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HEADER HYDROLASE() 23-MAY-97 1AKN
TITLE STRUCTURE OF BILE-SALT ACTIVATED LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BILE-SALT ACTIVATED LIPASE;
COMPND 3 CHAIN: NULL;
COMPND 4 SYNONYM: CARBOXYL ESTER LIPASE, STEROL ESTERASE,
COMPND 5 CHOLESTEROL ESTERASE, PANCREATIC LYSOPHOSPHOLIPASE;
COMPND 6 EC: 3.1.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGAN: PANCREAS
KEYWDS HYDROLASE, SERINE ESTERASE, LIPID DEGRADATION, GLYCOPROTEIN,
KEYWDS 2 SIGNAL, CARBOXYLIC ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.WANG,X.ZHANG
REVDAT 1 27-MAY-98 1AKN 0
JRNL AUTH X.WANG,C.S.WANG,J.TANG,F.DYDA,X.C.ZHANG
JRNL TITL THE CRYSTAL STRUCTURE OF BOVINE BILE SALT ACTIVATED
JRNL TITL 2 LIPASE: INSIGHTS INTO THE BILE SALT ACTIVATION
JRNL TITL 3 MECHANISM
JRNL REF STRUCTURE (LONDON) V. 5 1209 1997
JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 2005
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.8 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) : 2.8
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 17178
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.3
REMARK 3 FREE R VALUE TEST SET COUNT : 1706
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 : 4261
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 66.1
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.6
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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.5
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.8
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.32
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 : NAG.PAR
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NAG.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: AT FINAL STEP, ALL DATA IN
REMARK 3 8 - 2.8 A WERE USED TO CARRY OUT A RESTRAINED TEMPERATURE
REMARK 3 FACTOR REFINEMENT BY TNT.
REMARK 4
REMARK 4 1AKN COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 6
REMARK 6 RESIDUES 548 - 579 ARE MISSING.
REMARK 7
REMARK 7 SER 546 AND GLN 547 WERE BUILT AS GLY.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : DEC-1996
REMARK 200 TEMPERATURE (KELVIN) : 288
REMARK 200 PH : 7.
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 : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : R-AXIS II IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18614
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.8
REMARK 200 RESOLUTION RANGE LOW (A) : 33.7
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 2.53
REMARK 200 R MERGE (I) : 0.066
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.8
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.9
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.3
REMARK 200 R MERGE FOR SHELL (I) : 0.39
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.8
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: MRCHK
REMARK 200 STARTING MODEL: PDB ENTRY 1ACE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 Y-X,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,2/3-Z
REMARK 290 6555 -X,Y-X,1/3-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 -0.500041 -0.866033 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866018 -0.499959 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.16956
REMARK 290 SMTRY1 3 -0.499959 0.866033 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866018 -0.500041 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 96.33911
REMARK 290 SMTRY1 4 -0.500041 0.865985 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866018 0.500041 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000094 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 96.33911
REMARK 290 SMTRY1 6 -0.499959 -0.866080 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866018 0.499959 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 48.16956
REMARK 290
REMARK 290 REMARK: NULL
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER 546 CB OG
REMARK 470 GLN 547 CB CG CD OE1 NE2
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1AKN SWS P30122 1 - 18 NOT IN ATOMS LIST
REMARK 999 1AKN SWS P30122 566 - 597 NOT IN ATOMS LIST
REMARK 999
REMARK 999 RESIDUE 27 WAS DETERMINED TO BE ILE BY MASS SPECTROSCOPY.
