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HEADER HYDROLASE 06-DEC-96 1OIL
TITLE STRUCTURE OF LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TRIACYLGLYCEROL HYDROLASE;
COMPND 5 EC: 3.1.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS CEPACIA;
SOURCE 3 OTHER_DETAILS: PURCHASED FROM AMANO PHARMACEUTICAL CO., LTD
SOURCE 4 (LIPASE PS AMANO, LPSA001526)
KEYWDS HYDROLASE, TRIACYLGLYCEROL LIPASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.K.KIM,H.K.SONG,D.H.SHIN,S.W.SUH
REVDAT 1 15-MAY-97 1OIL 0
JRNL AUTH K.K.KIM,H.K.SONG,D.H.SHIN,K.Y.HWANG,S.W.SUH
JRNL TITL THE CRYSTAL STRUCTURE OF A TRIACYLGLYCEROL LIPASE
JRNL TITL 2 FROM PSEUDOMONAS CEPACIA REVEALS A HIGHLY OPEN
JRNL TITL 3 CONFORMATION IN THE ABSENCE OF A BOUND INHIBITOR
JRNL REF STRUCTURE (LONDON) V. 5 173 1997
JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 2005
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.K.KIM,K.Y.HWANG,H.S.JEON,S.KIM,R.M.SWEET,
REMARK 1 AUTH 2 C.H.YANG,S.W.SUH
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY
REMARK 1 TITL 2 CRYSTALLOGRAPHIC ANALYSIS OF LIPASE FROM
REMARK 1 TITL 3 PSEUDOMONAS CEPACIA
REMARK 1 REF J.MOL.BIOL. V. 227 1258 1992
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070
REMARK 2
REMARK 2 RESOLUTION. 2.1 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 79.1
REMARK 3 NUMBER OF REFLECTIONS : 28405
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE-R
REMARK 3 FREE R VALUE TEST SET SELECTION : X-PLOR
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.
REMARK 3 FREE R VALUE TEST SET COUNT : 2828
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.1
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 24.8
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 985
REMARK 3 BIN R VALUE (WORKING SET) : 0.231
REMARK 3 BIN FREE R VALUE : 0.384
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.6
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 115
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 : 4674
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 395
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.7
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.6
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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.67
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.2
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.62
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OIL COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 6
REMARK 6 THE UNUSUAL DIHEDRAL ANGLE OF SER 87 IN CHAINS A AND B IS
REMARK 6 ESSENTIAL FOR ITS CATALYTIC ACTIVITY.
REMARK 7
REMARK 7 INITIAL REFINEMENT WAS DONE WITH PSEUDO I2(1) SYMMETRY IN
REMARK 7 CCP4.
REMARK 7 SYMMETRY TRANSFORMATION LISTED BELOW:
REMARK 7 X, Y, Z
REMARK 7 -X, 1/2+Y, -Z
REMARK 7 1/2+X, 1/2+Y, 1/2+Z
REMARK 7 1/2-X, Y, 1/2+-Z
REMARK 7
REMARK 7 SYMMETRY OPERATIONS FOR NON-STANDARD SETTING:
REMARK 7 (0.50 0.49 0.50) TRANSLATION
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-1992
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : CU-KALPHA
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : FAST
REMARK 200 DETECTOR MANUFACTURER : ENRAF-NONIUS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MADNES
REMARK 200 DATA SCALING SOFTWARE : FOURIER SCALING
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29375
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.1
REMARK 200 RESOLUTION RANGE LOW (A) : 8.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 80.0
REMARK 200 DATA REDUNDANCY : 3.6
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04
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 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: CCP4, X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 23.71017
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 1 .. 320 B 1 .. 320 0.200
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
REMARK 800
REMARK 800 SITE_IDENTIFIER: BCT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
REMARK 850
REMARK 850 CORRECTION BEFORE RELEASE
REMARK 850 ORIGINAL DEPOSITION REVISED PRIOR TO RELEASE
REMARK 850 DATE REVISED: 08-JAN-1997 TRACKING NUMBER: T10205
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 REFERENCE: UNITED STATES PATENT 5,290,694.
