HEADER MEMBRANE PROTEIN 08-AUG-17 5OON
TITLE STRUCTURE OF UNDECAPRENYL-PYROPHOSPHATE PHOSPHATASE, BACA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNDECAPRENYL-DIPHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BACITRACIN RESISTANCE PROTEIN,UNDECAPRENYL PYROPHOSPHATE
COMPND 5 PHOSPHATASE;
COMPND 6 EC: 3.6.1.27;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: BACA, UPPP;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI DH1;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 536056
KEYWDS ANTIBIOTIC, BACTERIAL CELL WALL, ENZYME MECHANISM, ESCHERICHIA COLI,
KEYWDS 2 IN MESO IN SITU SERIAL CRYSTALLOGRAPHY, IMISX, INTERDIGITATED
KEYWDS 3 INVERTED TOPOLOGY REPEAT, LIPID CUBIC PHASE, MEMBRANE PROTEIN,
KEYWDS 4 PEPTIDOGLYCAN, PHOSPHATASE, PYROPHOSPHORYLASE, UNDECAPRENYL-
KEYWDS 5 PYROPHOSPHATE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.-Y.HUANG,V.OLIERIC,R.WARSHAMANAGE,M.WANG,N.HOWE,M.E.I.GHACHI,
AUTHOR 2 D.WEICHERT,F.KERFF,P.STANSFELD,T.TOUZE,M.CAFFREY
REVDAT 3 06-JUN-18 5OON 1 SOURCE DBREF SEQADV
REVDAT 2 28-MAR-18 5OON 1 JRNL
REVDAT 1 21-MAR-18 5OON 0
JRNL AUTH M.EL GHACHI,N.HOWE,C.Y.HUANG,V.OLIERIC,R.WARSHAMANAGE,
JRNL AUTH 2 T.TOUZE,D.WEICHERT,P.J.STANSFELD,M.WANG,F.KERFF,M.CAFFREY
JRNL TITL CRYSTAL STRUCTURE OF UNDECAPRENYL-PYROPHOSPHATE PHOSPHATASE
JRNL TITL 2 AND ITS ROLE IN PEPTIDOGLYCAN BIOSYNTHESIS.
JRNL REF NAT COMMUN V. 9 1078 2018
JRNL REFN ESSN 2041-1723
JRNL PMID 29540682
JRNL DOI 10.1038/S41467-018-03477-5
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12RC2_2821: ???)
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.320
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 19853
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 990
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 44.4611 - 4.9714 1.00 2697 142 0.1888 0.1944
REMARK 3 2 4.9714 - 3.9467 1.00 2696 140 0.1823 0.2459
REMARK 3 3 3.9467 - 3.4481 1.00 2682 143 0.1960 0.2259
REMARK 3 4 3.4481 - 3.1329 1.00 2689 140 0.2154 0.2635
REMARK 3 5 3.1329 - 2.9084 1.00 2685 142 0.2286 0.2730
REMARK 3 6 2.9084 - 2.7369 1.00 2698 140 0.2576 0.3163
REMARK 3 7 2.7369 - 2.5999 1.00 2716 143 0.2749 0.3397
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.450
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 : 0.006 2166
REMARK 3 ANGLE : 0.865 2929
REMARK 3 CHIRALITY : 0.047 344
REMARK 3 PLANARITY : 0.005 356
REMARK 3 DIHEDRAL : 11.626 1251
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 5OON COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1200005963.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAY-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19853
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 44.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 17.91
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 12.33
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.870
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXCD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40 % PEG-400, 0.3-0.5 M AMMONIUM
REMARK 280 CITRATE DIBASIC AND 0.1 M SODIUM CITRATE PH 5.0, LIPIDIC CUBIC
REMARK 280 PHASE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y+1/2,-Z
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 56.63000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 72.50000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 56.63000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 72.50000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 56.63000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 72.50000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 56.63000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 72.50000
REMARK 290 SMTRY3 8 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
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 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 MET A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 ASP A 3
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 LYS A 46 CG CD CE NZ
REMARK 470 LYS A 87 CG CD CE NZ
REMARK 470 LYS A 114 CG CD CE NZ
