HEADER HYDROLASE 31-AUG-03 1UKP
TITLE CRYSTAL STRUCTURE OF SOYBEAN BETA-AMYLASE MUTANT SUBSTITUTED AT
TITLE 2 SURFACE REGION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-AMYLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: 1,4-ALPHA-D-GLUCAN MALTOHYDROLASE;
COMPND 5 EC: 3.2.1.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GLYCINE MAX;
SOURCE 3 ORGANISM_COMMON: SOYBEAN;
SOURCE 4 ORGANISM_TAXID: 3847;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM105;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKK233-2
KEYWDS (ALPHA/BETA)8 BARREL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.N.KANG,M.ADACHI,B.MIKAMI,S.UTSUMI
REVDAT 4 25-OCT-23 1UKP 1 REMARK
REVDAT 3 10-NOV-21 1UKP 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1UKP 1 VERSN
REVDAT 1 10-FEB-04 1UKP 0
JRNL AUTH Y.N.KANG,M.ADACHI,B.MIKAMI,S.UTSUMI
JRNL TITL CHANGE IN THE CRYSTAL PACKING OF SOYBEAN BETA-AMYLASE
JRNL TITL 2 MUTANTS SUBSTITUTED AT A FEW SURFACE AMINO ACID RESIDUES
JRNL REF PROTEIN ENG. V. 16 809 2003
JRNL REFN ISSN 0269-2139
JRNL PMID 14631070
JRNL DOI 10.1093/PROTEIN/GZG109
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1432544.570
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 112238
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) : 0.200
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11213
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 16903
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1862
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.006
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15680
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 100
REMARK 3 SOLVENT ATOMS : 1005
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.04000
REMARK 3 B22 (A**2) : 0.72000
REMARK 3 B33 (A**2) : -0.68000
REMARK 3 B12 (A**2) : 1.34000
REMARK 3 B13 (A**2) : 2.96000
REMARK 3 B23 (A**2) : 0.22000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.19
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.25
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.810
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) : 1.130 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.670 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.930 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.800 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.46
REMARK 3 BSOL : 71.95
REMARK 3
REMARK 3 NCS MODEL : CONSTR
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UKP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1000005935.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.900
REMARK 200 MONOCHROMATOR : ROTATING-INCLINING DOUBLE
