HEADER HYDROLASE 27-JUL-07 2QQW
TITLE CRYSTAL STRUCTURE OF A CELL-WALL INVERTASE (D23A) FROM ARABIDOPSIS
TITLE 2 THALIANA IN COMPLEX WITH SUCROSE
CAVEAT 2QQW MAN B 3 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-FRUCTOFURANOSIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PUTATIVE BETA-FRUCTOFURANOSIDASE 1;
COMPND 5 EC: 3.2.1.26;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: ATBFRUCT1;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS HYDROLASE, INVERTASE, GLYCOSIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.LAMMENS,K.LE ROY,A.VAN LAERE,A.RABIJNS,W.VAN DEN ENDE
REVDAT 7 30-AUG-23 2QQW 1 REMARK
REVDAT 6 20-OCT-21 2QQW 1 SEQADV HETSYN
REVDAT 5 29-JUL-20 2QQW 1 CAVEAT COMPND REMARK HET
REVDAT 5 2 1 HETNAM FORMUL LINK SITE
REVDAT 5 3 1 ATOM
REVDAT 4 25-OCT-17 2QQW 1 REMARK
REVDAT 3 13-JUL-11 2QQW 1 VERSN
REVDAT 2 24-FEB-09 2QQW 1 VERSN
REVDAT 1 22-APR-08 2QQW 0
JRNL AUTH W.LAMMENS,K.LE ROY,A.VAN LAERE,A.RABIJNS,W.VAN DEN ENDE
JRNL TITL CRYSTAL STRUCTURES OF ARABIDOPSIS THALIANA CELL-WALL
JRNL TITL 2 INVERTASE MUTANTS IN COMPLEX WITH SUCROSE.
JRNL REF J.MOL.BIOL. V. 377 378 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18258263
JRNL DOI 10.1016/J.JMB.2007.12.074
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 12825
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 776
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1093
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3510
REMARK 3 BIN FREE R VALUE SET COUNT : 61
REMARK 3 BIN FREE R VALUE : 0.4220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4287
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 141
REMARK 3 SOLVENT ATOMS : 19
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.50
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) : 0.01000
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): 0.395
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.300
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.384
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4561 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6212 ; 1.333 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 532 ; 6.065 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 204 ;37.206 ;23.873
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 731 ;17.367 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;14.211 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 676 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3420 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2027 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3059 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 164 ; 0.149 ; 0.200
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): 21 ; 0.209 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.163 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 1 ; 0.020 ; 0.200
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): 2719 ; 0.495 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4323 ; 0.894 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2121 ; 0.905 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1889 ; 1.533 ; 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 2QQW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1000043942.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 1.0332
