HEADER HYDROLASE, MEMBRANE PROTEIN 09-MAY-01 1ILZ
TITLE OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE
TITLE 2 MUTANT PH 6.1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OUTER MEMBRANE PHOSPHOLIPASE A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OMPLA, DETERGENT-RESISTANT PHOSPHOLIPASE A, DR-PHOSPHOLIPASE
COMPND 5 A, PHOSPHATIDYLCHOLINE 1-ACYLHYDROLASE;
COMPND 6 EC: 3.1.1.32;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: PLDA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ANTI-PARALLEL BETA BARREL, MEMBRANE PHOSPHOLIPASE, MEMBRANE PROTEIN,
KEYWDS 2 SERINE HYDROLASE, CATALYTIC TRIAD, ASN ALA MUTATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.J.SNIJDER,J.H.VAN EERDE,R.L.KINGMA,K.H.KALK,N.DEKKER,M.R.EGMOND,
AUTHOR 2 B.W.DIJKSTRA
REVDAT 6 20-SEP-23 1ILZ 1 REMARK
REVDAT 5 21-DEC-22 1ILZ 1 SEQADV HETSYN
REVDAT 4 29-JUL-20 1ILZ 1 COMPND REMARK HETNAM SITE
REVDAT 3 24-FEB-09 1ILZ 1 VERSN
REVDAT 2 01-APR-03 1ILZ 1 JRNL
REVDAT 1 03-OCT-01 1ILZ 0
JRNL AUTH H.J.SNIJDER,J.H.VAN EERDE,R.L.KINGMA,K.H.KALK,N.DEKKER,
JRNL AUTH 2 M.R.EGMOND,B.W.DIJKSTRA
JRNL TITL STRUCTURAL INVESTIGATIONS OF THE ACTIVE-SITE MUTANT
JRNL TITL 2 ASN156ALA OF OUTER MEMBRANE PHOSPHOLIPASE A: FUNCTION OF THE
JRNL TITL 3 ASN-HIS INTERACTION IN THE CATALYTIC TRIAD.
JRNL REF PROTEIN SCI. V. 10 1962 2001
JRNL REFN ISSN 0961-8368
JRNL PMID 11567087
JRNL DOI 10.1110/PS.17701
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.J.SNIJDER,I.UBARRETXENA-BELANDIA,M.BLAAUW,K.H.KALK,
REMARK 1 AUTH 2 H.M.VERHEIJ,M.R.EGMOND,N.DEKKER,B.W.DIJKSTRA
REMARK 1 TITL STRUCTURAL EVIDENCE FOR DIMERIZATION-REGULATED ACTIVATION OF
REMARK 1 TITL 2 AN INTEGRAL MEMBRANE PHOSPHOLIPASE
REMARK 1 REF NATURE V. 401 717 1999
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/44890
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.BLAAUW,N.DEKKER,H.M.VERHEIJ,K.H.KALK,B.W.DIJKSTRA
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF OUTER
REMARK 1 TITL 2 MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI
REMARK 1 REF FEBS LETT. V. 373 10 1995
REMARK 1 REFN ISSN 0014-5793
REMARK 1 DOI 10.1016/0014-5793(95)01002-V
REMARK 2
REMARK 2 RESOLUTION. 2.50 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.00
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) (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 12728
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : THE SAME TEST SET WAS USED AS
REMARK 3 IN THE REFINEMENT OF THE
REMARK 3 NATIVE MONOMER STRUCTURE 1QD5,
REMARK 3 WHICH HAD BEEN SELECTED
REMARK 3 RANDOMLY.
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1231
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 : 2091
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 106
REMARK 3 SOLVENT ATOMS : 32
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) : -8.88200
REMARK 3 B22 (A**2) : -8.88200
REMARK 3 B33 (A**2) : 17.76500
REMARK 3 B12 (A**2) : -9.73500
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
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) : 0.006
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 : ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 BULK SOLVENT CORRECTION WAS APPLIED AS IMPLEMENTED IN CNS
REMARK 3 BULK SOLVENT: DENSITY LEVEL= 0.379342 E/A^3, B-FACTOR= 52.8672 A^2
REMARK 4
REMARK 4 1ILZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-01.
