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HEADER HYDROLASE 11-JUL-11 3STX
TITLE CRYSTAL STRUCTURE OF TOMATO METHYLKETONE SYNTHASE I H243A VARIANT
TITLE 2 COMPLEXED WITH BETA-KETOHEPTANOATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHYLKETONE SYNTHASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: 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 3STX 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. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 21093
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1083
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1483
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.4130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3944
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.12
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.01000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.290
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.211
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.738
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.862
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4056 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5510 ; 1.111 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 514 ; 5.361 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 142 ;36.208 ;25.070
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 701 ;15.441 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;13.444 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 649 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2962 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2580 ; 0.476 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4183 ; 0.865 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1476 ; 0.885 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1326 ; 1.445 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3STX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-11.
REMARK 100 THE RCSB ID CODE IS RCSB066646.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-AUG-07
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 : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21096
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 88.8
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.1900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.53100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.750
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 (%): 47.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MOPSO-NA+, 15% (W/V) PEG 8000,
REMARK 280 0.3M NABR, 2MM DITHIOTHREITOL, OVERNIGHT SOAK IN 1MM BETA-
REMARK 280 KETOHEPTANOATE, PH 7.0, 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 47.19350
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: 1760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 465 ASP B 216
REMARK 465 ALA B 217
REMARK 465 LEU B 218
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 -14.03 82.77
REMARK 500 HIS A 21 -164.44 -100.00
REMARK 500 ALA A 77 -72.22 -57.59
REMARK 500 ASN A 78 34.52 -81.79
REMARK 500 ALA A 87 -113.96 48.98
REMARK 500 LEU A 136 -125.63 46.19
REMARK 500 PRO A 150 142.39 -37.08
REMARK 500 ARG A 201 -81.85 -108.96
REMARK 500 ASP A 242 -158.75 -84.68
REMARK 500 PHE B 20 -19.12 79.19
REMARK 500 HIS B 21 -158.38 -98.29
REMARK 500 PRO B 76 160.36 -44.68
REMARK 500 ALA B 87 -106.02 52.68
REMARK 500 LEU B 136 -117.57 49.96
REMARK 500 ARG B 201 -79.92 -86.73
REMARK 500 ASP B 242 -153.79 -88.35
REMARK 500 VAL B 244 74.47 -111.96
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 BKA A 266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BKA 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: 3STV RELATED DB: PDB
REMARK 900 RELATED ID: 3STW RELATED DB: PDB
REMARK 900 RELATED ID: 3STY RELATED DB: PDB
DBREF 3STX A 1 265 UNP E0YCS2 E0YCS2_SOLHA 1 265
DBREF 3STX B 1 265 UNP E0YCS2 E0YCS2_SOLHA 1 265
SEQADV 3STX GLY A -1 UNP E0YCS2 EXPRESSION TAG
SEQADV 3STX SER A 0 UNP E0YCS2 EXPRESSION TAG
SEQADV 3STX ALA A 243 UNP E0YCS2 HIS 243 ENGINEERED MUTATION
SEQADV 3STX GLY B -1 UNP E0YCS2 EXPRESSION TAG
SEQADV 3STX SER B 0 UNP E0YCS2 EXPRESSION TAG
SEQADV 3STX ALA B 243 UNP E0YCS2 HIS 243 ENGINEERED MUTATION
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 ALA 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 ALA 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 BKA A 266 10
HET BKA B 266 10
HETNAM BKA 3-OXOHEPTANOIC ACID
FORMUL 3 BKA 2(C7 H12 O3)
FORMUL 5 HOH *160(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 65 1 6
HELIX 5 5 LEU A 65 LEU A 75 1 11
HELIX 6 6 LEU A 88 PHE A 100 1 13
HELIX 7 7 ASP A 120 LEU A 133 1 14
HELIX 8 8 GLY A 156 VAL A 164 1 9
HELIX 9 9 PRO A 169 ALA A 178 1 10
HELIX 10 10 LEU A 187 VAL A 195 1 9
HELIX 11 11 ARG A 201 VAL A 205 5 5
HELIX 12 12 ASP A 216 ASN A 230 1 15
HELIX 13 13 VAL A 244 LYS A 249 1 6
HELIX 14 14 LYS A 249 LYS A 265 1 17
HELIX 15 15 GLY B 22 CYS B 25 5 4
HELIX 16 16 TRP B 26 GLY B 37 1 12
HELIX 17 17 GLN B 54 ILE B 58 5 5
HELIX 18 18 ASN B 60 LEU B 75 1 16
HELIX 19 19 LEU B 88 PHE B 100 1 13
HELIX 20 20 ASP B 120 ALA B 131 1 12
HELIX 21 21 GLY B 156 VAL B 164 1 9
HELIX 22 22 PRO B 169 ALA B 178 1 10
HELIX 23 23 LEU B 187 VAL B 195 1 9
HELIX 24 24 ARG B 201 VAL B 205 5 5
HELIX 25 25 GLU B 221 ASN B 230 1 10
HELIX 26 26 VAL B 244 LYS B 249 1 6
HELIX 27 27 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 LEU A 15 O THR A 41
SHEET 3 A 6 ILE A 81 HIS A 86 1 O VAL A 84 N VAL A 14
SHEET 4 A 6 ILE A 104 LEU A 110 1 O VAL A 108 N LEU A 83
SHEET 5 A 6 ARG A 207 VAL A 211 1 O VAL A 208 N PHE A 109
SHEET 6 A 6 GLU A 234 GLU A 237 1 O LYS A 236 N PHE A 209
SHEET 1 B 3 CYS A 139 VAL A 140 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 PHE B 13 O ASN B 39
SHEET 3 C 6 ILE B 81 HIS B 86 1 O ILE B 82 N VAL B 14
SHEET 4 C 6 ILE B 104 LEU B 110 1 O VAL B 108 N LEU B 83
SHEET 5 C 6 LYS B 206 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 THR B 141 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 3 THR A 18 ALA A 87 VAL A 132
SITE 1 AC2 4 THR B 18 ALA B 87 ALA B 128 VAL B 132
CRYST1 48.237 94.387 60.077 90.00 97.59 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 0.020731 0.000000 0.002764 0.00000
SCALE2 0.000000 0.010595 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016793 0.00000
TER 1982 LYS A 265
TER 3951 LYS B 265
MASTER 302 0 2 27 18 0 2 6 4124 2 20 42
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