HEADER HYDROLASE/HYDROLASE INHIBITOR 16-DEC-91 1APT
TITLE CRYSTALLOGRAPHIC ANALYSIS OF A PEPSTATIN ANALOGUE BINDING TO THE
TITLE 2 ASPARTYL PROTEINASE PENICILLOPEPSIN AT 1.8 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PENICILLOPEPSIN;
COMPND 3 CHAIN: E;
COMPND 4 EC: 3.4.23.20;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INHIBITOR ISOVALERYL (IVA)-VAL-VAL-LYSTA-O-ET (LYSTA IS A
COMPND 8 LYSYL SIDE CHAIN ANALOGUE OF STATIN;
COMPND 9 CHAIN: I;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: TRANSITION STATE MIMIC INHIBITOR
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PENICILLIUM JANTHINELLUM;
SOURCE 3 ORGANISM_COMMON: PENICILLIUM VITALE;
SOURCE 4 ORGANISM_TAXID: 5079;
SOURCE 5 MOL_ID: 2
KEYWDS ACID PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.R.SIELECKI,M.N.G.JAMES
REVDAT 5 29-JUL-20 1APT 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE
REVDAT 4 13-JUL-11 1APT 1 VERSN
REVDAT 3 25-AUG-09 1APT 1 SOURCE
REVDAT 2 24-FEB-09 1APT 1 VERSN
REVDAT 1 31-JAN-94 1APT 0
JRNL AUTH M.N.G.JAMES,A.R.SIELECKI,J.MOULT
JRNL TITL CRYSTALLOGRAPHIC ANALYSIS OF A PEPSTATIN ANALOGUE BINDING TO
JRNL TITL 2 THE ASPARTYL PROTEINASE PENICILLOPEPSIN AT 1.8 ANGSTROMS
JRNL TITL 3 RESOLUTION
JRNL EDIT V.J.HRUBY, D.H.RICH
JRNL REF PEPTIDES: STRUCTURE AND V. 1 521 1983
JRNL REF 2 FUNCTION, PROCEEDINGS OF THE
JRNL REF 3 OF THE EIGHTH AMERICAN
JRNL REF 4 PEPTIDE SYMPOSIUM
JRNL PUBL PIERCE CHEMICAL COMPANY,ROCKFORD,IL
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.N.G.JAMES,A.R.SIELECKI,K.HAYAKAWA,M.H.GELB
REMARK 1 TITL CRYSTALLOGRAPHIC ANALYSIS OF TRANSITION STATE MIMICS BOUND
REMARK 1 TITL 2 TO PENICILLOPEPSIN: DIFLUOROSTATINE-AND
REMARK 1 TITL 3 DIFLUOROSTATONE-CONTAINING PEPTIDES
REMARK 1 REF BIOCHEMISTRY V. 31 3872 1992
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.N.G.JAMES,A.R.SIELECKI
REMARK 1 TITL ASPARTIC PROTEINASES AND THEIR CATALYTIC PATHWAY
REMARK 1 EDIT F.A.JURNAK, A.MCPHERSON
REMARK 1 REF BIOLOGICAL MACROMOLECULES V. 3 414 1987
REMARK 1 REF 2 AND ASSEMBLIES
REMARK 1 PUBL JOHN WILEY AND SONS,NEW YORK
REMARK 1 REFN ISSN 0-471-85142-6
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.N.G.JAMES,A.R.SIELECKI
REMARK 1 TITL STEREOCHEMICAL ANALYSIS OF PEPTIDE BOND HYDROLYSIS CATALYZED
REMARK 1 TITL 2 BY THE ASPARTIC PROTEINASE PENICILLOPEPSIN
REMARK 1 REF BIOCHEMISTRY V. 24 3701 1985
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH M.N.G.JAMES,A.R.SIELECKI,T.HOFMANN
REMARK 1 TITL X-RAY DIFFRACTION STUDIES ON PENICILLOPEPSIN AND ITS
REMARK 1 TITL 2 COMPLEXES: THE HYDROLYTIC MECHANISM
REMARK 1 EDIT V.KOSTKA
REMARK 1 REF ASPARTIC PROTEINASES AND 163 1985
REMARK 1 REF 2 THEIR INHIBITORS
REMARK 1 PUBL WALTER DE GRUYTER & CO.,BERLIN AND NEW YORK
REMARK 1 REFN
REMARK 1 REFERENCE 5
REMARK 1 AUTH T.HOFMANN,R.S.HODGES,M.N.G.JAMES
REMARK 1 TITL EFFECT OF PH ON THE ACTIVITIES OF PENICILLOPEPSIN AND
REMARK 1 TITL 2 RHIZOPUS PEPSIN AND A PROPOSAL FOR THE PRODUCTIVE SUBSTRATE
