HEADER HYDROLASE 07-FEB-08 3C7F
TITLE CRYSTAL STRUCTURE OF A GLYCOSIDE HYDROLASE FAMILY 43 ARABINOXYLAN
TITLE 2 ARABINOFURANOHYDROLASE FROM BACILLUS SUBTILIS IN COMPLEX WITH
TITLE 3 XYLOTRIOSE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: XYLANASE D;
COMPND 5 EC: 3.2.1.55;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: XYND;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS 5-BLADED BETA-PROPELLER FOLD, BETA-SANDWICH, XYLAN DEGRADATION,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.VANDERMARLIERE,T.M.BOURGOIS,M.D.WINN,S.VAN CAMPENHOUT,G.VOLCKAERT,
AUTHOR 2 S.V.STRELKOV,J.A.DELCOUR,A.RABIJNS,C.M.COURTIN
REVDAT 5 30-AUG-23 3C7F 1 HETSYN
REVDAT 4 29-JUL-20 3C7F 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 13-JUL-11 3C7F 1 VERSN
REVDAT 2 10-FEB-09 3C7F 1 JRNL VERSN
REVDAT 1 18-NOV-08 3C7F 0
JRNL AUTH E.VANDERMARLIERE,T.M.BOURGOIS,M.D.WINN,S.VAN CAMPENHOUT,
JRNL AUTH 2 G.VOLCKAERT,J.A.DELCOUR,S.V.STRELKOV,A.RABIJNS,C.M.COURTIN
JRNL TITL STRUCTURAL ANALYSIS OF A GLYCOSIDE HYDROLASE FAMILY 43
JRNL TITL 2 ARABINOXYLAN ARABINOFURANOHYDROLASE IN COMPLEX WITH
JRNL TITL 3 XYLOTETRAOSE REVEALS A DIFFERENT BINDING MECHANISM COMPARED
JRNL TITL 4 WITH OTHER MEMBERS OF THE SAME FAMILY.
JRNL REF BIOCHEM.J. V. 418 39 2009
JRNL REFN ISSN 0264-6021
JRNL PMID 18980579
JRNL DOI 10.1042/BJ20081256
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 73012
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 + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3871
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5268
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE SET COUNT : 278
REMARK 3 BIN FREE R VALUE : 0.2570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3658
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 579
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.56000
REMARK 3 B22 (A**2) : -0.22000
REMARK 3 B33 (A**2) : -0.34000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.073
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.074
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.043
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.159
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3850 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5239 ; 1.218 ; 1.932
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 492 ; 6.459 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 167 ;34.707 ;24.132
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 522 ;10.530 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;14.048 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 559 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3005 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1831 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2638 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 526 ; 0.143 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 13 ; 0.154 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 56 ; 0.263 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 39 ; 0.179 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2419 ; 0.631 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3848 ; 1.093 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1507 ; 1.577 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1388 ; 2.333 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3C7F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1000046435.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0788
