HEADER HYDROLASE 14-JUL-10 3AKH
TITLE CRYSTAL STRUCTURE OF EXO-1,5-ALPHA-L-ARABINOFURANOSIDASE COMPLEXED
TITLE 2 WITH ALPHA-1,5-L-ARABINOFURANOTRIOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE SECRETED ALPHA L-ARABINOFURANOSIDASE II;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 28-481;
COMPND 5 EC: 3.2.1.55;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES AVERMITILIS;
SOURCE 3 ORGANISM_TAXID: 227882;
SOURCE 4 STRAIN: MA-4680;
SOURCE 5 GENE: ABFA, SAV1043, SAV_1043;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET30
KEYWDS FIVE-BLADED BETA PROPELLER, BETA-TREFOIL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.FUJIMOTO,H.ICHINOSE,S.KANEKO
REVDAT 5 01-NOV-23 3AKH 1 HETSYN LINK
REVDAT 4 29-JUL-20 3AKH 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 11-OCT-17 3AKH 1 REMARK
REVDAT 2 03-NOV-10 3AKH 1 JRNL
REVDAT 1 25-AUG-10 3AKH 0
JRNL AUTH Z.FUJIMOTO,H.ICHINOSE,T.MAEHARA,M.HONDA,M.KITAOKA,S.KANEKO
JRNL TITL CRYSTAL STRUCTURE OF AN
JRNL TITL 2 EXO-1,5-{ALPHA}-L-ARABINOFURANOSIDASE FROM STREPTOMYCES
JRNL TITL 3 AVERMITILIS PROVIDES INSIGHTS INTO THE MECHANISM OF
JRNL TITL 4 SUBSTRATE DISCRIMINATION BETWEEN EXO- AND ENDO-TYPE ENZYMES
JRNL TITL 5 IN GLYCOSIDE HYDROLASE FAMILY 43.
JRNL REF J.BIOL.CHEM. V. 285 34134 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20739278
JRNL DOI 10.1074/JBC.M110.164251
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Z.FUJIMOTO,H.ICHINOSE,S.KANEKO
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF
REMARK 1 TITL 2 EXO-ALPHA-1,5-L-ARABINOFURANOSIDASE FROM STREPTOMYCES
REMARK 1 TITL 3 AVERMITILIS NBRC14893.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 64 1007 2008
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 18997327
REMARK 1 DOI 10.1107/S1744309108029692
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.ICHINOSE,M.YOSHIDA,Z.FUJIMOTO,S.KANEKO
REMARK 1 TITL CHARACTERIZATION OF A MODULAR ENZYME OF
REMARK 1 TITL 2 EXO-1,5-ALPHA-L-ARABINOFURANOSIDASE AND ARABINAN BINDING
REMARK 1 TITL 3 MODULE FROM STREPTOMYCES AVERMITILIS NBRC14893.
REMARK 1 REF APPL.MICROBIOL.BIOTECHNOL. V. 80 399 2008
REMARK 1 REFN ISSN 0175-7598
REMARK 1 PMID 18665359
REMARK 1 DOI 10.1007/S00253-008-1551-X
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 53483
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2877
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3815
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE SET COUNT : 230
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3518
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 81
REMARK 3 SOLVENT ATOMS : 578
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.05000
REMARK 3 B22 (A**2) : 0.22000
REMARK 3 B33 (A**2) : -0.17000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.071
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.109
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3701 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5054 ; 1.244 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 446 ; 5.878 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 174 ;28.278 ;23.276
