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HEADER HYDROLASE (CARBOXYLIC ESTER) 23-MAY-96 1LGY
TITLE LIPASE II FROM RHIZOPUS NIVEUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: LIPASE;
COMPND 5 EC: 3.1.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHIZOPUS NIVEUS;
SOURCE 3 ORGANISM_COMMON: FUNGUS;
SOURCE 4 ATCC: 4759
KEYWDS LIPASE, HYDROLASE (CARBOXYLIC ESTER)
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KOHNO,J.FUNATSU,B.MIKAMI,W.KUGIMIYA,T.MATSUO,Y.MORITA
REVDAT 1 23-DEC-96 1LGY 0
JRNL AUTH M.KOHNO,J.FUNATSU,B.MIKAMI,W.KUGIMIYA,T.MATSUO,
JRNL AUTH 2 Y.MORITA
JRNL TITL THE CRYSTAL STRUCTURE OF LIPASE II FROM RHIZOPUS
JRNL TITL 2 NIVEUS AT 2.2 ANGSTROMS RESOLUTION
JRNL REF J.BIOCHEM.(TOKYO) V. 120 505 1996
JRNL REFN ASTM JOBIAO JA ISSN 0021-924X 0418
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.KOHNO,W.KUGIMIYA,Y.HASHIMOTO,Y.MORITA
REMARK 1 TITL PURIFICATION, CHARACTERIZATION AND CRYSTALLIZATION
REMARK 1 TITL 2 OF TWO TYPES OF LIPASE FROM RHIZOPUS NIVEUS
REMARK 1 REF BIOSCI.BIOTECHNOL.BIOCHEM. V. 58 1007 1994
REMARK 1 REFN ASTM BBBIEJ JA ISSN 0916-8451 2094
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.KOHNO,W.KUGIMIYA,Y.HASHIMOTO,Y.MORITA
REMARK 1 TITL PRELIMINARY INVESTIGATION OF CRYSTALS OF LIPASE I
REMARK 1 TITL 2 FROM RHIZOPUS NIVEUS
REMARK 1 REF J.MOL.BIOL. V. 229 785 1993
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070
REMARK 2
REMARK 2 RESOLUTION. 2.2 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.2
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 40601
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.186
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 USING ALL DATA, NO SIGMA CUTOFF.
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 : 6204
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 OTHER ATOMS : 478
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.016 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : 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 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CHARMM
REMARK 3 MEAN B VALUE 22.6 ANGSTROMS**2
REMARK 3 ESD FROM LUZZATI PLOT 0.30 ANGSTROMS
REMARK 3 X-PLOR ALSO WAS USED.
REMARK 4
REMARK 4 1LGY COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JAN-1992
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) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : R-AXIS IIC/RIGAKU
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : RIGAKU
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53656
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 (%) : 86.7
REMARK 200 DATA REDUNDANCY : RIGAKU
REMARK 200 R MERGE (I) : 0.089
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 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 (%): 47.