REMARK 200 CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : OXFORD PX210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 137751
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 19.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 2.440
REMARK 200 R MERGE (I) : 0.12100
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) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.38300
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: CNS 1.1
REMARK 200 STARTING MODEL: PDB ENTRY 1BYB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM ACETATE, 2
REMARK 280 -MERCAPTOETHANOL, EDTA, PH 5.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER
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
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ALA A 1
REMARK 465 THR A 2
REMARK 465 SER A 3
REMARK 465 ASP A 4
REMARK 465 SER A 5
REMARK 465 ALA B 1
REMARK 465 THR B 2
REMARK 465 SER B 3
REMARK 465 ASP B 4
REMARK 465 SER B 5
REMARK 465 ALA C 1
REMARK 465 THR C 2
REMARK 465 SER C 3
REMARK 465 ASP C 4
REMARK 465 SER C 5
REMARK 465 ALA D 1
REMARK 465 THR D 2
REMARK 465 SER D 3
REMARK 465 ASP D 4
REMARK 465 SER D 5
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 ASP A 31 74.30 -111.91
REMARK 500 PHE A 92 31.70 -91.31
REMARK 500 PHE A 145 78.83 -105.84
REMARK 500 PRO A 201 48.85 -104.10
REMARK 500 TRP A 302 7.27 81.71
REMARK 500 PHE A 341 -160.13 -108.06
REMARK 500 ASP A 494 -99.89 -100.27
REMARK 500 ASP B 31 74.59 -112.85
REMARK 500 PHE B 92 30.58 -91.15
REMARK 500 PRO B 201 49.27 -102.94
REMARK 500 TRP B 302 7.98 81.20
REMARK 500 PHE B 341 -162.20 -107.59
REMARK 500 ASP B 494 -94.93 -103.78
REMARK 500 ASP C 31 72.98 -113.20
REMARK 500 PHE C 92 32.67 -93.20
REMARK 500 PRO C 201 56.41 -105.66
REMARK 500 GLU C 243 -8.83 -56.23
REMARK 500 TRP C 302 3.79 81.21
REMARK 500 PHE C 341 -162.44 -111.47
REMARK 500 ASP C 494 -98.16 -103.65
REMARK 500 ASP D 31 74.35 -113.06
REMARK 500 PHE D 92 33.50 -91.72
REMARK 500 PHE D 145 78.53 -108.12
REMARK 500 PRO D 201 49.54 -104.50
REMARK 500 TRP D 302 7.17 80.67
REMARK 500 PHE D 341 -161.25 -107.83
REMARK 500 ASP D 494 -96.45 -107.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B 372 0.08 SIDE CHAIN
REMARK 500 ARG C 372 0.14 SIDE CHAIN
REMARK 500 ARG D 372 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2008
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2009
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2010
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 2011
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2012
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2013
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2014
