HEADER ALPHA-AMYLASE 30-JAN-98 1BAG
TITLE ALPHA-AMYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH MALTOPENTAOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA-AMYLASE;
COMPND 5 EC: 3.2.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: COMPLEXED WITH MALTOPENTAOSE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: AMY;
SOURCE 5 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 1423;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: 207-25;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PUB110;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTUB111;
SOURCE 11 EXPRESSION_SYSTEM_GENE: AMY
KEYWDS ALPHA-AMYLASE, BACILLUS SUBTILIS, MALTOPENTAOSE, CATALYTIC-SITE
KEYWDS 2 MUTANT
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.FUJIMOTO,H.MIZUNO,K.TAKASE,N.DOUI
REVDAT 6 07-FEB-24 1BAG 1 REMARK
REVDAT 5 03-NOV-21 1BAG 1 SEQADV HETSYN
REVDAT 4 29-JUL-20 1BAG 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 04-AUG-09 1BAG 1 ATOM COMPND CONECT HET
REVDAT 3 2 1 HETATM HETNAM LINK SITE
REVDAT 2 24-FEB-09 1BAG 1 VERSN
REVDAT 1 21-OCT-98 1BAG 0
JRNL AUTH Z.FUJIMOTO,K.TAKASE,N.DOUI,M.MOMMA,T.MATSUMOTO,H.MIZUNO
JRNL TITL CRYSTAL STRUCTURE OF A CATALYTIC-SITE MUTANT ALPHA-AMYLASE
JRNL TITL 2 FROM BACILLUS SUBTILIS COMPLEXED WITH MALTOPENTAOSE.
JRNL REF J.MOL.BIOL. V. 277 393 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9514750
JRNL DOI 10.1006/JMBI.1997.1599
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.MIZUNO,Y.MORIMOTO,T.TSUKIHARA,T.MATSUMOTO,K.TAKASE
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES OF WILD TYPE
REMARK 1 TITL 2 AND CATALYTIC-SITE MUTANT ALPHA-AMYLASE FROM BACILLUS
REMARK 1 TITL 3 SUBTILIS
REMARK 1 REF J.MOL.BIOL. V. 234 1282 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.TAKASE,T.MATSUMOTO,H.MIZUNO,K.YAMANE
REMARK 1 TITL SITE-DIRECTED MUTAGENESIS OF ACTIVE SITE RESIDUES IN
REMARK 1 TITL 2 BACILLUS SUBTILIS ALPHA-AMYLASE
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1120 281 1992
REMARK 1 REFN ISSN 0006-3002
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.YAMANE,Y.HIRATA,T.FURUSATO,H.YAMAZAKI,A.NAKAYAMA
REMARK 1 TITL CHANGES IN THE PROPERTIES AND MOLECULAR WEIGHTS OF BACILLUS
REMARK 1 TITL 2 SUBTILIS M-TYPE AND N-TYPE ALPHA-AMYLASES RESULTING FROM A
REMARK 1 TITL 3 SPONTANEOUS DELETION
REMARK 1 REF J.BIOCHEM.(TOKYO) V. 96 1849 1984
REMARK 1 REFN ISSN 0021-924X
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 80.4
REMARK 3 NUMBER OF REFLECTIONS : 17162
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) : 0.198
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1676
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.65
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 49.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1563
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 174
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3322
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 59
REMARK 3 SOLVENT ATOMS : 146
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.33
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.51
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.210
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) : 3.240 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.420 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.440 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.800 ; 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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM3.CHO
REMARK 3 PARAMETER FILE 3 : PARAM19X.ION
REMARK 3 PARAMETER FILE 4 : PARAM19.SOL
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH3.CHO
REMARK 3 TOPOLOGY FILE 3 : TOPH19X.ION
REMARK 3 TOPOLOGY FILE 4 : TOPH19X.SOL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BAG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171525.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : OCT-95
REMARK 200 TEMPERATURE (KELVIN) : 288
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 4
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19373
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 80.4
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 44.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.19000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 10% PEG
REMARK 280 3350, 3.5 MM CALCIUM CHLORIDE, 10 MM TRIS/HCL, PH 7.5.
