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HEADER HYDROLASE 29-SEP-17 6ELX
TITLE ORYZA SATIVA DWARF14
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 BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS STRIGOLACTONE, STRIGOLACTONE RECEPTOR, D14, LIGAND BINDING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.ANDERSSON,G.H.CARLSSON,D.HASSE
REVDAT 1 09-MAY-18 6ELX 0
JRNL AUTH G.H.CARLSSON,D.HASSE,F.CARDINALE,C.PRANDI,I.ANDERSSON
JRNL TITL THE ELUSIVE LIGAND COMPLEXES OF THE DWARF14 STRIGOLACTONE
JRNL TITL 2 RECEPTOR.
JRNL REF J. EXP. BOT. V. 69 2345 2018
JRNL REFN ESSN 1460-2431
JRNL PMID 29394369
JRNL DOI 10.1093/JXB/ERY036
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2880: ???)
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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 107538
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.177
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 5357
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 44.6339 - 4.0384 0.99 4243 221 0.1551 0.1527
REMARK 3 2 4.0384 - 3.2057 0.99 4042 215 0.1380 0.1760
REMARK 3 3 3.2057 - 2.8006 0.99 4046 214 0.1552 0.1574
REMARK 3 4 2.8006 - 2.5445 1.00 4028 207 0.1577 0.1839
REMARK 3 5 2.5445 - 2.3622 0.99 3957 212 0.1540 0.1740
REMARK 3 6 2.3622 - 2.2229 0.99 3971 210 0.1507 0.1653
REMARK 3 7 2.2229 - 2.1116 0.99 3932 204 0.1468 0.1723
REMARK 3 8 2.1116 - 2.0197 0.99 3947 208 0.1486 0.1668
REMARK 3 9 2.0197 - 1.9419 0.99 3936 206 0.1547 0.1778
REMARK 3 10 1.9419 - 1.8749 0.98 3917 211 0.1607 0.1691
REMARK 3 11 1.8749 - 1.8163 0.97 3853 200 0.1702 0.1708
REMARK 3 12 1.8163 - 1.7644 0.98 3884 207 0.1583 0.1904
REMARK 3 13 1.7644 - 1.7179 0.99 3890 208 0.1614 0.1841
REMARK 3 14 1.7179 - 1.6760 0.97 3855 198 0.1627 0.1989
REMARK 3 15 1.6760 - 1.6379 0.98 3876 211 0.1626 0.1704
REMARK 3 16 1.6379 - 1.6030 0.98 3867 208 0.1636 0.2015
REMARK 3 17 1.6030 - 1.5710 0.95 3775 191 0.1685 0.1860
REMARK 3 18 1.5710 - 1.5413 0.97 3835 206 0.1755 0.1900
REMARK 3 19 1.5413 - 1.5138 0.97 3795 200 0.1761 0.1849
REMARK 3 20 1.5138 - 1.4881 0.97 3839 211 0.1765 0.2045
REMARK 3 21 1.4881 - 1.4641 0.97 3800 204 0.1897 0.2136
REMARK 3 22 1.4641 - 1.4416 0.96 3782 203 0.1898 0.2346
REMARK 3 23 1.4416 - 1.4204 0.97 3788 200 0.1975 0.2375
REMARK 3 24 1.4204 - 1.4004 0.94 3764 187 0.2002 0.2231
REMARK 3 25 1.4004 - 1.3815 0.86 3343 179 0.2162 0.2186
REMARK 3 26 1.3815 - 1.3635 0.76 3019 137 0.2138 0.2349
REMARK 3 27 1.3635 - 1.3465 0.69 2737 130 0.2108 0.2230
REMARK 3 28 1.3465 - 1.3302 0.63 2482 126 0.2163 0.2379
REMARK 3 29 1.3302 - 1.3148 0.58 2291 144 0.2286 0.2553
REMARK 3 30 1.3148 - 1.3000 0.54 2069 129 0.2339 0.2377
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.45
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 : 0.005 4579
REMARK 3 ANGLE : 0.785 6298
REMARK 3 CHIRALITY : 0.076 729
REMARK 3 PLANARITY : 0.005 823
REMARK 3 DIHEDRAL : 2.918 3331
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 6ELX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1200006825.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99188
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 107538
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 44.610
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.05099
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.1500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.41840
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: PHENIX