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 529 ;11.879 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;15.570 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 554 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2853 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2225 ; 0.657 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3583 ; 1.189 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1476 ; 1.727 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1471 ; 2.774 ; 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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3AKH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000029363.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97000
REMARK 200 MONOCHROMATOR : NUMERICAL LINK TYPE SI(111)
REMARK 200 DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56484
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 39.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 14.60
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 53.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.40
REMARK 200 R MERGE FOR SHELL (I) : 0.25700
REMARK 200 R SYM FOR SHELL (I) : 0.25700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.530
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3AKF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M SODIUM CITRATE, 0.2M SODIUM
REMARK 280 CHLORIDE, 0.1M TRIS, PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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 20.61850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.98100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.67050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.98100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.61850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.67050
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, C, D
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 0
REMARK 465 THR A 1
REMARK 465 ALA A 2
REMARK 465 PRO A 3
REMARK 465 ALA A 4
REMARK 465 SER A 5
REMARK 465 PRO A 6
REMARK 465 SER A 7
REMARK 465 VAL A 8
REMARK 465 LEU A 456
REMARK 465 ALA A 457
REMARK 465 ALA A 458
REMARK 465 ALA A 459
REMARK 465 LEU A 460
REMARK 465 GLU A 461
REMARK 465 HIS A 462
REMARK 465 HIS A 463
REMARK 465 HIS A 464
REMARK 465 HIS A 465
REMARK 465 HIS A 466
REMARK 465 HIS A 467
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 ASN A 159 -63.26 -95.44
REMARK 500 SER A 214 -179.19 62.61
REMARK 500 THR A 216 31.84 -80.95
REMARK 500 ASP A 217 -153.13 -104.34
REMARK 500 HIS A 260 70.83 37.67
REMARK 500 ASN A 433 -12.95 73.36
REMARK 500 SER A 441 -30.17 -134.32
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 NA A 502 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 79 OE2
REMARK 620 2 HOH A 682 O 96.6
REMARK 620 3 HOH A 690 O 96.0 95.0
REMARK 620 4 HOH A 779 O 126.5 81.6 137.5
REMARK 620 5 HOH A 827 O 85.0 173.1 91.5 92.1
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3AKF RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT LIGAND
REMARK 900 RELATED ID: 3AKG RELATED DB: PDB
REMARK 900 RELATED ID: 3AKI RELATED DB: PDB