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 2015
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2016
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2017
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2018
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 2019
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BYA RELATED DB: PDB
REMARK 900 SOYBEAN BETA-AMYLASE (APO FORM)
REMARK 900 RELATED ID: 1BYB RELATED DB: PDB
REMARK 900 SOYBEAN BETA-AMYLASE REACTED WITH 200MM MALTOSE AND COMPLEXED WITH
REMARK 900 MALTOTETRAOSE
REMARK 900 RELATED ID: 1BYC RELATED DB: PDB
REMARK 900 SOYBEAN BETA-AMYLASE REACTED WITH 8MM MALTOSE AND COMPLEXED WITH
REMARK 900 MALTOTETRAOSE
REMARK 900 RELATED ID: 1BYD RELATED DB: PDB
REMARK 900 SOYBEAN BETA-AMYLASE REACTED WITH 100MM MALTAL AND COMPLEXED WITH 2-
REMARK 900 DEOXYMALTOSE
REMARK 900 RELATED ID: 1BFN RELATED DB: PDB
REMARK 900 RECOMBINANT SOYBEAN BETA-AMYLASE COMPLEXED WITH BETA-CYCLODEXTRIN
REMARK 900 RELATED ID: 1FA2 RELATED DB: PDB
REMARK 900 SWEET POTATO BETA-AMYLASE
REMARK 900 RELATED ID: 1UKO RELATED DB: PDB
REMARK 900 SOYBEAN BETA-AMYLASE D374Y, L481R, P487D MUTANT
DBREF 1UKP A 1 495 UNP P10538 AMYB_SOYBN 1 495
DBREF 1UKP B 1 495 UNP P10538 AMYB_SOYBN 1 495
DBREF 1UKP C 1 495 UNP P10538 AMYB_SOYBN 1 495
DBREF 1UKP D 1 495 UNP P10538 AMYB_SOYBN 1 495
SEQADV 1UKP LEU A 76 UNP P10538 PHE 76 SEE REMARK 999
SEQADV 1UKP GLY A 202 UNP P10538 ARG 202 SEE REMARK 999
SEQADV 1UKP TYR A 374 UNP P10538 ASP 374 ENGINEERED MUTATION
SEQADV 1UKP ARG A 399 UNP P10538 LYS 399 SEE REMARK 999
SEQADV 1UKP SER A 462 UNP P10538 LYS 462 ENGINEERED MUTATION
SEQADV 1UKP ARG A 481 UNP P10538 LEU 481 ENGINEERED MUTATION
SEQADV 1UKP ASP A 487 UNP P10538 PRO 487 ENGINEERED MUTATION
SEQADV 1UKP LEU B 76 UNP P10538 PHE 76 SEE REMARK 999
SEQADV 1UKP GLY B 202 UNP P10538 ARG 202 SEE REMARK 999
SEQADV 1UKP TYR B 374 UNP P10538 ASP 374 ENGINEERED MUTATION
SEQADV 1UKP ARG B 399 UNP P10538 LYS 399 SEE REMARK 999
SEQADV 1UKP SER B 462 UNP P10538 LYS 462 ENGINEERED MUTATION
SEQADV 1UKP ARG B 481 UNP P10538 LEU 481 ENGINEERED MUTATION
SEQADV 1UKP ASP B 487 UNP P10538 PRO 487 ENGINEERED MUTATION
SEQADV 1UKP LEU C 76 UNP P10538 PHE 76 SEE REMARK 999
SEQADV 1UKP GLY C 202 UNP P10538 ARG 202 SEE REMARK 999
SEQADV 1UKP TYR C 374 UNP P10538 ASP 374 ENGINEERED MUTATION
SEQADV 1UKP ARG C 399 UNP P10538 LYS 399 SEE REMARK 999
SEQADV 1UKP SER C 462 UNP P10538 LYS 462 ENGINEERED MUTATION
SEQADV 1UKP ARG C 481 UNP P10538 LEU 481 ENGINEERED MUTATION
SEQADV 1UKP ASP C 487 UNP P10538 PRO 487 ENGINEERED MUTATION
SEQADV 1UKP LEU D 76 UNP P10538 PHE 76 SEE REMARK 999