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76939
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : 8.30000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.32200
REMARK 200 R SYM FOR SHELL (I) : 32.2000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MRBUMP
REMARK 200 STARTING MODEL: PDB ENTRIES 1W9T, 1GYH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4.0 M NA FORMATE, 1.0 M LITHIUM
REMARK 280 CHLORIDE, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 34.31350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.18400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.83100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.18400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.31350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.83100
REMARK 290 SMTRY3 4 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: PISA
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 DISTANCE
REMARK 500 O3 XYP B 2 O HOH A 2158 2.04
REMARK 500 OE1 GLU A 225 O HOH A 2158 2.04
REMARK 500 O HOH A 2579 O HOH A 2585 2.11
REMARK 500 O HOH A 2321 O HOH A 2597 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 ALA A 7 -33.26 -147.14
REMARK 500 MET A 70 -2.30 80.68
REMARK 500 ASN A 85 -130.73 56.28
REMARK 500 SER A 123 -139.33 53.73
REMARK 500 VAL A 185 -118.08 47.64
REMARK 500 PHE A 224 -58.35 -132.30
REMARK 500 GLU A 225 -168.48 -172.08
REMARK 500 GLN A 307 47.52 -94.42
REMARK 500 ASP A 427 -39.90 75.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 803 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 359 OE1
REMARK 620 2 GLU A 361 OE1 103.5
REMARK 620 3 GLU A 361 OE2 88.7 52.0
REMARK 620 4 ASN A 383 OD1 81.2 132.5 81.3
REMARK 620 5 GLN A 384 O 160.6 77.1 76.4 84.3
REMARK 620 6 ASP A 480 O 83.0 75.3 122.8 150.8 115.5
REMARK 620 7 ASP A 480 OD1 102.3 137.3 160.7 84.7 89.1 74.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 804 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 368 O
REMARK 620 2 SER A 388 O 103.8
REMARK 620 3 GLN A 390 OE1 162.7 93.2
REMARK 620 4 ASP A 393 OD2 91.9 91.7 91.2
REMARK 620 5 HOH A2194 O 85.9 92.0 89.9 176.1
REMARK 620 6 HOH A2371 O 84.4 168.4 79.4 79.7 96.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 805 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2078 O
REMARK 620 2 HOH A2117 O 85.5
REMARK 620 3 HOH A2170 O 153.8 74.4
REMARK 620 4 HOH A2250 O 98.1 81.6 95.4
REMARK 620 5 HOH A2565 O 145.9 126.9 52.7 97.3
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3C7E RELATED DB: PDB
REMARK 900 RELATED ID: 3C7G RELATED DB: PDB
REMARK 900 RELATED ID: 3C7H RELATED DB: PDB
REMARK 900 RELATED ID: 3C7O RELATED DB: PDB
DBREF 3C7F A 1 487 UNP Q45071 Q45071_BACSU 27 513
SEQRES 1 A 487 ALA THR SER THR THR ILE ALA LYS HIS ILE GLY ASN SER