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 43
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 3555 -Y,X,3/4+Z
REMARK 290 4555 Y,-X,1/4+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 68.94650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 103.41975
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 34.47325
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 SYMMETRY
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS:
REMARK 295
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
REMARK 295 VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE
REMARK 295 MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
REMARK 295 YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
REMARK 295 SECOND. CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS
REMARK 295 FOR WHICH 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 M1 A 5 .. 269 B 5 .. 269 0.361
REMARK 295 M2 C 5 .. 269 C A .. 269 0.453
REMARK 525
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 403 DISTANCE = 5.06 ANGSTROMS
REMARK 525 0 HOH 408 DISTANCE = 5.69 ANGSTROMS
REMARK 525 0 HOH 496 DISTANCE = 5.20 ANGSTROMS
REMARK 525 0 HOH 631 DISTANCE = 7.31 ANGSTROMS
REMARK 525 0 HOH 642 DISTANCE = 7.93 ANGSTROMS
REMARK 525 0 HOH 694 DISTANCE = 5.61 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE
REMARK 850
REMARK 850 CORRECTION BEFORE RELEASE
REMARK 850 ORIGINAL DEPOSITION REVISED PRIOR TO RELEASE
REMARK 850 DATE REVISED: 02-OCT-1996 TRACKING NUMBER: T8768
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1LGY A SWS P21811 1 - 127 NOT IN ATOMS LIST
REMARK 999 1LGY B SWS P21811 1 - 127 NOT IN ATOMS LIST
REMARK 999 1LGY C SWS P21811 1 - 127 NOT IN ATOMS LIST
DBREF 1LGY A 5 269 SWS P21811 LIP_RHIDL 128 392
DBREF 1LGY B 5 269 SWS P21811 LIP_RHIDL 128 392
DBREF 1LGY C 5 269 SWS P21811 LIP_RHIDL 128 392
SEQRES 1 A 269 SER ASP GLY GLY LYS VAL VAL ALA ALA THR THR ALA GLN
SEQRES 2 A 269 ILE GLN GLU PHE THR LYS TYR ALA GLY ILE ALA ALA THR
SEQRES 3 A 269 ALA TYR CYS ARG SER VAL VAL PRO GLY ASN LYS TRP ASP
SEQRES 4 A 269 CYS VAL GLN CYS GLN LYS TRP VAL PRO ASP GLY LYS ILE
SEQRES 5 A 269 ILE THR THR PHE THR SER LEU LEU SER ASP THR ASN GLY
SEQRES 6 A 269 TYR VAL LEU ARG SER ASP LYS GLN LYS THR ILE TYR LEU
SEQRES 7 A 269 VAL PHE ARG GLY THR ASN SER PHE ARG SER ALA ILE THR
SEQRES 8 A 269 ASP ILE VAL PHE ASN PHE SER ASP TYR LYS PRO VAL LYS
SEQRES 9 A 269 GLY ALA LYS VAL HIS ALA GLY PHE LEU SER SER TYR GLU
SEQRES 10 A 269 GLN VAL VAL ASN ASP TYR PHE PRO VAL VAL GLN GLU GLN