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 36.29500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.50500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.03000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.50500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.29500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.03000
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 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: 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 TYR A 67 34.99 -95.08
REMARK 500 THR A 103 -167.35 -123.85
REMARK 500 GLU A 182 159.65 -49.87
REMARK 500 THR A 200 -167.97 -120.80
REMARK 500 ASP A 212 -161.33 -172.13
REMARK 500 ALA A 214 34.05 -98.89
REMARK 500 LEU A 244 37.23 -90.45
REMARK 500 ILE A 249 35.49 -90.28
REMARK 500 MET A 281 170.00 -49.95
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 433 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 89 OE2
REMARK 620 2 GLU A 276 OE2 73.9
REMARK 620 3 GLU A 276 OE1 122.1 50.2
REMARK 620 4 GLY A 313 O 87.2 94.4 83.6
REMARK 620 5 HOH A 494 O 148.4 137.7 88.8 90.0
REMARK 620 6 HOH A 524 O 85.9 70.9 88.8 165.1 102.7
REMARK 620 7 HOH A 526 O 70.4 144.3 163.1 85.8 78.0 104.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 431 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 101 OD1
REMARK 620 2 THR A 137 O 142.6
REMARK 620 3 ASP A 146 OD1 80.6 113.7
REMARK 620 4 ASP A 146 OD2 127.9 75.2 47.3
REMARK 620 5 HIS A 180 O 69.4 80.7 141.8 154.3
REMARK 620 6 HOH A 509 O 122.0 73.2 135.2 99.1 82.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 432 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 169 O
REMARK 620 2 ASP A 171 OD2 80.8
REMARK 620 3 ASP A 171 OD1 92.7 49.7
REMARK 620 4 HOH A 470 O 165.8 97.8 76.0
REMARK 620 5 HOH A 482 O 76.5 111.0 67.4 91.0
REMARK 620 6 HOH A 538 O 96.3 147.1 162.3 92.6 99.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CA1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE (ADVENTITIOUS).
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE (ADVENTITIOUS).
DBREF 1BAG A 1 425 UNP P00691 AMY_BACSU 42 466
SEQADV 1BAG PHE A 105 UNP P00691 SER 146 VARIANT
SEQADV 1BAG GLU A 163 UNP P00691 ASP 204 VARIANT
SEQADV 1BAG GLN A 208 UNP P00691 GLU 249 ENGINEERED MUTATION
SEQRES 1 A 425 LEU THR ALA PRO SER ILE LYS SER GLY THR ILE LEU HIS
SEQRES 2 A 425 ALA TRP ASN TRP SER PHE ASN THR LEU LYS HIS ASN MET
SEQRES 3 A 425 LYS ASP ILE HIS ASP ALA GLY TYR THR ALA ILE GLN THR
SEQRES 4 A 425 SER PRO ILE ASN GLN VAL LYS GLU GLY ASN GLN GLY ASP
SEQRES 5 A 425 LYS SER MET SER ASN TRP TYR TRP LEU TYR GLN PRO THR
SEQRES 6 A 425 SER TYR GLN ILE GLY ASN ARG TYR LEU GLY THR GLU GLN