DBREF 1OIL A 1 320 PDB 1OIL 1OIL 1 320
DBREF 1OIL B 1 320 PDB 1OIL 1OIL 1 320
SEQRES 1 A 320 ALA ASP ASN TYR ALA ALA THR ARG TYR PRO ILE ILE LEU
SEQRES 2 A 320 VAL HIS GLY LEU THR GLY THR ASP LYS TYR ALA GLY VAL
SEQRES 3 A 320 LEU GLU TYR TRP TYR GLY ILE GLN GLU ASP LEU GLN GLN
SEQRES 4 A 320 ARG GLY ALA THR VAL TYR VAL ALA ASN LEU SER GLY PHE
SEQRES 5 A 320 GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU
SEQRES 6 A 320 LEU ALA TYR VAL LYS THR VAL LEU ALA ALA THR GLY ALA
SEQRES 7 A 320 THR LYS VAL ASN LEU VAL GLY HIS SER GLN GLY GLY LEU
SEQRES 8 A 320 THR SER ARG TYR VAL ALA ALA VAL ALA PRO ASP LEU VAL
SEQRES 9 A 320 ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER
SEQRES 10 A 320 GLU PHE ALA ASP PHE VAL GLN GLY VAL LEU ALA TYR ASP
SEQRES 11 A 320 PRO THR GLY LEU SER SER THR VAL ILE ALA ALA PHE VAL
SEQRES 12 A 320 ASN VAL PHE GLY ILE LEU THR SER SER SER ASN ASN THR
SEQRES 13 A 320 ASN GLN ASP ALA LEU ALA ALA LEU LYS THR LEU THR THR
SEQRES 14 A 320 ALA GLN ALA ALA THR TYR ASN GLN ASN TYR PRO SER ALA
SEQRES 15 A 320 GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA PRO
SEQRES 16 A 320 THR GLU THR VAL GLY GLY ASN THR HIS LEU LEU TYR SER
SEQRES 17 A 320 TRP ALA GLY THR ALA ILE GLN PRO THR ILE SER VAL PHE
SEQRES 18 A 320 GLY VAL THR GLY ALA THR ASP THR SER THR ILE PRO LEU
SEQRES 19 A 320 VAL ASP PRO ALA ASN ALA LEU ASP PRO SER THR LEU ALA
SEQRES 20 A 320 LEU PHE GLY THR GLY THR VAL MET VAL ASN ARG GLY SER
SEQRES 21 A 320 GLY GLN ASN ASP GLY VAL VAL SER LYS CYS SER ALA LEU
SEQRES 22 A 320 TYR GLY GLN VAL LEU SER THR SER TYR LYS TRP ASN HIS
SEQRES 23 A 320 LEU ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA
SEQRES 24 A 320 ASN ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS ALA
SEQRES 25 A 320 ASN ARG LEU LYS LEU ALA GLY VAL
SEQRES 1 B 320 ALA ASP ASN TYR ALA ALA THR ARG TYR PRO ILE ILE LEU
SEQRES 2 B 320 VAL HIS GLY LEU THR GLY THR ASP LYS TYR ALA GLY VAL
SEQRES 3 B 320 LEU GLU TYR TRP TYR GLY ILE GLN GLU ASP LEU GLN GLN
SEQRES 4 B 320 ARG GLY ALA THR VAL TYR VAL ALA ASN LEU SER GLY PHE
SEQRES 5 B 320 GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU
SEQRES 6 B 320 LEU ALA TYR VAL LYS THR VAL LEU ALA ALA THR GLY ALA
SEQRES 7 B 320 THR LYS VAL ASN LEU VAL GLY HIS SER GLN GLY GLY LEU
SEQRES 8 B 320 THR SER ARG TYR VAL ALA ALA VAL ALA PRO ASP LEU VAL
SEQRES 9 B 320 ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER
SEQRES 10 B 320 GLU PHE ALA ASP PHE VAL GLN GLY VAL LEU ALA TYR ASP
SEQRES 11 B 320 PRO THR GLY LEU SER SER THR VAL ILE ALA ALA PHE VAL
SEQRES 12 B 320 ASN VAL PHE GLY ILE LEU THR SER SER SER ASN ASN THR
SEQRES 13 B 320 ASN GLN ASP ALA LEU ALA ALA LEU LYS THR LEU THR THR
SEQRES 14 B 320 ALA GLN ALA ALA THR TYR ASN GLN ASN TYR PRO SER ALA
SEQRES 15 B 320 GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA PRO
SEQRES 16 B 320 THR GLU THR VAL GLY GLY ASN THR HIS LEU LEU TYR SER
SEQRES 17 B 320 TRP ALA GLY THR ALA ILE GLN PRO THR ILE SER VAL PHE
SEQRES 18 B 320 GLY VAL THR GLY ALA THR ASP THR SER THR ILE PRO LEU
SEQRES 19 B 320 VAL ASP PRO ALA ASN ALA LEU ASP PRO SER THR LEU ALA
