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HEADER HYDROLASE 01-SEP-15 5DJ5
TITLE CRYSTAL STRUCTURE OF RICE DWARF14 IN COMPLEX WITH SYNTHETIC
TITLE 2 STRIGOLACTONE GR24
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE STRIGOLACTONE ESTERASE D14;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: ALPHA/BETA HYDROLASE RESIDUES 52-318;
COMPND 5 SYNONYM: PROTEIN DWARF-14,PROTEIN DWARF-88,PROTEIN HIGH-TILLERING
COMPND 6 DWARF 2;
COMPND 7 EC: 3.1.-.-;
COMPND 8 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: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSUMO
KEYWDS ALPHA/BETA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.E.ZHOU,L.-H.ZHAO,W.YI,Z.-S.WU,Y.LIU,Y.KANG,L.HOU,P.W.DE WAAL,S.LI,
AUTHOR 2 Y.JIANG,K.MELCHER,H.E.XU
REVDAT 1 28-OCT-15 5DJ5 0
JRNL AUTH L.H.ZHAO,X.E.ZHOU,W.YI,Z.WU,Y.LIU,Y.KANG,L.HOU,P.W.DE WAAL,
JRNL AUTH 2 S.LI,Y.JIANG,A.SCAFFIDI,G.R.FLEMATTI,S.M.SMITH,V.Q.LAM,
JRNL AUTH 3 P.R.GRIFFIN,Y.WANG,J.LI,K.MELCHER,H.E.XU
JRNL TITL DESTABILIZATION OF STRIGOLACTONE RECEPTOR DWARF14 BY BINDING
JRNL TITL 2 OF LIGAND AND E3-LIGASE SIGNALING EFFECTOR DWARF3.
JRNL REF CELL RES. 2015
JRNL REFN ISSN 1001-0602
JRNL PMID 26470846
JRNL DOI 10.1038/CR.2015.122
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.3
REMARK 3 NUMBER OF REFLECTIONS : 17868
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1254
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.60
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.740
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 : 0.008 4258
REMARK 3 ANGLE : 1.147 5811
REMARK 3 CHIRALITY : 0.123 672
REMARK 3 PLANARITY : 0.006 753
REMARK 3 DIHEDRAL : 12.713 1533
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 5DJ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213301.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
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 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17932
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 41.202
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.7
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13600
REMARK 200 FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.2
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.65400
REMARK 200 R SYM FOR SHELL (I) : 0.65400
REMARK 200 FOR SHELL : 1.100
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: 4IH9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, ETHYLENE GLYCOL, PH 7.5,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 298K
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 24.20000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.28500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.94000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.28500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.20000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.94000
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 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 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 SER A 2
