HEADER LIPID TRANSPORT, MEMBRANE PROTEIN 19-JUL-05 2ACO
TITLE XRAY STRUCTURE OF BLC DIMER IN COMPLEX WITH VACCENIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OUTER MEMBRANE LIPOPROTEIN BLC;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: BLC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 TUNER PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: GATEWY PDEST17
KEYWDS LIPOCALIN, FATTY ACID, E.COLI, LIPID TRANSPORT, MEMBRANE
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR V.CAMPANACCI,R.E.BISHOP,L.REESE,S.BLANGY,M.TEGONI,
AUTHOR 2 C.CAMBILLAU
REVDAT 3 24-FEB-09 2ACO 1 VERSN
REVDAT 2 12-SEP-06 2ACO 1 JRNL
REVDAT 1 01-AUG-06 2ACO 0
JRNL AUTH V.CAMPANACCI,R.E.BISHOP,S.BLANGY,M.TEGONI,
JRNL AUTH 2 C.CAMBILLAU
JRNL TITL THE MEMBRANE BOUND BACTERIAL LIPOCALIN BLC IS A
JRNL TITL 2 FUNCTIONAL DIMER WITH BINDING PREFERENCE FOR
JRNL TITL 3 LYSOPHOSPHOLIPIDS.
JRNL REF FEBS LETT. V. 580 4877 2006
JRNL REFN ISSN 0014-5793
JRNL PMID 16920109
JRNL DOI 10.1016/J.FEBSLET.2006.07.086
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 37259
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2314
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2641
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2360
REMARK 3 BIN FREE R VALUE SET COUNT : 143
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2684
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 449
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.60000
REMARK 3 B22 (A**2) : -0.52000
REMARK 3 B33 (A**2) : -0.08000
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): 0.112
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.112
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.073
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.334
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2775 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2471 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3752 ; 1.289 ; 1.940
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5721 ; 0.793 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 331 ; 6.864 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 385 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3107 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 641 ; 0.007 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 494 ; 0.231 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2973 ; 0.258 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1650 ; 0.082 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 314 ; 0.207 ; 0.200
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): 8 ; 0.157 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 59 ; 0.294 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 43 ; 0.205 ; 0.200
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): 1652 ; 0.679 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2650 ; 1.300 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1123 ; 2.221 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1102 ; 3.689 ; 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 : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2ACO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-05.
REMARK 100 THE RCSB ID CODE IS RCSB033745.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-04
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 : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37259
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 59.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : 0.13700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.32700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1QWD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE 800-900 MM, SODIUM
