| content |
HEADER SERINE ESTERASE 26-OCT-96 1OXM
TITLE STRUCTURE OF CUTINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSARIUM SOLANI PISI;
SOURCE 3 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: MIRY
KEYWDS HYDROLASE, SERINE ESTERASE, GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LONGHI,C.CAMBILLAU
REVDAT 1 15-MAY-97 1OXM 0
JRNL AUTH S.LONGHI,M.MANNESSE,H.M.VERHEIJ,G.H.DE HAAS,
JRNL AUTH 2 M.EGMOND,E.KNOOPS-MOUTHUY,C.CAMBILLAU
JRNL TITL CRYSTAL STRUCTURE OF CUTINASE COVALENTLY INHIBITED
JRNL TITL 2 BY A TRIGLYCERIDE ANALOGUE
JRNL REF PROTEIN SCI. V. 6 275 1997
JRNL REFN ASTM PRCIEI US ISSN 0961-8368 0795
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.LONGHI,A.NICOLAS,L.CREVELD,M.EGMOND,C.T.VERRIPS,
REMARK 1 AUTH 2 J.DE VLIEG,C.MARTINEZ,C.CAMBILLAU
REMARK 1 TITL DYNAMICS OF FUSARIUM SOLANI CUTINASE INVESTIGATED
REMARK 1 TITL 2 THROUGH STRUCTURAL COMPARISON AMONG DIFFERENT
REMARK 1 TITL 3 CRYSTAL FORMS OF ITS VARIANTS
REMARK 1 REF PROTEINS: STRUCT.,FUNCT., V. 26 442 1996
REMARK 1 REF 2 GENET.
REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 0867
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.NICOLAS,M.EGMOND,C.T.VERRIPS,J.DE VLIEG,
REMARK 1 AUTH 2 S.LONGHI,C.CAMBILLAU,C.MARTINEZ
REMARK 1 TITL CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO
REMARK 1 TITL 2 THE STABILIZATION OF THE OXYANION TRANSITION STATE
REMARK 1 REF BIOCHEMISTRY V. 35 398 1996
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.MARTINEZ,A.NICOLAS,H.VAN TILBEURGH,M.P.EGLOFF,
REMARK 1 AUTH 2 C.CUDREY,R.VERGER,C.CAMBILLAU
REMARK 1 TITL CUTINASE, A LIPOLYTIC ENZYME WITH A PREFORMED
REMARK 1 TITL 2 OXYANION HOLE
REMARK 1 REF BIOCHEMISTRY V. 33 83 1994
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033
REMARK 1 REFERENCE 4
REMARK 1 AUTH C.MARTINEZ,P.DE GEUS,M.LAUWEREYS,G.MATTHYSSENS,
REMARK 1 AUTH 2 C.CAMBILLAU
REMARK 1 TITL FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME WITH
REMARK 1 TITL 2 A CATALYTIC SERINE ACCESSIBLE TO SOLVENT
REMARK 1 REF NATURE V. 356 615 1992
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 15569
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : R-FREE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.
REMARK 3 FREE R VALUE TEST SET COUNT : 777
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 : 3542
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 209
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) : 0.15
REMARK 3 ESD FROM SIGMAA (A) : 0.28
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) : 0.0065
REMARK 3 BOND ANGLES (DEGREES) : 1.325
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 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 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 FINAL RMS COORD. SHIFT 0.029 ANGSTROMS
REMARK 3
REMARK 3 MEAN B (A**2) MOLECULE A : MAIN : 20.2
REMARK 3 MEAN B (A**2) MOLECULE A : SIDE : 23.3
REMARK 3 MEAN B (A**2) MOLECULE B : MAIN : 34.7
REMARK 3 MEAN B (A**2) MOLECULE B : SIDE : 36.9
REMARK 3 MEAN B (A**2) : SOLV : 45.1
REMARK 3
REMARK 3 RMSD BOND DISTANCE MOLECULE A : 0.007 A
REMARK 3 RMSD BOND DISTANCE MOLECULE B : 0.006 A
REMARK 3
REMARK 3 RMSD ANGLE DISTANCE MOLECULE A : 1.37 DEG
REMARK 3 RMSD ANGLE DISTANCE MOLECULE B : 1.28 DEG
REMARK 3
REMARK 3 BULK SOLVENT CORRECTION WAS APPLIED.
REMARK 4
REMARK 4 1OXM COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 6
REMARK 6 THERE ARE TWO MOLECULES PER ASYMMETRIC UNIT.
REMARK 7
REMARK 7 WT CUTINASE COVALENTLY INHIBITED BY THE TRIGLYCERIDE
REMARK 7 ANALOGUE TC4 BOUND TO THE CATALYTIC SERINE (RESIDUES A 120
REMARK 7 AND B 120).