SEQRES 7 A 425 GLU PHE LYS GLU MET CYS ALA ALA ALA GLU GLU TYR GLY
SEQRES 8 A 425 ILE LYS VAL ILE VAL ASP ALA VAL ILE ASN HIS THR THR
SEQRES 9 A 425 PHE ASP TYR ALA ALA ILE SER ASN GLU VAL LYS SER ILE
SEQRES 10 A 425 PRO ASN TRP THR HIS GLY ASN THR GLN ILE LYS ASN TRP
SEQRES 11 A 425 SER ASP ARG TRP ASP VAL THR GLN ASN SER LEU LEU GLY
SEQRES 12 A 425 LEU TYR ASP TRP ASN THR GLN ASN THR GLN VAL GLN SER
SEQRES 13 A 425 TYR LEU LYS ARG PHE LEU GLU ARG ALA LEU ASN ASP GLY
SEQRES 14 A 425 ALA ASP GLY PHE ARG PHE ASP ALA ALA LYS HIS ILE GLU
SEQRES 15 A 425 LEU PRO ASP ASP GLY SER TYR GLY SER GLN PHE TRP PRO
SEQRES 16 A 425 ASN ILE THR ASN THR SER ALA GLU PHE GLN TYR GLY GLN
SEQRES 17 A 425 ILE LEU GLN ASP SER ALA SER ARG ASP ALA ALA TYR ALA
SEQRES 18 A 425 ASN TYR MET ASP VAL THR ALA SER ASN TYR GLY HIS SER
SEQRES 19 A 425 ILE ARG SER ALA LEU LYS ASN ARG ASN LEU GLY VAL SER
SEQRES 20 A 425 ASN ILE SER HIS TYR ALA SER ASP VAL SER ALA ASP LYS
SEQRES 21 A 425 LEU VAL THR TRP VAL GLU SER HIS ASP THR TYR ALA ASN
SEQRES 22 A 425 ASP ASP GLU GLU SER THR TRP MET SER ASP ASP ASP ILE
SEQRES 23 A 425 ARG LEU GLY TRP ALA VAL ILE ALA SER ARG SER GLY SER
SEQRES 24 A 425 THR PRO LEU PHE PHE SER ARG PRO GLU GLY GLY GLY ASN
SEQRES 25 A 425 GLY VAL ARG PHE PRO GLY LYS SER GLN ILE GLY ASP ARG
SEQRES 26 A 425 GLY SER ALA LEU PHE GLU ASP GLN ALA ILE THR ALA VAL
SEQRES 27 A 425 ASN ARG PHE HIS ASN VAL MET ALA GLY GLN PRO GLU GLU
SEQRES 28 A 425 LEU SER ASN PRO ASN GLY ASN ASN GLN ILE PHE MET ASN
SEQRES 29 A 425 GLN ARG GLY SER HIS GLY VAL VAL LEU ALA ASN ALA GLY
SEQRES 30 A 425 SER SER SER VAL SER ILE ASN THR ALA THR LYS LEU PRO
SEQRES 31 A 425 ASP GLY ARG TYR ASP ASN LYS ALA GLY ALA GLY SER PHE
SEQRES 32 A 425 GLN VAL ASN ASP GLY LYS LEU THR GLY THR ILE ASN ALA
SEQRES 33 A 425 ARG SER VAL ALA VAL LEU TYR PRO ASP
HET BGC B 1 12
HET GLC B 2 11
HET GLC B 3 11
HET GLC B 4 11
HET GLC B 5 11
HET CA A 431 1
HET CA A 432 1
HET CA A 433 1
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM CA CALCIUM ION
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 2 BGC C6 H12 O6
FORMUL 2 GLC 4(C6 H12 O6)
FORMUL 3 CA 3(CA 2+)
FORMUL 6 HOH *146(H2 O)
HELIX 1 AA1 PHE A 19 ASP A 31 1 13
HELIX 2 AA2 GLU A 77 GLU A 89 1 13
HELIX 3 BH1 ASN A 112 LYS A 115 1 4
HELIX 4 BA1 ARG A 133 GLN A 138 1 6
HELIX 5 AA3 THR A 152 ASP A 168 1 17
HELIX 6 AA4 PHE A 193 ILE A 197 1 5
HELIX 7 AA5 ASP A 217 TYR A 223 1 7
HELIX 8 AA6 SER A 229 LEU A 244 1 16
HELIX 9 AH1 HIS A 268 ALA A 272 1 5
HELIX 10 AA7 ASP A 283 ALA A 294 1 12
HELIX 11 AA8 ASP A 332 VAL A 344 1 13
SHEET 1 AS1 8 ILE A 11 HIS A 13 0
SHEET 2 AS1 8 ALA A 36 GLN A 38 1 N GLN A 38 O LEU A 12
