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HEADER HYDROLASE 30-JUL-97 1AQL
TITLE CRYSTAL STRUCTURE OF BOVINE BILE-SALT ACTIVATED LIPASE
TITLE 2 COMPLEXED WITH TAUROCHOLATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BILE-SALT ACTIVATED LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CARBOXYL ESTER LIPASE, STEROL ESTERASE,
COMPND 5 CHOLESTEROL ESTERASE, PANCREATIC LYSOPHOSPHOLIPASE;
COMPND 6 EC: 3.1.1.13
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
EXPDTA X-RAY DIFFRACTION
AUTHOR X.WANG,X.ZHANG
REVDAT 1 05-AUG-98 1AQL 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)) : 1.5
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 79.5
REMARK 3 NUMBER OF REFLECTIONS : 31019
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 : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.0
REMARK 3 FREE R VALUE TEST SET COUNT : 3117
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 : 8330
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 168
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.5
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.7
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.6379
REMARK 3 B22 (A**2) : -9.2577
REMARK 3 B33 (A**2) : 4.6198
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 0.0000
REMARK 3 B23 (A**2) : 0.0000
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.5
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.92
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.326
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 : RESTRAINTS
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 PARAMETER FILE 3 : TCH.PAR
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NAG.TOP
REMARK 3 TOPOLOGY FILE 3 : TCH.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: AT FINAL STEP, A RESTRAINED
REMARK 3 TEMPERATURE FACTOR REFINEMENT WAS CARRIED OUT BY TNT.
REMARK 4
REMARK 4 1AQL COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 6
REMARK 6 NO COORDINATES ARE PRESENT FOR RESIDUES FOR THE C-TERMIANL
REMARK 6 REGION 533 - 579 BECAUSE OF LACK OF INTERTERPRATABLE
REMARK 6 ELECTRON DENSITY.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAR-1997
REMARK 200 TEMPERATURE (KELVIN) : 293
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 : SIEMENS ROTATING ANODE
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : MULTIWIRE
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SADIE
REMARK 200 DATA SCALING SOFTWARE : SAINT
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33877
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.8
REMARK 200 RESOLUTION RANGE LOW (A) : 17.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.7
REMARK 200 DATA REDUNDANCY : 1.8
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.117
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1
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 (%) : 48.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.3
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.206
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.4
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 1AKN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.5
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 65.11265
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.04538
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 65.11265
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.04538
REMARK 290 SMTRY3 4 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 .. 532 C 1 .. 532 0.324
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1AQL A SWS P30122 1 - 18 NOT IN ATOMS LIST
REMARK 999 1AQL A SWS P30122 551 - 597 NOT IN ATOMS LIST
REMARK 999 1AQL B SWS P30122 1 - 18 NOT IN ATOMS LIST
REMARK 999 1AQL B SWS P30122 551 - 597 NOT IN ATOMS LIST
REMARK 999
REMARK 999 RESIDUE 27 WAS DETERMINED TO BE ILE BY MASS SPECTROSCOPY.