SEQRES 11 A 269 LEU THR ALA HIS PRO THR TYR LYS VAL ILE VAL THR GLY
SEQRES 12 A 269 HIS SER LEU GLY GLY ALA GLN ALA LEU LEU ALA GLY MET
SEQRES 13 A 269 ASP LEU TYR GLN ARG GLU PRO ARG LEU SER PRO LYS ASN
SEQRES 14 A 269 LEU SER ILE PHE THR VAL GLY GLY PRO ARG VAL GLY ASN
SEQRES 15 A 269 PRO THR PHE ALA TYR TYR VAL GLU SER THR GLY ILE PRO
SEQRES 16 A 269 PHE GLN ARG THR VAL HIS LYS ARG ASP ILE VAL PRO HIS
SEQRES 17 A 269 VAL PRO PRO GLN SER PHE GLY PHE LEU HIS PRO GLY VAL
SEQRES 18 A 269 GLU SER TRP ILE LYS SER GLY THR SER ASN VAL GLN ILE
SEQRES 19 A 269 CYS THR SER GLU ILE GLU THR LYS ASP CYS SER ASN SER
SEQRES 20 A 269 ILE VAL PRO PHE THR SER ILE LEU ASP HIS LEU SER TYR
SEQRES 21 A 269 PHE ASP ILE ASN GLU GLY SER CYS LEU
SEQRES 1 B 269 SER ASP GLY GLY LYS VAL VAL ALA ALA THR THR ALA GLN
SEQRES 2 B 269 ILE GLN GLU PHE THR LYS TYR ALA GLY ILE ALA ALA THR
SEQRES 3 B 269 ALA TYR CYS ARG SER VAL VAL PRO GLY ASN LYS TRP ASP
SEQRES 4 B 269 CYS VAL GLN CYS GLN LYS TRP VAL PRO ASP GLY LYS ILE
SEQRES 5 B 269 ILE THR THR PHE THR SER LEU LEU SER ASP THR ASN GLY
SEQRES 6 B 269 TYR VAL LEU ARG SER ASP LYS GLN LYS THR ILE TYR LEU
SEQRES 7 B 269 VAL PHE ARG GLY THR ASN SER PHE ARG SER ALA ILE THR
SEQRES 8 B 269 ASP ILE VAL PHE ASN PHE SER ASP TYR LYS PRO VAL LYS
SEQRES 9 B 269 GLY ALA LYS VAL HIS ALA GLY PHE LEU SER SER TYR GLU
SEQRES 10 B 269 GLN VAL VAL ASN ASP TYR PHE PRO VAL VAL GLN GLU GLN
SEQRES 11 B 269 LEU THR ALA HIS PRO THR TYR LYS VAL ILE VAL THR GLY
SEQRES 12 B 269 HIS SER LEU GLY GLY ALA GLN ALA LEU LEU ALA GLY MET
SEQRES 13 B 269 ASP LEU TYR GLN ARG GLU PRO ARG LEU SER PRO LYS ASN
SEQRES 14 B 269 LEU SER ILE PHE THR VAL GLY GLY PRO ARG VAL GLY ASN
SEQRES 15 B 269 PRO THR PHE ALA TYR TYR VAL GLU SER THR GLY ILE PRO
SEQRES 16 B 269 PHE GLN ARG THR VAL HIS LYS ARG ASP ILE VAL PRO HIS
SEQRES 17 B 269 VAL PRO PRO GLN SER PHE GLY PHE LEU HIS PRO GLY VAL
SEQRES 18 B 269 GLU SER TRP ILE LYS SER GLY THR SER ASN VAL GLN ILE
SEQRES 19 B 269 CYS THR SER GLU ILE GLU THR LYS ASP CYS SER ASN SER
SEQRES 20 B 269 ILE VAL PRO PHE THR SER ILE LEU ASP HIS LEU SER TYR
SEQRES 21 B 269 PHE ASP ILE ASN GLU GLY SER CYS LEU
SEQRES 1 C 269 SER ASP GLY GLY LYS VAL VAL ALA ALA THR THR ALA GLN
SEQRES 2 C 269 ILE GLN GLU PHE THR LYS TYR ALA GLY ILE ALA ALA THR
SEQRES 3 C 269 ALA TYR CYS ARG SER VAL VAL PRO GLY ASN LYS TRP ASP
SEQRES 4 C 269 CYS VAL GLN CYS GLN LYS TRP VAL PRO ASP GLY LYS ILE
SEQRES 5 C 269 ILE THR THR PHE THR SER LEU LEU SER ASP THR ASN GLY
SEQRES 6 C 269 TYR VAL LEU ARG SER ASP LYS GLN LYS THR ILE TYR LEU