REMARK 200 MONOCHROMATOR : FIXED EXIT DOUBLE CRYSTAL SI
REMARK 200 [111], HORIZONTALLY FOCUSSING
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12825
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.410
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
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) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2AC1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CACODYLATE, 0.1M ZINC
REMARK 280 ACETATE, 22.5% PEG 8000, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.65267
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 16.82633
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 LYS A 265
REMARK 465 MET A 266
REMARK 465 ASP A 267
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 LEU A 530 CA - CB - CG ANGL. DEV. = 16.4 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 PHE A 12 14.81 -147.35
REMARK 500 ASN A 19 -175.02 78.21
REMARK 500 ASN A 22 -131.15 -126.26
REMARK 500 LEU A 60 -2.54 72.80
REMARK 500 SER A 73 -9.76 -151.82
REMARK 500 ASP A 77 18.85 -146.90
REMARK 500 LEU A 122 55.98 33.96
REMARK 500 SER A 146 60.18 -151.46
REMARK 500 PHE A 147 77.92 -151.30
REMARK 500 ASP A 149 71.35 67.18
REMARK 500 HIS A 170 -88.16 -125.90
REMARK 500 LEU A 184 -30.56 -133.07
REMARK 500 CYS A 204 59.25 38.21
REMARK 500 ASN A 352 54.96 32.46
REMARK 500 LEU A 418 55.51 39.13
REMARK 500 ARG A 437 35.94 -76.54
REMARK 500 ASN A 441 41.14 -90.58
REMARK 500 HIS A 485 -66.76 64.15
REMARK 500 ASN A 519 107.88 -164.67
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 ZN A1102 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 194 NE2
REMARK 620 2 ASP A 196 OD1 111.9
REMARK 620 3 ASP A 196 OD2 105.8 56.0
REMARK 620 N 1 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AC1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A CELL-WALL INVERTASE FROM ARABIDOPSIS THALIANA
REMARK 900 RELATED ID: 2OXB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A CELL-WALL INVERTASE (E203Q) FROM ARABIDOPSIS
REMARK 900 THALIANA IN COMPLEX WITH SUCROSE
REMARK 900 RELATED ID: 2QQV RELATED DB: PDB
DBREF 2QQW A 5 541 UNP Q43866 Q43866_ARATH 48 584
SEQADV 2QQW ALA A 23 UNP Q43866 ASP 66 ENGINEERED MUTATION
SEQRES 1 A 537 ASN GLN PRO TYR ARG THR GLY PHE HIS PHE GLN PRO PRO
SEQRES 2 A 537 LYS ASN TRP MET ASN ALA PRO ASN GLY PRO MET ILE TYR
SEQRES 3 A 537 LYS GLY ILE TYR HIS LEU PHE TYR GLN TRP ASN PRO LYS
SEQRES 4 A 537 GLY ALA VAL TRP GLY ASN ILE VAL TRP ALA HIS SER THR
SEQRES 5 A 537 SER THR ASP LEU ILE ASN TRP ASP PRO HIS PRO PRO ALA
SEQRES 6 A 537 ILE PHE PRO SER ALA PRO PHE ASP ILE ASN GLY CYS TRP
SEQRES 7 A 537 SER GLY SER ALA THR ILE LEU PRO ASN GLY LYS PRO VAL
SEQRES 8 A 537 ILE LEU TYR THR GLY ILE ASP PRO LYS ASN GLN GLN VAL
SEQRES 9 A 537 GLN ASN ILE ALA GLU PRO LYS ASN LEU SER ASP PRO TYR
SEQRES 10 A 537 LEU ARG GLU TRP LYS LYS SER PRO LEU ASN PRO LEU MET
SEQRES 11 A 537 ALA PRO ASP ALA VAL ASN GLY ILE ASN ALA SER SER PHE
SEQRES 12 A 537 ARG ASP PRO THR THR ALA TRP LEU GLY GLN ASP LYS LYS
SEQRES 13 A 537 TRP ARG VAL ILE ILE GLY SER LYS ILE HIS ARG ARG GLY