DBREF 1AQL A 1 532 SWS P30122 BAL_BOVIN 19 550
DBREF 1AQL B 1 532 SWS P30122 BAL_BOVIN 19 550
SEQADV 1AQL ILE A 27 SWS P30122 VAL 45 CONFLICT
SEQADV 1AQL ILE B 27 SWS P30122 VAL 45 CONFLICT
SEQRES 1 A 532 ALA LYS LEU GLY SER VAL TYR THR GLU GLY GLY PHE VAL
SEQRES 2 A 532 GLU GLY VAL ASN LYS LYS LEU SER LEU PHE GLY ASP SER
SEQRES 3 A 532 ILE ASP ILE PHE LYS GLY ILE PRO PHE ALA ALA ALA PRO
SEQRES 4 A 532 LYS ALA LEU GLU LYS PRO GLU ARG HIS PRO GLY TRP GLN
SEQRES 5 A 532 GLY THR LEU LYS ALA LYS SER PHE LYS LYS ARG CYS LEU
SEQRES 6 A 532 GLN ALA THR LEU THR GLN ASP SER THR TYR GLY ASN GLU
SEQRES 7 A 532 ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO GLN GLY ARG
SEQRES 8 A 532 LYS GLU VAL SER HIS ASP LEU PRO VAL MET ILE TRP ILE
SEQRES 9 A 532 TYR GLY GLY ALA PHE LEU MET GLY ALA SER GLN GLY ALA
SEQRES 10 A 532 ASN PHE LEU SER ASN TYR LEU TYR ASP GLY GLU GLU ILE
SEQRES 11 A 532 ALA THR ARG GLY ASN VAL ILE VAL VAL THR PHE ASN TYR
SEQRES 12 A 532 ARG VAL GLY PRO LEU GLY PHE LEU SER THR GLY ASP SER
SEQRES 13 A 532 ASN LEU PRO GLY ASN TYR GLY LEU TRP ASP GLN HIS MET
SEQRES 14 A 532 ALA ILE ALA TRP VAL LYS ARG ASN ILE GLU ALA PHE GLY
SEQRES 15 A 532 GLY ASP PRO ASP ASN ILE THR LEU PHE GLY GLU SER ALA
SEQRES 16 A 532 GLY GLY ALA SER VAL SER LEU GLN THR LEU SER PRO TYR
SEQRES 17 A 532 ASN LYS GLY LEU ILE LYS ARG ALA ILE SER GLN SER GLY
SEQRES 18 A 532 VAL GLY LEU CYS PRO TRP ALA ILE GLN GLN ASP PRO LEU
SEQRES 19 A 532 PHE TRP ALA LYS ARG ILE ALA GLU LYS VAL GLY CYS PRO
SEQRES 20 A 532 VAL ASP ASP THR SER LYS MET ALA GLY CYS LEU LYS ILE
SEQRES 21 A 532 THR ASP PRO ARG ALA LEU THR LEU ALA TYR LYS LEU PRO
SEQRES 22 A 532 LEU GLY SER THR GLU TYR PRO LYS LEU HIS TYR LEU SER
SEQRES 23 A 532 PHE VAL PRO VAL ILE ASP GLY ASP PHE ILE PRO ASP ASP
SEQRES 24 A 532 PRO VAL ASN LEU TYR ALA ASN ALA ALA ASP VAL ASP TYR
SEQRES 25 A 532 ILE ALA GLY THR ASN ASP MET ASP GLY HIS LEU PHE VAL
SEQRES 26 A 532 GLY MET ASP VAL PRO ALA ILE ASN SER ASN LYS GLN ASP
SEQRES 27 A 532 VAL THR GLU GLU ASP PHE TYR LYS LEU VAL SER GLY LEU
SEQRES 28 A 532 THR VAL THR LYS GLY LEU ARG GLY ALA ASN ALA THR TYR
SEQRES 29 A 532 GLU VAL TYR THR GLU PRO TRP ALA GLN ASP SER SER GLN
SEQRES 30 A 532 GLU THR ARG LYS LYS THR MET VAL ASP LEU GLU THR ASP
SEQRES 31 A 532 ILE LEU PHE LEU ILE PRO THR LYS ILE ALA VAL ALA GLN
SEQRES 32 A 532 HIS LYS SER HIS ALA LYS SER ALA ASN THR TYR THR TYR
SEQRES 33 A 532 LEU PHE SER GLN PRO SER ARG MET PRO ILE TYR PRO LYS