DBREF 3AKH A 1 454 UNP Q82P90 Q82P90_STRAW 28 481
SEQADV 3AKH MET A 0 UNP Q82P90 EXPRESSION TAG
SEQADV 3AKH LYS A 455 UNP Q82P90 EXPRESSION TAG
SEQADV 3AKH LEU A 456 UNP Q82P90 EXPRESSION TAG
SEQADV 3AKH ALA A 457 UNP Q82P90 EXPRESSION TAG
SEQADV 3AKH ALA A 458 UNP Q82P90 EXPRESSION TAG
SEQADV 3AKH ALA A 459 UNP Q82P90 EXPRESSION TAG
SEQADV 3AKH LEU A 460 UNP Q82P90 EXPRESSION TAG
SEQADV 3AKH GLU A 461 UNP Q82P90 EXPRESSION TAG
SEQADV 3AKH HIS A 462 UNP Q82P90 EXPRESSION TAG
SEQADV 3AKH HIS A 463 UNP Q82P90 EXPRESSION TAG
SEQADV 3AKH HIS A 464 UNP Q82P90 EXPRESSION TAG
SEQADV 3AKH HIS A 465 UNP Q82P90 EXPRESSION TAG
SEQADV 3AKH HIS A 466 UNP Q82P90 EXPRESSION TAG
SEQADV 3AKH HIS A 467 UNP Q82P90 EXPRESSION TAG
SEQRES 1 A 468 MET THR ALA PRO ALA SER PRO SER VAL THR PHE THR ASN
SEQRES 2 A 468 PRO LEU ALA GLU LYS ARG ALA ASP PRO HIS ILE PHE LYS
SEQRES 3 A 468 HIS THR ASP GLY TYR TYR TYR PHE THR ALA THR VAL PRO
SEQRES 4 A 468 GLU TYR ASP ARG ILE VAL LEU ARG ARG ALA THR THR LEU
SEQRES 5 A 468 GLN GLY LEU ALA THR ALA PRO GLU THR THR ILE TRP THR
SEQRES 6 A 468 LYS HIS ALA SER GLY VAL MET GLY ALA HIS ILE TRP ALA
SEQRES 7 A 468 PRO GLU ILE HIS PHE ILE ASP GLY LYS TRP TYR VAL TYR
SEQRES 8 A 468 PHE ALA ALA GLY SER THR SER ASP VAL TRP ALA ILE ARG
SEQRES 9 A 468 MET TYR VAL LEU GLU SER GLY ALA ALA ASN PRO LEU THR
SEQRES 10 A 468 GLY SER TRP THR GLU LYS GLY GLN ILE ALA THR PRO VAL
SEQRES 11 A 468 SER SER PHE SER LEU ASP ALA THR THR PHE VAL VAL ASN
SEQRES 12 A 468 GLY VAL ARG HIS LEU ALA TRP ALA GLN ARG ASN PRO ALA
SEQRES 13 A 468 GLU ASP ASN ASN THR SER LEU PHE ILE ALA LYS MET ALA
SEQRES 14 A 468 ASN PRO TRP THR ILE SER GLY THR PRO THR GLU ILE SER
SEQRES 15 A 468 GLN PRO THR LEU SER TRP GLU THR VAL GLY TYR LYS VAL
SEQRES 16 A 468 ASN GLU GLY PRO ALA VAL ILE GLN HIS GLY GLY LYS VAL
SEQRES 17 A 468 PHE LEU THR TYR SER ALA SER ALA THR ASP ALA ASN TYR
SEQRES 18 A 468 CYS LEU GLY MET LEU SER ALA SER ALA SER ALA ASP LEU
SEQRES 19 A 468 LEU ASN ALA ALA SER TRP THR LYS SER SER GLN PRO VAL
SEQRES 20 A 468 PHE LYS THR SER GLU ALA THR GLY GLN TYR GLY PRO GLY
SEQRES 21 A 468 HIS ASN SER PHE THR VAL SER GLU ASP GLY LYS SER ASP
SEQRES 22 A 468 ILE LEU VAL TYR HIS ASP ARG ASN TYR LYS ASP ILE SER
SEQRES 23 A 468 GLY ASP PRO LEU ASN ASP PRO ASN ARG ARG THR ARG LEU
SEQRES 24 A 468 GLN LYS VAL TYR TRP ASN ALA ASP GLY THR PRO ASN PHE
SEQRES 25 A 468 GLY ILE PRO VAL ALA ASP GLY VAL THR PRO VAL ARG PHE
SEQRES 26 A 468 SER SER TYR ASN TYR PRO ASP ARG TYR ILE ARG HIS TRP
SEQRES 27 A 468 ASP PHE ARG ALA ARG ILE GLU ALA ASN VAL THR ASN LEU
SEQRES 28 A 468 ALA ASP SER GLN PHE ARG VAL VAL THR GLY LEU ALA GLY
SEQRES 29 A 468 SER GLY THR ILE SER LEU GLU SER ALA ASN TYR PRO GLY
SEQRES 30 A 468 TYR TYR LEU ARG HIS LYS ASN TYR GLU VAL TRP VAL GLU
SEQRES 31 A 468 LYS ASN ASP GLY SER SER ALA PHE LYS ASN ASP ALA SER
SEQRES 32 A 468 PHE SER ARG ARG ALA GLY LEU ALA ASP SER ALA ASP GLY
SEQRES 33 A 468 ILE ALA PHE GLU SER TYR ASN TYR PRO GLY ARG TYR LEU
SEQRES 34 A 468 ARG HIS TYR GLU ASN LEU LEU ARG ILE GLN PRO VAL SER
SEQRES 35 A 468 THR ALA LEU ASP ARG GLN ASP ALA THR PHE TYR ALA GLU