REMARK 470 LYS A 214 CG CD CE NZ
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 26 78.57 68.04
REMARK 500 SER A 173 93.15 72.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OLC A 305
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG A 301 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 162 O
REMARK 620 2 CYS A 162 SG 93.0
REMARK 620 3 CYS A 165 SG 85.0 162.8
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 305
DBREF 5OON A 1 273 UNP C3SU37 C3SU37_ECOLX 1 273
SEQADV 5OON MET A -8 UNP C3SU37 INITIATING METHIONINE
SEQADV 5OON HIS A -7 UNP C3SU37 EXPRESSION TAG
SEQADV 5OON HIS A -6 UNP C3SU37 EXPRESSION TAG
SEQADV 5OON HIS A -5 UNP C3SU37 EXPRESSION TAG
SEQADV 5OON HIS A -4 UNP C3SU37 EXPRESSION TAG
SEQADV 5OON HIS A -3 UNP C3SU37 EXPRESSION TAG
SEQADV 5OON HIS A -2 UNP C3SU37 EXPRESSION TAG
SEQADV 5OON GLY A -1 UNP C3SU37 EXPRESSION TAG
SEQADV 5OON SER A 0 UNP C3SU37 EXPRESSION TAG
SEQRES 1 A 282 MET HIS HIS HIS HIS HIS HIS GLY SER MET SER ASP MET
SEQRES 2 A 282 HIS SER LEU LEU ILE ALA ALA ILE LEU GLY VAL VAL GLU
SEQRES 3 A 282 GLY LEU THR GLU PHE LEU PRO VAL SER SER THR GLY HIS
SEQRES 4 A 282 MET ILE ILE VAL GLY HIS LEU LEU GLY PHE GLU GLY ASP
SEQRES 5 A 282 THR ALA LYS THR PHE GLU VAL VAL ILE GLN LEU GLY SER
SEQRES 6 A 282 ILE LEU ALA VAL VAL VAL MET PHE TRP ARG ARG LEU PHE
SEQRES 7 A 282 GLY LEU ILE GLY ILE HIS PHE GLY ARG PRO LEU GLN HIS
SEQRES 8 A 282 GLU GLY GLU SER LYS GLY ARG LEU THR LEU ILE HIS ILE
SEQRES 9 A 282 LEU LEU GLY MET ILE PRO ALA VAL VAL LEU GLY LEU LEU
SEQRES 10 A 282 PHE HIS ASP THR ILE LYS SER LEU PHE ASN PRO ILE ASN
SEQRES 11 A 282 VAL MET TYR ALA LEU VAL VAL GLY GLY LEU LEU LEU ILE
SEQRES 12 A 282 ALA ALA GLU CYS LEU LYS PRO LYS GLU PRO ARG ALA PRO
SEQRES 13 A 282 GLY LEU ASP ASP MET THR TYR ARG GLN ALA PHE MET ILE
SEQRES 14 A 282 GLY CYS PHE GLN CYS LEU ALA LEU TRP PRO GLY PHE SER
SEQRES 15 A 282 ARG SER GLY ALA THR ILE SER GLY GLY MET LEU MET GLY
SEQRES 16 A 282 VAL SER ARG TYR ALA ALA SER GLU PHE SER PHE LEU LEU
SEQRES 17 A 282 ALA VAL PRO MET MET MET GLY ALA THR ALA LEU ASP LEU
SEQRES 18 A 282 TYR LYS SER TRP GLY PHE LEU THR SER GLY ASP ILE PRO
SEQRES 19 A 282 MET PHE ALA VAL GLY PHE ILE THR ALA PHE VAL VAL ALA
SEQRES 20 A 282 LEU ILE ALA ILE LYS THR PHE LEU GLN LEU ILE LYS ARG
SEQRES 21 A 282 ILE SER PHE ILE PRO PHE ALA ILE TYR ARG PHE ILE VAL
SEQRES 22 A 282 ALA ALA ALA VAL TYR VAL VAL PHE PHE
HET HG A 301 1
HET HG A 302 1
HET TRS A 303 8
HET OLC A 304 25
HET OLC A 305 22
HETNAM HG MERCURY (II) ION
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETSYN TRS TRIS BUFFER
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 HG 2(HG 2+)
FORMUL 4 TRS C4 H12 N O3 1+
FORMUL 5 OLC 2(C21 H40 O4)
FORMUL 7 HOH *6(H2 O)
HELIX 1 AA1 MET A 4 GLU A 21 1 18
HELIX 2 AA2 SER A 26 GLY A 39 1 14
HELIX 3 AA3 GLY A 42 PHE A 64 1 23
HELIX 4 AA4 PHE A 64 ILE A 72 1 9
HELIX 5 AA5 THR A 91 PHE A 109 1 19
HELIX 6 AA6 PHE A 109 SER A 115 1 7
HELIX 7 AA7 ASN A 118 LYS A 140 1 23
HELIX 8 AA8 GLY A 148 MET A 152 5 5
HELIX 9 AA9 THR A 153 GLN A 164 1 12
HELIX 10 AB1 CYS A 165 TRP A 169 5 5
HELIX 11 AB2 SER A 173 MET A 185 1 13
HELIX 12 AB3 SER A 188 SER A 215 1 28
HELIX 13 AB4 TRP A 216 LEU A 219 5 4
HELIX 14 AB5 GLY A 222 ILE A 249 1 28
HELIX 15 AB6 PHE A 254 PHE A 273 1 20
LINK SG CYS A 138 HG HG A 302 1555 1555 2.97
LINK O CYS A 162 HG HG A 301 1555 1555 2.77
LINK SG CYS A 162 HG HG A 301 1555 1555 2.69
LINK SG CYS A 165 HG HG A 301 1555 1555 2.46
SITE 1 AC1 3 PRO A 101 CYS A 162 CYS A 165
SITE 1 AC2 1 CYS A 138
SITE 1 AC3 3 ARG A 145 ARG A 155 MET A 185
SITE 1 AC4 8 LEU A 19 HIS A 30 ILE A 74 HIS A 75
SITE 2 AC4 8 LEU A 248 ARG A 251 ILE A 252 TYR A 260
SITE 1 AC5 6 LEU A 105 VAL A 128 ALA A 135 CYS A 138
SITE 2 AC5 6 LEU A 139 TYR A 154
CRYST1 113.260 145.000 40.490 90.00 90.00 90.00 C 2 2 2 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 0.008829 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006897 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024697 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