REMARK 8
REMARK 8 THE CATALYTIC SER 120 OF BOTH MOLECULES IN THE
REMARK 8 ASYMMETRIC UNIT LIES IN AN UNFAVORABLE REGION OF THE
REMARK 8 RAMACHANDRAN PLOT (EPSILON CONFORMATION) WHICH IS TYPICAL
REMARK 8 OF ALL MEMBERS OF THE ALPHA/BETA HYDROLASE SUPERFAMILY.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : 30 CM IMAGE PLATE (MODE
REMARK 200 SMALL)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MARXDS
REMARK 200 DATA SCALING SOFTWARE : MARSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15569
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.30
REMARK 200 RESOLUTION RANGE LOW (A) : 30.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 200 DATA REDUNDANCY : 2.94
REMARK 200 R MERGE (I) : 0.0523
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.13
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.3
REMARK 200 R MERGE FOR SHELL (I) : 0.1768
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.90
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NATIVE STRUCTURE AT 1.6 ANGSTROMS (PDB
REMARK 200 ENTRY 1CUS)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000 IN HEPES 0.1 M PH 7
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 34.59968
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 A 17 .. 212 B 17 .. 212 0.347
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. SOME OF THESE MAY BE ATOMS
REMARK 500 LOCATED ON SPECIAL POSITIONS IN THE CELL. ATOMS WITH
REMARK 500 NON-BLANK ALTERNATE LOCATION INDICATORS ARE NOT INCLUDED
REMARK 500 IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 H VAL A 169 1HD2 ASN A 27 1655 1.33
REMARK 500 1HD2 ASN A 27 H VAL A 169 1455 1.33
REMARK 500 3HZ LYS A 65 2H HOH 606 1455 1.37
REMARK 500 2H HOH 606 3HZ LYS A 65 1655 1.37
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 0 HOH 586 DISTANCE = 7.04 ANGSTROMS
REMARK 525 0 HOH 614 DISTANCE = 5.57 ANGSTROMS
REMARK 525 0 HOH 663 DISTANCE = 5.71 ANGSTROMS
REMARK 525 0 HOH 683 DISTANCE = 6.13 ANGSTROMS
REMARK 525 0 HOH 688 DISTANCE = 8.04 ANGSTROMS
REMARK 525 0 HOH 702 DISTANCE = 29.62 ANGSTROMS
REMARK 525 0 HOH 703 DISTANCE = 8.58 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 CHAIN: A, (R)-1,2-DIBUTYL-CARBAMOYLGLYCERO-3-O-P-
REMARK 600 NITROPHENYLBUTYL-PHOSPHONATE.
REMARK 600 TC4 A 901, THE BINDING OF THE INHIBITOR CAUSES THE RELEASE
REMARK 600 P-NITROPHENOL.
REMARK 600 CHAIN: B, (R)-1,2-DIBUTYL-CARBAMOYLGLYCERO-3-O-P-
REMARK 600 NITROPHENYLBUTYL-PHOSPHONATE.
REMARK 600 TC4 B 901, THE BINDING OF THE INHIBITOR CAUSES THE RELEASE
REMARK 600 P-NITROPHENOL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: TC4
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1OXM A SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1OXM A SWS P00590 229 - 230 NOT IN ATOMS LIST
REMARK 999 1OXM B SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1OXM B SWS P00590 229 - 230 NOT IN ATOMS LIST
REMARK 999
REMARK 999 NO DENSITY HAS BEEN DETECTED FOR AN ARG SIDE CHAIN FOR
REMARK 999 RESIDUE 32 IN ANY CUTINASE VARIANT STRUCTURE SOLVED SO FAR.
REMARK 999 THE RESIDUE IS PRESENTED AS ALA IN THIS ENTRY.
