HEADER HYDROLASE 23-OCT-01 1GOQ
TITLE THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS - ROOM
TITLE 2 TEMPERATURE XYLOBIOSE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: XYLANASE, 1,4-BETA-D-XYLAN XYLANOHYDROLASE;
COMPND 5 EC: 3.2.1.8
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOASCUS AURANTIACUS;
SOURCE 3 ORGANISM_TAXID: 5087
KEYWDS XYLANASE, FAMILY 10, PLANT CELL WALL DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.LO LEGGIO,S.LARSEN
REVDAT 7 13-DEC-23 1GOQ 1 HETSYN LINK
REVDAT 6 29-JUL-20 1GOQ 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE ATOM
REVDAT 5 11-MAR-20 1GOQ 1 SEQRES
REVDAT 4 08-MAY-19 1GOQ 1 REMARK LINK
REVDAT 3 22-OCT-14 1GOQ 1 REMARK VERSN FORMUL
REVDAT 2 24-FEB-09 1GOQ 1 VERSN
REVDAT 1 07-DEC-01 1GOQ 0
JRNL AUTH L.LO LEGGIO,S.KALOGIANNIS,K.ECKERT,S.C.M.TEIXEIRA,M.K.BHAT,
JRNL AUTH 2 C.ANDREI,R.W.PICKERSGILL,S.LARSEN
JRNL TITL SUBSTRATE SPECIFICITY AND SUBSITE MOBILITY IN T. AURANTIACUS
JRNL TITL 2 XYLANASE 10A
JRNL REF FEBS LETT. V. 509 303 2001
JRNL REFN ISSN 0014-5793
JRNL PMID 11741607
JRNL DOI 10.1016/S0014-5793(01)03177-5
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.TEIXEIRA,L.LO LEGGIO,R.PICKERSGILL,C.CARDIN
REMARK 1 TITL ANISOTROPIC REFINEMENT OF THE STRUCTURE OF THERMOASCUS
REMARK 1 TITL 2 AURANTIACUS XYLANASE I
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 57 385 2001
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 11223515
REMARK 1 DOI 10.1107/S0907444900019089
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.LO LEGGIO,S.KALOGIANNIS,M.K.BHAT,R.W.PICKERSGILL
REMARK 1 TITL HIGH RESOLUTION STRUCTURE AND SEQUENCE OF T. AURANTIACUS
REMARK 1 TITL 2 XYLANASE I: IMPLICATIONS FOR THE EVOLUTION OF
REMARK 1 TITL 3 THERMOSTABILITY IN FAMILY 10 XYLANASES AND ENZYMES WITH
REMARK 1 TITL 4 BETA/ALPHA BARREL ARCHITECTURE
REMARK 1 REF PROTEINS V. 36 295 1999
REMARK 1 REFN ISSN 0887-3585
REMARK 1 PMID 10409823
REMARK 1 REFERENCE 3
REMARK 1 AUTH R.PICKERSGILL,G.HARRIS,L.LO LEGGIO,O.MAYANS,J.JENKINS
REMARK 1 TITL SUPERFAMILIES: THE 4/7 SUPERFAMILY OF BETA/ ALPHA-BARREL
REMARK 1 TITL 2 GLYCOSIDASES AND THE RIGHT-HANDED PARALLEL BETA-HELIX
REMARK 1 TITL 3 SUPERFAMILY
REMARK 1 REF BIOCHEM.SOC.TRANS. V. 26 190 1998
REMARK 1 REFN ISSN 0300-5127
REMARK 1 PMID 9649746
REMARK 1 REFERENCE 4
REMARK 1 AUTH L.LO LEGGIO
REMARK 1 TITL STRUCTURE SOLUTION OF THERMOASCUS AURANTIACUS XYLANASE.
