HEADER ANTIBIOTIC 25-APR-00 1EWF
TITLE THE 1.7 ANGSTROM CRYSTAL STRUCTURE OF BPI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BACTERICIDAL/PERMEABILITY-INCREASING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BPI;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_CELL: OVARY CELLS;
SOURCE 9 OTHER_DETAILS: MAMMALIAN CHO CELLS USED FOR RECOMBINANT EXPRESSION
SOURCE 10 OF THE PROTEIN
KEYWDS BACTERICIDAL, PERMEABILITY-INCREASING, LIPID-BINDING,
KEYWDS 2 LIPOPOLYSACCHARIDE-BINDING, ANTIBIOTIC
EXPDTA X-RAY DIFFRACTION
AUTHOR G.KLEIGER,L.J.BEAMER,R.GROTHE,P.MALLICK,D.EISENBERG
REVDAT 6 03-NOV-21 1EWF 1 REMARK SEQADV
REVDAT 5 31-JAN-18 1EWF 1 REMARK
REVDAT 4 27-JUL-11 1EWF 1 REMARK
REVDAT 3 24-FEB-09 1EWF 1 VERSN
REVDAT 2 01-APR-03 1EWF 1 JRNL
REVDAT 1 21-JUN-00 1EWF 0
JRNL AUTH G.KLEIGER,L.J.BEAMER,R.GROTHE,P.MALLICK,D.EISENBERG
JRNL TITL THE 1.7 A CRYSTAL STRUCTURE OF BPI: A STUDY OF HOW TWO
JRNL TITL 2 DISSIMILAR AMINO ACID SEQUENCES CAN ADOPT THE SAME FOLD.
JRNL REF J.MOL.BIOL. V. 299 1019 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10843855
JRNL DOI 10.1006/JMBI.2000.3805
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.J.BEAMER,S.F.CARROLL,D.EISENBERG
REMARK 1 TITL CRYSTAL STRUCTURE OF HUMAN BPI AND TWO BOUND PHOSPHOLIPIDS
REMARK 1 TITL 2 AT 2.4 ANGSTROM RESOLUTION
REMARK 1 REF SCIENCE V. 276 1861 1997
REMARK 1 REFN ISSN 0036-8075
REMARK 1 DOI 10.1126/SCIENCE.276.5320.1861
REMARK 2
REMARK 2 RESOLUTION. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 47197
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 SELECTION OF 10
REMARK 3 PERCENT OF ALL DATA
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4755
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 : 3521
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 97
REMARK 3 SOLVENT ATOMS : 387
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.00
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 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) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 2.000
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) : 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: NULL
REMARK 4
REMARK 4 1EWF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1000010960.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-98
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.975
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47198
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.30
REMARK 200 R MERGE FOR SHELL (I) : 0.20100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12 % PEG 6000, 0.2 M MG ACETATE, 0.1 M
REMARK 280 NA CACODYLATE, PH 6.8, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 16K, TEMPERATURE 289.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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 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 92.16000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 15.61500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 92.16000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 15.61500
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: 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 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 VAL A 1 CG1 CG2
REMARK 470 LYS A 33 CG CD CE NZ
REMARK 470 LYS A 44 CG CD CE NZ
REMARK 470 HIS A 45 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 86 CD CE NZ
REMARK 470 LYS A 95 CG CD CE NZ
REMARK 470 LYS A 99 CG CD CE NZ
REMARK 470 LYS A 118 CG CD CE NZ
REMARK 470 ASN A 232 CG OD1 ND2
REMARK 470 HIS A 233 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 234 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A 235 CG OD1 ND2
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 O HOH A 626 O HOH A 774 2.07
REMARK 500 N ASN A 82 O HOH A 665 2.09
REMARK 500 O HOH A 609 O HOH A 823 2.12
REMARK 500 O HOH A 779 O HOH A 855 2.14
REMARK 500 O PRO A 303 O HOH A 870 2.15
REMARK 500 O LEU A 302 O HOH A 930 2.17
REMARK 500 O HOH A 700 O HOH A 906 2.19
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 LYS A 44 N - CA - C ANGL. DEV. = 18.6 DEGREES
REMARK 500 HIS A 45 N - CA - C ANGL. DEV. = -27.4 DEGREES
REMARK 500 GLY A 47 N - CA - C ANGL. DEV. = 17.1 DEGREES
REMARK 500 LYS A 48 N - CA - C ANGL. DEV. = 21.1 DEGREES
REMARK 500 GLY A 49 N - CA - C ANGL. DEV. = 28.0 DEGREES
REMARK 500 PRO A 64 C - N - CA ANGL. DEV. = 11.8 DEGREES
REMARK 500 PRO A 303 C - N - CA ANGL. DEV. = 9.3 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 ILE A 43 98.75 -172.28
REMARK 500 LYS A 44 178.43 -20.70
REMARK 500 HIS A 45 -9.33 146.65
REMARK 500 LEU A 46 106.25 141.72
REMARK 500 LYS A 48 -93.53 -27.26
REMARK 500 VAL A 74 -50.52 -122.77
REMARK 500 ARG A 96 -115.40 59.46
REMARK 500 GLU A 185 -44.90 -134.74
REMARK 500 VAL A 195 -74.99 -100.07
REMARK 500 PRO A 286 139.78 -35.76
REMARK 500 PRO A 303 -106.84 -47.93
REMARK 500 TYR A 336 76.56 -118.44
REMARK 500 SER A 350 -3.58 77.07
REMARK 500 GLU A 371 109.12 -167.35
REMARK 500 TYR A 407 -60.15 -90.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 189 0.06 SIDE CHAIN
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 PC1 A 578
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PC1 A 577
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PC1 A 578
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BP1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BPI AT ROOM TEMPERATURE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 A NATURALLY OCCURRING POLYMORPHISM EXISTS AT RESIDUE 185 FOR HUMAN
REMARK 999 BPI. THE CLONE USED FOR EXPRESSION OF BPI HAS GLU AT THIS POSITION,
REMARK 999 ALTHOUGH THE CLONE FOR THE SWISSPROT ENTRY HAS LYS AT THE SAME
REMARK 999 POSITION.
