| content |
HEADER HYDROLASE 18-APR-97 3LIP
TITLE OPEN CONFORMATION OF PSEUDOMONAS CEPACIA LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIACYL-GLYCEROL-HYDROLASE;
COMPND 3 CHAIN: NULL;
COMPND 4 SYNONYM: LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 BIOLOGICAL_UNIT: MONOMER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS CEPACIA
SOURCE 3 (BURKHOLDERIA CEPACIA)
KEYWDS HYDROLASE, LIPASE, PSEUDOMONADACEAE, CATALYTIC TRIAD,
KEYWDS 2 OXYANION, OPEN, WITHOUT INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.LANG,D.SCHOMBURG
REVDAT 1 16-JUN-97 3LIP 0
JRNL AUTH J.D.SCHRAG,Y.LI,M.CYGLER,D.LANG,T.BURGDORF,
JRNL AUTH 2 H.J.HECHT,R.SCHMID,D.SCHOMBURG,T.J.RYDEL,
JRNL AUTH 3 J.D.OLIVER,L.C.STRICKLAND,C.M.DUNAWAY,S.B.LARSON,
JRNL AUTH 4 J.DAY,A.MCPHERSON
JRNL TITL THE OPEN CONFORMATION OF A PSEUDOMONAS LIPASE
JRNL REF STRUCTURE (LONDON) V. 5 187 1997
JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 2005
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH U.BORNSCHEUER,O.W.REIF,R.LAUSCH,R.FREITAG,
REMARK 1 AUTH 2 T.SCHEPER,F.N.KOLISIS,U.MENGE
REMARK 1 TITL LIPASE OF PSEUDOMONAS CEPACIA FOR BIOTECHNOLOGICAL
REMARK 1 TITL 2 PURPOSES: PURIFICATION, CRYSTALLIZATION AND
REMARK 1 TITL 3 CHARACTERIZATION
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1201 55 1994
REMARK 1 REFN ASTM BBACAQ NE ISSN 0006-3002 0113
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.A.LANG,B.HOFMANN,T.BURGDORF,L.HAALCK,H.-J.HECHT,
REMARK 1 AUTH 2 F.SPENER,R.D.SCHMID,D.SCHOMBURG
REMARK 1 TITL STRUCTURE ELUCIDATION OF TWO LIPASES OF THE
REMARK 1 TITL 2 PSEUDOMONAS FAMILY
REMARK 1 REF CLOSING MEETING OF THE EC 26 1994
REMARK 1 REF 2 BRIDGE LIPASE T-PROJECT
REMARK 1 REF 3 "CHARACTERIZATION OF LIPASES
REMARK 1 REF 4 FOR INDUSTRIAL APPLICATIONS:
REMARK 1 REF 5 3D STRUCTURE AND CATALYTIC
REMARK 1 REF 6 MECHANISM", PROGRAMME,
REMARK 1 REF 7 ABSTRACTS & PARTICIPANTS,
REMARK 1 REF 8 INTERNATIONAL WORKSHOP,
REMARK 1 REF 9 BENDOR ISLAND, BANDOL,
REMARK 1 REF 10 FRANCE, SEPTEMBER 14-17,
REMARK 1 REF 11 1994
REMARK 1 REFN ASTM FR ISBN 2138
REMARK 2
REMARK 2 RESOLUTION. 2.0 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) : 2.0
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.
REMARK 3 NUMBER OF REFLECTIONS : 17424
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.188
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) : 0.188
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) : 17424
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2338
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 193
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.95
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) : 0.2
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.0
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.02 ; 0.02
REMARK 3 ANGLE DISTANCE (A) : 0.039 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.052 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; 0.050
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.015 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.086 ; 0.08
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.174 ; 0.30
REMARK 3 MULTIPLE TORSION (A) : 0.138 ; 0.30
REMARK 3 H-BOND (X...Y) (A) : NULL ; 0.30
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; 0.30
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : 15.0 ; NULL
REMARK 3 PLANAR (DEGREES) : 2.387 ; 3.0
REMARK 3 STAGGERED (DEGREES) : 12.031; 15.0
REMARK 3 TRANSVERSE (DEGREES) : 23.919; 15.0
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.512 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.406 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.474 ; 1.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.02 ; 1.50
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3LIP COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 6
REMARK 6 DENSITY FOR RESIDUES 217 - 223 IS FRAGMENTED. THEREFORE
REMARK 6 THIS REGION WAS MODELED STEREOCHEMICALLY.