SEQRES 34 A 532 TRP MET GLY ALA ASP HIS ALA ASP ASP LEU GLN TYR VAL
SEQRES 35 A 532 PHE GLY LYS PRO PHE ALA THR PRO LEU GLY TYR ARG ALA
SEQRES 36 A 532 GLN ASP ARG THR VAL SER LYS ALA MET ILE ALA TYR TRP
SEQRES 37 A 532 THR ASN PHE ALA ARG THR GLY ASP PRO ASN THR GLY HIS
SEQRES 38 A 532 SER THR VAL PRO ALA ASN TRP ASP PRO TYR THR LEU GLU
SEQRES 39 A 532 ASP ASP ASN TYR LEU GLU ILE ASN LYS GLN MET ASP SER
SEQRES 40 A 532 ASN SER MET LYS LEU HIS LEU ARG THR ASN TYR LEU GLN
SEQRES 41 A 532 PHE TRP THR GLN THR TYR GLN ALA LEU PRO THR VAL
SEQRES 1 B 532 ALA LYS LEU GLY SER VAL TYR THR GLU GLY GLY PHE VAL
SEQRES 2 B 532 GLU GLY VAL ASN LYS LYS LEU SER LEU PHE GLY ASP SER
SEQRES 3 B 532 ILE ASP ILE PHE LYS GLY ILE PRO PHE ALA ALA ALA PRO
SEQRES 4 B 532 LYS ALA LEU GLU LYS PRO GLU ARG HIS PRO GLY TRP GLN
SEQRES 5 B 532 GLY THR LEU LYS ALA LYS SER PHE LYS LYS ARG CYS LEU
SEQRES 6 B 532 GLN ALA THR LEU THR GLN ASP SER THR TYR GLY ASN GLU
SEQRES 7 B 532 ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO GLN GLY ARG
SEQRES 8 B 532 LYS GLU VAL SER HIS ASP LEU PRO VAL MET ILE TRP ILE
SEQRES 9 B 532 TYR GLY GLY ALA PHE LEU MET GLY ALA SER GLN GLY ALA
SEQRES 10 B 532 ASN PHE LEU SER ASN TYR LEU TYR ASP GLY GLU GLU ILE
SEQRES 11 B 532 ALA THR ARG GLY ASN VAL ILE VAL VAL THR PHE ASN TYR
SEQRES 12 B 532 ARG VAL GLY PRO LEU GLY PHE LEU SER THR GLY ASP SER
SEQRES 13 B 532 ASN LEU PRO GLY ASN TYR GLY LEU TRP ASP GLN HIS MET
SEQRES 14 B 532 ALA ILE ALA TRP VAL LYS ARG ASN ILE GLU ALA PHE GLY
SEQRES 15 B 532 GLY ASP PRO ASP ASN ILE THR LEU PHE GLY GLU SER ALA
SEQRES 16 B 532 GLY GLY ALA SER VAL SER LEU GLN THR LEU SER PRO TYR
SEQRES 17 B 532 ASN LYS GLY LEU ILE LYS ARG ALA ILE SER GLN SER GLY
SEQRES 18 B 532 VAL GLY LEU CYS PRO TRP ALA ILE GLN GLN ASP PRO LEU
SEQRES 19 B 532 PHE TRP ALA LYS ARG ILE ALA GLU LYS VAL GLY CYS PRO
SEQRES 20 B 532 VAL ASP ASP THR SER LYS MET ALA GLY CYS LEU LYS ILE
SEQRES 21 B 532 THR ASP PRO ARG ALA LEU THR LEU ALA TYR LYS LEU PRO
SEQRES 22 B 532 LEU GLY SER THR GLU TYR PRO LYS LEU HIS TYR LEU SER
SEQRES 23 B 532 PHE VAL PRO VAL ILE ASP GLY ASP PHE ILE PRO ASP ASP
SEQRES 24 B 532 PRO VAL ASN LEU TYR ALA ASN ALA ALA ASP VAL ASP TYR
SEQRES 25 B 532 ILE ALA GLY THR ASN ASP MET ASP GLY HIS LEU PHE VAL
SEQRES 26 B 532 GLY MET ASP VAL PRO ALA ILE ASN SER ASN LYS GLN ASP
SEQRES 27 B 532 VAL THR GLU GLU ASP PHE TYR LYS LEU VAL SER GLY LEU
SEQRES 28 B 532 THR VAL THR LYS GLY LEU ARG GLY ALA ASN ALA THR TYR
SEQRES 29 B 532 GLU VAL TYR THR GLU PRO TRP ALA GLN ASP SER SER GLN