SEQRES 14 A 537 LEU ALA ILE THR TYR THR SER LYS ASP PHE LEU LYS TRP
SEQRES 15 A 537 GLU LYS SER PRO GLU PRO LEU HIS TYR ASP ASP GLY SER
SEQRES 16 A 537 GLY MET TRP GLU CYS PRO ASP PHE PHE PRO VAL THR ARG
SEQRES 17 A 537 PHE GLY SER ASN GLY VAL GLU THR SER SER PHE GLY GLU
SEQRES 18 A 537 PRO ASN GLU ILE LEU LYS HIS VAL LEU LYS ILE SER LEU
SEQRES 19 A 537 ASP ASP THR LYS HIS ASP TYR TYR THR ILE GLY THR TYR
SEQRES 20 A 537 ASP ARG VAL LYS ASP LYS PHE VAL PRO ASP ASN GLY PHE
SEQRES 21 A 537 LYS MET ASP GLY THR ALA PRO ARG TYR ASP TYR GLY LYS
SEQRES 22 A 537 TYR TYR ALA SER LYS THR PHE PHE ASP SER ALA LYS ASN
SEQRES 23 A 537 ARG ARG ILE LEU TRP GLY TRP THR ASN GLU SER SER SER
SEQRES 24 A 537 VAL GLU ASP ASP VAL GLU LYS GLY TRP SER GLY ILE GLN
SEQRES 25 A 537 THR ILE PRO ARG LYS ILE TRP LEU ASP ARG SER GLY LYS
SEQRES 26 A 537 GLN LEU ILE GLN TRP PRO VAL ARG GLU VAL GLU ARG LEU
SEQRES 27 A 537 ARG THR LYS GLN VAL LYS ASN LEU ARG ASN LYS VAL LEU
SEQRES 28 A 537 LYS SER GLY SER ARG LEU GLU VAL TYR GLY VAL THR ALA
SEQRES 29 A 537 ALA GLN ALA ASP VAL GLU VAL LEU PHE LYS VAL ARG ASP
SEQRES 30 A 537 LEU GLU LYS ALA ASP VAL ILE GLU PRO SER TRP THR ASP
SEQRES 31 A 537 PRO GLN LEU ILE CYS SER LYS MET ASN VAL SER VAL LYS
SEQRES 32 A 537 SER GLY LEU GLY PRO PHE GLY LEU MET VAL LEU ALA SER
SEQRES 33 A 537 LYS ASN LEU GLU GLU TYR THR SER VAL TYR PHE ARG ILE
SEQRES 34 A 537 PHE LYS ALA ARG GLN ASN SER ASN LYS TYR VAL VAL LEU
SEQRES 35 A 537 MET CYS SER ASP GLN SER ARG SER SER LEU LYS GLU ASP
SEQRES 36 A 537 ASN ASP LYS THR THR TYR GLY ALA PHE VAL ASP ILE ASN
SEQRES 37 A 537 PRO HIS GLN PRO LEU SER LEU ARG ALA LEU ILE ASP HIS
SEQRES 38 A 537 SER VAL VAL GLU SER PHE GLY GLY LYS GLY ARG ALA CYS
SEQRES 39 A 537 ILE THR SER ARG VAL TYR PRO LYS LEU ALA ILE GLY LYS
SEQRES 40 A 537 SER SER HIS LEU PHE ALA PHE ASN TYR GLY TYR GLN SER
SEQRES 41 A 537 VAL ASP VAL LEU ASN LEU ASN ALA TRP SER MET ASN SER
SEQRES 42 A 537 ALA GLN ILE SER
MODRES 2QQW ASN A 116 ASN GLYCOSYLATION SITE
MODRES 2QQW ASN A 143 ASN GLYCOSYLATION SITE
MODRES 2QQW ASN A 299 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET MAN B 3 11
HET MAN B 4 11
HET MAN B 5 11
HET MAN B 6 11
HET NAG C 1 14
HET NAG C 2 14
HET GLC D 1 11
HET FRU D 2 12
HET NAG A 770 14
HET ZN A1101 1
HET ZN A1102 1
HET ZN A1103 1
HET ZN A1104 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM FRU BETA-D-FRUCTOFURANOSE
HETNAM ZN ZINC ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN FRU BETA-D-FRUCTOSE; D-FRUCTOSE; FRUCTOSE
FORMUL 2 NAG 5(C8 H15 N O6)
FORMUL 2 MAN 4(C6 H12 O6)
FORMUL 4 GLC C6 H12 O6
FORMUL 4 FRU C6 H12 O6
FORMUL 6 ZN 4(ZN 2+)
FORMUL 10 HOH *19(H2 O)
HELIX 1 1 SER A 303 GLY A 311 1 9
HELIX 2 2 ARG A 337 ARG A 343 5 7
HELIX 3 3 ASP A 381 ALA A 385 5 5
HELIX 4 4 ASP A 394 MET A 402 1 9
HELIX 5 5 ILE A 509 SER A 513 5 5
SHEET 1 A 5 ASP A 64 ILE A 70 0
SHEET 2 A 5 VAL A 51 SER A 57 -1 N THR A 56 O ASP A 64
SHEET 3 A 5 ILE A 33 ASN A 41 -1 N TRP A 40 O VAL A 51
SHEET 4 A 5 ASN A 19 TYR A 30 -1 N ASN A 25 O PHE A 37
SHEET 5 A 5 TRP A 312 SER A 313 1 O SER A 313 N MET A 21
SHEET 1 B 4 CYS A 81 ILE A 88 0
SHEET 2 B 4 PRO A 94 ILE A 101 -1 O VAL A 95 N THR A 87
SHEET 3 B 4 GLN A 107 PRO A 114 -1 O ASN A 110 N TYR A 98
