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HEADER SERINE HYDROLASE 01-SEP-98 1BS9
TITLE ACETYLXYLAN ESTERASE FROM P. PURPUROGENUM REFINED AT
TITLE 2 1.10 ANGSTROMS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL XYLAN ESTERASE;
COMPND 3 CHAIN: NULL;
COMPND 4 EC: 3.1.1.6
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PENICILLIUM PURPUROGENUM
KEYWDS SERINE HYDROLASE, ESTERASE, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.GHOSH,M.ERMAN,M.W.SAWICKI,P.LALA,D.R.WEEKS,N.LI,
AUTHOR 2 W.PANGBORN,D.J.THIEL,H.JORNVALL,J.EYZAGUIRRE
REVDAT 1 18-MAY-99 1BS9 0
JRNL AUTH D.GHOSH,M.ERMAN,M.SAWICKI,P.LALA,D.R.WEEKS,N.LI,
JRNL AUTH 2 W.PANGBORN,D.J.THIEL,H.JORNVALL,R.GUTIERREZ,
JRNL AUTH 3 J.EYZAGUIRRE
JRNL TITL DETERMINATION OF A PROTEIN STRUCTURE BY IODINATION:
JRNL TITL 2 THE STRUCTURE OF IODINATED ACETYLXYLAN ESTERASE
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 55 779 1999
JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449 0766
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 99.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 69.2
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1226
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1279
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.1816
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 2232
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 43972
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.1109
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.1159
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.1689
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 1946
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 38151
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1450
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 143
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 1576.50
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 1203.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 4
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 14389
REMARK 3 NUMBER OF RESTRAINTS : 16950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 ANGLE DISTANCES (A) : 0.029
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.0270
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.079
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.091
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.063
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.046
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BS9 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : FEB-1995
REMARK 200 TEMPERATURE (KELVIN) : 287
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : PRINCETON
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44040
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.10
REMARK 200 RESOLUTION RANGE LOW (A) : 99.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 69.3
REMARK 200 DATA REDUNDANCY : 3.4
REMARK 200 R MERGE (I) : 0.059
REMARK 200 R SYM (I) : NONE
REMARK 200 FOR THE DATA SET : 32
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 45
REMARK 200 DATA REDUNDANCY IN SHELL : 2.5
REMARK 200 R MERGE FOR SHELL (I) : 0.37
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.0
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-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 17.44287
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.21351
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.49152
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.21351
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.44287
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.49152
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: 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 15 DEGREES (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION
REMARK 500 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 0 ALA 173 C-1 - N - CA ANGL. DEV. = 15.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: THESE THREE RESIDUES FORM THE CATALYTIC
REMARK 800 TRIAD
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1BS9 GB 2944191 1 - 27 NOT IN ATOMS LIST
DBREF 1BS9 1 207 GB 2944191 AAC39371 28 234
SEQRES 1 207 SER CYS PRO ALA ILE HIS VAL PHE GLY ALA ARG GLU THR
SEQRES 2 207 THR ALA SER PRO GLY TYR GLY SER SER SER THR VAL VAL
SEQRES 3 207 ASN GLY VAL LEU SER ALA TYR PRO GLY SER THR ALA GLU
SEQRES 4 207 ALA ILE ASN TYR PRO ALA CYS GLY GLY GLN SER SER CYS
SEQRES 5 207 GLY GLY ALA SER TYR SER SER SER VAL ALA GLN GLY ILE
SEQRES 6 207 ALA ALA VAL ALA SER ALA VAL ASN SER PHE ASN SER GLN
SEQRES 7 207 CYS PRO SER THR LYS ILE VAL LEU VAL GLY TYR SER GLN
SEQRES 8 207 GLY GLY GLU ILE MET ASP VAL ALA LEU CYS GLY GLY GLY
SEQRES 9 207 ASP PRO ASN GLN GLY TYR THR ASN THR ALA VAL GLN LEU
SEQRES 10 207 SER SER SER ALA VAL ASN MET VAL LYS ALA ALA ILE PHE
SEQRES 11 207 MET GLY ASP PRO MET PHE ARG ALA GLY LEU SER TYR GLU
SEQRES 12 207 VAL GLY THR CYS ALA ALA GLY GLY PHE ASP GLN ARG PRO
SEQRES 13 207 ALA GLY PHE SER CYS PRO SER ALA ALA LYS ILE LYS SER
SEQRES 14 207 TYR CYS ASP ALA SER ASP PRO TYR CYS CYS ASN GLY SER
SEQRES 15 207 ASN ALA ALA THR HIS GLN GLY TYR GLY SER GLU TYR GLY
SEQRES 16 207 SER GLN ALA LEU ALA PHE VAL LYS SER LYS LEU GLY
HET SO4 208 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S1 2-
FORMUL 3 HOH *143(H2 O1)
HELIX 1 1 GLY 20 ALA 32 5 13
HELIX 2 2 SER 50 CYS 52 5 3
HELIX 3 3 TYR 57 GLN 78 1 22
HELIX 4 4 SER 90 CYS 101 5 12
HELIX 5 5 PRO 106 GLN 108 5 3
HELIX 6 6 SER 119 MET 124 1 6
HELIX 7 7 ALA 164 LYS 166 5 3
HELIX 8 8 ALA 184 GLN 188 1 5
HELIX 9 9 TYR 190 LYS 205 1 16
SHEET 1 A 5 THR 37 ALA 40 0
SHEET 2 A 5 ILE 5 ALA 10 1 N VAL 7 O THR 37
SHEET 3 A 5 LYS 83 TYR 89 1 N LYS 83 O HIS 6
SHEET 4 A 5 VAL 125 MET 131 1 N LYS 126 O ILE 84
SHEET 5 A 5 ILE 167 TYR 170 1 N LYS 168 O ALA 128
SSBOND 1 CYS 2 CYS 79
SSBOND 2 CYS 46 CYS 52
SSBOND 3 CYS 101 CYS 161
SSBOND 4 CYS 147 CYS 179
SSBOND 5 CYS 171 CYS 178
SITE 1 CAT 3 SER 90 ASP 175 HIS 187
CRYST1 34.886 60.983 72.425 90.00 90.00 90.00 P 21 21 21 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 0.028665 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016398 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013807 0.00000
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