SEQADV 1UKP GLY D 202 UNP P10538 ARG 202 SEE REMARK 999
SEQADV 1UKP TYR D 374 UNP P10538 ASP 374 ENGINEERED MUTATION
SEQADV 1UKP ARG D 399 UNP P10538 LYS 399 SEE REMARK 999
SEQADV 1UKP SER D 462 UNP P10538 LYS 462 ENGINEERED MUTATION
SEQADV 1UKP ARG D 481 UNP P10538 LEU 481 ENGINEERED MUTATION
SEQADV 1UKP ASP D 487 UNP P10538 PRO 487 ENGINEERED MUTATION
SEQRES 1 A 495 ALA THR SER ASP SER ASN MET LEU LEU ASN TYR VAL PRO
SEQRES 2 A 495 VAL TYR VAL MET LEU PRO LEU GLY VAL VAL ASN VAL ASP
SEQRES 3 A 495 ASN VAL PHE GLU ASP PRO ASP GLY LEU LYS GLU GLN LEU
SEQRES 4 A 495 LEU GLN LEU ARG ALA ALA GLY VAL ASP GLY VAL MET VAL
SEQRES 5 A 495 ASP VAL TRP TRP GLY ILE ILE GLU LEU LYS GLY PRO LYS
SEQRES 6 A 495 GLN TYR ASP TRP ARG ALA TYR ARG SER LEU LEU GLN LEU
SEQRES 7 A 495 VAL GLN GLU CYS GLY LEU THR LEU GLN ALA ILE MET SER
SEQRES 8 A 495 PHE HIS GLN CYS GLY GLY ASN VAL GLY ASP ILE VAL ASN
SEQRES 9 A 495 ILE PRO ILE PRO GLN TRP VAL LEU ASP ILE GLY GLU SER
SEQRES 10 A 495 ASN HIS ASP ILE PHE TYR THR ASN ARG SER GLY THR ARG
SEQRES 11 A 495 ASN LYS GLU TYR LEU THR VAL GLY VAL ASP ASN GLU PRO
SEQRES 12 A 495 ILE PHE HIS GLY ARG THR ALA ILE GLU ILE TYR SER ASP
SEQRES 13 A 495 TYR MET LYS SER PHE ARG GLU ASN MET SER ASP PHE LEU
SEQRES 14 A 495 GLU SER GLY LEU ILE ILE ASP ILE GLU VAL GLY LEU GLY
SEQRES 15 A 495 PRO ALA GLY GLU LEU ARG TYR PRO SER TYR PRO GLN SER
SEQRES 16 A 495 GLN GLY TRP GLU PHE PRO GLY ILE GLY GLU PHE GLN CYS
SEQRES 17 A 495 TYR ASP LYS TYR LEU LYS ALA ASP PHE LYS ALA ALA VAL
SEQRES 18 A 495 ALA ARG ALA GLY HIS PRO GLU TRP GLU LEU PRO ASP ASP
SEQRES 19 A 495 ALA GLY LYS TYR ASN ASP VAL PRO GLU SER THR GLY PHE
SEQRES 20 A 495 PHE LYS SER ASN GLY THR TYR VAL THR GLU LYS GLY LYS
SEQRES 21 A 495 PHE PHE LEU THR TRP TYR SER ASN LYS LEU LEU ASN HIS
SEQRES 22 A 495 GLY ASP GLN ILE LEU ASP GLU ALA ASN LYS ALA PHE LEU
SEQRES 23 A 495 GLY CYS LYS VAL LYS LEU ALA ILE LYS VAL SER GLY ILE
SEQRES 24 A 495 HIS TRP TRP TYR LYS VAL GLU ASN HIS ALA ALA GLU LEU
SEQRES 25 A 495 THR ALA GLY TYR TYR ASN LEU ASN ASP ARG ASP GLY TYR
SEQRES 26 A 495 ARG PRO ILE ALA ARG MET LEU SER ARG HIS HIS ALA ILE
SEQRES 27 A 495 LEU ASN PHE THR CYS LEU GLU MET ARG ASP SER GLU GLN
SEQRES 28 A 495 PRO SER ASP ALA LYS SER GLY PRO GLN GLU LEU VAL GLN
SEQRES 29 A 495 GLN VAL LEU SER GLY GLY TRP ARG GLU TYR ILE ARG VAL
SEQRES 30 A 495 ALA GLY GLU ASN ALA LEU PRO ARG TYR ASP ALA THR ALA
SEQRES 31 A 495 TYR ASN GLN ILE ILE LEU ASN ALA ARG PRO GLN GLY VAL
SEQRES 32 A 495 ASN ASN ASN GLY PRO PRO LYS LEU SER MET PHE GLY VAL
SEQRES 33 A 495 THR TYR LEU ARG LEU SER ASP ASP LEU LEU GLN LYS SER
SEQRES 34 A 495 ASN PHE ASN ILE PHE LYS LYS PHE VAL LEU LYS MET HIS