DBREF 1AKN 1 547 SWS P30122 BAL_BOVIN 19 565
SEQADV 1AKN ILE 27 SWS P30122 VAL 45 CONFLICT
SEQRES 1 579 ALA LYS LEU GLY SER VAL TYR THR GLU GLY GLY PHE VAL
SEQRES 2 579 GLU GLY VAL ASN LYS LYS LEU SER LEU PHE GLY ASP SER
SEQRES 3 579 ILE ASP ILE PHE LYS GLY ILE PRO PHE ALA ALA ALA PRO
SEQRES 4 579 LYS ALA LEU GLU LYS PRO GLU ARG HIS PRO GLY TRP GLN
SEQRES 5 579 GLY THR LEU LYS ALA LYS SER PHE LYS LYS ARG CYS LEU
SEQRES 6 579 GLN ALA THR LEU THR GLN ASP SER THR TYR GLY ASN GLU
SEQRES 7 579 ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO GLN GLY ARG
SEQRES 8 579 LYS GLU VAL SER HIS ASP LEU PRO VAL MET ILE TRP ILE
SEQRES 9 579 TYR GLY GLY ALA PHE LEU MET GLY ALA SER GLN GLY ALA
SEQRES 10 579 ASN PHE LEU SER ASN TYR LEU TYR ASP GLY GLU GLU ILE
SEQRES 11 579 ALA THR ARG GLY ASN VAL ILE VAL VAL THR PHE ASN TYR
SEQRES 12 579 ARG VAL GLY PRO LEU GLY PHE LEU SER THR GLY ASP SER
SEQRES 13 579 ASN LEU PRO GLY ASN TYR GLY LEU TRP ASP GLN HIS MET
SEQRES 14 579 ALA ILE ALA TRP VAL LYS ARG ASN ILE GLU ALA PHE GLY
SEQRES 15 579 GLY ASP PRO ASP ASN ILE THR LEU PHE GLY GLU SER ALA
SEQRES 16 579 GLY GLY ALA SER VAL SER LEU GLN THR LEU SER PRO TYR
SEQRES 17 579 ASN LYS GLY LEU ILE LYS ARG ALA ILE SER GLN SER GLY
SEQRES 18 579 VAL GLY LEU CYS PRO TRP ALA ILE GLN GLN ASP PRO LEU
SEQRES 19 579 PHE TRP ALA LYS ARG ILE ALA GLU LYS VAL GLY CYS PRO
SEQRES 20 579 VAL ASP ASP THR SER LYS MET ALA GLY CYS LEU LYS ILE
SEQRES 21 579 THR ASP PRO ARG ALA LEU THR LEU ALA TYR LYS LEU PRO
SEQRES 22 579 LEU GLY SER THR GLU TYR PRO LYS LEU HIS TYR LEU SER
SEQRES 23 579 PHE VAL PRO VAL ILE ASP GLY ASP PHE ILE PRO ASP ASP
SEQRES 24 579 PRO VAL ASN LEU TYR ALA ASN ALA ALA ASP VAL ASP TYR
SEQRES 25 579 ILE ALA GLY THR ASN ASP MET ASP GLY HIS LEU PHE VAL
SEQRES 26 579 GLY MET ASP VAL PRO ALA ILE ASN SER ASN LYS GLN ASP
SEQRES 27 579 VAL THR GLU GLU ASP PHE TYR LYS LEU VAL SER GLY LEU
SEQRES 28 579 THR VAL THR LYS GLY LEU ARG GLY ALA ASN ALA THR TYR
SEQRES 29 579 GLU VAL TYR THR GLU PRO TRP ALA GLN ASP SER SER GLN
SEQRES 30 579 GLU THR ARG LYS LYS THR MET VAL ASP LEU GLU THR ASP
SEQRES 31 579 ILE LEU PHE LEU ILE PRO THR LYS ILE ALA VAL ALA GLN
SEQRES 32 579 HIS LYS SER HIS ALA LYS SER ALA ASN THR TYR THR TYR
SEQRES 33 579 LEU PHE SER GLN PRO SER ARG MET PRO ILE TYR PRO LYS
SEQRES 34 579 TRP MET GLY ALA ASP HIS ALA ASP ASP LEU GLN TYR VAL