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 O ALA B 4 O HOH B 301 2.18
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 SER A 97 -117.42 57.59
REMARK 500 SER B 97 -116.21 56.76
REMARK 500 THR B 244 164.69 173.81
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 B 397 DISTANCE = 6.60 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GR2 A 800
DBREF 5DJ5 A 2 268 UNP Q10QA5 D14_ORYSJ 52 318
DBREF 5DJ5 B 2 268 UNP Q10QA5 D14_ORYSJ 52 318
SEQRES 1 A 267 SER GLY ALA LYS LEU LEU GLN ILE LEU ASN VAL ARG VAL
SEQRES 2 A 267 VAL GLY SER GLY GLU ARG VAL VAL VAL LEU SER HIS GLY
SEQRES 3 A 267 PHE GLY THR ASP GLN SER ALA TRP SER ARG VAL LEU PRO
SEQRES 4 A 267 TYR LEU THR ARG ASP HIS ARG VAL VAL LEU TYR ASP LEU
SEQRES 5 A 267 VAL CYS ALA GLY SER VAL ASN PRO ASP HIS PHE ASP PHE
SEQRES 6 A 267 ARG ARG TYR ASP ASN LEU ASP ALA TYR VAL ASP ASP LEU
SEQRES 7 A 267 LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG CYS ALA
SEQRES 8 A 267 PHE VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE LEU
SEQRES 9 A 267 ALA SER ILE ARG ARG PRO ASP LEU PHE ALA LYS LEU VAL
SEQRES 10 A 267 LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP SER ASP
SEQRES 11 A 267 TYR HIS GLY GLY PHE GLU LEU GLU GLU ILE GLN GLN VAL
SEQRES 12 A 267 PHE ASP ALA MET GLY ALA ASN TYR SER ALA TRP ALA THR
SEQRES 13 A 267 GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO ALA
SEQRES 14 A 267 ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES 15 A 267 PRO ASP ILE SER LEU HIS VAL CYS GLN THR VAL PHE LYS
SEQRES 16 A 267 THR ASP LEU ARG GLY VAL LEU GLY MET VAL ARG ALA PRO
SEQRES 17 A 267 CYS VAL VAL VAL GLN THR THR ARG ASP VAL SER VAL PRO
SEQRES 18 A 267 ALA SER VAL ALA ALA TYR LEU LYS ALA HIS LEU GLY GLY
SEQRES 19 A 267 ARG THR THR VAL GLU PHE LEU GLN THR GLU GLY HIS LEU
SEQRES 20 A 267 PRO HIS LEU SER ALA PRO SER LEU LEU ALA GLN VAL LEU
SEQRES 21 A 267 ARG ARG ALA LEU ALA ARG TYR
SEQRES 1 B 267 SER GLY ALA LYS LEU LEU GLN ILE LEU ASN VAL ARG VAL
SEQRES 2 B 267 VAL GLY SER GLY GLU ARG VAL VAL VAL LEU SER HIS GLY
SEQRES 3 B 267 PHE GLY THR ASP GLN SER ALA TRP SER ARG VAL LEU PRO
SEQRES 4 B 267 TYR LEU THR ARG ASP HIS ARG VAL VAL LEU TYR ASP LEU
SEQRES 5 B 267 VAL CYS ALA GLY SER VAL ASN PRO ASP HIS PHE ASP PHE
SEQRES 6 B 267 ARG ARG TYR ASP ASN LEU ASP ALA TYR VAL ASP ASP LEU
SEQRES 7 B 267 LEU ALA ILE LEU ASP ALA LEU ARG ILE PRO ARG CYS ALA
SEQRES 8 B 267 PHE VAL GLY HIS SER VAL SER ALA MET ILE GLY ILE LEU
SEQRES 9 B 267 ALA SER ILE ARG ARG PRO ASP LEU PHE ALA LYS LEU VAL
SEQRES 10 B 267 LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP SER ASP
SEQRES 11 B 267 TYR HIS GLY GLY PHE GLU LEU GLU GLU ILE GLN GLN VAL
SEQRES 12 B 267 PHE ASP ALA MET GLY ALA ASN TYR SER ALA TRP ALA THR
SEQRES 13 B 267 GLY TYR ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO ALA
SEQRES 14 B 267 ALA VAL GLN GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES 15 B 267 PRO ASP ILE SER LEU HIS VAL CYS GLN THR VAL PHE LYS