REMARK 7
REMARK 7 THE ELECTRON DENSITY FOR THE RESIDUES THR 18, SER 87, THR
REMARK 7 217 AND LEU 234 IS WELL DEFINED IN SPITE OF DIHEDRAL
REMARK 7 ANGLES OF THESE RESIDUES LYING OUTSIDE THEIR EXPECTED
REMARK 7 RANGE.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAY-1994
REMARK 200 TEMPERATURE (KELVIN) : 283
REMARK 200 PH : 8.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17688
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.0
REMARK 200 RESOLUTION RANGE LOW (A) : 18.7
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.3
REMARK 200 DATA REDUNDANCY : 2.0
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.095
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) : 2.0
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.63
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.183
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1CVL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 29-30 % N-PROPANOL, 0.1 M TRIS
REMARK 280 HCL BUFFER, PH 8.4-8.7, AT 12 DEGREES IN FOUR WEEKS,
REMARK 280 PROTEIN CONCENTRATION 22 MG/ML
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+Y,-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 45.64959
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.64961
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.64959
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.64961
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 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 O HOH 533 O HOH 583 4545 0.27
REMARK 500 O HOH 583 O HOH 533 4555 0.27
REMARK 500 O HOH 579 O HOH 478 4556 0.53
REMARK 500 O HOH 478 O HOH 579 4546 0.53
REMARK 500 O HOH 547 O HOH 586 4545 1.65
REMARK 500 O HOH 586 O HOH 547 4555 1.65
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD RESIDUES.
REMARK 800
REMARK 800 SITE_IDENTIFIER: OXY
REMARK 800 SITE_DESCRIPTION: OXYANION HOLE.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 3LIP SWS P22088 1 - 44 NOT IN ATOMS LIST
REMARK 999
REMARK 999 REFERENCE: THIS SEQUENCE MATCHES THAT REFERENCED IN
REMARK 999 NAKANISHI ET AL. (1991): CLONING, SEQUENCING, REGULATION
REMARK 999 OF THE LIPASE GENE FROM PSEUDOMONAS SP. M 12-33. IN
REMARK 999 LIPASES: STRUCTURE, MECHANISM, GENETIC ENGINEERING. GBF
REMARK 999 MONOGRAPHS NO. 16 (ALBERGHINA, SCHMID, VERGER EDS.) VCH,
REMARK 999 WEINHEIM, PP. 263-266.
DBREF 3LIP 1 320 SWS P22088 LIP_BURCE 45 364
SEQADV 3LIP ASP 2 SWS P22088 ALA 46 CONFLICT
SEQADV 3LIP ASN 3 SWS P22088 GLY 47 CONFLICT
SEQADV 3LIP THR 18 SWS P22088 SER 62 CONFLICT
SEQADV 3LIP ARG 40 SWS P22088 ASN 84 CONFLICT
SEQADV 3LIP THR 92 SWS P22088 SER 136 CONFLICT
SEQADV 3LIP GLY 125 SWS P22088 ASP 169 CONFLICT
SEQADV 3LIP THR 137 SWS P22088 SER 181 CONFLICT
SEQADV 3LIP ASN 154 SWS P22088 HIS 198 CONFLICT
SEQADV 3LIP LYS 165 SWS P22088 GLN 209 CONFLICT
SEQADV 3LIP GLN 171 SWS P22088 ARG 215 CONFLICT
SEQADV 3LIP ILE 218 SWS P22088 LEU 262 CONFLICT
SEQADV 3LIP ILE 232 SWS P22088 LEU 276 CONFLICT
SEQADV 3LIP ALA 240 SWS P22088 VAL 284 CONFLICT
SEQADV 3LIP PRO 243 SWS P22088 LEU 287 CONFLICT
SEQADV 3LIP VAL 256 SWS P22088 ILE 300 CONFLICT
SEQADV 3LIP VAL 266 SWS P22088 LEU 310 CONFLICT
SEQADV 3LIP GLN 276 SWS P22088 LYS 320 CONFLICT
SEQADV 3LIP ASN 300 SWS P22088 TYR 344 CONFLICT