REMARK 1 TITL 2 STRUCTURAL STUDIES OF XYLANASES AND ENDOGLUCANASES
REMARK 1 EDIT UNIVERSITY OF LONDON
REMARK 1 REF STRUCTURAL STUDIES OF 194 1997
REMARK 1 REF 2 XYLANASES AND ENDOGLUCANASES
REMARK 1 PUBL LONDON, UK : UNIVERSITY OF LONDON
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.3
REMARK 3 NUMBER OF REFLECTIONS : 19293
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) : 0.167
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.400
REMARK 3 FREE R VALUE TEST SET COUNT : 1922
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 44.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1543
REMARK 3 BIN R VALUE (WORKING SET) : 0.2370
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 164
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2312
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 131
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.26600
REMARK 3 B22 (A**2) : -0.11500
REMARK 3 B33 (A**2) : -1.15100
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.18600
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.16
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.13
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.700
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) : 1.494 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.116 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.647 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.728 ; 2.500
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 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GOQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1290008745.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : R-AXIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20709
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.0
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.17000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 37.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.33800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: 1GOK
REMARK 200
REMARK 200 REMARK: THE PH OF CRYSTALLIZATION WAS NOT BUFFERED
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROPS CONTAINING 1:1 RATIO OF
REMARK 280 20-30 MG/ML PROTEIN SOLUTION AND RESERVOIR SOLUTION (12 % TO 25 %
REMARK 280 PEG 6,000). THE CRYSTAL WAS SOAKED IN 0.5 M XYLOBIOSE, PH 7.00,
REMARK 280 VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
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
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 29.78000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 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 GLN A 303 CA C O CB CG CD OE1
REMARK 470 GLN A 303 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 22 -175.62 -171.83
REMARK 500 ASN A 47 -23.19 -143.85
REMARK 500 ASP A 164 83.84 -153.55
REMARK 500 GLU A 237 47.90 -140.98
REMARK 500 VAL A 269 -65.54 -105.29
REMARK 500 THR A 280 67.34 33.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: OLIGOSACCHARIDE METABOLISM
REMARK 630 MOLECULE NAME: BETA-D-XYLOPYRANOSE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 XYP A 403
REMARK 630 XYP A 404
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: NULL
REMARK 630 DETAILS: OLIGOSACCHARIDE
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FXM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE THERMOASCUS AURANTIACUS XYLANASE I
REMARK 900 RELATED ID: 1GOK RELATED DB: PDB
REMARK 900 THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS
REMARK 900 RELATED ID: 1GOM RELATED DB: PDB
REMARK 900 THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS
REMARK 900 RELATED ID: 1GOO RELATED DB: PDB
REMARK 900 THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS
REMARK 900 RELATED ID: 1GOQ RELATED DB: PDB
REMARK 900 THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS
REMARK 900 RELATED ID: 1GOR RELATED DB: PDB
REMARK 900 THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS - XYLOBIOSE
REMARK 900 COMPLEX AT 100 K
REMARK 900 RELATED ID: 1TAX RELATED DB: PDB
REMARK 900 THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS
REMARK 900 RELATED ID: 1TIX RELATED DB: PDB