DBREF 1EWF A 1 456 UNP P17213 BPI_HUMAN 28 483
SEQADV 1EWF GLU A 185 UNP P17213 LYS 212 SEE REMARK 999
SEQADV 1EWF ALA A 351 UNP P17213 SER 378 ENGINEERED MUTATION
SEQRES 1 A 456 VAL ASN PRO GLY VAL VAL VAL ARG ILE SER GLN LYS GLY
SEQRES 2 A 456 LEU ASP TYR ALA SER GLN GLN GLY THR ALA ALA LEU GLN
SEQRES 3 A 456 LYS GLU LEU LYS ARG ILE LYS ILE PRO ASP TYR SER ASP
SEQRES 4 A 456 SER PHE LYS ILE LYS HIS LEU GLY LYS GLY HIS TYR SER
SEQRES 5 A 456 PHE TYR SER MET ASP ILE ARG GLU PHE GLN LEU PRO SER
SEQRES 6 A 456 SER GLN ILE SER MET VAL PRO ASN VAL GLY LEU LYS PHE
SEQRES 7 A 456 SER ILE SER ASN ALA ASN ILE LYS ILE SER GLY LYS TRP
SEQRES 8 A 456 LYS ALA GLN LYS ARG PHE LEU LYS MET SER GLY ASN PHE
SEQRES 9 A 456 ASP LEU SER ILE GLU GLY MET SER ILE SER ALA ASP LEU
SEQRES 10 A 456 LYS LEU GLY SER ASN PRO THR SER GLY LYS PRO THR ILE
SEQRES 11 A 456 THR CYS SER SER CYS SER SER HIS ILE ASN SER VAL HIS
SEQRES 12 A 456 VAL HIS ILE SER LYS SER LYS VAL GLY TRP LEU ILE GLN
SEQRES 13 A 456 LEU PHE HIS LYS LYS ILE GLU SER ALA LEU ARG ASN LYS
SEQRES 14 A 456 MET ASN SER GLN VAL CYS GLU LYS VAL THR ASN SER VAL
SEQRES 15 A 456 SER SER GLU LEU GLN PRO TYR PHE GLN THR LEU PRO VAL
SEQRES 16 A 456 MET THR LYS ILE ASP SER VAL ALA GLY ILE ASN TYR GLY
SEQRES 17 A 456 LEU VAL ALA PRO PRO ALA THR THR ALA GLU THR LEU ASP
SEQRES 18 A 456 VAL GLN MET LYS GLY GLU PHE TYR SER GLU ASN HIS HIS
SEQRES 19 A 456 ASN PRO PRO PRO PHE ALA PRO PRO VAL MET GLU PHE PRO
SEQRES 20 A 456 ALA ALA HIS ASP ARG MET VAL TYR LEU GLY LEU SER ASP
SEQRES 21 A 456 TYR PHE PHE ASN THR ALA GLY LEU VAL TYR GLN GLU ALA
SEQRES 22 A 456 GLY VAL LEU LYS MET THR LEU ARG ASP ASP MET ILE PRO
SEQRES 23 A 456 LYS GLU SER LYS PHE ARG LEU THR THR LYS PHE PHE GLY
SEQRES 24 A 456 THR PHE LEU PRO GLU VAL ALA LYS LYS PHE PRO ASN MET
SEQRES 25 A 456 LYS ILE GLN ILE HIS VAL SER ALA SER THR PRO PRO HIS
SEQRES 26 A 456 LEU SER VAL GLN PRO THR GLY LEU THR PHE TYR PRO ALA
SEQRES 27 A 456 VAL ASP VAL GLN ALA PHE ALA VAL LEU PRO ASN SER ALA
SEQRES 28 A 456 LEU ALA SER LEU PHE LEU ILE GLY MET HIS THR THR GLY
SEQRES 29 A 456 SER MET GLU VAL SER ALA GLU SER ASN ARG LEU VAL GLY
SEQRES 30 A 456 GLU LEU LYS LEU ASP ARG LEU LEU LEU GLU LEU LYS HIS
SEQRES 31 A 456 SER ASN ILE GLY PRO PHE PRO VAL GLU LEU LEU GLN ASP
SEQRES 32 A 456 ILE MET ASN TYR ILE VAL PRO ILE LEU VAL LEU PRO ARG
SEQRES 33 A 456 VAL ASN GLU LYS LEU GLN LYS GLY PHE PRO LEU PRO THR
SEQRES 34 A 456 PRO ALA ARG VAL GLN LEU TYR ASN VAL VAL LEU GLN PRO
SEQRES 35 A 456 HIS GLN ASN PHE LEU LEU PHE GLY ALA ASP VAL VAL TYR
SEQRES 36 A 456 LYS
HET PC1 A 577 54