DBREF 1OXM A 17 212 SWS P00590 CUTI_FUSSO 33 228
DBREF 1OXM B 17 212 SWS P00590 CUTI_FUSSO 33 228
SEQADV 1OXM ALA A 32 SWS P00590 ARG 48 CONFLICT
SEQADV 1OXM ALA B 32 SWS P00590 ARG 48 CONFLICT
SEQRES 1 A 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG
SEQRES 2 A 214 GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY
SEQRES 3 A 214 ASN SER ALA SER CYS ALA ASP VAL ILE PHE ILE TYR ALA
SEQRES 4 A 214 ARG GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY
SEQRES 5 A 214 PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS
SEQRES 6 A 214 ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG
SEQRES 7 A 214 ALA THR LEU GLY ASP ASN ALA LEU PRO ARG GLY THR SER
SEQRES 8 A 214 SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN
SEQRES 9 A 214 ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY
SEQRES 10 A 214 GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE
SEQRES 11 A 214 GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY
SEQRES 12 A 214 THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG
SEQRES 13 A 214 GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL
SEQRES 14 A 214 PHE CYS ASN THR GLY ASP LEU VAL CYS THR GLY SER LEU
SEQRES 15 A 214 ILE VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA
SEQRES 16 A 214 ARG GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG
SEQRES 17 A 214 ALA VAL ARG GLY SER ALA
SEQRES 1 B 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG
SEQRES 2 B 214 GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY
SEQRES 3 B 214 ASN SER ALA SER CYS ALA ASP VAL ILE PHE ILE TYR ALA
SEQRES 4 B 214 ARG GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY
SEQRES 5 B 214 PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS
SEQRES 6 B 214 ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG
SEQRES 7 B 214 ALA THR LEU GLY ASP ASN ALA LEU PRO ARG GLY THR SER
SEQRES 8 B 214 SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN
SEQRES 9 B 214 ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY
SEQRES 10 B 214 GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE
SEQRES 11 B 214 GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY
SEQRES 12 B 214 THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG
SEQRES 13 B 214 GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL
SEQRES 14 B 214 PHE CYS ASN THR GLY ASP LEU VAL CYS THR GLY SER LEU
SEQRES 15 B 214 ILE VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA
SEQRES 16 B 214 ARG GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG
SEQRES 17 B 214 ALA VAL ARG GLY SER ALA
HET TC4 A 901 28
HET TC4 B 901 28
HETNAM TC4 1,2-DIHEXANOYL-3-PENTANOYL PHOSPHOGLYCEROL
FORMUL 3 TC4 2(C17 H34 N2 O6 P1)
FORMUL 4 HOH *209(H2 O1)
HELIX 1 1 ASP A 22 ASN A 25 1 4
HELIX 2 2 SER A 28 SER A 30 5 3
HELIX 3 3 GLY A 49 PHE A 63 1 15
HELIX 4 4 GLY A 82 ALA A 85 5 4
HELIX 5 5 SER A 92 LYS A 108 1 17
HELIX 6 6 SER A 120 ASP A 132 5 13
HELIX 7 7 SER A 135 LYS A 140 1 6
HELIX 8 8 ALA A 164 ARG A 166 5 3
HELIX 9 9 LEU A 176 THR A 179 5 4
HELIX 10 10 ALA A 186 LEU A 189 5 4
HELIX 11 11 GLY A 192 ARG A 196 1 5
HELIX 12 12 PRO A 198 VAL A 210 1 13
HELIX 13 13 ASP B 22 ASN B 25 1 4
HELIX 14 14 SER B 28 SER B 30 5 3
HELIX 15 15 GLY B 49 PHE B 63 1 15
HELIX 16 16 GLY B 82 ALA B 85 5 4
HELIX 17 17 SER B 92 LYS B 108 1 17
HELIX 18 18 GLN B 121 ASP B 132 1 12
HELIX 19 19 SER B 135 LYS B 140 1 6
HELIX 20 20 ALA B 164 ARG B 166 5 3
HELIX 21 21 LEU B 176 THR B 179 5 4
HELIX 22 22 ALA B 186 LEU B 189 5 4
HELIX 23 23 GLY B 192 ARG B 196 1 5
HELIX 24 24 PRO B 198 VAL B 210 1 13
SHEET 1 A 5 VAL A 68 GLY A 72 0
SHEET 2 A 5 VAL A 34 ALA A 39 1 N VAL A 34 O TRP A 69
SHEET 3 A 5 THR A 113 TYR A 119 1 N THR A 113 O ILE A 35
SHEET 4 A 5 THR A 144 PHE A 147 1 N VAL A 145 O ALA A 116
SHEET 5 A 5 THR A 167 PHE A 170 1 N LYS A 168 O THR A 144
SHEET 1 B 5 VAL B 68 GLY B 72 0
SHEET 2 B 5 VAL B 34 ALA B 39 1 N VAL B 34 O TRP B 69
SHEET 3 B 5 THR B 113 TYR B 119 1 N THR B 113 O ILE B 35
SHEET 4 B 5 ILE B 141 PHE B 147 1 N ALA B 142 O LEU B 114
SHEET 5 B 5 THR B 167 PHE B 170 1 N LYS B 168 O THR B 144
SSBOND 1 CYS A 31 CYS A 109
SSBOND 2 CYS A 171 CYS A 178
SSBOND 3 CYS B 31 CYS B 109
SSBOND 4 CYS B 171 CYS B 178
LINK P1 TC4 A 901 OG SER A 120
LINK P1 TC4 B 901 OG SER B 120
SITE 1 TC4 6 SER A 120 SER B 120 HIS A 188 HIS B 188
SITE 2 TC4 6 ASP A 175 ASP B 175
CRYST1 37.200 69.200 73.300 90.00 93.80 90.00 P 1 21 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 0.026882 0.000000 0.001785 0.00000
SCALE2 0.000000 0.014451 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013673 0.00000
MTRIX1 1 -0.623890 -0.464330 -0.628620 65.85388 1
MTRIX2 1 -0.379250 -0.523430 0.763010 78.72206 1
MTRIX3 1 -0.683330 0.714440 0.150470 -12.47664 1 |