SEQRES 16 B 267 THR ASP LEU ARG GLY VAL LEU GLY MET VAL ARG ALA PRO
SEQRES 17 B 267 CYS VAL VAL VAL GLN THR THR ARG ASP VAL SER VAL PRO
SEQRES 18 B 267 ALA SER VAL ALA ALA TYR LEU LYS ALA HIS LEU GLY GLY
SEQRES 19 B 267 ARG THR THR VAL GLU PHE LEU GLN THR GLU GLY HIS LEU
SEQRES 20 B 267 PRO HIS LEU SER ALA PRO SER LEU LEU ALA GLN VAL LEU
SEQRES 21 B 267 ARG ARG ALA LEU ALA ARG TYR
HET GR2 A 800 22
HETNAM GR2 (3E,3AR,8BS)-3-({[(2R)-4-METHYL-5-OXO-2,5-DIHYDROFURAN-
HETNAM 2 GR2 2-YL]OXY}METHYLIDENE)-3,3A,4,8B-TETRAHYDRO-2H-
HETNAM 3 GR2 INDENO[1,2-B]FURAN-2-ONE
FORMUL 3 GR2 C17 H14 O5
FORMUL 4 HOH *163(H2 O)
HELIX 1 AA1 GLY A 3 LEU A 10 1 8
HELIX 2 AA2 ASP A 31 SER A 36 5 6
HELIX 3 AA3 VAL A 38 THR A 43 1 6
HELIX 4 AA4 ASN A 60 PHE A 64 5 5
HELIX 5 AA5 ARG A 67 ASN A 71 5 5
HELIX 6 AA6 LEU A 72 LEU A 86 1 15
HELIX 7 AA7 SER A 97 ARG A 110 1 14
HELIX 8 AA8 GLU A 137 ASN A 151 1 15
HELIX 9 AA9 ASN A 151 GLY A 165 1 15
HELIX 10 AB1 VAL A 168 ASN A 181 1 14
HELIX 11 AB2 ARG A 183 LYS A 196 1 14
HELIX 12 AB3 LEU A 199 VAL A 206 5 8
HELIX 13 AB4 PRO A 222 LEU A 233 1 12
HELIX 14 AB5 LEU A 248 ALA A 253 1 6
HELIX 15 AB6 ALA A 253 LEU A 265 1 13
HELIX 16 AB7 GLY B 3 LEU B 10 1 8
HELIX 17 AB8 ASP B 31 SER B 36 5 6
HELIX 18 AB9 VAL B 38 ARG B 44 1 7
HELIX 19 AC1 ASN B 60 PHE B 64 5 5
HELIX 20 AC2 ARG B 67 ASP B 70 5 4
HELIX 21 AC3 ASN B 71 LEU B 86 1 16
HELIX 22 AC4 SER B 97 ARG B 110 1 14
HELIX 23 AC5 GLU B 137 ASN B 151 1 15
HELIX 24 AC6 ASN B 151 GLY B 165 1 15
HELIX 25 AC7 VAL B 168 ASN B 181 1 14
HELIX 26 AC8 ARG B 183 LYS B 196 1 14
HELIX 27 AC9 LEU B 199 VAL B 206 5 8
HELIX 28 AD1 PRO B 222 LEU B 233 1 12
HELIX 29 AD2 LEU B 248 ALA B 253 1 6
HELIX 30 AD3 ALA B 253 LEU B 265 1 13
SHEET 1 AA1 7 ARG A 13 VAL A 15 0
SHEET 2 AA1 7 HIS A 46 LEU A 50 -1 O VAL A 48 N VAL A 15
SHEET 3 AA1 7 ARG A 20 SER A 25 1 N ARG A 20 O ARG A 47
SHEET 4 AA1 7 CYS A 91 HIS A 96 1 O VAL A 94 N VAL A 23
SHEET 5 AA1 7 PHE A 114 ILE A 120 1 O ALA A 115 N CYS A 91
SHEET 6 AA1 7 CYS A 210 GLN A 214 1 O VAL A 213 N LEU A 119
SHEET 7 AA1 7 THR A 237 PHE A 241 1 O THR A 238 N VAL A 212
SHEET 1 AA2 7 ARG B 13 GLY B 16 0
SHEET 2 AA2 7 ARG B 47 LEU B 50 -1 O VAL B 48 N VAL B 15
SHEET 3 AA2 7 VAL B 21 SER B 25 1 N VAL B 22 O VAL B 49
SHEET 4 AA2 7 CYS B 91 HIS B 96 1 O VAL B 94 N VAL B 23
SHEET 5 AA2 7 PHE B 114 ILE B 120 1 O VAL B 118 N PHE B 93
SHEET 6 AA2 7 CYS B 210 GLN B 214 1 O VAL B 213 N LEU B 119
SHEET 7 AA2 7 THR B 237 PHE B 241 1 O THR B 238 N VAL B 212
SITE 1 AC1 9 PHE A 28 SER A 97 VAL A 98 VAL A 144
SITE 2 AC1 9 TYR A 159 CYS A 191 VAL A 219 SER A 220
SITE 3 AC1 9 HIS A 247
CRYST1 48.400 87.880 118.570 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 0.020661 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011379 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008434 0.00000
TER 2068 TYR A 268
TER 4139 TYR B 268
MASTER 253 0 1 30 14 0 3 6 4301 2 22 42
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