SEQRES 30 B 532 GLU THR ARG LYS LYS THR MET VAL ASP LEU GLU THR ASP
SEQRES 31 B 532 ILE LEU PHE LEU ILE PRO THR LYS ILE ALA VAL ALA GLN
SEQRES 32 B 532 HIS LYS SER HIS ALA LYS SER ALA ASN THR TYR THR TYR
SEQRES 33 B 532 LEU PHE SER GLN PRO SER ARG MET PRO ILE TYR PRO LYS
SEQRES 34 B 532 TRP MET GLY ALA ASP HIS ALA ASP ASP LEU GLN TYR VAL
SEQRES 35 B 532 PHE GLY LYS PRO PHE ALA THR PRO LEU GLY TYR ARG ALA
SEQRES 36 B 532 GLN ASP ARG THR VAL SER LYS ALA MET ILE ALA TYR TRP
SEQRES 37 B 532 THR ASN PHE ALA ARG THR GLY ASP PRO ASN THR GLY HIS
SEQRES 38 B 532 SER THR VAL PRO ALA ASN TRP ASP PRO TYR THR LEU GLU
SEQRES 39 B 532 ASP ASP ASN TYR LEU GLU ILE ASN LYS GLN MET ASP SER
SEQRES 40 B 532 ASN SER MET LYS LEU HIS LEU ARG THR ASN TYR LEU GLN
SEQRES 41 B 532 PHE TRP THR GLN THR TYR GLN ALA LEU PRO THR VAL
MODRES 1AQL ASN A 361 ASN N-GLYCOSYLATION SITE
MODRES 1AQL ASN B 361 ASN N-GLYCOSYLATION SITE
HET NAG A 600 14
HET TCH A 601 35
HET TCH A 602 35
HET NAG B 600 14
HET TCH B 601 35
HET TCH B 602 35
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM TCH TAUROCHOLIC ACID
FORMUL 3 NAG 2(C8 H15 N1 O6)
FORMUL 4 TCH 4(C26 H45 N1 O7 S1)
HELIX 1 1 GLU A 129 GLY A 134 1 6
HELIX 2 2 GLY A 146 PHE A 150 1 5
HELIX 3 3 TYR A 162 ARG A 176 1 15
HELIX 4 4 GLU A 179 PHE A 181 5 3
HELIX 5 5 SER A 194 LEU A 205 1 12
HELIX 6 6 PRO A 207 ASN A 209 5 3
HELIX 7 7 PRO A 226 ALA A 228 5 3
HELIX 8 8 PRO A 233 LYS A 243 1 11
HELIX 9 9 THR A 251 ILE A 260 1 10
HELIX 10 10 PRO A 263 LEU A 268 1 6
HELIX 11 11 LYS A 281 HIS A 283 5 3
HELIX 12 12 PRO A 300 LEU A 303 1 4
HELIX 13 13 ASN A 306 ASP A 309 5 4
HELIX 14 14 ASP A 320 ASP A 328 5 9
HELIX 15 15 GLU A 341 TYR A 367 1 27
HELIX 16 16 ASP A 374 LEU A 392 5 19
HELIX 17 17 LEU A 394 HIS A 407 1 14
HELIX 18 18 ASP A 438 VAL A 442 1 5
HELIX 19 19 LYS A 445 ALA A 448 1 4
HELIX 20 20 ALA A 455 THR A 474 1 20
HELIX 21 21 THR A 516 THR A 523 1 8
HELIX 22 22 THR A 525 ALA A 528 1 4
HELIX 23 23 GLU B 128 GLY B 134 1 7
HELIX 24 24 PRO B 147 PHE B 150 1 4
HELIX 25 25 TYR B 162 ASN B 177 1 16
HELIX 26 26 GLU B 179 PHE B 181 5 3
HELIX 27 27 SER B 194 LEU B 205 5 12
HELIX 28 28 PRO B 207 ASN B 209 5 3
HELIX 29 29 PRO B 233 VAL B 244 1 12
HELIX 30 30 THR B 251 ILE B 260 1 10
HELIX 31 31 PRO B 263 THR B 267 1 5
HELIX 32 32 LYS B 281 TYR B 284 5 4
HELIX 33 33 PRO B 300 ALA B 305 1 6
HELIX 34 34 ALA B 307 ASP B 309 5 3
HELIX 35 35 ASP B 320 ASP B 328 5 9
HELIX 36 36 GLU B 341 LEU B 351 1 11