REMARK 100 THE DEPOSITION ID IS D_1000013399.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 6.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, CCP4 (TRUNCATE)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 150605
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 31.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 11.80
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : 0.03700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 39.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.11300
REMARK 200 R SYM FOR SHELL (I) : 0.11300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.300
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: STARTING MODEL 1QD5 WITH THE ACTIVE SITE RESIDUES
REMARK 200 TRUNCATED TO ALA AND ALL WATERS AND DETERGENT MOLECULES REMOVED.
REMARK 200 ALL REMAINING ATOMS HAVE BEEN GIVEN A RANDOM SHIFT OF ALMOST 0.5
REMARK 200 ANGSTROM IN ALL DIRECTIONS.
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, CALCIUM CHLORIDE, BIS-TRIS
REMARK 280 BUFFER, PH 6.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.89500
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 67.79000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 67.79000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 33.89500
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 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 ALA A -5
REMARK 465 ARG A -4
REMARK 465 ILE A -3
REMARK 465 ARG A -2
REMARK 465 ALA A -1
REMARK 465 PRO A 0
REMARK 465 GLN A 1
REMARK 465 GLU A 2
REMARK 465 ALA A 3
REMARK 465 THR A 4
REMARK 465 VAL A 5
REMARK 465 LYS A 6
REMARK 465 GLU A 7
REMARK 465 VAL A 8
REMARK 465 HIS A 9
REMARK 465 ASP A 10
REMARK 465 ALA A 11
REMARK 465 PRO A 12
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 VAL A 14 103.60 63.11
REMARK 500 TYR A 35 -83.91 -99.34
REMARK 500 TRP A 78 95.26 -169.99
REMARK 500 SER A 107 65.75 37.89
REMARK 500 ASP A 125 62.22 -153.85
REMARK 500 ASN A 185 70.06 -173.50
REMARK 500 LEU A 265 -84.08 -94.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 ATOMS C5'-C8' OF BOG 503 LACK INTERPRETABLE
REMARK 600 ELECTRON DENSITY.
REMARK 600 ATOMS C3'-C8' OF BOG 504 HAVE MISSING ELECTRON
REMARK 600 DENSITY.
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 BOG A 503
REMARK 610 BOG A 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QD5 RELATED DB: PDB
REMARK 900 NATIVE OMPLA
REMARK 900 RELATED ID: 1QD6 RELATED DB: PDB
REMARK 900 NATIVE OMPLA IN DIMERIC ARRANGEMENT
REMARK 900 RELATED ID: 1FW2 RELATED DB: PDB
REMARK 900 NATIVE MONOMER CA2+ BOUND
REMARK 900 RELATED ID: 1ILD RELATED DB: PDB
REMARK 900 N156A OMPLA AT PH 4.6
REMARK 900 RELATED ID: 1FW3 RELATED DB: PDB
REMARK 900 DIMER CA2+ FREE
REMARK 900 RELATED ID: 1IM0 RELATED DB: PDB
REMARK 900 N156A OMPLA AT PH 8.3
DBREF 1ILZ A 1 269 UNP P0A921 PA1_ECOLI 21 289
SEQADV 1ILZ ALA A -5 UNP P0A921 EXPRESSION TAG
SEQADV 1ILZ ARG A -4 UNP P0A921 EXPRESSION TAG
SEQADV 1ILZ ILE A -3 UNP P0A921 EXPRESSION TAG
SEQADV 1ILZ ARG A -2 UNP P0A921 EXPRESSION TAG
SEQADV 1ILZ ALA A -1 UNP P0A921 EXPRESSION TAG
SEQADV 1ILZ PRO A 0 UNP P0A921 EXPRESSION TAG