REMARK 280 BORATE 50 MM, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 28.95050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.51000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.66850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.51000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.95050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.66850
REMARK 290 SMTRY3 4 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 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 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 GLY B 176
REMARK 465 SER B 177
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 177 OG
REMARK 470 HIS B 10 CG ND1 CD2 CE1 NE2
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 OG SER A 22 O HOH A 388 1.87
REMARK 500 O HOH A 250 O HOH A 389 2.08
REMARK 500 O HOH A 218 O HOH B 733 2.12
REMARK 500 O HOH A 291 O HOH A 387 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 ASP A 122 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP B 122 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP B 122 CB - CG - OD2 ANGL. DEV. = 7.8 DEGREES
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 ARG A 26 -4.21 77.31
REMARK 500 ARG B 26 -5.02 77.56
REMARK 500 PHE B 109 107.75 -165.09
REMARK 500 PRO B 111 45.01 -85.45
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 VCA B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QWD RELATED DB: PDB
REMARK 900 NATIVE UNLIGANDED PROTEIN
DBREF 2ACO A 23 177 UNP P0A901 BLC_ECOLI 23 177
DBREF 2ACO B 23 177 UNP P0A901 BLC_ECOLI 23 177
SEQADV 2ACO HIS A 5 UNP P0A901 EXPRESSION TAG
SEQADV 2ACO HIS A 6 UNP P0A901 EXPRESSION TAG
SEQADV 2ACO HIS A 7 UNP P0A901 EXPRESSION TAG
SEQADV 2ACO HIS A 8 UNP P0A901 EXPRESSION TAG
SEQADV 2ACO HIS A 9 UNP P0A901 EXPRESSION TAG
SEQADV 2ACO HIS A 10 UNP P0A901 EXPRESSION TAG
SEQADV 2ACO LEU A 11 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO GLU A 12 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO SER A 13 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO THR A 14 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO SER A 15 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO LEU A 16 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO TYR A 17 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO LYS A 18 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO LYS A 19 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO ALA A 20 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO GLY A 21 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO SER A 22 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO HIS B 5 UNP P0A901 EXPRESSION TAG
SEQADV 2ACO HIS B 6 UNP P0A901 EXPRESSION TAG
SEQADV 2ACO HIS B 7 UNP P0A901 EXPRESSION TAG
SEQADV 2ACO HIS B 8 UNP P0A901 EXPRESSION TAG
SEQADV 2ACO HIS B 9 UNP P0A901 EXPRESSION TAG
SEQADV 2ACO HIS B 10 UNP P0A901 EXPRESSION TAG
SEQADV 2ACO LEU B 11 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO GLU B 12 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO SER B 13 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO THR B 14 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO SER B 15 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO LEU B 16 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO TYR B 17 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO LYS B 18 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO LYS B 19 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO ALA B 20 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO GLY B 21 UNP P0A901 CLONING ARTIFACT
SEQADV 2ACO SER B 22 UNP P0A901 CLONING ARTIFACT
SEQRES 1 A 173 HIS HIS HIS HIS HIS HIS LEU GLU SER THR SER LEU TYR
SEQRES 2 A 173 LYS LYS ALA GLY SER THR PRO PRO ARG GLY VAL THR VAL