SEQRES 35 A 495 ALA ASP GLN ASP TYR CYS ALA ASN PRO GLN LYS TYR ASN
SEQRES 36 A 495 HIS ALA ILE THR PRO LEU SER PRO SER ALA PRO LYS ILE
SEQRES 37 A 495 PRO ILE GLU VAL LEU LEU GLU ALA THR LYS PRO THR ARG
SEQRES 38 A 495 PRO PHE PRO TRP LEU ASP GLU THR ASP MET LYS VAL ASP
SEQRES 39 A 495 GLY
SEQRES 1 B 495 ALA THR SER ASP SER ASN MET LEU LEU ASN TYR VAL PRO
SEQRES 2 B 495 VAL TYR VAL MET LEU PRO LEU GLY VAL VAL ASN VAL ASP
SEQRES 3 B 495 ASN VAL PHE GLU ASP PRO ASP GLY LEU LYS GLU GLN LEU
SEQRES 4 B 495 LEU GLN LEU ARG ALA ALA GLY VAL ASP GLY VAL MET VAL
SEQRES 5 B 495 ASP VAL TRP TRP GLY ILE ILE GLU LEU LYS GLY PRO LYS
SEQRES 6 B 495 GLN TYR ASP TRP ARG ALA TYR ARG SER LEU LEU GLN LEU
SEQRES 7 B 495 VAL GLN GLU CYS GLY LEU THR LEU GLN ALA ILE MET SER
SEQRES 8 B 495 PHE HIS GLN CYS GLY GLY ASN VAL GLY ASP ILE VAL ASN
SEQRES 9 B 495 ILE PRO ILE PRO GLN TRP VAL LEU ASP ILE GLY GLU SER
SEQRES 10 B 495 ASN HIS ASP ILE PHE TYR THR ASN ARG SER GLY THR ARG
SEQRES 11 B 495 ASN LYS GLU TYR LEU THR VAL GLY VAL ASP ASN GLU PRO
SEQRES 12 B 495 ILE PHE HIS GLY ARG THR ALA ILE GLU ILE TYR SER ASP
SEQRES 13 B 495 TYR MET LYS SER PHE ARG GLU ASN MET SER ASP PHE LEU
SEQRES 14 B 495 GLU SER GLY LEU ILE ILE ASP ILE GLU VAL GLY LEU GLY
SEQRES 15 B 495 PRO ALA GLY GLU LEU ARG TYR PRO SER TYR PRO GLN SER
SEQRES 16 B 495 GLN GLY TRP GLU PHE PRO GLY ILE GLY GLU PHE GLN CYS
SEQRES 17 B 495 TYR ASP LYS TYR LEU LYS ALA ASP PHE LYS ALA ALA VAL
SEQRES 18 B 495 ALA ARG ALA GLY HIS PRO GLU TRP GLU LEU PRO ASP ASP
SEQRES 19 B 495 ALA GLY LYS TYR ASN ASP VAL PRO GLU SER THR GLY PHE
SEQRES 20 B 495 PHE LYS SER ASN GLY THR TYR VAL THR GLU LYS GLY LYS
SEQRES 21 B 495 PHE PHE LEU THR TRP TYR SER ASN LYS LEU LEU ASN HIS
SEQRES 22 B 495 GLY ASP GLN ILE LEU ASP GLU ALA ASN LYS ALA PHE LEU
SEQRES 23 B 495 GLY CYS LYS VAL LYS LEU ALA ILE LYS VAL SER GLY ILE
SEQRES 24 B 495 HIS TRP TRP TYR LYS VAL GLU ASN HIS ALA ALA GLU LEU
SEQRES 25 B 495 THR ALA GLY TYR TYR ASN LEU ASN ASP ARG ASP GLY TYR
SEQRES 26 B 495 ARG PRO ILE ALA ARG MET LEU SER ARG HIS HIS ALA ILE
SEQRES 27 B 495 LEU ASN PHE THR CYS LEU GLU MET ARG ASP SER GLU GLN
SEQRES 28 B 495 PRO SER ASP ALA LYS SER GLY PRO GLN GLU LEU VAL GLN
SEQRES 29 B 495 GLN VAL LEU SER GLY GLY TRP ARG GLU TYR ILE ARG VAL
SEQRES 30 B 495 ALA GLY GLU ASN ALA LEU PRO ARG TYR ASP ALA THR ALA
SEQRES 31 B 495 TYR ASN GLN ILE ILE LEU ASN ALA ARG PRO GLN GLY VAL
SEQRES 32 B 495 ASN ASN ASN GLY PRO PRO LYS LEU SER MET PHE GLY VAL
SEQRES 33 B 495 THR TYR LEU ARG LEU SER ASP ASP LEU LEU GLN LYS SER
SEQRES 34 B 495 ASN PHE ASN ILE PHE LYS LYS PHE VAL LEU LYS MET HIS