REMARK 1 TITL 3 BINDING MODE IN PENICILLOPEPSIN
REMARK 1 REF BIOCHEMISTRY V. 23 635 1984
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 6
REMARK 1 AUTH M.N.G.JAMES,A.R.SIELECKI
REMARK 1 TITL STRUCTURE AND REFINEMENT OF PENICILLOPEPSIN AT 1.8 ANGSTROMS
REMARK 1 TITL 2 RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 163 299 1983
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 7
REMARK 1 AUTH M.N.G.JAMES,A.SIELECKI,F.SALITURO,D.H.RICH,T.HOFMANN
REMARK 1 TITL CONFORMATIONAL FLEXIBILITY IN THE ACTIVE SITES OF ASPARTYL
REMARK 1 TITL 2 PROTEINASES REVEALED BY A PEPSTATIN FRAGMENT BINDING TO
REMARK 1 TITL 3 PENICILLOPEPSIN
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 79 6137 1982
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 22494
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.135
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2401
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 247
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 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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.015 ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1APT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171108.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 48.78500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.23500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 48.78500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.23500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH E 411 LIES ON A SPECIAL POSITION.
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 E 142 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 TYR E 165 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 TYR E 198 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP E 206 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP E 222 CB - CG - OD2 ANGL. DEV. = -8.9 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 PHE E 208 -176.42 -171.45
REMARK 500 ASP E 279 33.54 -146.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 LTA IS AN O-ETHYL ANALOGUE OF STATINE IN WHICH THE
REMARK 600 LEUCINE-LIKE SIDE CHAIN OF STATINE HAS BEEN REPLACED BY THE
REMARK 600 LYSINE-LIKE SIDE CHAIN.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1APU RELATED DB: PDB
REMARK 900 RELATED ID: 1APV RELATED DB: PDB
REMARK 900 RELATED ID: 1APW RELATED DB: PDB
DBREF 1APT E 1 323 UNP P00798 PENP_PENJA 1 323
DBREF 1APT I 4 1 PDB 1APT 1APT 4 1
SEQRES 1 E 323 ALA ALA SER GLY VAL ALA THR ASN THR PRO THR ALA ASN
SEQRES 2 E 323 ASP GLU GLU TYR ILE THR PRO VAL THR ILE GLY GLY THR
SEQRES 3 E 323 THR LEU ASN LEU ASN PHE ASP THR GLY SER ALA ASP LEU
SEQRES 4 E 323 TRP VAL PHE SER THR GLU LEU PRO ALA SER GLN GLN SER
SEQRES 5 E 323 GLY HIS SER VAL TYR ASN PRO SER ALA THR GLY LYS GLU
SEQRES 6 E 323 LEU SER GLY TYR THR TRP SER ILE SER TYR GLY ASP GLY
SEQRES 7 E 323 SER SER ALA SER GLY ASN VAL PHE THR ASP SER VAL THR
SEQRES 8 E 323 VAL GLY GLY VAL THR ALA HIS GLY GLN ALA VAL GLN ALA
