 137 ASN C 151 1 15
HELIX 33 33 ASN C 151 GLY C 165 1 15
HELIX 34 34 PRO C 169 MET C 182 1 14
HELIX 35 35 ARG C 183 ASN C 196 1 14
HELIX 36 36 GLY C 201 VAL C 206 1 6
HELIX 37 37 SER C 224 HIS C 232 1 9
HELIX 38 38 LEU C 248 ALA C 253 1 6
HELIX 39 39 ALA C 253 ARG C 263 1 11
HELIX 40 40 ASP D 31 ILE D 38 5 8
HELIX 41 41 LEU D 39 GLN D 44 1 6
HELIX 42 42 ASN D 60 PHE D 64 5 5
HELIX 43 43 ASP D 73 LEU D 86 1 14
HELIX 44 44 SER D 97 ARG D 110 1 14
HELIX 45 45 GLU D 137 ASN D 151 1 15
HELIX 46 46 ASN D 151 GLY D 165 1 15
HELIX 47 47 PRO D 169 MET D 182 1 14
HELIX 48 48 ARG D 183 SER D 197 1 15
HELIX 49 49 GLY D 201 VAL D 206 1 6
HELIX 50 50 SER D 224 HIS D 232 1 9
HELIX 51 51 LEU D 248 ALA D 253 1 6
HELIX 52 52 ALA D 253 ARG D 263 1 11
SHEET 1 A 3 VAL A 14 GLY A 16 0
SHEET 2 A 3 ARG A 47 TYR A 51 -1 O VAL A 48 N VAL A 15
SHEET 3 A 3 ILE A 21 ALA A 25 1 N LEU A 24 O VAL A 49
SHEET 1 B 4 VAL A 94 HIS A 96 0
SHEET 2 B 4 ILE A 118 ILE A 120 1 O ILE A 120 N GLY A 95
SHEET 3 B 4 CYS A 211 GLN A 214 1 O CYS A 211 N LEU A 119
SHEET 4 B 4 GLU A 240 THR A 241 1 O GLU A 240 N GLN A 214
SHEET 1 C 3 ARG B 13 VAL B 15 0
SHEET 2 C 3 VAL B 48 TYR B 51 -1 O VAL B 48 N VAL B 15
SHEET 3 C 3 PHE B 23 ALA B 25 1 N LEU B 24 O VAL B 49
SHEET 1 D 4 VAL B 94 HIS B 96 0
SHEET 2 D 4 ILE B 118 ILE B 120 1 O ILE B 120 N GLY B 95
SHEET 3 D 4 CYS B 211 GLN B 214 1 O CYS B 211 N LEU B 119
SHEET 4 D 4 GLU B 240 THR B 241 1 O GLU B 240 N VAL B 212
SHEET 1 E 3 VAL C 14 GLY C 16 0
SHEET 2 E 3 ARG C 47 LEU C 50 -1 O VAL C 48 N VAL C 15
SHEET 3 E 3 ILE C 21 LEU C 24 1 N LEU C 24 O VAL C 49
SHEET 1 F 4 VAL C 94 HIS C 96 0
SHEET 2 F 4 ILE C 118 ILE C 120 1 O ILE C 120 N GLY C 95
SHEET 3 F 4 CYS C 211 GLN C 214 1 O CYS C 211 N LEU C 119
SHEET 4 F 4 GLU C 240 THR C 241 1 O GLU C 240 N GLN C 214
SHEET 1 G 3 VAL D 14 VAL D 15 0
SHEET 2 G 3 VAL D 48 TYR D 51 -1 O VAL D 48 N VAL D 15
SHEET 3 G 3 PHE D 23 ALA D 25 1 N LEU D 24 O VAL D 49
SHEET 1 H 4 ALA D 92 HIS D 96 0
SHEET 2 H 4 LYS D 116 ILE D 120 1 O ILE D 120 N GLY D 95
SHEET 3 H 4 THR D 210 GLN D 214 1 O CYS D 211 N LEU D 119
SHEET 4 H 4 GLU D 240 THR D 241 1 O GLU D 240 N GLN D 214
CISPEP 1 LEU A 265 PRO A 266 0 -0.24
CISPEP 2 LEU B 265 PRO B 266 0 1.60
CISPEP 3 LEU C 265 PRO C 266 0 -0.21
CISPEP 4 LEU D 265 PRO D 266 0 -0.17
CRYST1 184.856 44.629 160.967 90.00 121.07 90.00 C 1 2 1 16
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 0.005410 0.000000 0.003259 0.00000
SCALE2 0.000000 0.022407 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007253 0.00000
TER 2041 PRO A 266
TER 4082 PRO B 266
TER 6123 PRO C 266
TER 8164 PRO D 266
MASTER 384 0 0 52 28 0 0 6 8160 4 0 84
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