SHEET 3 AS1 8 LYS A 93 ALA A 98 1 N ILE A 95 O ILE A 37
SHEET 4 AS1 8 GLY A 172 PHE A 175 1 N ARG A 174 O VAL A 96
SHEET 5 AS1 8 PHE A 204 GLY A 207 1 N TYR A 206 O PHE A 173
SHEET 6 AS1 8 ASP A 225 THR A 227 1 N ASP A 225 O GLN A 205
SHEET 7 AS1 8 LEU A 261 THR A 263 1 N VAL A 262 O VAL A 226
SHEET 8 AS1 8 THR A 300 PHE A 304 1 N THR A 300 O LEU A 261
SHEET 1 AS2 2 ASN A 43 VAL A 45 0
SHEET 2 AS2 2 PRO A 64 TYR A 67 -1 N SER A 66 O GLN A 44
SHEET 1 AS3 2 ILE A 69 ASN A 71 0
SHEET 2 AS3 2 GLY A 75 THR A 76 -1 N GLY A 75 O ASN A 71
SHEET 1 BS1 3 HIS A 102 THR A 103 0
SHEET 2 BS1 3 TYR A 145 TRP A 147 -1 N TYR A 145 O THR A 103
SHEET 3 BS1 3 THR A 121 GLY A 123 -1 N GLY A 123 O ASP A 146
SHEET 1 CS1 4 GLU A 350 SER A 353 0
SHEET 2 CS1 4 ILE A 361 ARG A 366 -1 N GLN A 365 O GLU A 351
SHEET 3 CS1 4 GLY A 370 ASN A 375 -1 N VAL A 372 O ASN A 364
SHEET 4 CS1 4 SER A 418 LEU A 422 -1 N ALA A 420 O LEU A 373
SHEET 1 CS2 4 VAL A 381 ALA A 386 0
SHEET 2 CS2 4 LYS A 409 ILE A 414 -1 N LEU A 410 O THR A 385
SHEET 3 CS2 4 SER A 402 ASN A 406 -1 N GLN A 404 O THR A 411
SHEET 4 CS2 4 GLY A 392 ASP A 395 -1
LINK O4 BGC B 1 C1 GLC B 2 1555 1555 1.40
LINK O4 GLC B 2 C1 GLC B 3 1555 1555 1.42
LINK O4 GLC B 3 C1 GLC B 4 1555 1555 1.39
LINK O4 GLC B 4 C1 GLC B 5 1555 1555 1.40
LINK OE2 GLU A 89 CA CA A 433 3555 1555 2.71
LINK OD1 ASN A 101 CA CA A 431 1555 1555 2.45
LINK O THR A 137 CA CA A 431 1555 1555 2.43
LINK OD1 ASP A 146 CA CA A 431 1555 1555 2.52
LINK OD2 ASP A 146 CA CA A 431 1555 1555 2.90
LINK O GLY A 169 CA CA A 432 1555 1555 2.31
LINK OD2 ASP A 171 CA CA A 432 1555 1555 2.59
LINK OD1 ASP A 171 CA CA A 432 1555 1555 2.60
LINK O HIS A 180 CA CA A 431 1555 1555 2.34
LINK OE2 GLU A 276 CA CA A 433 1555 1555 2.56
LINK OE1 GLU A 276 CA CA A 433 1555 1555 2.60
LINK O GLY A 313 CA CA A 433 1555 1555 2.32
LINK CA CA A 431 O HOH A 509 1555 1555 2.46
LINK CA CA A 432 O HOH A 470 1555 1555 2.45
LINK CA CA A 432 O HOH A 482 1555 1555 2.53
LINK CA CA A 432 O HOH A 538 1555 1555 2.42
LINK CA CA A 433 O HOH A 494 1555 1555 2.61
LINK CA CA A 433 O HOH A 524 1555 1555 2.45
LINK CA CA A 433 O HOH A 526 1555 1555 2.37
SITE 1 CA1 5 ASN A 101 THR A 137 ASP A 146 HIS A 180
SITE 2 CA1 5 HOH A 509
SITE 1 CA2 5 GLY A 169 ASP A 171 HOH A 470 HOH A 482
SITE 2 CA2 5 HOH A 538
SITE 1 CA3 6 GLU A 89 GLU A 276 GLY A 313 HOH A 494
SITE 2 CA3 6 HOH A 524 HOH A 526
CRYST1 72.590 74.060 117.010 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 0.013776 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013503 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008546 0.00000
(ATOM LINES ARE NOT SHOWN.)
END