SEQRES 7 C 269 VAL PHE ARG GLY THR ASN SER PHE ARG SER ALA ILE THR
SEQRES 8 C 269 ASP ILE VAL PHE ASN PHE SER ASP TYR LYS PRO VAL LYS
SEQRES 9 C 269 GLY ALA LYS VAL HIS ALA GLY PHE LEU SER SER TYR GLU
SEQRES 10 C 269 GLN VAL VAL ASN ASP TYR PHE PRO VAL VAL GLN GLU GLN
SEQRES 11 C 269 LEU THR ALA HIS PRO THR TYR LYS VAL ILE VAL THR GLY
SEQRES 12 C 269 HIS SER LEU GLY GLY ALA GLN ALA LEU LEU ALA GLY MET
SEQRES 13 C 269 ASP LEU TYR GLN ARG GLU PRO ARG LEU SER PRO LYS ASN
SEQRES 14 C 269 LEU SER ILE PHE THR VAL GLY GLY PRO ARG VAL GLY ASN
SEQRES 15 C 269 PRO THR PHE ALA TYR TYR VAL GLU SER THR GLY ILE PRO
SEQRES 16 C 269 PHE GLN ARG THR VAL HIS LYS ARG ASP ILE VAL PRO HIS
SEQRES 17 C 269 VAL PRO PRO GLN SER PHE GLY PHE LEU HIS PRO GLY VAL
SEQRES 18 C 269 GLU SER TRP ILE LYS SER GLY THR SER ASN VAL GLN ILE
SEQRES 19 C 269 CYS THR SER GLU ILE GLU THR LYS ASP CYS SER ASN SER
SEQRES 20 C 269 ILE VAL PRO PHE THR SER ILE LEU ASP HIS LEU SER TYR
SEQRES 21 C 269 PHE ASP ILE ASN GLU GLY SER CYS LEU
FORMUL 4 HOH *478(H2 O1)
HELIX 1 1 THR A 11 TYR A 28 1 18
HELIX 2 2 VAL A 41 TRP A 46 1 6
HELIX 3 3 PHE A 86 THR A 91 1 6
HELIX 4 4 ALA A 110 ALA A 133 1 24
HELIX 5 5 SER A 145 ARG A 161 5 17
HELIX 6 6 PRO A 183 THR A 192 1 10
HELIX 7 7 VAL A 206 HIS A 208 5 3
HELIX 8 8 GLN A 212 PHE A 214 5 3
HELIX 9 9 SER A 245 SER A 247 5 3
HELIX 10 10 LEU A 255 LEU A 258 5 4
HELIX 11 11 THR B 11 TYR B 28 1 18
HELIX 12 12 VAL B 41 TRP B 46 1 6
HELIX 13 13 PHE B 86 ASP B 92 1 7
HELIX 14 14 ALA B 110 ALA B 133 1 24
HELIX 15 15 SER B 145 ARG B 161 5 17
HELIX 16 16 PRO B 183 THR B 192 1 10
HELIX 17 17 VAL B 206 HIS B 208 5 3
HELIX 18 18 GLN B 212 PHE B 214 5 3
HELIX 19 19 SER B 245 ILE B 248 5 4
HELIX 20 20 ILE B 254 ASP B 256 5 3
HELIX 21 21 THR C 11 TYR C 28 1 18
HELIX 22 22 VAL C 41 TRP C 46 1 6
HELIX 23 23 ASP C 71 GLN C 73 5 3
HELIX 24 24 PHE C 86 ASP C 92 1 7
HELIX 25 25 ALA C 110 ALA C 133 1 24
HELIX 26 26 SER C 145 ARG C 161 5 17
HELIX 27 27 PRO C 183 SER C 191 1 9
HELIX 28 28 VAL C 206 HIS C 208 5 3
HELIX 29 29 GLN C 212 PHE C 214 5 3
HELIX 30 30 SER C 245 ILE C 248 5 4
HELIX 31 31 ILE C 254 HIS C 257 5 4
SHEET 1 A 9 VAL A 6 ALA A 8 0
SHEET 2 A 9 ASN A 231 CYS A 235 -1 N ILE A 234 O VAL A 7
SHEET 3 A 9 VAL A 221 SER A 227 -1 N SER A 227 O ASN A 231
SHEET 4 A 9 PRO A 195 HIS A 201 1 N ARG A 198 O VAL A 221
SHEET 5 A 9 LEU A 170 VAL A 175 1 N ILE A 172 O PRO A 195
SHEET 6 A 9 LYS A 138 HIS A 144 1 N VAL A 139 O SER A 171
SHEET 7 A 9 THR A 75 ARG A 81 1 N ILE A 76 O LYS A 138