SEQRES 2 A 487 ASN PRO LEU ILE ASP HIS HIS LEU GLY ALA ASP PRO VAL
SEQRES 3 A 487 ALA LEU THR TYR ASN GLY ARG VAL TYR ILE TYR MET SER
SEQRES 4 A 487 SER ASP ASP TYR GLU TYR ASN SER ASN GLY THR ILE LYS
SEQRES 5 A 487 ASP ASN SER PHE ALA ASN LEU ASN ARG VAL PHE VAL ILE
SEQRES 6 A 487 SER SER ALA ASP MET VAL ASN TRP THR ASP HIS GLY ALA
SEQRES 7 A 487 ILE PRO VAL ALA GLY ALA ASN GLY ALA ASN GLY GLY ARG
SEQRES 8 A 487 GLY ILE ALA LYS TRP ALA GLY ALA SER TRP ALA PRO SER
SEQRES 9 A 487 ILE ALA VAL LYS LYS ILE ASN GLY LYS ASP LYS PHE PHE
SEQRES 10 A 487 LEU TYR PHE ALA ASN SER GLY GLY GLY ILE GLY VAL LEU
SEQRES 11 A 487 THR ALA ASP SER PRO ILE GLY PRO TRP THR ASP PRO ILE
SEQRES 12 A 487 GLY LYS PRO LEU VAL THR PRO SER THR PRO GLY MET SER
SEQRES 13 A 487 GLY VAL VAL TRP LEU PHE ASP PRO ALA VAL PHE VAL ASP
SEQRES 14 A 487 ASP ASP GLY THR GLY TYR LEU TYR ALA GLY GLY GLY VAL
SEQRES 15 A 487 PRO GLY VAL SER ASN PRO THR GLN GLY GLN TRP ALA ASN
SEQRES 16 A 487 PRO LYS THR ALA ARG VAL ILE LYS LEU GLY PRO ASP MET
SEQRES 17 A 487 THR SER VAL VAL GLY SER ALA SER THR ILE ASP ALA PRO
SEQRES 18 A 487 PHE MET PHE GLU ASP SER GLY LEU HIS LYS TYR ASN GLY
SEQRES 19 A 487 THR TYR TYR TYR SER TYR CYS ILE ASN PHE GLY GLY THR
SEQRES 20 A 487 HIS PRO ALA ASP LYS PRO PRO GLY GLU ILE GLY TYR MET
SEQRES 21 A 487 THR SER SER SER PRO MET GLY PRO PHE THR TYR ARG GLY
SEQRES 22 A 487 HIS PHE LEU LYS ASN PRO GLY ALA PHE PHE GLY GLY GLY
SEQRES 23 A 487 GLY ASN ASN HIS HIS ALA VAL PHE ASN PHE LYS ASN GLU
SEQRES 24 A 487 TRP TYR VAL VAL TYR HIS ALA GLN THR VAL SER SER ALA
SEQRES 25 A 487 LEU PHE GLY ALA GLY LYS GLY TYR ARG SER PRO HIS ILE
SEQRES 26 A 487 ASN LYS LEU VAL HIS ASN ALA ASP GLY SER ILE GLN GLU
SEQRES 27 A 487 VAL ALA ALA ASN TYR ALA GLY VAL THR GLN ILE SER ASN
SEQRES 28 A 487 LEU ASN PRO TYR ASN ARG VAL GLU ALA GLU THR PHE ALA
SEQRES 29 A 487 TRP ASN GLY ARG ILE LEU THR GLU LYS SER THR ALA PRO
SEQRES 30 A 487 GLY GLY PRO VAL ASN ASN GLN HIS VAL THR SER ILE GLN
SEQRES 31 A 487 ASN GLY ASP TRP ILE ALA VAL GLY ASN ALA ASP PHE GLY
SEQRES 32 A 487 ALA GLY GLY ALA ARG SER PHE LYS ALA ASN VAL ALA SER
SEQRES 33 A 487 THR LEU GLY GLY LYS ILE GLU VAL ARG LEU ASP SER ALA
SEQRES 34 A 487 ASP GLY LYS LEU VAL GLY THR LEU ASN VAL PRO SER THR
SEQRES 35 A 487 GLY GLY ALA GLN THR TRP ARG GLU ILE GLU THR ALA VAL
SEQRES 36 A 487 SER GLY ALA THR GLY VAL HIS LYS VAL PHE PHE VAL PHE
SEQRES 37 A 487 THR GLY THR GLY THR GLY ASN LEU PHE ASN PHE ASP TYR
SEQRES 38 A 487 TRP GLN PHE THR GLN ARG
HET XYP B 1 10
HET XYP B 2 9
HET XYP B 3 9
HET CA A 803 1
HET NA A 804 1
HET NA A 805 1
HET FMT A2055 3
HET GOL A1733 6
HET FMT A2056 3
HET FMT A2057 3
HET FMT A2058 3
HET FMT A2059 3
HET FMT A2060 3
HET FMT A2061 3
HET GOL A2062 6
HET GOL A2063 6
HET GOL A2064 6
HETNAM XYP BETA-D-XYLOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM FMT FORMIC ACID
HETNAM GOL GLYCEROL
HETSYN XYP BETA-D-XYLOSE; D-XYLOSE; XYLOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 XYP 3(C5 H10 O5)
FORMUL 3 CA CA 2+
FORMUL 4 NA 2(NA 1+)
FORMUL 6 FMT 7(C H2 O2)
FORMUL 7 GOL 4(C3 H8 O3)
FORMUL 17 HOH *579(H2 O)
