| content |
HEADER HYDROLASE 11-JUL-11 3STV
TITLE CRYSTAL STRUCTURE OF TOMATO METHYLKETONE SYNTHASE I COMPLEXED WITH 3-
TITLE 2 HYDROXYOCTANOATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHYLKETONE SYNTHASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LYCOPERSICON HIRSUTUM F. GLABRATUM;
SOURCE 3 ORGANISM_TAXID: 283673;
SOURCE 4 GENE: MKS1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHIS9GW
KEYWDS METHYLKETONE, ALPHA/BETA HYDROLASE, DECARBOXYLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.E.AULDRIDGE,M.B.AUSTIN,J.P.NOEL
REVDAT 1 02-MAY-12 3STV 0
JRNL AUTH M.E.AULDRIDGE,Y.GUO,M.B.AUSTIN,J.RAMSEY,E.FRIDMAN,
JRNL AUTH 2 E.PICHERSKY,J.P.NOEL
JRNL TITL EMERGENT DECARBOXYLASE ACTIVITY AND ATTENUATION OF
JRNL TITL 2 {ALPHA}/{BETA}-HYDROLASE ACTIVITY DURING THE EVOLUTION OF
JRNL TITL 3 METHYLKETONE BIOSYNTHESIS IN TOMATO
JRNL REF PLANT CELL 2012
JRNL REFN ESSN 1532-298X
JRNL DOI 10.1105/TPC.111.093997
REMARK 2
REMARK 2 RESOLUTION. 2.20 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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 26450
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1319
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 : 3975
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 218
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.97
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.79500
REMARK 3 B22 (A**2) : -1.54800
REMARK 3 B33 (A**2) : 0.75300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.50500
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) : 1.984 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.994 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.053 ; 2.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.278 ; 4.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 44.46
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : 3HO.PAR
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : 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
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3STV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-11.
REMARK 100 THE RCSB ID CODE IS RCSB066644.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JAN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL1-5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97944
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26450
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 19.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.8500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.51700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.490
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 7YAS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M PIPES-NA+, 22% (W/V) PEG 8000,
REMARK 280 0.3M NABR, 2MM DITHIOTHREITOL, 4 HR SOAK IN 1MM 3-
REMARK 280 HYDROXYOCTANOATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 46.19000
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 LYS A 3
REMARK 465 SER A 4
REMARK 465 MET A 5
REMARK 465 SER A 6
REMARK 465 PRO A 7
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 LYS B 3
REMARK 465 SER B 4
REMARK 465 MET B 5
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 PHE A 20 -20.68 73.12
REMARK 500 PRO A 76 172.58 -53.92
REMARK 500 ALA A 77 -71.49 -56.44
