HEADER HYDROLASE 11-SEP-09 3A72
TITLE HIGH RESOLUTION STRUCTURE OF PENICILLIUM CHRYSOGENUM ALPHA-L-
TITLE 2 ARABINANASE COMPLEXED WITH ARABINOBIOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXO-ARABINANASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 24-378;
COMPND 5 SYNONYM: EXO-1,5-ALPHA-L-ARABINANASE;
COMPND 6 EC: 3.2.1.55;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PENICILLIUM CHRYSOGENUM;
SOURCE 3 ORGANISM_COMMON: PENICILLIUM NOTATUM;
SOURCE 4 ORGANISM_TAXID: 5076;
SOURCE 5 STRAIN: 31B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS ARABINASE, GLYCOSYL HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.SOGABE
REVDAT 4 01-NOV-23 3A72 1 HETSYN LINK
REVDAT 3 29-JUL-20 3A72 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 25-MAY-11 3A72 1 JRNL
REVDAT 1 15-SEP-10 3A72 0
JRNL AUTH Y.SOGABE,T.KITATANI,A.YAMAGUCHI,T.KINOSHITA,H.ADACHI,
JRNL AUTH 2 K.TAKANO,T.INOUE,Y.MORI,H.MATSUMURA,T.SAKAMOTO,T.TADA
JRNL TITL HIGH-RESOLUTION STRUCTURE OF EXO-ARABINANASE FROM
JRNL TITL 2 PENICILLIUM CHRYSOGENUM
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 67 415 2011
JRNL REFN ISSN 0907-4449
JRNL PMID 21543843
JRNL DOI 10.1107/S0907444911006299
REMARK 2
REMARK 2 RESOLUTION. 1.04 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 186439
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.104
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : 0.125
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.263
REMARK 3 FREE R VALUE TEST SET COUNT : 9813
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) : 1.04
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.07
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13407
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE SET COUNT : 672
REMARK 3 BIN FREE R VALUE : 0.2540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2771
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 546
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 6.94
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.023
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.024
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.013
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.247
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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: ANISOTROPIC REFINEMENT REDUCED FREE R
REMARK 3 (NO CUTOFF)
REMARK 4
REMARK 4 3A72 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1000028892.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-DEC-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 SI(11
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 196659
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.040
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.36300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP, REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 3A71
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% MPD, 0.1M SODIUM ACETATE, PH 4.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.0K
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 33.47950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.78700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.55850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.78700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.47950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.55850
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 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 SER A 24
REMARK 465 SER A 25
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TYR A 41 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 LYS A 85 CD - CE - NZ ANGL. DEV. = 32.6 DEGREES
REMARK 500 TRP A 173 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 ARG A 192 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 TRP A 212 CD1 - NE1 - CE2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TYR A 247 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 GLU A 254 O - C - N ANGL. DEV. = -10.3 DEGREES
REMARK 500 THR A 255 C - N - CA ANGL. DEV. = 15.3 DEGREES
REMARK 500 ARG A 350 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 366 NE - CZ - NH1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 366 NE - CZ - NH2 ANGL. DEV. = 11.8 DEGREES