SEQRES 3 A 173 VAL ASN ASN PHE ASP ALA LYS ARG TYR LEU GLY THR TRP
SEQRES 4 A 173 TYR GLU ILE ALA ARG PHE ASP HIS ARG PHE GLU ARG GLY
SEQRES 5 A 173 LEU GLU LYS VAL THR ALA THR TYR SER LEU ARG ASP ASP
SEQRES 6 A 173 GLY GLY LEU ASN VAL ILE ASN LYS GLY TYR ASN PRO ASP
SEQRES 7 A 173 ARG GLY MET TRP GLN GLN SER GLU GLY LYS ALA TYR PHE
SEQRES 8 A 173 THR GLY ALA PRO THR ARG ALA ALA LEU LYS VAL SER PHE
SEQRES 9 A 173 PHE GLY PRO PHE TYR GLY GLY TYR ASN VAL ILE ALA LEU
SEQRES 10 A 173 ASP ARG GLU TYR ARG HIS ALA LEU VAL CYS GLY PRO ASP
SEQRES 11 A 173 ARG ASP TYR LEU TRP ILE LEU SER ARG THR PRO THR ILE
SEQRES 12 A 173 SER ASP GLU VAL LYS GLN GLU MET LEU ALA VAL ALA THR
SEQRES 13 A 173 ARG GLU GLY PHE ASP VAL SER LYS PHE ILE TRP VAL GLN
SEQRES 14 A 173 GLN PRO GLY SER
SEQRES 1 B 173 HIS HIS HIS HIS HIS HIS LEU GLU SER THR SER LEU TYR
SEQRES 2 B 173 LYS LYS ALA GLY SER THR PRO PRO ARG GLY VAL THR VAL
SEQRES 3 B 173 VAL ASN ASN PHE ASP ALA LYS ARG TYR LEU GLY THR TRP
SEQRES 4 B 173 TYR GLU ILE ALA ARG PHE ASP HIS ARG PHE GLU ARG GLY
SEQRES 5 B 173 LEU GLU LYS VAL THR ALA THR TYR SER LEU ARG ASP ASP
SEQRES 6 B 173 GLY GLY LEU ASN VAL ILE ASN LYS GLY TYR ASN PRO ASP
SEQRES 7 B 173 ARG GLY MET TRP GLN GLN SER GLU GLY LYS ALA TYR PHE
SEQRES 8 B 173 THR GLY ALA PRO THR ARG ALA ALA LEU LYS VAL SER PHE
SEQRES 9 B 173 PHE GLY PRO PHE TYR GLY GLY TYR ASN VAL ILE ALA LEU
SEQRES 10 B 173 ASP ARG GLU TYR ARG HIS ALA LEU VAL CYS GLY PRO ASP
SEQRES 11 B 173 ARG ASP TYR LEU TRP ILE LEU SER ARG THR PRO THR ILE
SEQRES 12 B 173 SER ASP GLU VAL LYS GLN GLU MET LEU ALA VAL ALA THR
SEQRES 13 B 173 ARG GLU GLY PHE ASP VAL SER LYS PHE ILE TRP VAL GLN
SEQRES 14 B 173 GLN PRO GLY SER
HET VCA B 501 20
HETNAM VCA VACCENIC ACID
HETSYN VCA (11E)-OCTADEC-11-ENOIC ACID
FORMUL 3 VCA C18 H34 O2
FORMUL 4 HOH *449(H2 O)
HELIX 1 1 ASP A 35 LEU A 40 5 6
HELIX 2 2 HIS A 51 ARG A 55 5 5
HELIX 3 3 SER A 148 GLU A 162 1 15
HELIX 4 4 ASP A 165 PHE A 169 5 5
HELIX 5 5 ASP B 35 LEU B 40 5 6
HELIX 6 6 HIS B 51 ARG B 55 5 5
HELIX 7 7 SER B 148 GLU B 162 1 15
HELIX 8 8 ASP B 165 SER B 167 5 3
SHEET 1 A 2 THR A 14 TYR A 17 0
SHEET 2 A 2 VAL A 28 VAL A 31 -1 O VAL A 30 N SER A 15
SHEET 1 B10 ILE A 170 TRP A 171 0
SHEET 2 B10 GLY A 41 ARG A 48 -1 N ARG A 48 O ILE A 170
SHEET 3 B10 LEU A 138 SER A 142 -1 O SER A 142 N TYR A 44
SHEET 4 B10 HIS A 127 CYS A 131 -1 N ALA A 128 O LEU A 141
SHEET 5 B10 PHE A 112 LEU A 121 -1 N ASN A 117 O CYS A 131
SHEET 6 B10 ALA A 103 PHE A 109 -1 N VAL A 106 O GLY A 114
SHEET 7 B10 MET A 85 PHE A 95 -1 N LYS A 92 O SER A 107
SHEET 8 B10 LEU A 72 ASN A 80 -1 N GLY A 78 O GLN A 87
SHEET 9 B10 GLU A 58 LEU A 66 -1 N GLU A 58 O TYR A 79
SHEET 10 B10 GLY A 41 ARG A 48 -1 N GLY A 41 O TYR A 64
SHEET 1 C 2 THR B 14 TYR B 17 0
SHEET 2 C 2 VAL B 28 VAL B 31 -1 O VAL B 30 N SER B 15
SHEET 1 D10 PHE B 169 TRP B 171 0
SHEET 2 D10 GLY B 41 PHE B 49 -1 N ARG B 48 O ILE B 170
SHEET 3 D10 LEU B 138 SER B 142 -1 O SER B 142 N TYR B 44
SHEET 4 D10 HIS B 127 CYS B 131 -1 N ALA B 128 O LEU B 141
SHEET 5 D10 GLY B 114 LEU B 121 -1 N ASN B 117 O CYS B 131
SHEET 6 D10 ALA B 103 SER B 107 -1 N LEU B 104 O TYR B 116
SHEET 7 D10 MET B 85 PHE B 95 -1 N TYR B 94 O LYS B 105
SHEET 8 D10 LEU B 72 ASN B 80 -1 N LEU B 72 O ALA B 93
SHEET 9 D10 GLU B 58 LEU B 66 -1 N GLU B 58 O TYR B 79
SHEET 10 D10 GLY B 41 PHE B 49 -1 N TRP B 43 O ALA B 62
SITE 1 AC1 9 ARG A 52 PHE A 112 PHE B 53 GLU B 54
SITE 2 AC1 9 ASN B 76 PHE B 109 GLY B 114 GLY B 115
SITE 3 AC1 9 TRP B 139
CRYST1 57.901 81.337 89.020 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 0.017271 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012295 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011233 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