REMARK 500 ALA A 87 -111.10 44.91
REMARK 500 MET A 114 66.01 -118.48
REMARK 500 VAL A 132 -55.77 -123.27
REMARK 500 LEU A 136 -115.91 44.67
REMARK 500 PRO A 149 152.18 -48.17
REMARK 500 VAL A 164 -60.04 -103.33
REMARK 500 ARG A 201 -80.27 -113.88
REMARK 500 ASP A 216 87.28 -157.00
REMARK 500 ASP A 242 -156.34 -94.72
REMARK 500 PHE B 20 -18.10 76.90
REMARK 500 ALA B 77 -32.46 -28.51
REMARK 500 ALA B 87 -110.50 48.69
REMARK 500 ASN B 118 -77.38 -95.41
REMARK 500 LEU B 136 -118.75 44.69
REMARK 500 VAL B 195 77.03 -105.64
REMARK 500 ARG B 201 -74.40 -100.30
REMARK 500 ALA B 217 -62.87 -96.74
REMARK 500 TYR B 264 48.92 -106.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3HO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 266
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3STT RELATED DB: PDB
REMARK 900 RELATED ID: 3STU RELATED DB: PDB
REMARK 900 RELATED ID: 3STW RELATED DB: PDB
REMARK 900 RELATED ID: 3STX RELATED DB: PDB
REMARK 900 RELATED ID: 3STY RELATED DB: PDB
DBREF 3STV A 1 265 UNP E0YCS2 E0YCS2_SOLHA 1 265
DBREF 3STV B 1 265 UNP E0YCS2 E0YCS2_SOLHA 1 265
SEQADV 3STV GLY A -1 UNP E0YCS2 EXPRESSION TAG
SEQADV 3STV SER A 0 UNP E0YCS2 EXPRESSION TAG
SEQADV 3STV GLY B -1 UNP E0YCS2 EXPRESSION TAG
SEQADV 3STV SER B 0 UNP E0YCS2 EXPRESSION TAG
SEQRES 1 A 267 GLY SER MET GLU LYS SER MET SER PRO PHE VAL LYS LYS
SEQRES 2 A 267 HIS PHE VAL LEU VAL HIS THR ALA PHE HIS GLY ALA TRP
SEQRES 3 A 267 CYS TRP TYR LYS ILE VAL ALA LEU MET ARG SER SER GLY
SEQRES 4 A 267 HIS ASN VAL THR ALA LEU ASP LEU GLY ALA SER GLY ILE
SEQRES 5 A 267 ASN PRO LYS GLN ALA LEU GLN ILE PRO ASN PHE SER ASP
SEQRES 6 A 267 TYR LEU SER PRO LEU MET GLU PHE MET ALA SER LEU PRO
SEQRES 7 A 267 ALA ASN GLU LYS ILE ILE LEU VAL GLY HIS ALA LEU GLY
SEQRES 8 A 267 GLY LEU ALA ILE SER LYS ALA MET GLU THR PHE PRO GLU
SEQRES 9 A 267 LYS ILE SER VAL ALA VAL PHE LEU SER GLY LEU MET PRO
SEQRES 10 A 267 GLY PRO ASN ILE ASP ALA THR THR VAL CYS THR LYS ALA
SEQRES 11 A 267 GLY SER ALA VAL LEU GLY GLN LEU ASP ASN CYS VAL THR
SEQRES 12 A 267 TYR GLU ASN GLY PRO THR ASN PRO PRO THR THR LEU ILE
SEQRES 13 A 267 ALA GLY PRO LYS PHE LEU ALA THR ASN VAL TYR HIS LEU
SEQRES 14 A 267 SER PRO ILE GLU ASP LEU ALA LEU ALA THR ALA LEU VAL
SEQRES 15 A 267 ARG PRO LEU TYR LEU TYR LEU ALA GLU ASP ILE SER LYS
SEQRES 16 A 267 GLU VAL VAL LEU SER SER LYS ARG TYR GLY SER VAL LYS
SEQRES 17 A 267 ARG VAL PHE ILE VAL ALA THR GLU ASN ASP ALA LEU LYS
SEQRES 18 A 267 LYS GLU PHE LEU LYS LEU MET ILE GLU LYS ASN PRO PRO
SEQRES 19 A 267 ASP GLU VAL LYS GLU ILE GLU GLY SER ASP HIS VAL THR
SEQRES 20 A 267 MET MET SER LYS PRO GLN GLN LEU PHE THR THR LEU LEU
SEQRES 21 A 267 SER ILE ALA ASN LYS TYR LYS
SEQRES 1 B 267 GLY SER MET GLU LYS SER MET SER PRO PHE VAL LYS LYS
SEQRES 2 B 267 HIS PHE VAL LEU VAL HIS THR ALA PHE HIS GLY ALA TRP
SEQRES 3 B 267 CYS TRP TYR LYS ILE VAL ALA LEU MET ARG SER SER GLY
SEQRES 4 B 267 HIS ASN VAL THR ALA LEU ASP LEU GLY ALA SER GLY ILE
SEQRES 5 B 267 ASN PRO LYS GLN ALA LEU GLN ILE PRO ASN PHE SER ASP
SEQRES 6 B 267 TYR LEU SER PRO LEU MET GLU PHE MET ALA SER LEU PRO
SEQRES 7 B 267 ALA ASN GLU LYS ILE ILE LEU VAL GLY HIS ALA LEU GLY
SEQRES 8 B 267 GLY LEU ALA ILE SER LYS ALA MET GLU THR PHE PRO GLU
SEQRES 9 B 267 LYS ILE SER VAL ALA VAL PHE LEU SER GLY LEU MET PRO