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 ARG A 45 -54.05 78.57
REMARK 500 TYR A 48 69.15 70.98
REMARK 500 LEU A 209 -0.89 68.53
REMARK 500 MET A 230 63.38 68.86
REMARK 500 SER A 289 146.67 77.35
REMARK 500 SER A 290 69.08 39.81
REMARK 500 ASN A 364 42.11 -140.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3A71 RELATED DB: PDB
DBREF 3A72 A 24 378 UNP Q7ZA77 Q7ZA77_PENCH 24 378
SEQRES 1 A 355 SER SER PRO THR SER LEU THR ASN VAL THR ILE PHE SER
SEQRES 2 A 355 PRO PRO SER ASP TYR ILE VAL PRO ARG THR LEU TYR PRO
SEQRES 3 A 355 ARG ASN GLU GLN LEU PRO ASN GLY ASP LEU LEU ALA THR
SEQRES 4 A 355 TRP GLU ASN TYR SER PRO GLU PRO PRO ALA VAL TYR PHE
SEQRES 5 A 355 PRO ILE TYR ARG SER LYS ASP HIS GLY LYS THR TRP ASN
SEQRES 6 A 355 GLU ILE SER ARG VAL HIS ASP THR VAL ASN GLY TYR GLY
SEQRES 7 A 355 LEU ARG TYR GLN PRO PHE LEU TYR SER LEU PRO GLU ARG
SEQRES 8 A 355 VAL GLY SER PHE LYS LYS GLY THR LEU LEU LEU ALA GLY
SEQRES 9 A 355 SER SER ILE PRO THR ASP LEU SER SER THR ASP ILE VAL
SEQRES 10 A 355 LEU TYR ALA SER GLN ASP ASP GLY MET THR TRP ASP PHE
SEQRES 11 A 355 VAL SER HIS ILE ALA ALA GLY GLY GLU ALA ARG PRO ASN
SEQRES 12 A 355 ASN GLY LEU THR PRO VAL TRP GLU PRO PHE LEU LEU ALA
SEQRES 13 A 355 ASN LYS GLY LYS LEU ILE CYS TYR TYR SER ASP GLN ARG
SEQRES 14 A 355 ASP ASN ALA THR TYR GLY GLN THR MET VAL HIS GLN VAL
SEQRES 15 A 355 THR ASN ASP LEU LYS ASN TRP GLY PRO VAL VAL GLU ASP
SEQRES 16 A 355 VAL THR TYR PRO THR TYR THR ASP ARG PRO GLY MET PRO
SEQRES 17 A 355 VAL VAL THR LYS LEU PRO ASN GLY GLN TYR PHE TYR VAL
SEQRES 18 A 355 TYR GLU TYR GLY SER PHE PHE GLY THR GLU THR TYR SER
SEQRES 19 A 355 PHE PRO LEU TYR TYR ARG LEU SER SER ASP PRO GLU ASN
SEQRES 20 A 355 ILE ALA SER ALA PRO GLY GLN ARG LEU VAL VAL SER SER
SEQRES 21 A 355 GLY THR GLN PRO THR SER SER PRO TYR ALA VAL TRP THR
SEQRES 22 A 355 PRO TYR GLY GLY GLU ASN GLY THR ILE ILE VAL SER SER
SEQRES 23 A 355 GLY THR GLN GLY THR LEU PHE ILE ASN LYS ALA LEU GLY
SEQRES 24 A 355 GLU GLY GLU TRP THR GLU ILE PRO CYS PRO GLU GLU HIS
SEQRES 25 A 355 GLY TYR THR ARG ALA LEU ARG VAL LEU SER GLU ASP GLY
SEQRES 26 A 355 GLY ARG TYR LEU VAL VAL ASN SER ALA GLY VAL LEU LEU
SEQRES 27 A 355 GLY GLU ASN ASN ARG VAL SER VAL SER VAL MET ASP LEU
SEQRES 28 A 355 LYS GLU VAL LEU
HET AHR B 1 10
HET AHR B 2 9
HETNAM AHR ALPHA-L-ARABINOFURANOSE
HETSYN AHR ALPHA-L-ARABINOSE; L-ARABINOSE; ARABINOSE
FORMUL 2 AHR 2(C5 H10 O5)
FORMUL 3 HOH *546(H2 O)
HELIX 1 1 SER A 345 ARG A 350 1 6
HELIX 2 2 LEU A 374 LEU A 378 1 5
SHEET 1 A 4 LEU A 29 PHE A 35 0
SHEET 2 A 4 VAL A 367 ASP A 373 -1 O VAL A 367 N PHE A 35
SHEET 3 A 4 TYR A 351 SER A 356 -1 N VAL A 354 O SER A 370
SHEET 4 A 4 ALA A 340 VAL A 343 -1 N ARG A 342 O VAL A 353
SHEET 1 B 4 THR A 46 GLN A 53 0
SHEET 2 B 4 LEU A 59 ASN A 65 -1 O GLU A 64 N LEU A 47
SHEET 3 B 4 PHE A 75 SER A 80 -1 O TYR A 78 N ALA A 61
SHEET 4 B 4 ASN A 88 VAL A 93 -1 O ILE A 90 N ILE A 77
SHEET 1 C 4 LEU A 102 SER A 110 0
SHEET 2 C 4 LEU A 123 SER A 129 -1 O SER A 128 N TYR A 104
SHEET 3 C 4 THR A 137 SER A 144 -1 O ASP A 138 N SER A 129
SHEET 4 C 4 ASP A 152 GLY A 160 -1 O ILE A 157 N ILE A 139
SHEET 1 D 4 VAL A 172 ASN A 180 0
SHEET 2 D 4 LYS A 183 ASP A 190 -1 O ILE A 185 N LEU A 178
SHEET 3 D 4 THR A 200 THR A 206 -1 O THR A 200 N ASP A 190
SHEET 4 D 4 VAL A 216 VAL A 219 -1 O VAL A 216 N HIS A 203
SHEET 1 E 4 ARG A 227 LYS A 235 0
SHEET 2 E 4 TYR A 241 GLY A 248 -1 O VAL A 244 N VAL A 232
SHEET 3 E 4 LEU A 260 SER A 265 -1 O SER A 265 N TYR A 241
SHEET 4 E 4 GLN A 277 ARG A 278 -1 O GLN A 277 N TYR A 262
SHEET 1 F 4 TYR A 292 THR A 296 0
SHEET 2 F 4 THR A 304 SER A 308 -1 O ILE A 306 N VAL A 294
SHEET 3 F 4 LEU A 315 ASN A 318 -1 O ASN A 318 N ILE A 305
SHEET 4 F 4 THR A 327 ILE A 329 -1 O ILE A 329 N LEU A 315
LINK O5 AHR B 1 C1 AHR B 2 1555 1555 1.41
CISPEP 1 VAL A 43 PRO A 44 0 14.90
CISPEP 2 GLU A 69 PRO A 70 0 -4.54
CISPEP 3 PRO A 70 PRO A 71 0 -2.84
CRYST1 66.959 77.117 79.574 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 0.014935 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012967 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012567 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
