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HEADER HYDROLASE 18-FEB-00 1EH5
TITLE CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1
TITLE 2 COMPLEXED WITH PALMITATE
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_COMMON: BACULOVIRUS;
SOURCE 5 EXPRESSION_SYSTEM_CELL: SF21 CELLS;
SOURCE 6 OTHER_DETAILS: 10 L BIOREACTOR
KEYWDS ALPHA/BETA HYDROLASE, GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.BELLIZZI III,J.WIDOM,C.KEMP,J.Y.LU,A.K.DAS,S.L.HOFMANN,
AUTHOR 2 J.CLARDY
REVDAT 1 26-APR-00 1EH5 0
JRNL AUTH J.J.BELLIZZI III,J.WIDOM,C.KEMP,J.Y.LU,A.K.DAS,
JRNL AUTH 2 S.L.HOFMANN,J.CLARDY
JRNL TITL THE CRYSTAL STRUCTURE OF PALMITOYL PROTEIN
JRNL TITL 2 THIOESTERASE 1 AND THE MOLECULAR BASIS OF
JRNL TITL 3 INFANTILE NEURONAL CEROID LIPOFUSCINOSIS
JRNL REF PROC.NAT.ACAD.SCI.USA V. 97 4573 2000
JRNL REFN ASTM PNASA6 US ISSN 0027-8424
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.VESA,E.HELLSTEN,L.A.VERKRUYSE,L.A.CAMP,J.RAPOLA,
REMARK 1 AUTH 2 P.SANTAVUORI,S.L.HOFMANN,L.PELTONEN
REMARK 1 TITL MUTATIONS IN THE PALMITOYL PROTEIN THIOESTERASE
REMARK 1 TITL 2 GENE CAUSING INFANTILE NEURONAL CEROID
REMARK 1 TITL 3 LIPOFUSCINOSIS
REMARK 1 REF NATURE V. 376 584 1995
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.A.CAMP,S.L.HOFMANN
REMARK 1 TITL PURIFICATION AND PROPERTIES OF A PALMITOYL PROTEIN
REMARK 1 TITL 2 THIOESTERASE THAT CLEAVES PALMITATE FROM H-RAS
REMARK 1 REF J.BIOL.CHEM. V. 268 22566 1993
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.50 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 PALMITATE WITH XPLO2D
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 1390208.41000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 10620
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) : 0.226
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 512
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.012
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1628
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE : 0.3740
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 92
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.039
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 : 73
REMARK 3 SOLVENT ATOMS : 36
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.330
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) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.39
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.83
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) : 2.09 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.36 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.80 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.04 ; 2.500
REMARK 3
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 49.51
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : CARBOHYDRATE.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 1EH5 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 6
REMARK 6 ASN197, ASN212 AND ASN232 ARE GLYCOSYLATED. THE OG OF
REMARK 6 SER115 IS COVALENTLY MODIFIED BY PALMITATE.
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-FEB-2000.
REMARK 100 THE RCSB ID CODE IS RCSB010565.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAR-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 : APS
REMARK 200 BEAMLINE : 14BMD
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0088
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM-4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, TRUNCATE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46474
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 21.064
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.14800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.36200
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: DIFFERENCE FOURIER
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1EI9 (UNCOMPLEXED PPT1)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.8
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 55% POLYPROPYLENE GLYCOL 400,
REMARK 280 100 MM BIS-TRIS PH 6.5
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 64.46000
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 32.23000
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 96.69000
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 64.46000
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 96.69000
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 32.23000
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: 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 MET A 41 CE MET A 41 SD -0.082
REMARK 500 MET A 51 CE MET A 51 SD 0.108
REMARK 500 MET A 274 CE MET A 274 SD -0.062
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 CYS A 46 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 SER A 50 C - N - CA ANGL. DEV. = -9.0 DEGREES
REMARK 500 PHE A 85 N - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 MET A 133 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 TRP A 186 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 HIS A 198 N - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 LEU A 292 CA - CB - CG ANGL. DEV. = 9.0 DEGREES
REMARK 500 HIS A 300 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EI9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1
DBREF 1EH5 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 1EH5 ASN A 197 ASN GLYCOSYLATION SITE
MODRES 1EH5 ASN A 232 ASN GLYCOSYLATION SITE
MODRES 1EH5 ASN A 212 ASN GLYCOSYLATION SITE
HET NAG A 400 14
HET NAG A 410 14
HET NAG B 420 14
HET NAG B 421 14
HET PLM A 430 17
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM PLM PALMITIC ACID
HETSYN NAG NAG
FORMUL 2 NAG 4(C8 H15 N1 O6)
FORMUL 5 PLM C16 H32 O2
FORMUL 6 HOH *36(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 THR A 166 1 10
HELIX 7 7 ASN A 173 GLU A 178 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 301 GLU A 306 1 6
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 O4 NAG B 420 C1 NAG B 421
LINK ND2 ASN A 197 C1 NAG A 400
LINK ND2 ASN A 232 C1 NAG B 420
LINK C1 NAG A 410 ND2 ASN A 212
LINK C1 PLM A 430 OG SER A 115
CISPEP 1 SER A 130 PRO A 131 0 -0.39
CISPEP 2 ASP A 237 PRO A 238 0 0.32
CRYST1 67.520 67.520 128.920 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 0.014810 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014810 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007757 0.00000
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