HET PC1 A 578 43
HETNAM PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
HETSYN PC1 3-SN-PHOSPHATIDYLCHOLINE
FORMUL 2 PC1 2(C44 H88 N O8 P)
FORMUL 4 HOH *387(H2 O)
HELIX 1 1 GLN A 11 LYS A 30 1 20
HELIX 2 2 LYS A 148 LYS A 150 5 3
HELIX 3 3 VAL A 151 ILE A 162 1 12
HELIX 4 4 ILE A 162 GLU A 185 1 24
HELIX 5 5 GLU A 185 GLN A 191 1 7
HELIX 6 6 ASP A 260 ALA A 273 1 14
HELIX 7 7 ASP A 283 ILE A 285 5 3
HELIX 8 8 THR A 294 THR A 300 1 7
HELIX 9 9 GLU A 304 PHE A 309 1 6
HELIX 10 10 PRO A 397 LEU A 400 5 4
HELIX 11 11 LEU A 401 VAL A 413 1 13
HELIX 12 12 VAL A 413 GLY A 424 1 12
SHEET 1 A 6 ALA A 214 THR A 215 0
SHEET 2 A 6 THR A 219 MET A 224 -1 N ASP A 221 O ALA A 214
SHEET 3 A 6 VAL A 5 SER A 10 -1 O VAL A 5 N MET A 224
SHEET 4 A 6 VAL A 254 SER A 259 -1 O TYR A 255 N ARG A 8
SHEET 5 A 6 PHE A 446 TYR A 455 -1 O LEU A 447 N LEU A 258
SHEET 6 A 6 VAL A 433 HIS A 443 -1 N GLN A 434 O VAL A 454
SHEET 1 B 9 TYR A 37 SER A 40 0
SHEET 2 B 9 HIS A 50 GLN A 62 -1 N TYR A 51 O ASP A 39
SHEET 3 B 9 GLY A 75 LYS A 95 -1 O ASN A 84 N GLN A 62
SHEET 4 B 9 SER A 66 VAL A 71 -1 O GLN A 67 N SER A 79
SHEET 5 B 9 GLY A 75 LYS A 95 -1 O GLY A 75 N VAL A 71
SHEET 6 B 9 LEU A 98 ASN A 122 -1 N LEU A 98 O LYS A 95
SHEET 7 B 9 LYS A 127 HIS A 138 -1 O LYS A 127 N ASN A 122
SHEET 8 B 9 LEU A 98 ASN A 122 -1 O SER A 112 N HIS A 138
SHEET 9 B 9 SER A 141 HIS A 145 -1 O SER A 141 N GLU A 109
SHEET 1 C 3 MET A 196 LYS A 198 0
SHEET 2 C 3 GLY A 204 ASN A 206 -1 O ILE A 205 N THR A 197
SHEET 3 C 3 GLU A 227 TYR A 229 -1 O GLU A 227 N ASN A 206
SHEET 1 D 5 LYS A 277 ARG A 281 0
SHEET 2 D 5 ILE A 314 SER A 319 -1 O ILE A 316 N LEU A 280
SHEET 3 D 5 ALA A 338 VAL A 346 -1 N ASP A 340 O SER A 319
SHEET 4 D 5 LEU A 352 HIS A 361 -1 N ALA A 353 O ALA A 345
SHEET 5 D 5 LEU A 385 SER A 391 -1 N LEU A 385 O HIS A 361
SSBOND 1 CYS A 135 CYS A 175 1555 1555 2.05
SITE 1 AC1 19 ALA A 17 GLY A 21 ALA A 24 SER A 181
SITE 2 AC1 19 GLU A 185 LEU A 186 TYR A 189 PHE A 190
SITE 3 AC1 19 LEU A 193 VAL A 222 VAL A 254 LEU A 256
SITE 4 AC1 19 LEU A 427 PRO A 428 ARG A 432 LEU A 435
SITE 5 AC1 19 VAL A 453 TYR A 455 HOH A 968
SITE 1 AC2 12 PHE A 263 TYR A 270 LEU A 276 LYS A 277
SITE 2 AC2 12 LEU A 326 PHE A 335 MET A 366 VAL A 368
SITE 3 AC2 12 LEU A 381 VAL A 417 LYS A 420 PHE A 425
CRYST1 184.320 31.230 80.660 90.00 103.20 90.00 C 1 2 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 0.005425 0.000000 0.001273 0.00000
SCALE2 0.000000 0.032020 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012734 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