SEQRES 35 B 495 ALA ASP GLN ASP TYR CYS ALA ASN PRO GLN LYS TYR ASN
SEQRES 36 B 495 HIS ALA ILE THR PRO LEU SER PRO SER ALA PRO LYS ILE
SEQRES 37 B 495 PRO ILE GLU VAL LEU LEU GLU ALA THR LYS PRO THR ARG
SEQRES 38 B 495 PRO PHE PRO TRP LEU ASP GLU THR ASP MET LYS VAL ASP
SEQRES 39 B 495 GLY
SEQRES 1 C 495 ALA THR SER ASP SER ASN MET LEU LEU ASN TYR VAL PRO
SEQRES 2 C 495 VAL TYR VAL MET LEU PRO LEU GLY VAL VAL ASN VAL ASP
SEQRES 3 C 495 ASN VAL PHE GLU ASP PRO ASP GLY LEU LYS GLU GLN LEU
SEQRES 4 C 495 LEU GLN LEU ARG ALA ALA GLY VAL ASP GLY VAL MET VAL
SEQRES 5 C 495 ASP VAL TRP TRP GLY ILE ILE GLU LEU LYS GLY PRO LYS
SEQRES 6 C 495 GLN TYR ASP TRP ARG ALA TYR ARG SER LEU LEU GLN LEU
SEQRES 7 C 495 VAL GLN GLU CYS GLY LEU THR LEU GLN ALA ILE MET SER
SEQRES 8 C 495 PHE HIS GLN CYS GLY GLY ASN VAL GLY ASP ILE VAL ASN
SEQRES 9 C 495 ILE PRO ILE PRO GLN TRP VAL LEU ASP ILE GLY GLU SER
SEQRES 10 C 495 ASN HIS ASP ILE PHE TYR THR ASN ARG SER GLY THR ARG
SEQRES 11 C 495 ASN LYS GLU TYR LEU THR VAL GLY VAL ASP ASN GLU PRO
SEQRES 12 C 495 ILE PHE HIS GLY ARG THR ALA ILE GLU ILE TYR SER ASP
SEQRES 13 C 495 TYR MET LYS SER PHE ARG GLU ASN MET SER ASP PHE LEU
SEQRES 14 C 495 GLU SER GLY LEU ILE ILE ASP ILE GLU VAL GLY LEU GLY
SEQRES 15 C 495 PRO ALA GLY GLU LEU ARG TYR PRO SER TYR PRO GLN SER
SEQRES 16 C 495 GLN GLY TRP GLU PHE PRO GLY ILE GLY GLU PHE GLN CYS
SEQRES 17 C 495 TYR ASP LYS TYR LEU LYS ALA ASP PHE LYS ALA ALA VAL
SEQRES 18 C 495 ALA ARG ALA GLY HIS PRO GLU TRP GLU LEU PRO ASP ASP
SEQRES 19 C 495 ALA GLY LYS TYR ASN ASP VAL PRO GLU SER THR GLY PHE
SEQRES 20 C 495 PHE LYS SER ASN GLY THR TYR VAL THR GLU LYS GLY LYS
SEQRES 21 C 495 PHE PHE LEU THR TRP TYR SER ASN LYS LEU LEU ASN HIS
SEQRES 22 C 495 GLY ASP GLN ILE LEU ASP GLU ALA ASN LYS ALA PHE LEU
SEQRES 23 C 495 GLY CYS LYS VAL LYS LEU ALA ILE LYS VAL SER GLY ILE
SEQRES 24 C 495 HIS TRP TRP TYR LYS VAL GLU ASN HIS ALA ALA GLU LEU
SEQRES 25 C 495 THR ALA GLY TYR TYR ASN LEU ASN ASP ARG ASP GLY TYR
SEQRES 26 C 495 ARG PRO ILE ALA ARG MET LEU SER ARG HIS HIS ALA ILE
SEQRES 27 C 495 LEU ASN PHE THR CYS LEU GLU MET ARG ASP SER GLU GLN
SEQRES 28 C 495 PRO SER ASP ALA LYS SER GLY PRO GLN GLU LEU VAL GLN
SEQRES 29 C 495 GLN VAL LEU SER GLY GLY TRP ARG GLU TYR ILE ARG VAL
SEQRES 30 C 495 ALA GLY GLU ASN ALA LEU PRO ARG TYR ASP ALA THR ALA
SEQRES 31 C 495 TYR ASN GLN ILE ILE LEU ASN ALA ARG PRO GLN GLY VAL
SEQRES 32 C 495 ASN ASN ASN GLY PRO PRO LYS LEU SER MET PHE GLY VAL
SEQRES 33 C 495 THR TYR LEU ARG LEU SER ASP ASP LEU LEU GLN LYS SER
SEQRES 34 C 495 ASN PHE ASN ILE PHE LYS LYS PHE VAL LEU LYS MET HIS
SEQRES 35 C 495 ALA ASP GLN ASP TYR CYS ALA ASN PRO GLN LYS TYR ASN