SEQADV 1ILZ ALA A 156 UNP P0A921 ASN 176 EXPRESSION TAG
SEQRES 1 A 275 ALA ARG ILE ARG ALA PRO GLN GLU ALA THR VAL LYS GLU
SEQRES 2 A 275 VAL HIS ASP ALA PRO ALA VAL ARG GLY SER ILE ILE ALA
SEQRES 3 A 275 ASN MET LEU GLN GLU HIS ASP ASN PRO PHE THR LEU TYR
SEQRES 4 A 275 PRO TYR ASP THR ASN TYR LEU ILE TYR THR GLN THR SER
SEQRES 5 A 275 ASP LEU ASN LYS GLU ALA ILE ALA SER TYR ASP TRP ALA
SEQRES 6 A 275 GLU ASN ALA ARG LYS ASP GLU VAL LYS PHE GLN LEU SER
SEQRES 7 A 275 LEU ALA PHE PRO LEU TRP ARG GLY ILE LEU GLY PRO ASN
SEQRES 8 A 275 SER VAL LEU GLY ALA SER TYR THR GLN LYS SER TRP TRP
SEQRES 9 A 275 GLN LEU SER ASN SER GLU GLU SER SER PRO PHE ARG GLU
SEQRES 10 A 275 THR ASN TYR GLU PRO GLN LEU PHE LEU GLY PHE ALA THR
SEQRES 11 A 275 ASP TYR ARG PHE ALA GLY TRP THR LEU ARG ASP VAL GLU
SEQRES 12 A 275 MET GLY TYR ASN HIS ASP SER ASN GLY ARG SER ASP PRO
SEQRES 13 A 275 THR SER ARG SER TRP ALA ARG LEU TYR THR ARG LEU MET
SEQRES 14 A 275 ALA GLU ASN GLY ASN TRP LEU VAL GLU VAL LYS PRO TRP
SEQRES 15 A 275 TYR VAL VAL GLY ASN THR ASP ASP ASN PRO ASP ILE THR
SEQRES 16 A 275 LYS TYR MET GLY TYR TYR GLN LEU LYS ILE GLY TYR HIS
SEQRES 17 A 275 LEU GLY ASP ALA VAL LEU SER ALA LYS GLY GLN TYR ASN
SEQRES 18 A 275 TRP ASN THR GLY TYR GLY GLY ALA GLU LEU GLY LEU SER
SEQRES 19 A 275 TYR PRO ILE THR LYS HIS VAL ARG LEU TYR THR GLN VAL
SEQRES 20 A 275 TYR SER GLY TYR GLY GLU SER LEU ILE ASP TYR ASN PHE
SEQRES 21 A 275 ASN GLN THR ARG VAL GLY VAL GLY VAL MET LEU ASN ASP
SEQRES 22 A 275 LEU PHE
HET BOG A 500 20
HET BOG A 501 20
HET BOG A 502 20
HET BOG A 503 16
HET BOG A 504 14
HET MPD A 600 8
HET MPD A 601 8
HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN BOG BETA-OCTYLGLUCOSIDE; OCTYL BETA-D-GLUCOSIDE; OCTYL D-
HETSYN 2 BOG GLUCOSIDE; OCTYL GLUCOSIDE
FORMUL 2 BOG 5(C14 H28 O6)
FORMUL 7 MPD 2(C6 H14 O2)
FORMUL 9 HOH *32(H2 O)
HELIX 1 1 SER A 17 GLN A 24 1 8
HELIX 2 2 TRP A 58 ALA A 62 5 5
HELIX 3 3 ASN A 102 SER A 106 5 5
HELIX 4 4 ASP A 187 GLY A 193 1 7
SHEET 1 A14 TYR A 33 PRO A 34 0
SHEET 2 A14 ASP A 65 ARG A 79 -1 N ALA A 74 O TYR A 33
SHEET 3 A14 SER A 86 TRP A 98 -1 O LEU A 88 N LEU A 77
SHEET 4 A14 PHE A 109 PHE A 128 -1 N ARG A 110 O TRP A 97
SHEET 5 A14 TRP A 131 SER A 144 -1 O TRP A 131 N PHE A 128
SHEET 6 A14 SER A 154 ASN A 166 -1 N TRP A 155 O ASP A 143
SHEET 7 A14 TRP A 169 VAL A 179 -1 N TRP A 169 O ASN A 166
SHEET 8 A14 TYR A 195 LEU A 203 -1 O GLN A 196 N LYS A 174
SHEET 9 A14 ALA A 206 TYR A 214 -1 O ALA A 206 N LEU A 203
SHEET 10 A14 GLY A 221 PRO A 230 -1 N GLY A 222 O GLN A 213
SHEET 11 A14 ARG A 236 TYR A 245 -1 N LEU A 237 O TYR A 229
SHEET 12 A14 ASN A 255 MET A 264 -1 O GLN A 256 N GLY A 244
SHEET 13 A14 TYR A 39 THR A 45 -1 N LEU A 40 O VAL A 263
SHEET 14 A14 ASP A 65 ARG A 79 -1 O GLU A 66 N THR A 43
CISPEP 1 ASP A 149 PRO A 150 0 0.01
CRYST1 78.168 78.168 101.685 90.00 90.00 120.00 P 31 2 1 6
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 0.012793 0.007386 0.000000 0.00000
SCALE2 0.000000 0.014772 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009834 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