REMARK 900 THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 1-26 REFER TO THE SIGNAL PEPTIDE
REMARK 999 IT IS NOT KNOWN IF GLN 303 IS PRESENT IN THE CRYSTAL
DBREF 1GOQ A 1 303 UNP P23360 XYNA_THEAU 27 329
SEQRES 1 A 303 PCA ALA ALA GLN SER VAL ASP GLN LEU ILE LYS ALA ARG
SEQRES 2 A 303 GLY LYS VAL TYR PHE GLY VAL ALA THR ASP GLN ASN ARG
SEQRES 3 A 303 LEU THR THR GLY LYS ASN ALA ALA ILE ILE GLN ALA ASP
SEQRES 4 A 303 PHE GLY GLN VAL THR PRO GLU ASN SER MET LYS TRP ASP
SEQRES 5 A 303 ALA THR GLU PRO SER GLN GLY ASN PHE ASN PHE ALA GLY
SEQRES 6 A 303 ALA ASP TYR LEU VAL ASN TRP ALA GLN GLN ASN GLY LYS
SEQRES 7 A 303 LEU ILE ARG GLY HIS THR LEU VAL TRP HIS SER GLN LEU
SEQRES 8 A 303 PRO SER TRP VAL SER SER ILE THR ASP LYS ASN THR LEU
SEQRES 9 A 303 THR ASN VAL MET LYS ASN HIS ILE THR THR LEU MET THR
SEQRES 10 A 303 ARG TYR LYS GLY LYS ILE ARG ALA TRP ASP VAL VAL ASN
SEQRES 11 A 303 GLU ALA PHE ASN GLU ASP GLY SER LEU ARG GLN THR VAL
SEQRES 12 A 303 PHE LEU ASN VAL ILE GLY GLU ASP TYR ILE PRO ILE ALA
SEQRES 13 A 303 PHE GLN THR ALA ARG ALA ALA ASP PRO ASN ALA LYS LEU
SEQRES 14 A 303 TYR ILE ASN ASP TYR ASN LEU ASP SER ALA SER TYR PRO
SEQRES 15 A 303 LYS THR GLN ALA ILE VAL ASN ARG VAL LYS GLN TRP ARG
SEQRES 16 A 303 ALA ALA GLY VAL PRO ILE ASP GLY ILE GLY SER GLN THR
SEQRES 17 A 303 HIS LEU SER ALA GLY GLN GLY ALA GLY VAL LEU GLN ALA
SEQRES 18 A 303 LEU PRO LEU LEU ALA SER ALA GLY THR PRO GLU VAL ALA
SEQRES 19 A 303 ILE THR GLU LEU ASP VAL ALA GLY ALA SER PRO THR ASP
SEQRES 20 A 303 TYR VAL ASN VAL VAL ASN ALA CYS LEU ASN VAL GLN SER
SEQRES 21 A 303 CYS VAL GLY ILE THR VAL TRP GLY VAL ALA ASP PRO ASP
SEQRES 22 A 303 SER TRP ARG ALA SER THR THR PRO LEU LEU PHE ASP GLY
SEQRES 23 A 303 ASN PHE ASN PRO LYS PRO ALA TYR ASN ALA ILE VAL GLN
SEQRES 24 A 303 ASP LEU GLN GLN
MODRES 1GOQ PCA A 1 GLU PYROGLUTAMIC ACID
HET PCA A 1 8
HET XYP B 1 10
HET XYP B 2 9
HET XYP C 1 10
HET XYP C 2 9
HET XYP A 403 10
HET XYP A 404 10
HETNAM PCA PYROGLUTAMIC ACID
HETNAM XYP BETA-D-XYLOPYRANOSE
HETSYN XYP BETA-D-XYLOSE; D-XYLOSE; XYLOSE
FORMUL 1 PCA C5 H7 N O3
FORMUL 2 XYP 6(C5 H10 O5)
FORMUL 6 HOH *131(H2 O)
HELIX 1 1 SER A 5 ARG A 13 1 9
HELIX 2 2 ASP A 23 THR A 28 1 6
HELIX 3 3 LYS A 31 PHE A 40 1 10
HELIX 4 4 LYS A 50 GLU A 55 1 6
HELIX 5 5 PHE A 63 ASN A 76 1 14
HELIX 6 6 PRO A 92 SER A 97 1 6
HELIX 7 7 ASP A 100 TYR A 119 1 20
HELIX 8 8 THR A 142 GLY A 149 1 8
HELIX 9 9 ASP A 151 ASP A 164 1 14
HELIX 10 10 TYR A 181 ALA A 197 1 17
HELIX 11 11 GLN A 214 SER A 227 1 14
HELIX 12 12 SER A 244 VAL A 258 1 15
HELIX 13 13 ASP A 271 SER A 274 5 4
HELIX 14 14 ARG A 276 THR A 280 5 5
HELIX 15 15 LYS A 291 GLN A 302 1 12
SHEET 1 AA11 TYR A 17 THR A 22 0
SHEET 2 AA11 CYS A 261 VAL A 266 1 O ILE A 264 N GLY A 19
SHEET 3 AA11 GLU A 232 VAL A 240 1 O VAL A 233 N VAL A 262
SHEET 4 AA11 GLY A 203 SER A 206 1 O ILE A 204 N ALA A 234
SHEET 5 AA11 LYS A 168 ASP A 173 1 O LEU A 169 N GLY A 203
SHEET 6 AA11 ALA A 125 ASN A 130 1 O TRP A 126 N TYR A 170
SHEET 7 AA11 LEU A 79 VAL A 86 1 O GLY A 82 N ASP A 127
SHEET 8 AA11 GLN A 42 PRO A 45 1 O VAL A 43 N ARG A 81
SHEET 9 AA11 TYR A 17 THR A 22 1 O VAL A 20 N THR A 44
SHEET 10 AA11 CYS A 261 VAL A 266 1 O ILE A 264 N GLY A 19
SHEET 11 AA11 TYR A 17 THR A 22 1 O TYR A 17 N ILE A 264
SSBOND 1 CYS A 255 CYS A 261 1555 1555 2.03
LINK C PCA A 1 N ALA A 2 1555 1555 1.33
LINK O4 XYP B 1 C1 XYP B 2 1555 1555 1.43
LINK O4 XYP C 1 C1 XYP C 2 1555 1555 1.42
CISPEP 1 HIS A 83 THR A 84 0 -1.66
CRYST1 46.060 59.560 51.130 90.00 110.80 90.00 P 1 21 1 2
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 0.021711 0.000000 0.008247 0.00000
SCALE2 0.000000 0.016790 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020921 0.00000
HETATM 1 N PCA A 1 10.646 4.262 27.147 1.00 35.35 N
HETATM 2 CA PCA A 1 10.171 2.861 27.240 1.00 33.02 C
HETATM 3 CB PCA A 1 11.419 2.000 27.145 1.00 33.52 C
HETATM 4 CG PCA A 1 12.582 2.982 26.990 1.00 39.23 C
HETATM 5 CD PCA A 1 11.964 4.362 27.006 1.00 38.95 C
HETATM 6 OE PCA A 1 12.604 5.421 26.902 1.00 44.95 O
HETATM 7 C PCA A 1 9.392 2.559 28.548 1.00 32.21 C
HETATM 8 O PCA A 1 9.806 2.931 29.642 1.00 32.72 O
(ATOM LINES ARE NOT SHOWN.)
END