SEQRES 36 C 495 HIS ALA ILE THR PRO LEU SER PRO SER ALA PRO LYS ILE
SEQRES 37 C 495 PRO ILE GLU VAL LEU LEU GLU ALA THR LYS PRO THR ARG
SEQRES 38 C 495 PRO PHE PRO TRP LEU ASP GLU THR ASP MET LYS VAL ASP
SEQRES 39 C 495 GLY
SEQRES 1 D 495 ALA THR SER ASP SER ASN MET LEU LEU ASN TYR VAL PRO
SEQRES 2 D 495 VAL TYR VAL MET LEU PRO LEU GLY VAL VAL ASN VAL ASP
SEQRES 3 D 495 ASN VAL PHE GLU ASP PRO ASP GLY LEU LYS GLU GLN LEU
SEQRES 4 D 495 LEU GLN LEU ARG ALA ALA GLY VAL ASP GLY VAL MET VAL
SEQRES 5 D 495 ASP VAL TRP TRP GLY ILE ILE GLU LEU LYS GLY PRO LYS
SEQRES 6 D 495 GLN TYR ASP TRP ARG ALA TYR ARG SER LEU LEU GLN LEU
SEQRES 7 D 495 VAL GLN GLU CYS GLY LEU THR LEU GLN ALA ILE MET SER
SEQRES 8 D 495 PHE HIS GLN CYS GLY GLY ASN VAL GLY ASP ILE VAL ASN
SEQRES 9 D 495 ILE PRO ILE PRO GLN TRP VAL LEU ASP ILE GLY GLU SER
SEQRES 10 D 495 ASN HIS ASP ILE PHE TYR THR ASN ARG SER GLY THR ARG
SEQRES 11 D 495 ASN LYS GLU TYR LEU THR VAL GLY VAL ASP ASN GLU PRO
SEQRES 12 D 495 ILE PHE HIS GLY ARG THR ALA ILE GLU ILE TYR SER ASP
SEQRES 13 D 495 TYR MET LYS SER PHE ARG GLU ASN MET SER ASP PHE LEU
SEQRES 14 D 495 GLU SER GLY LEU ILE ILE ASP ILE GLU VAL GLY LEU GLY
SEQRES 15 D 495 PRO ALA GLY GLU LEU ARG TYR PRO SER TYR PRO GLN SER
SEQRES 16 D 495 GLN GLY TRP GLU PHE PRO GLY ILE GLY GLU PHE GLN CYS
SEQRES 17 D 495 TYR ASP LYS TYR LEU LYS ALA ASP PHE LYS ALA ALA VAL
SEQRES 18 D 495 ALA ARG ALA GLY HIS PRO GLU TRP GLU LEU PRO ASP ASP
SEQRES 19 D 495 ALA GLY LYS TYR ASN ASP VAL PRO GLU SER THR GLY PHE
SEQRES 20 D 495 PHE LYS SER ASN GLY THR TYR VAL THR GLU LYS GLY LYS
SEQRES 21 D 495 PHE PHE LEU THR TRP TYR SER ASN LYS LEU LEU ASN HIS
SEQRES 22 D 495 GLY ASP GLN ILE LEU ASP GLU ALA ASN LYS ALA PHE LEU
SEQRES 23 D 495 GLY CYS LYS VAL LYS LEU ALA ILE LYS VAL SER GLY ILE
SEQRES 24 D 495 HIS TRP TRP TYR LYS VAL GLU ASN HIS ALA ALA GLU LEU
SEQRES 25 D 495 THR ALA GLY TYR TYR ASN LEU ASN ASP ARG ASP GLY TYR
SEQRES 26 D 495 ARG PRO ILE ALA ARG MET LEU SER ARG HIS HIS ALA ILE
SEQRES 27 D 495 LEU ASN PHE THR CYS LEU GLU MET ARG ASP SER GLU GLN
SEQRES 28 D 495 PRO SER ASP ALA LYS SER GLY PRO GLN GLU LEU VAL GLN
SEQRES 29 D 495 GLN VAL LEU SER GLY GLY TRP ARG GLU TYR ILE ARG VAL
SEQRES 30 D 495 ALA GLY GLU ASN ALA LEU PRO ARG TYR ASP ALA THR ALA
SEQRES 31 D 495 TYR ASN GLN ILE ILE LEU ASN ALA ARG PRO GLN GLY VAL
SEQRES 32 D 495 ASN ASN ASN GLY PRO PRO LYS LEU SER MET PHE GLY VAL
SEQRES 33 D 495 THR TYR LEU ARG LEU SER ASP ASP LEU LEU GLN LYS SER
SEQRES 34 D 495 ASN PHE ASN ILE PHE LYS LYS PHE VAL LEU LYS MET HIS
SEQRES 35 D 495 ALA ASP GLN ASP TYR CYS ALA ASN PRO GLN LYS TYR ASN
SEQRES 36 D 495 HIS ALA ILE THR PRO LEU SER PRO SER ALA PRO LYS ILE