SEQRES 35 579 PHE GLY LYS PRO PHE ALA THR PRO LEU GLY TYR ARG ALA
SEQRES 36 579 GLN ASP ARG THR VAL SER LYS ALA MET ILE ALA TYR TRP
SEQRES 37 579 THR ASN PHE ALA ARG THR GLY ASP PRO ASN THR GLY HIS
SEQRES 38 579 SER THR VAL PRO ALA ASN TRP ASP PRO TYR THR LEU GLU
SEQRES 39 579 ASP ASP ASN TYR LEU GLU ILE ASN LYS GLN MET ASP SER
SEQRES 40 579 ASN SER MET LYS LEU HIS LEU ARG THR ASN TYR LEU GLN
SEQRES 41 579 PHE TRP THR GLN THR TYR GLN ALA LEU PRO THR VAL THR
SEQRES 42 579 SER ALA GLY ALA SER LEU LEU PRO PRO GLU ASP ASN SER
SEQRES 43 579 GLN ALA SER PRO VAL PRO PRO ALA ASP ASN SER GLY ALA
SEQRES 44 579 PRO THR GLU PRO SER ALA GLY ASP SER GLU VAL ALA GLN
SEQRES 45 579 MET PRO VAL VAL ILE GLY PHE
HET NAG 600 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG C8 H15 N1 O6
HELIX 1 1 GLU 128 GLY 134 1 7
HELIX 2 2 PRO 147 PHE 150 1 4
HELIX 3 3 TYR 162 PHE 181 1 20
HELIX 4 4 PRO 185 ASN 187 5 3
HELIX 5 5 SER 194 LEU 205 5 12
HELIX 6 6 PRO 207 ASN 209 5 3
HELIX 7 7 PRO 233 LYS 243 1 11
HELIX 8 8 THR 251 ILE 260 1 10
HELIX 9 9 PRO 263 LEU 268 1 6
HELIX 10 10 PRO 300 ASN 302 5 3
HELIX 11 11 TYR 304 ALA 307 5 4
HELIX 12 12 HIS 322 ASP 328 1 7
HELIX 13 13 GLU 341 TYR 367 1 27
HELIX 14 14 GLN 377 LEU 392 1 16
HELIX 15 15 LEU 394 SER 406 1 13
HELIX 16 16 LEU 439 VAL 442 1 4
HELIX 17 17 LYS 445 ALA 448 1 4
HELIX 18 18 ALA 455 THR 474 1 20
HELIX 19 19 SER 507 SER 509 5 3
HELIX 20 20 THR 516 THR 523 1 8
HELIX 21 21 THR 525 ALA 528 1 4
SHEET 1 A 3 SER 5 THR 8 0
SHEET 2 A 3 GLY 11 GLU 14 -1 N VAL 13 O VAL 6
SHEET 3 A 3 THR 54 LYS 56 1 N LEU 55 O PHE 12
SHEET 1 B11 VAL 16 LYS 19 0
SHEET 2 B11 SER 26 PRO 34 -1 N ILE 29 O VAL 16
SHEET 3 B11 TYR 82 GLN 89 -1 N GLN 89 O SER 26
SHEET 4 B11 ILE 137 PHE 141 -1 N THR 140 O ASN 84
SHEET 5 B11 VAL 100 ILE 104 1 N MET 101 O ILE 137
SHEET 6 B11 ILE 188 GLU 193 1 N THR 189 O VAL 100
SHEET 7 B11 ARG 215 GLN 219 1 N ARG 215 O LEU 190
SHEET 8 B11 ASP 311 ASN 317 1 N ASP 311 O ALA 216
SHEET 9 B11 THR 413 PHE 418 1 N TYR 414 O TYR 312
SHEET 10 B11 ASN 497 ILE 501 1 N LEU 499 O LEU 417
SHEET 11 B11 MET 510 LEU 512 -1 N LYS 511 O TYR 498
LINK C1 NAG 600 ND2 ASN 361
CRYST1 94.390 94.390 144.510 90.00 90.00 120.00 P 31 2 1 6
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 0.010594 0.006117 0.000000 0.00000
SCALE2 0.000000 0.012233 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006920 0.00000 |