SHEET 4 B 4 TRP A 125 LYS A 127 -1 O LYS A 126 N GLU A 113
SHEET 1 C 4 PHE A 147 PRO A 150 0
SHEET 2 C 4 TRP A 161 LYS A 168 -1 O GLY A 166 N ARG A 148
SHEET 3 C 4 GLY A 173 SER A 180 -1 O SER A 180 N TRP A 161
SHEET 4 C 4 TRP A 186 LYS A 188 -1 O GLU A 187 N THR A 179
SHEET 1 D 4 TRP A 154 LEU A 155 0
SHEET 2 D 4 TRP A 161 LYS A 168 -1 O ARG A 162 N TRP A 154
SHEET 3 D 4 GLY A 173 SER A 180 -1 O SER A 180 N TRP A 161
SHEET 4 D 4 TYR A 195 ASP A 196 -1 O ASP A 196 N GLY A 173
SHEET 1 E 4 TRP A 202 THR A 211 0
SHEET 2 E 4 LEU A 230 LEU A 238 -1 O SER A 237 N GLU A 203
SHEET 3 E 4 HIS A 243 ASP A 252 -1 O GLY A 249 N HIS A 232
SHEET 4 E 4 LYS A 257 PRO A 260 -1 O VAL A 259 N THR A 250
SHEET 1 F 3 TYR A 279 ASP A 286 0
SHEET 2 F 3 ARG A 291 THR A 298 -1 O TRP A 295 N LYS A 282
SHEET 3 F 3 ILE A 315 GLN A 316 -1 O ILE A 315 N THR A 298
SHEET 1 G 4 TYR A 279 ASP A 286 0
SHEET 2 G 4 ARG A 291 THR A 298 -1 O TRP A 295 N LYS A 282
SHEET 3 G 4 ARG A 320 LEU A 324 -1 O ARG A 320 N LEU A 294
SHEET 4 G 4 LEU A 331 PRO A 335 -1 O TRP A 334 N LYS A 321
SHEET 1 H 6 LYS A 348 LEU A 355 0
SHEET 2 H 6 VAL A 525 SER A 534 -1 O VAL A 527 N LYS A 353
SHEET 3 H 6 GLN A 370 LYS A 378 -1 N ASP A 372 O TRP A 533
SHEET 4 H 6 LEU A 477 ASP A 484 -1 O ILE A 483 N ALA A 371
SHEET 5 H 6 VAL A 487 GLY A 492 -1 O PHE A 491 N ARG A 480
SHEET 6 H 6 ALA A 497 ARG A 502 -1 O ILE A 499 N SER A 490
SHEET 1 I 5 SER A 359 VAL A 363 0
SHEET 2 I 5 HIS A 514 ASN A 519 -1 O LEU A 515 N VAL A 363
SHEET 3 I 5 LEU A 410 ALA A 419 -1 N MET A 416 O PHE A 516
SHEET 4 I 5 THR A 427 LYS A 435 -1 O THR A 427 N VAL A 417
SHEET 5 I 5 ASP A 386 VAL A 387 1 N ASP A 386 O LYS A 435
SHEET 1 J 6 SER A 359 VAL A 363 0
SHEET 2 J 6 HIS A 514 ASN A 519 -1 O LEU A 515 N VAL A 363
SHEET 3 J 6 LEU A 410 ALA A 419 -1 N MET A 416 O PHE A 516
SHEET 4 J 6 THR A 427 LYS A 435 -1 O THR A 427 N VAL A 417
SHEET 5 J 6 TYR A 443 ASP A 450 -1 O ASP A 450 N SER A 428
SHEET 6 J 6 TYR A 465 VAL A 469 -1 O TYR A 465 N SER A 449
SSBOND 1 CYS A 399 CYS A 448 1555 1555 2.04
LINK ND2 ASN A 116 C1 NAG A 770 1555 1555 1.44
LINK ND2 ASN A 143 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN A 299 C1 NAG B 1 1555 1555 1.43
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.43
LINK O4 NAG B 2 C1 MAN B 3 1555 1555 1.45
LINK O6 MAN B 3 C1 MAN B 4 1555 1555 1.43
LINK O3 MAN B 3 C1 MAN B 6 1555 1555 1.46
LINK O2 MAN B 4 C1 MAN B 5 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.46
LINK C1 GLC D 1 O2 FRU D 2 1555 1555 1.43
LINK OD2 ASP A 64 ZN ZN A1104 1555 1555 2.26
LINK NE2 HIS A 194 ZN ZN A1102 1555 1555 2.29
LINK OD1 ASP A 196 ZN ZN A1102 1555 1555 2.31
LINK OD2 ASP A 196 ZN ZN A1102 1555 1555 2.36
LINK NE2 HIS A 474 ZN ZN A1101 1555 1555 2.19
CISPEP 1 ASN A 131 PRO A 132 0 -1.66
CISPEP 2 ASN A 262 GLY A 263 0 0.56
CISPEP 3 GLY A 263 PHE A 264 0 -12.49
CISPEP 4 GLY A 268 THR A 269 0 3.20
CISPEP 5 GLY A 411 PRO A 412 0 3.14
CRYST1 105.877 105.877 50.479 90.00 90.00 120.00 P 32 3
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 0.009445 0.005453 0.000000 0.00000
SCALE2 0.000000 0.010906 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019810 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