SEQRES 9 E 323 ALA GLN GLN ILE SER ALA GLN PHE GLN GLN ASP THR ASN
SEQRES 10 E 323 ASN ASP GLY LEU LEU GLY LEU ALA PHE SER SER ILE ASN
SEQRES 11 E 323 THR VAL GLN PRO GLN SER GLN THR THR PHE PHE ASP THR
SEQRES 12 E 323 VAL LYS SER SER LEU ALA GLN PRO LEU PHE ALA VAL ALA
SEQRES 13 E 323 LEU LYS HIS GLN GLN PRO GLY VAL TYR ASP PHE GLY PHE
SEQRES 14 E 323 ILE ASP SER SER LYS TYR THR GLY SER LEU THR TYR THR
SEQRES 15 E 323 GLY VAL ASP ASN SER GLN GLY PHE TRP SER PHE ASN VAL
SEQRES 16 E 323 ASP SER TYR THR ALA GLY SER GLN SER GLY ASP GLY PHE
SEQRES 17 E 323 SER GLY ILE ALA ASP THR GLY THR THR LEU LEU LEU LEU
SEQRES 18 E 323 ASP ASP SER VAL VAL SER GLN TYR TYR SER GLN VAL SER
SEQRES 19 E 323 GLY ALA GLN GLN ASP SER ASN ALA GLY GLY TYR VAL PHE
SEQRES 20 E 323 ASP CYS SER THR ASN LEU PRO ASP PHE SER VAL SER ILE
SEQRES 21 E 323 SER GLY TYR THR ALA THR VAL PRO GLY SER LEU ILE ASN
SEQRES 22 E 323 TYR GLY PRO SER GLY ASP GLY SER THR CYS LEU GLY GLY
SEQRES 23 E 323 ILE GLN SER ASN SER GLY ILE GLY PHE SER ILE PHE GLY
SEQRES 24 E 323 ASP ILE PHE LEU LYS SER GLN TYR VAL VAL PHE ASP SER
SEQRES 25 E 323 ASP GLY PRO GLN LEU GLY PHE ALA PRO GLN ALA
SEQRES 1 I 4 IVA VAL VAL LTA
MODRES 1APT SER E 3 SER GLYCOSYLATION SITE
HET IVA I 4 6
HET LTA I 1 15
HET MAN E 334 11
HETNAM IVA ISOVALERIC ACID
HETNAM LTA 4,8-DIAMINO-3-HYDROXY-OCTANOIC ACID ETHYL ESTER
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETSYN LTA STATINE ANALOGUE
FORMUL 2 IVA C5 H10 O2
FORMUL 2 LTA C10 H22 N2 O3
FORMUL 3 MAN C6 H12 O6
FORMUL 4 HOH *247(H2 O)
HELIX 1 1 ALA E 12 GLU E 15 5 4
HELIX 2 2 PRO E 47 SER E 52 1 6
HELIX 3 3 ASN E 58 GLY E 63 1 6
HELIX 4 4 SER E 109 ASP E 115 1 7
HELIX 5 5 PHE E 126 ASN E 130 5 5
HELIX 6 6 THR E 139 LYS E 145 1 7
HELIX 7 7 ASP E 171 LYS E 174 5 4
HELIX 8 8 ASP E 222 SER E 231 1 10
HELIX 9 9 PRO E 268 ILE E 272 1 5
HELIX 10 10 GLY E 299 LYS E 304 1 6
SHEET 1 A 7 TYR E 263 VAL E 267 0
SHEET 2 A 7 PHE E 256 ILE E 260 -1 O PHE E 256 N VAL E 267
SHEET 3 A 7 SER E 192 ALA E 200 -1 N ASP E 196 O SER E 259
SHEET 4 A 7 GLN E 203 ALA E 212 -1 O GLN E 203 N ALA E 200
SHEET 5 A 7 SER E 296 PHE E 298 1 N SER E 296 O SER E 209
SHEET 6 A 7 LEU E 219 LEU E 221 -1 N LEU E 220 O ILE E 297
SHEET 7 A 7 ILE E 287 SER E 289 1 N GLN E 288 O LEU E 219
SHEET 1 B 4 GLN E 237 ASP E 239 0
SHEET 2 B 4 GLY E 244 PHE E 247 -1 O GLY E 244 N ASP E 239
SHEET 3 B 4 CYS E 283 GLY E 285 -1 N CYS E 283 O PHE E 247
SHEET 4 B 4 ASN E 273 PRO E 276 -1 N TYR E 274 O LEU E 284
SSBOND 1 CYS E 249 CYS E 283 1555 1555 2.07
LINK OG SER E 3 C1 MAN E 334 1555 1555 1.42
LINK N LTA I 1 C VAL I 2 1555 1555 1.33
LINK N VAL I 3 C IVA I 4 1555 1555 1.30
CISPEP 1 GLN E 133 PRO E 134 0 2.36
CISPEP 2 GLY E 314 PRO E 315 0 -2.87
CRYST1 97.570 46.470 66.390 90.00 116.15 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 0.010249 0.000000 0.005032 0.00000
SCALE2 0.000000 0.021519 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016780 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