SEQRES 36 A 468 LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET AHR B 1 10
HET AHR B 2 9
HET AHR C 1 10
HET AHR C 2 9
HET AHR D 1 10
HET AHR D 2 9
HET CL A 501 1
HET NA A 502 1
HET AHR A 541 10
HET GOL A 597 6
HET GOL A 599 6
HETNAM AHR ALPHA-L-ARABINOFURANOSE
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
HETSYN AHR ALPHA-L-ARABINOSE; L-ARABINOSE; ARABINOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 AHR 7(C5 H10 O5)
FORMUL 5 CL CL 1-
FORMUL 6 NA NA 1+
FORMUL 8 GOL 2(C3 H8 O3)
FORMUL 10 HOH *578(H2 O)
HELIX 1 1 LEU A 51 ALA A 57 5 7
HELIX 2 2 LEU A 185 THR A 189 5 5
HELIX 3 3 ASN A 235 TRP A 239 5 5
HELIX 4 4 ASP A 287 ASP A 291 5 5
HELIX 5 5 ASN A 349 SER A 353 5 5
HELIX 6 6 SER A 394 ALA A 401 1 8
HELIX 7 7 THR A 442 ALA A 449 1 8
SHEET 1 A 2 THR A 11 ASN A 12 0
SHEET 2 A 2 GLY A 318 VAL A 319 -1 O GLY A 318 N ASN A 12
SHEET 1 B 4 ALA A 19 LYS A 25 0
SHEET 2 B 4 TYR A 31 THR A 36 -1 O THR A 36 N ALA A 19
SHEET 3 B 4 ARG A 42 ALA A 48 -1 O ALA A 48 N TYR A 31
SHEET 4 B 4 THR A 60 THR A 64 -1 O THR A 60 N LEU A 45
SHEET 1 C 4 ALA A 73 ILE A 83 0
SHEET 2 C 4 LYS A 86 GLY A 94 -1 O LYS A 86 N ILE A 83
SHEET 3 C 4 ARG A 103 SER A 109 -1 O SER A 109 N TRP A 87
SHEET 4 C 4 THR A 120 GLN A 124 -1 O LYS A 122 N VAL A 106
SHEET 1 D 4 SER A 133 VAL A 141 0
SHEET 2 D 4 VAL A 144 GLN A 151 -1 O HIS A 146 N PHE A 139
SHEET 3 D 4 SER A 161 ASN A 169 -1 O PHE A 163 N TRP A 149
SHEET 4 D 4 THR A 172 SER A 181 -1 O ILE A 180 N LEU A 162
SHEET 1 E 4 ASN A 195 HIS A 203 0
SHEET 2 E 4 LYS A 206 ALA A 213 -1 O PHE A 208 N ILE A 201
SHEET 3 E 4 CYS A 221 SER A 228 -1 O ALA A 227 N VAL A 207
SHEET 4 E 4 THR A 240 LYS A 241 -1 O THR A 240 N SER A 226
SHEET 1 F 3 TYR A 256 VAL A 265 0
SHEET 2 F 3 ASP A 272 ARG A 279 -1 O ARG A 279 N TYR A 256
SHEET 3 F 3 ARG A 295 LYS A 300 -1 O ARG A 297 N TYR A 276
SHEET 1 G 2 TYR A 302 TRP A 303 0
SHEET 2 G 2 PRO A 309 ASN A 310 -1 O ASN A 310 N TYR A 302
SHEET 1 H 2 PHE A 324 SER A 326 0
SHEET 2 H 2 PHE A 451 ALA A 453 -1 O TYR A 452 N SER A 325
SHEET 1 I 2 TYR A 333 TRP A 337 0
SHEET 2 I 2 ARG A 340 GLU A 344 -1 O GLU A 344 N TYR A 333
SHEET 1 J 2 PHE A 355 THR A 359 0
SHEET 2 J 2 ILE A 367 SER A 371 -1 O GLU A 370 N ARG A 356
SHEET 1 K 2 TYR A 377 LYS A 382 0
SHEET 2 K 2 GLU A 385 LYS A 390 -1 O TRP A 387 N ARG A 380
SHEET 1 L 2 PHE A 403 ALA A 407 0
SHEET 2 L 2 ILE A 416 SER A 420 -1 O GLU A 419 N SER A 404
SHEET 1 M 2 ARG A 426 TYR A 431 0
SHEET 2 M 2 LEU A 434 PRO A 439 -1 O GLN A 438 N TYR A 427
LINK O5 AHR B 1 C1 AHR B 2 1555 1555 1.45
LINK O5 AHR C 1 C1 AHR C 2 1555 1555 1.42
LINK O5 AHR D 1 C1 AHR D 2 1555 1555 1.45
LINK OE2 GLU A 79 NA NA A 502 1555 1555 2.21
LINK NA NA A 502 O HOH A 682 1555 1555 2.29
LINK NA NA A 502 O HOH A 690 1555 1555 2.19
LINK NA NA A 502 O HOH A 779 1555 1555 2.44
LINK NA NA A 502 O HOH A 827 1555 1555 2.27
CISPEP 1 ASN A 12 PRO A 13 0 4.18
CRYST1 41.237 91.341 135.962 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 0.024250 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010948 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007355 0.00000
(ATOM LINES ARE NOT SHOWN.)
END