HELIX 37 37 VAL B 353 TYR B 367 5 15
HELIX 38 38 ASP B 374 SER B 376 5 3
HELIX 39 39 GLU B 378 LEU B 392 1 15
HELIX 40 40 LEU B 394 HIS B 407 1 14
HELIX 41 41 ASP B 438 VAL B 442 1 5
HELIX 42 42 LYS B 445 ALA B 448 1 4
HELIX 43 43 PRO B 450 GLY B 452 5 3
HELIX 44 44 ALA B 455 THR B 474 1 20
HELIX 45 45 SER B 507 SER B 509 5 3
HELIX 46 46 THR B 516 THR B 523 1 8
HELIX 47 47 THR B 525 ALA B 528 1 4
SHEET 1 A 3 SER A 5 TYR A 7 0
SHEET 2 A 3 PHE A 12 GLU A 14 -1 N VAL A 13 O VAL A 6
SHEET 3 A 3 THR A 54 LYS A 56 1 N LEU A 55 O PHE A 12
SHEET 1 B11 VAL A 16 LYS A 19 0
SHEET 2 B11 SER A 26 PHE A 30 -1 N ILE A 29 O VAL A 16
SHEET 3 B11 LEU A 83 GLN A 89 -1 N GLN A 89 O SER A 26
SHEET 4 B11 VAL A 136 PHE A 141 -1 N THR A 140 O ASN A 84
SHEET 5 B11 PRO A 99 TRP A 103 1 N PRO A 99 O ILE A 137
SHEET 6 B11 ILE A 188 GLU A 193 1 N THR A 189 O VAL A 100
SHEET 7 B11 ARG A 215 GLN A 219 1 N ARG A 215 O LEU A 190
SHEET 8 B11 ASP A 311 ASN A 317 1 N ASP A 311 O ALA A 216
SHEET 9 B11 THR A 413 PHE A 418 1 N TYR A 414 O TYR A 312
SHEET 10 B11 ASN A 497 ILE A 501 1 N LEU A 499 O LEU A 417
SHEET 11 B11 MET A 510 LEU A 512 -1 N LYS A 511 O TYR A 498
SHEET 1 C 3 SER B 5 TYR B 7 0
SHEET 2 C 3 PHE B 12 GLU B 14 -1 N VAL B 13 O VAL B 6
SHEET 3 C 3 THR B 54 LYS B 56 1 N LEU B 55 O PHE B 12
SHEET 1 D11 VAL B 16 LYS B 19 0
SHEET 2 D11 SER B 26 PRO B 34 -1 N ILE B 29 O VAL B 16
SHEET 3 D11 TYR B 82 GLN B 89 -1 N GLN B 89 O SER B 26
SHEET 4 D11 ILE B 137 PHE B 141 -1 N THR B 140 O ASN B 84
SHEET 5 D11 VAL B 100 ILE B 104 1 N MET B 101 O ILE B 137
SHEET 6 D11 ILE B 188 GLU B 193 1 N THR B 189 O VAL B 100
SHEET 7 D11 ARG B 215 GLN B 219 1 N ARG B 215 O LEU B 190
SHEET 8 D11 ASP B 311 ASN B 317 1 N ASP B 311 O ALA B 216
SHEET 9 D11 THR B 413 PHE B 418 1 N TYR B 414 O TYR B 312
SHEET 10 D11 ASN B 497 ILE B 501 1 N LEU B 499 O LEU B 417
SHEET 11 D11 MET B 510 LEU B 512 -1 N LYS B 511 O TYR B 498
SSBOND 1 CYS A 64 CYS A 80
SSBOND 2 CYS A 246 CYS A 257
SSBOND 3 CYS B 64 CYS B 80
SSBOND 4 CYS B 246 CYS B 257
LINK C1 NAG A 600 ND2 ASN A 361
LINK C1 NAG B 600 ND2 ASN B 361
CRYST1 130.230 104.090 120.180 90.00 90.00 90.00 P 21 21 2 8
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 0.007679 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009607 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008321 0.00000
MTRIX1 1 0.352585 0.466940 0.810957 -24.62283 1
MTRIX2 1 0.334720 -0.872206 0.356677 73.21277 1
MTRIX3 1 0.873868 0.145684 -0.463821 4.79749 1 |