SHEET 8 A 9 THR A 63 SER A 70 -1 N SER A 70 O THR A 75
SHEET 9 A 9 LYS A 51 SER A 58 -1 N SER A 58 O THR A 63
SHEET 1 B 2 PHE A 97 ASP A 99 0
SHEET 2 B 2 LYS A 107 HIS A 109 -1 N VAL A 108 O SER A 98
SHEET 1 C 9 VAL B 6 ALA B 8 0
SHEET 2 C 9 ASN B 231 CYS B 235 -1 N ILE B 234 O VAL B 7
SHEET 3 C 9 VAL B 221 SER B 227 -1 N SER B 227 O ASN B 231
SHEET 4 C 9 PHE B 196 HIS B 201 1 N ARG B 198 O VAL B 221
SHEET 5 C 9 LEU B 170 VAL B 175 1 N ILE B 172 O GLN B 197
SHEET 6 C 9 LYS B 138 HIS B 144 1 N VAL B 139 O SER B 171
SHEET 7 C 9 THR B 75 ARG B 81 1 N ILE B 76 O LYS B 138
SHEET 8 C 9 THR B 63 SER B 70 -1 N SER B 70 O THR B 75
SHEET 9 C 9 LYS B 51 SER B 58 -1 N SER B 58 O THR B 63
SHEET 1 D 2 PHE B 97 ASP B 99 0
SHEET 2 D 2 LYS B 107 HIS B 109 -1 N VAL B 108 O SER B 98
SHEET 1 E 9 VAL C 6 ALA C 8 0
SHEET 2 E 9 ASN C 231 CYS C 235 -1 N ILE C 234 O VAL C 7
SHEET 3 E 9 VAL C 221 SER C 227 -1 N SER C 227 O ASN C 231
SHEET 4 E 9 PRO C 195 HIS C 201 1 N ARG C 198 O VAL C 221
SHEET 5 E 9 LEU C 170 VAL C 175 1 N ILE C 172 O PRO C 195
SHEET 6 E 9 LYS C 138 HIS C 144 1 N VAL C 139 O SER C 171
SHEET 7 E 9 THR C 75 ARG C 81 1 N ILE C 76 O LYS C 138
SHEET 8 E 9 THR C 63 SER C 70 -1 N SER C 70 O THR C 75
SHEET 9 E 9 LYS C 51 SER C 58 -1 N SER C 58 O THR C 63
SHEET 1 F 2 PHE C 97 ASP C 99 0
SHEET 2 F 2 LYS C 107 HIS C 109 -1 N VAL C 108 O SER C 98
SSBOND 1 CYS A 29 CYS A 268
SSBOND 2 CYS A 40 CYS A 43
SSBOND 3 CYS A 235 CYS A 244
SSBOND 4 CYS B 29 CYS B 268
SSBOND 5 CYS B 40 CYS B 43
SSBOND 6 CYS B 235 CYS B 244
SSBOND 7 CYS C 29 CYS C 268
SSBOND 8 CYS C 40 CYS C 43
SSBOND 9 CYS C 235 CYS C 244
CISPEP 1 VAL A 33 PRO A 34 0 4.07
CISPEP 2 VAL A 209 PRO A 210 0 -19.29
CISPEP 3 VAL A 249 PRO A 250 0 0.25
CISPEP 4 VAL B 33 PRO B 34 0 17.46
CISPEP 5 VAL B 209 PRO B 210 0 -27.34
CISPEP 6 VAL B 249 PRO B 250 0 -0.53
CISPEP 7 VAL C 33 PRO C 34 0 2.08
CISPEP 8 VAL C 209 PRO C 210 0 -15.88
CISPEP 9 VAL C 249 PRO C 250 0 1.39
SITE 1 CAT 3 SER A 145 ASP A 204 HIS A 257
CRYST1 83.700 83.700 137.900 90.00 90.00 90.00 P 43 12
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 0.011947 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011947 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007252 0.00000
MTRIX1 1 -0.999623 0.025854 -0.009201 123.02810 1
MTRIX2 1 -0.026266 -0.998509 0.047852 124.36960 1
MTRIX3 1 -0.007951 0.048076 0.998812 -2.09610 1
MTRIX1 2 -0.071585 -0.698060 0.712452 77.62610 1
MTRIX2 2 -0.608659 0.596448 0.523244 54.86810 1
MTRIX3 2 -0.790196 -0.396184 -0.467577 140.70500 1 |