HELIX 1 1 GLY A 86 ARG A 91 5 6
HELIX 2 2 THR A 189 ASN A 195 1 7
HELIX 3 3 ASN A 278 GLY A 284 1 7
HELIX 4 4 GLN A 307 GLY A 315 1 9
SHEET 1 A 5 ALA A 23 TYR A 30 0
SHEET 2 A 5 ARG A 33 SER A 39 -1 O TYR A 35 N LEU A 28
SHEET 3 A 5 VAL A 62 SER A 67 -1 O ILE A 65 N ILE A 36
SHEET 4 A 5 TRP A 73 ILE A 79 -1 O THR A 74 N SER A 66
SHEET 5 A 5 THR A 362 PHE A 363 -1 O PHE A 363 N TRP A 73
SHEET 1 B 2 GLU A 44 TYR A 45 0
SHEET 2 B 2 ILE A 51 LYS A 52 -1 O LYS A 52 N GLU A 44
SHEET 1 C 3 TRP A 101 ILE A 110 0
SHEET 2 C 3 LYS A 113 ALA A 121 -1 O ALA A 121 N TRP A 101
SHEET 3 C 3 ILE A 127 ALA A 132 -1 O GLY A 128 N PHE A 120
SHEET 1 D 4 ALA A 165 VAL A 168 0
SHEET 2 D 4 GLY A 174 GLY A 179 -1 O TYR A 177 N ALA A 165
SHEET 3 D 4 ALA A 199 LEU A 204 -1 O ILE A 202 N LEU A 176
SHEET 4 D 4 VAL A 211 ILE A 218 -1 O SER A 216 N VAL A 201
SHEET 1 E 4 MET A 223 TYR A 232 0
SHEET 2 E 4 THR A 235 ILE A 242 -1 O TYR A 237 N HIS A 230
SHEET 3 E 4 ILE A 257 SER A 262 -1 O SER A 262 N TYR A 236
SHEET 4 E 4 THR A 270 LEU A 276 -1 O ARG A 272 N TYR A 259
SHEET 1 F 3 HIS A 291 PHE A 296 0
SHEET 2 F 3 GLU A 299 ALA A 306 -1 O TYR A 301 N PHE A 294
SHEET 3 F 3 SER A 322 LYS A 327 -1 O ASN A 326 N VAL A 302
SHEET 1 G 4 VAL A 358 GLU A 359 0
SHEET 2 G 4 ASN A 478 GLN A 486 -1 O TRP A 482 N VAL A 358
SHEET 3 G 4 ALA A 407 ALA A 415 -1 N LYS A 411 O GLN A 483
SHEET 4 G 4 ARG A 449 ALA A 454 -1 O ILE A 451 N ALA A 412
SHEET 1 H 5 TRP A 365 GLY A 367 0
SHEET 2 H 5 TRP A 394 ASP A 401 -1 O TRP A 394 N GLY A 367
SHEET 3 H 5 VAL A 461 THR A 469 -1 O PHE A 466 N ILE A 395
SHEET 4 H 5 GLY A 420 LEU A 426 -1 N ARG A 425 O PHE A 465
SHEET 5 H 5 LEU A 433 VAL A 439 -1 O LEU A 437 N ILE A 422
SHEET 1 I 2 LEU A 370 LYS A 373 0
SHEET 2 I 2 GLN A 384 THR A 387 -1 O THR A 387 N LEU A 370
LINK O4 XYP B 1 C1 XYP B 2 1555 1555 1.44
LINK O4 XYP B 2 C1 XYP B 3 1555 1555 1.43
LINK OE1 GLU A 359 CA CA A 803 1555 1555 2.33
LINK OE1 GLU A 361 CA CA A 803 1555 1555 2.51
LINK OE2 GLU A 361 CA CA A 803 1555 1555 2.50
LINK O ARG A 368 NA NA A 804 1555 1555 2.38
LINK OD1 ASN A 383 CA CA A 803 1555 1555 2.39
LINK O GLN A 384 CA CA A 803 1555 1555 2.37
LINK O SER A 388 NA NA A 804 1555 1555 2.33
LINK OE1 GLN A 390 NA NA A 804 1555 1555 2.31
LINK OD2 ASP A 393 NA NA A 804 1555 1555 2.31
LINK O ASP A 480 CA CA A 803 1555 1555 2.48
LINK OD1 ASP A 480 CA CA A 803 1555 1555 2.35
LINK NA NA A 804 O HOH A2194 1555 1555 2.37
LINK NA NA A 804 O HOH A2371 1555 1555 2.58
LINK NA NA A 805 O HOH A2078 1555 1555 2.26
LINK NA NA A 805 O HOH A2117 1555 1555 2.32
LINK NA NA A 805 O HOH A2170 1555 1555 2.31
LINK NA NA A 805 O HOH A2250 1555 1555 2.83
LINK NA NA A 805 O HOH A2565 1555 1555 2.65
CISPEP 1 ASN A 14 PRO A 15 0 -10.45
CISPEP 2 GLY A 137 PRO A 138 0 2.89
CISPEP 3 GLY A 267 PRO A 268 0 5.26
CISPEP 4 GLY A 367 ARG A 368 0 -19.15
CISPEP 5 THR A 473 GLY A 474 0 4.08
CRYST1 68.627 73.662 106.368 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 0.014572 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013576 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009401 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