SEQRES 10 B 267 GLY PRO ASN ILE ASP ALA THR THR VAL CYS THR LYS ALA
SEQRES 11 B 267 GLY SER ALA VAL LEU GLY GLN LEU ASP ASN CYS VAL THR
SEQRES 12 B 267 TYR GLU ASN GLY PRO THR ASN PRO PRO THR THR LEU ILE
SEQRES 13 B 267 ALA GLY PRO LYS PHE LEU ALA THR ASN VAL TYR HIS LEU
SEQRES 14 B 267 SER PRO ILE GLU ASP LEU ALA LEU ALA THR ALA LEU VAL
SEQRES 15 B 267 ARG PRO LEU TYR LEU TYR LEU ALA GLU ASP ILE SER LYS
SEQRES 16 B 267 GLU VAL VAL LEU SER SER LYS ARG TYR GLY SER VAL LYS
SEQRES 17 B 267 ARG VAL PHE ILE VAL ALA THR GLU ASN ASP ALA LEU LYS
SEQRES 18 B 267 LYS GLU PHE LEU LYS LEU MET ILE GLU LYS ASN PRO PRO
SEQRES 19 B 267 ASP GLU VAL LYS GLU ILE GLU GLY SER ASP HIS VAL THR
SEQRES 20 B 267 MET MET SER LYS PRO GLN GLN LEU PHE THR THR LEU LEU
SEQRES 21 B 267 SER ILE ALA ASN LYS TYR LYS
HET 3HO A 301 11
HET BR B 266 1
HETNAM 3HO (3S)-3-HYDROXYOCTANOIC ACID
HETNAM BR BROMIDE ION
FORMUL 3 3HO C8 H16 O3
FORMUL 4 BR BR 1-
FORMUL 5 HOH *218(H2 O)
HELIX 1 1 GLY A 22 CYS A 25 5 4
HELIX 2 2 TRP A 26 SER A 36 1 11
HELIX 3 3 GLN A 54 ILE A 58 5 5
HELIX 4 4 ASN A 60 LEU A 75 1 16
HELIX 5 5 LEU A 88 PHE A 100 1 13
HELIX 6 6 ASP A 120 ALA A 131 1 12
HELIX 7 7 GLY A 156 VAL A 164 1 9
HELIX 8 8 PRO A 169 ALA A 178 1 10
HELIX 9 9 LEU A 187 VAL A 195 1 9
HELIX 10 10 ARG A 201 VAL A 205 5 5
HELIX 11 11 ASP A 216 ASN A 230 1 15
HELIX 12 12 VAL A 244 LYS A 249 1 6
HELIX 13 13 LYS A 249 TYR A 264 1 16
HELIX 14 14 GLY B 22 CYS B 25 5 4
HELIX 15 15 TRP B 26 GLY B 37 1 12
HELIX 16 16 GLN B 54 ILE B 58 5 5
HELIX 17 17 ASN B 60 LEU B 75 1 16
HELIX 18 18 LEU B 88 PHE B 100 1 13
HELIX 19 19 ASP B 120 LEU B 133 1 14
HELIX 20 20 GLY B 156 VAL B 164 1 9
HELIX 21 21 PRO B 169 VAL B 180 1 12
HELIX 22 22 LEU B 187 VAL B 195 1 9
HELIX 23 23 ARG B 201 VAL B 205 5 5
HELIX 24 24 LYS B 219 ASN B 230 1 12
HELIX 25 25 VAL B 244 LYS B 249 1 6
HELIX 26 26 LYS B 249 TYR B 264 1 16
SHEET 1 A 6 ASN A 39 LEU A 43 0
SHEET 2 A 6 HIS A 12 VAL A 16 1 N PHE A 13 O THR A 41
SHEET 3 A 6 ILE A 81 HIS A 86 1 O VAL A 84 N VAL A 16
SHEET 4 A 6 ILE A 104 LEU A 110 1 O VAL A 108 N LEU A 83
SHEET 5 A 6 LYS A 206 VAL A 211 1 O LYS A 206 N ALA A 107
SHEET 6 A 6 GLU A 234 GLU A 237 1 O GLU A 234 N PHE A 209
SHEET 1 B 3 CYS A 139 THR A 141 0
SHEET 2 B 3 THR A 152 ILE A 154 -1 O ILE A 154 N CYS A 139
SHEET 3 B 3 LEU A 183 TYR A 184 -1 O LEU A 183 N LEU A 153
SHEET 1 C 6 ASN B 39 LEU B 43 0
SHEET 2 C 6 HIS B 12 VAL B 16 1 N LEU B 15 O THR B 41
SHEET 3 C 6 ILE B 81 HIS B 86 1 O VAL B 84 N VAL B 16
SHEET 4 C 6 ILE B 104 LEU B 110 1 O VAL B 108 N LEU B 83
SHEET 5 C 6 ARG B 207 ALA B 212 1 O VAL B 208 N PHE B 109
SHEET 6 C 6 GLU B 234 ILE B 238 1 O LYS B 236 N VAL B 211
SHEET 1 D 3 CYS B 139 VAL B 140 0
SHEET 2 D 3 THR B 152 ILE B 154 -1 O ILE B 154 N CYS B 139
SHEET 3 D 3 LEU B 183 TYR B 184 -1 O LEU B 183 N LEU B 153
SITE 1 AC1 8 THR A 18 ALA A 128 GLY A 129 HIS A 243
SITE 2 AC1 8 HOH A 309 HOH A 317 HOH A 338 HOH A 351
SITE 1 AC2 2 THR B 18 HIS B 243
CRYST1 48.038 92.380 60.596 90.00 97.56 90.00 P 1 21 1 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 0.020817 0.000000 0.002763 0.00000
SCALE2 0.000000 0.010825 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016647 0.00000
TER 1982 LYS A 265
TER 3977 LYS B 265
MASTER 292 0 2 26 18 0 3 6 4205 2 11 42
END |