SEQRES 1 320 ALA ASP ASN TYR ALA ALA THR ARG TYR PRO ILE ILE LEU
SEQRES 2 320 VAL HIS GLY LEU THR GLY THR ASP LYS TYR ALA GLY VAL
SEQRES 3 320 LEU GLU TYR TRP TYR GLY ILE GLN GLU ASP LEU GLN GLN
SEQRES 4 320 ARG GLY ALA THR VAL TYR VAL ALA ASN LEU SER GLY PHE
SEQRES 5 320 GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU
SEQRES 6 320 LEU ALA TYR VAL LYS THR VAL LEU ALA ALA THR GLY ALA
SEQRES 7 320 THR LYS VAL ASN LEU VAL GLY HIS SER GLN GLY GLY LEU
SEQRES 8 320 THR SER ARG TYR VAL ALA ALA VAL ALA PRO ASP LEU VAL
SEQRES 9 320 ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER
SEQRES 10 320 GLU PHE ALA ASP PHE VAL GLN GLY VAL LEU ALA TYR ASP
SEQRES 11 320 PRO THR GLY LEU SER SER THR VAL ILE ALA ALA PHE VAL
SEQRES 12 320 ASN VAL PHE GLY ILE LEU THR SER SER SER ASN ASN THR
SEQRES 13 320 ASN GLN ASP ALA LEU ALA ALA LEU LYS THR LEU THR THR
SEQRES 14 320 ALA GLN ALA ALA THR TYR ASN GLN ASN TYR PRO SER ALA
SEQRES 15 320 GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA PRO
SEQRES 16 320 THR GLU THR VAL GLY GLY ASN THR HIS LEU LEU TYR SER
SEQRES 17 320 TRP ALA GLY THR ALA ILE GLN PRO THR ILE SER VAL PHE
SEQRES 18 320 GLY VAL THR GLY ALA THR ASP THR SER THR ILE PRO LEU
SEQRES 19 320 VAL ASP PRO ALA ASN ALA LEU ASP PRO SER THR LEU ALA
SEQRES 20 320 LEU PHE GLY THR GLY THR VAL MET VAL ASN ARG GLY SER
SEQRES 21 320 GLY GLN ASN ASP GLY VAL VAL SER LYS CYS SER ALA LEU
SEQRES 22 320 TYR GLY GLN VAL LEU SER THR SER TYR LYS TRP ASN HIS
SEQRES 23 320 LEU ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA
SEQRES 24 320 ASN ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS ALA
SEQRES 25 320 ASN ARG LEU LYS LEU ALA GLY VAL
HET CA 321 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA1 2+
FORMUL 3 HOH *193(H2 O1)
HELIX 1 1 ILE 33 GLN 39 1 7
HELIX 2 2 ARG 61 THR 76 1 16
HELIX 3 3 GLY 89 VAL 99 5 11
HELIX 4 4 GLU 118 LEU 127 1 10
HELIX 5 5 LEU 134 THR 150 1 17
HELIX 6 6 ALA 160 THR 166 1 7
HELIX 7 7 THR 169 ASN 178 1 10
HELIX 8 8 ALA 238 LEU 241 5 4
HELIX 9 9 SER 244 VAL 256 1 13
HELIX 10 10 LYS 269 ALA 272 1 4
HELIX 11 11 PRO 304 ALA 318 1 15
SHEET 1 A1 6 VAL 44 VAL 46 0
SHEET 2 A1 6 PRO 10 VAL 14 1 N ILE 11 O TYR 45
SHEET 3 A1 6 VAL 81 HIS 86 1 N ASN 82 O PRO 10
SHEET 4 A1 6 VAL 104 ILE 110 1 N ALA 105 O VAL 81
SHEET 5 A1 6 THR 203 GLY 211 1 N LEU 205 O VAL 107
SHEET 6 A1 6 THR 196 THR 198 -1 N GLU 197 O HIS 204
SHEET 1 A2 6 VAL 44 VAL 46 0
SHEET 2 A2 6 PRO 10 VAL 14 1 N ILE 11 O TYR 45
SHEET 3 A2 6 VAL 81 HIS 86 1 N ASN 82 O PRO 10
SHEET 4 A2 6 VAL 104 ILE 110 1 N ALA 105 O VAL 81
SHEET 5 A2 6 THR 203 GLY 211 1 N LEU 205 O VAL 107
SHEET 6 A2 6 GLN 276 TYR 282 1 N SER 279 O SER 208
SHEET 1 B 2 LYS 22 TYR 23 0
SHEET 2 B 2 LEU 27 GLU 28 -1 N LEU 27 O TYR 23
SHEET 1 C 2 ILE 214 VAL 220 0
SHEET 2 C 2 VAL 223 ASP 228 -1 N THR 227 O GLN 215
LINK CA CA 321 OD1 ASP 288
LINK CA CA 321 O GLN 292
LINK CA CA 321 O VAL 296
LINK CA CA 321 O HOH 452
LINK CA CA 321 OD1 ASP 242
LINK CA CA 321 O HOH 467
CISPEP 1 GLN 292 LEU 293 0 -1.88
SITE 1 ACT 3 SER 87 HIS 286 ASP 264
SITE 1 OXY 2 LEU 17 GLN 88
CRYST1 91.300 47.300 85.400 90.00 121.40 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 0.010953 0.000000 0.006686 0.00000
SCALE2 0.000000 0.021142 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013719 0.00000 |