SEQRES 20 B 320 LEU PHE GLY THR GLY THR VAL MET VAL ASN ARG GLY SER
SEQRES 21 B 320 GLY GLN ASN ASP GLY VAL VAL SER LYS CYS SER ALA LEU
SEQRES 22 B 320 TYR GLY GLN VAL LEU SER THR SER TYR LYS TRP ASN HIS
SEQRES 23 B 320 LEU ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA
SEQRES 24 B 320 ASN ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS ALA
SEQRES 25 B 320 ASN ARG LEU LYS LEU ALA GLY VAL
HET CA A 401 1
HET CA B 401 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 2(CA1 2+)
FORMUL 4 HOH *395(H2 O1)
HELIX 1 1 TYR A 23 GLY A 25 5 3
HELIX 2 2 ILE A 33 GLN A 39 1 7
HELIX 3 3 ARG A 61 THR A 76 1 16
HELIX 4 4 SER A 87 VAL A 99 5 13
HELIX 5 5 PRO A 101 LEU A 103 5 3
HELIX 6 6 GLU A 118 TYR A 129 1 12
HELIX 7 7 LEU A 134 THR A 150 1 17
HELIX 8 8 ALA A 160 LEU A 167 1 8
HELIX 9 9 THR A 169 ASN A 178 1 10
HELIX 10 10 PRO A 237 LEU A 241 5 5
HELIX 11 11 SER A 244 ARG A 258 1 15
HELIX 12 12 LYS A 269 ALA A 272 1 4
HELIX 13 13 ASP A 288 ILE A 290 5 3
HELIX 14 14 PRO A 304 ALA A 318 1 15
HELIX 15 15 TYR B 23 GLY B 25 5 3
HELIX 16 16 ILE B 33 GLN B 39 1 7
HELIX 17 17 ARG B 61 THR B 76 1 16
HELIX 18 18 SER B 87 VAL B 99 5 13
HELIX 19 19 PRO B 101 LEU B 103 5 3
HELIX 20 20 GLU B 118 TYR B 129 1 12
HELIX 21 21 LEU B 134 THR B 150 1 17
HELIX 22 22 ALA B 160 THR B 166 1 7
HELIX 23 23 THR B 169 ASN B 178 1 10
HELIX 24 24 PRO B 237 LEU B 241 5 5
HELIX 25 25 PRO B 243 ARG B 258 1 16
HELIX 26 26 LYS B 269 ALA B 272 1 4
HELIX 27 27 ASP B 288 ILE B 290 5 3
HELIX 28 28 PRO B 304 ALA B 318 1 15
SHEET 1 A 6 VAL A 44 VAL A 46 0
SHEET 2 A 6 PRO A 10 VAL A 14 1 N ILE A 11 O TYR A 45
SHEET 3 A 6 VAL A 81 HIS A 86 1 N ASN A 82 O PRO A 10
SHEET 4 A 6 VAL A 104 ILE A 110 1 N ALA A 105 O VAL A 81
SHEET 5 A 6 ASN A 202 TRP A 209 1 N LEU A 205 O VAL A 107
SHEET 6 A 6 THR A 196 VAL A 199 -1 N VAL A 199 O ASN A 202
SHEET 1 B 2 ILE A 214 PRO A 216 0
SHEET 2 B 2 ALA A 226 ASP A 228 -1 N THR A 227 O GLN A 215
SHEET 1 C 6 VAL B 44 VAL B 46 0
SHEET 2 C 6 PRO B 10 VAL B 14 1 N ILE B 11 O TYR B 45
SHEET 3 C 6 VAL B 81 HIS B 86 1 N ASN B 82 O PRO B 10
SHEET 4 C 6 VAL B 104 ILE B 110 1 N ALA B 105 O VAL B 81
SHEET 5 C 6 ASN B 202 TRP B 209 1 N LEU B 205 O VAL B 107
SHEET 6 C 6 THR B 196 VAL B 199 -1 N VAL B 199 O ASN B 202
SHEET 1 D 2 ILE B 214 PRO B 216 0
SHEET 2 D 2 ALA B 226 ASP B 228 -1 N THR B 227 O GLN B 215
SHEET 1 E 2 TYR A 207 TRP A 209 0
SHEET 2 E 2 GLN A 276 SER A 279 1 N GLN A 276 O SER A 208
SHEET 1 F 2 TYR B 207 TRP B 209 0
SHEET 2 F 2 GLN B 276 SER B 279 1 N GLN B 276 O SER B 208
SSBOND 1 CYS A 190 CYS A 270
SSBOND 2 CYS B 190 CYS B 270
LINK CA CA B 401 OD1 ASP B 288
LINK CA CA B 401 O VAL B 296
SITE 1 ACT 3 SER A 87 HIS A 286 ASP A 264
SITE 1 BCT 3 SER B 87 HIS B 286 ASP B 264
CRYST1 85.230 47.420 86.530 90.00 116.11 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 0.011733 0.000000 0.005750 0.00000
SCALE2 0.000000 0.021088 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012870 0.00000
MTRIX1 1 0.999902 -0.013957 -0.001365 23.63000 1
MTRIX2 1 0.013944 0.999866 -0.008608 23.45000 1
MTRIX3 1 0.001485 0.008589 0.999962 38.85000 1 |