1EXW-pdb | HEADER HYDROLASE 04-MAY-00 1EXW
TITLE CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1
TITLE 2 COMPLEXED WITH HEXADECYLSULFONYL FLUORIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PALMITOYL PROTEIN THIOESTERASE 1;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.2.22;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 EXPRESSION_SYSTEM: BACULOVIRUS;
SOURCE 5 EXPRESSION_SYSTEM_CELL: SF21 CELLS
KEYWDS ALPHA/BETA HYDROLASE, PALMITOYL PROTEIN THIOESTERASE, PMSF
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.BELLIZZI III,J.CLARDY
REVDAT 1 02-AUG-00 1EXW 0
JRNL AUTH A.K.DAS,J.J.BELLIZZI III,S.TANDEL,E.BIEHL,J.CLARDY,
JRNL AUTH 2 S.L.HOFMANN
JRNL TITL STRUCTURAL BASIS FOR THE INSENSITIVITY OF A SERINE
JRNL TITL 2 ENZYME (PALMITOYL-PROTEIN THIOESTERASE) TO
JRNL TITL 3 PHENYLMETHANESULFONYL FLUORIDE
JRNL REF J.BIOL.CHEM. V. 275 23847 2000
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : GENERATED PARAMETER/TOPOLOGY FILES
REMARK 3 FOR HDSF WITH XPLO2D
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 12638
REMARK 3
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 630
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.011
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1961
REMARK 3 BIN R VALUE (WORKING SET) : 0.3250
REMARK 3 BIN FREE R VALUE : 0.3790
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 100
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.038
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2210
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 75
REMARK 3 SOLVENT ATOMS : 40
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.13000
REMARK 3 B22 (A**2) : 7.13000
REMARK 3 B33 (A**2) : -14.27000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.340
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.48
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.49
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.70
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 51.33
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 : PARAM
REMARK 3 PARAMETER FILE 2 : PARAM
REMARK 3 PARAMETER FILE 3 : PARAM
REMARK 3 PARAMETER FILE 4 : HDS.PAR
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 4 : HDS.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: USED SIMULATED ANNEALING,
REMARK 3 ENERGY MINIMIZATION, INDIVIDUAL B-FACTOR REFINEMENT. USED
REMARK 3 ISOTROPIC B-FACTOR CORRECTION AND BULK SOLVENT CORRECTION
REMARK 4
REMARK 4 1EXW COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-2000.
REMARK 100 THE RCSB ID CODE IS RCSB011005.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-1999
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9100
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM-4 CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, TRUNCATE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79642
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 36.270
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.21600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 55% PPG 400, 0.1 M BIS TRIS
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
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,1/4+Z
REMARK 290 4555 Y,-X,3/4+Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,1/2-Z
REMARK 290 7555 Y,X,3/4-Z
REMARK 290 8555 -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 64.01500
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 32.00750
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 96.02250
REMARK 290 SMTRY1 5 -1.000000 0.000000 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 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 64.01500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 96.02250
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 32.00750
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 OE2 GLU A 294 OH TYR A 298 2.13
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. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED 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 NH1 ARG A 191 OD2 ASP A 28 7545 2.15
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 286 CG GLU A 286 CB -0.119
REMARK 500 GLU A 286 CD GLU A 286 CG 0.099
REMARK 500 HIS A 289 CG HIS A 289 CB 0.059
REMARK 500 GLN A 291 CD GLN A 291 CG -0.067
REMARK 500 GLN A 291 OE1 GLN A 291 CD 0.080
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 HIS A 66 CB - CA - C ANGL. DEV. =-11.9 DEGREES