REMARK 200 STARTING MODEL: 1WOM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES PH 7.0, 2-METHYLPENTANDIOL,
REMARK 280 VAPOR DIFFUSION, HANGING 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 24.06000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.47000
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 59.47000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.06000
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 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 -124.27 64.44
REMARK 500 ASN A 201 78.75 -161.80
REMARK 500 ALA A 303 55.48 -145.01
REMARK 500 ASP B 81 -168.46 -129.88
REMARK 500 ASP B 95 17.89 -140.73
REMARK 500 SER B 147 -127.37 62.98
REMARK 500 ARG B 175 123.80 -171.93
REMARK 500 ASP B 179 88.20 -160.22
REMARK 500 SER B 180 -118.03 55.57
REMARK 500 ASP B 181 -16.45 70.41
REMARK 500 ASP B 181 25.73 -79.27
REMARK 500 ASN B 201 82.85 -156.79
REMARK 500 ALA B 303 56.08 -142.43
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 809 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 810 DISTANCE = 5.95 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MRD A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 405
DBREF 6ELX A 52 318 UNP Q10QA5 D14_ORYSJ 52 318
DBREF 6ELX B 52 318 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 MRD A 401 8
HET GOL A 402 6
HET GOL A 403 6
HET GOL A 404 6
HET MPD B 401 8
HET GOL B 402 6
HET GOL B 403 6
HET GOL B 404 6
HET GOL B 405 6
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
HETNAM GOL GLYCEROL
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 MRD C6 H14 O2
FORMUL 4 GOL 7(C3 H8 O3)
FORMUL 7 MPD C6 H14 O2
FORMUL 12 HOH *605(H2 O)
HELIX 1 AA1 SER A 52 LEU A 60 1 9
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 LYS A 246 1 14
HELIX 12 AB3 LEU A 249 VAL A 256 5 8
HELIX 13 AB4 ALA A 273 LEU A 283 1 11
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 GLY B 53 LEU B 60 1 8
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 PRO B 272 LEU B 283 1 12
HELIX 29 AD2 LEU B 298 ALA B 303 1 6
HELIX 30 AD3 ALA B 303 ALA B 316 1 14
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 VAL A 99
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 263 N LEU A 169
SHEET 7 AA1 7 THR A 287 PHE A 291 1 O GLU A 290 N GLN A 264
SHEET 1 AA2 7 ARG B 63 GLY B 66 0
SHEET 2 AA2 7 ARG B 97 TYR B 101 -1 O LEU B 100 N ARG B 63
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
SITE 1 AC1 5 TYR A 209 SER A 270 HOH A 502 HOH A 522
SITE 2 AC1 5 HOH A 680
SITE 1 AC2 5 TYR A 182 HIS A 183 SER A 274 VAL A 275
SITE 2 AC2 5 TYR A 278
SITE 1 AC3 7 ARG A 94 ASP A 95 ARG A 312 ASP B 112
SITE 2 AC3 7 HIS B 113 PHE B 114 HOH B 660
SITE 1 AC4 6 LEU A 56 ILE A 59 HIS A 113 ARG A 118
SITE 2 AC4 6 TYR A 119 ASP A 128
SITE 1 AC5 4 TYR B 209 PHE B 245 SER B 270 HOH B 520
SITE 1 AC6 8 ASP B 181 TYR B 182 HIS B 183 GLY B 208
SITE 2 AC6 8 LEU B 212 SER B 274 VAL B 275 HOH B 527
SITE 1 AC7 4 VAL A 252 ARG B 97 LEU B 136 HOH B 602
SITE 1 AC8 4 ARG B 175 LEU B 177 LYS B 246 ASP B 248
SITE 1 AC9 6 ASP B 120 GLN B 242 THR B 243 LYS B 246
SITE 2 AC9 6 HOH B 536 HOH B 554
CRYST1 48.120 88.640 118.940 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 0.020781 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011282 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008408 0.00000
TER 2169 TYR A 318
TER 4384 TYR B 318
MASTER 304 0 9 30 14 0 15 6 4785 2 58 42
END |