REMARK 500 PHE A 85 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 TRP A 186 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 GLU A 286 OE1 - CD - OE2 ANGL. DEV. = -8.8 DEGREES
REMARK 500 GLU A 286 CG - CD - OE2 ANGL. DEV. = 11.1 DEGREES
REMARK 500 HIS A 289 CB - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 BEFORE REACTION WITH THE PROTEIN, THE LIGAND
REMARK 600 HSF WAS 1-HEXADECYLSULFONYL FLUORIDE. THE FLUORINE
REMARK 600 IS LOST DURING REACTION. THE S1 OF HDR 430 IS
REMARK 600 COVALENTLY BOUND TO THE OG OF SER 115.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EI9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1
REMARK 900 RELATED ID: 1EH5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1
REMARK 900 COMPLEXED WITH PALMITATE
DBREF 1EXW A 28 306 SWS P45478 PPT_BOVIN 28 306
SEQRES 1 A 279 ASP PRO PRO ALA PRO LEU PRO LEU VAL ILE TRP HIS GLY
SEQRES 2 A 279 MET GLY ASP SER CYS CYS ASN PRO LEU SER MET GLY ALA
SEQRES 3 A 279 ILE LYS LYS MET VAL GLU LYS LYS ILE PRO GLY ILE HIS
SEQRES 4 A 279 VAL LEU SER LEU GLU ILE GLY LYS THR LEU ARG GLU ASP
SEQRES 5 A 279 VAL GLU ASN SER PHE PHE LEU ASN VAL ASN SER GLN VAL
SEQRES 6 A 279 THR THR VAL CYS GLN ILE LEU ALA LYS ASP PRO LYS LEU
SEQRES 7 A 279 GLN GLN GLY TYR ASN ALA MET GLY PHE SER GLN GLY GLY
SEQRES 8 A 279 GLN PHE LEU ARG ALA VAL ALA GLN ARG CYS PRO SER PRO
SEQRES 9 A 279 PRO MET VAL ASN LEU ILE SER VAL GLY GLY GLN HIS GLN
SEQRES 10 A 279 GLY VAL PHE GLY LEU PRO ARG CYS PRO GLY GLU SER SER
SEQRES 11 A 279 HIS ILE CYS ASP PHE ILE ARG LYS THR LEU ASN ALA GLY
SEQRES 12 A 279 ALA TYR ASN LYS ALA ILE GLN GLU ARG LEU VAL GLN ALA
SEQRES 13 A 279 GLU TYR TRP HIS ASP PRO ILE ARG GLU ASP ILE TYR ARG
SEQRES 14 A 279 ASN HIS SER ILE PHE LEU ALA ASP ILE ASN GLN GLU ARG
SEQRES 15 A 279 GLY VAL ASN GLU SER TYR LYS LYS ASN LEU MET ALA LEU
SEQRES 16 A 279 LYS LYS PHE VAL MET VAL LYS PHE LEU ASN ASP THR ILE
SEQRES 17 A 279 VAL ASP PRO VAL ASP SER GLU TRP PHE GLY PHE TYR ARG
SEQRES 18 A 279 SER GLY GLN ALA LYS GLU THR ILE PRO LEU GLN GLU SER
SEQRES 19 A 279 THR LEU TYR THR GLN ASP ARG LEU GLY LEU LYS ALA MET
SEQRES 20 A 279 ASP LYS ALA GLY GLN LEU VAL PHE LEU ALA LEU GLU GLY
SEQRES 21 A 279 ASP HIS LEU GLN LEU SER GLU GLU TRP PHE TYR ALA HIS
SEQRES 22 A 279 ILE ILE PRO PHE LEU GLU
MODRES 1EXW ASN A 197 ASN GLYCOSYLATION SITE
MODRES 1EXW ASN A 212 ASN GLYCOSYLATION SITE
MODRES 1EXW ASN A 232 ASN GLYCOSYLATION SITE
MODRES 1EXW SER A 115 SER MODIFIED BY HSF
HET NAG A 400 14
HET NAG A 410 14
HET NAG B 420 14
HET NAG B 421 14
HET HSF A 430 19
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM HSF 1-HEXADECYLSULFONYL FLUORIDE
HETSYN NAG NAG
FORMUL 2 NAG 4(C8 H15 N1 O6)
FORMUL 5 HSF C16 H33 O2 S1 F1
FORMUL 6 HOH *40(H2 O1)
HELIX 1 1 SER A 50 ILE A 62 1 13
HELIX 2 2 THR A 75 LEU A 86 1 12
HELIX 3 3 ASN A 87 LYS A 101 1 15
HELIX 4 4 ASP A 102 GLN A 106 5 5
HELIX 5 5 GLN A 116 CYS A 128 1 13
HELIX 6 6 SER A 157 TYR A 172 1 16
HELIX 7 7 ALA A 175 LEU A 180 1 6
HELIX 8 8 VAL A 181 TYR A 185 5 5
HELIX 9 9 ARG A 191 SER A 199 1 9
HELIX 10 10 PHE A 201 ASN A 206 1 6
HELIX 11 11 ASN A 212 ALA A 221 1 10
HELIX 12 12 PRO A 238 PHE A 244 5 7
HELIX 13 13 PRO A 257 GLU A 260 5 4
HELIX 14 14 SER A 261 GLN A 266 1 6
HELIX 15 15 GLY A 270 ALA A 277 1 8
HELIX 16 16 SER A 293 ILE A 301 1 9
HELIX 17 17 ILE A 302 GLU A 306 5 5
SHEET 1 A 6 VAL A 67 SER A 69 0
SHEET 2 A 6 LEU A 35 TRP A 38 1 O LEU A 35 N LEU A 68
SHEET 3 A 6 TYR A 109 PHE A 114 1 O ASN A 110 N VAL A 36
SHEET 4 A 6 MET A 133 VAL A 139 1 N VAL A 134 O TYR A 109
SHEET 5 A 6 LYS A 224 PHE A 230 1 O LYS A 224 N LEU A 136
SHEET 6 A 6 LEU A 280 LEU A 285 1 O VAL A 281 N MET A 227
SHEET 1 B 2 PHE A 246 TYR A 247 0
SHEET 2 B 2 THR A 255 ILE A 256 -1 N ILE A 256 O PHE A 246
SSBOND 1 CYS A 45 CYS A 46
SSBOND 2 CYS A 96 CYS A 128
SSBOND 3 CYS A 152 CYS A 160
LINK ND2 ASN A 197 C1 NAG A 400
LINK ND2 ASN A 212 C1 NAG A 410
LINK ND2 ASN A 232 C1 NAG B 420
LINK O4 NAG B 420 C1 NAG B 421
LINK S1 HSF A 430 OG SER A 115
CISPEP 1 SER A 130 PRO A 131 0 0.09
CISPEP 2 ASP A 237 PRO A 238 0 1.70
CRYST1 69.060 69.060 128.030 90.00 90.00 90.00 P 41 2 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 0.014480 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014480 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007811 0.00000
END
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