SEQRES 37 D 495 PRO ILE GLU VAL LEU LEU GLU ALA THR LYS PRO THR ARG
SEQRES 38 D 495 PRO PHE PRO TRP LEU ASP GLU THR ASP MET LYS VAL ASP
SEQRES 39 D 495 GLY
HET SO4 A2000 5
HET SO4 A2004 5
HET SO4 A2008 5
HET SO4 A2012 5
HET SO4 A2016 5
HET SO4 B2001 5
HET SO4 B2005 5
HET SO4 B2009 5
HET SO4 B2013 5
HET SO4 B2017 5
HET SO4 C2002 5
HET SO4 C2006 5
HET SO4 C2007 5
HET SO4 C2010 5
HET SO4 C2014 5
HET SO4 C2018 5
HET SO4 D2003 5
HET SO4 D2011 5
HET SO4 D2015 5
HET SO4 D2019 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 20(O4 S 2-)
FORMUL 25 HOH *1005(H2 O)
HELIX 1 1 ASN A 6 TYR A 11 5 6
HELIX 2 2 ASP A 31 ALA A 45 1 15
HELIX 3 3 TRP A 56 GLU A 60 1 5
HELIX 4 4 TRP A 69 CYS A 82 1 14
HELIX 5 5 PRO A 108 ASN A 118 1 11
HELIX 6 6 VAL A 137 ASP A 140 5 4
HELIX 7 7 THR A 149 MET A 165 1 17
HELIX 8 8 MET A 165 SER A 171 1 7
HELIX 9 9 GLY A 182 GLU A 186 5 5
HELIX 10 10 PRO A 193 GLY A 197 5 5
HELIX 11 11 ASP A 210 ALA A 224 1 15
HELIX 12 12 VAL A 241 THR A 245 5 5
HELIX 13 13 GLY A 252 VAL A 255 5 4
HELIX 14 14 THR A 256 LEU A 286 1 31
HELIX 15 15 HIS A 308 GLY A 315 1 8
HELIX 16 16 TYR A 325 ARG A 334 1 10
HELIX 17 17 ARG A 347 GLN A 351 5 5
HELIX 18 18 PRO A 352 LYS A 356 5 5
HELIX 19 19 GLY A 358 GLU A 373 1 16
HELIX 20 20 ASP A 387 ARG A 399 1 13
HELIX 21 21 GLN A 427 HIS A 442 1 16
HELIX 22 22 ASN A 450 ASN A 455 5 6
HELIX 23 23 PRO A 469 LEU A 474 1 6
HELIX 24 24 GLU A 475 LYS A 478 5 4
HELIX 25 25 ASN B 6 TYR B 11 5 6
HELIX 26 26 ASP B 31 ALA B 45 1 15
HELIX 27 27 TRP B 56 GLU B 60 1 5
HELIX 28 28 TRP B 69 CYS B 82 1 14
HELIX 29 29 PRO B 108 ASN B 118 1 11
HELIX 30 30 VAL B 137 ASP B 140 5 4
HELIX 31 31 THR B 149 MET B 165 1 17
HELIX 32 32 MET B 165 SER B 171 1 7
HELIX 33 33 GLY B 182 GLU B 186 5 5
HELIX 34 34 PRO B 193 GLY B 197 5 5
HELIX 35 35 ASP B 210 ALA B 224 1 15
HELIX 36 36 VAL B 241 THR B 245 5 5
HELIX 37 37 GLY B 252 VAL B 255 5 4
HELIX 38 38 THR B 256 LEU B 286 1 31
HELIX 39 39 HIS B 308 GLY B 315 1 8
HELIX 40 40 TYR B 325 ARG B 334 1 10
HELIX 41 41 ARG B 347 GLN B 351 5 5
HELIX 42 42 PRO B 352 LYS B 356 5 5
HELIX 43 43 GLY B 358 GLU B 373 1 16
HELIX 44 44 ASP B 387 ARG B 399 1 13
HELIX 45 45 SER B 422 GLN B 427 1 6
HELIX 46 46 GLN B 427 HIS B 442 1 16
HELIX 47 47 ASN B 450 ASN B 455 5 6
HELIX 48 48 PRO B 469 LEU B 474 1 6
HELIX 49 49 GLU B 475 LYS B 478 5 4
HELIX 50 50 ASN C 6 TYR C 11 5 6
HELIX 51 51 ASP C 31 ALA C 45 1 15
HELIX 52 52 TRP C 56 GLU C 60 1 5
HELIX 53 53 TRP C 69 CYS C 82 1 14
HELIX 54 54 PRO C 108 ASN C 118 1 11
HELIX 55 55 VAL C 137 ASP C 140 5 4
HELIX 56 56 THR C 149 MET C 165 1 17
HELIX 57 57 MET C 165 SER C 171 1 7
HELIX 58 58 GLY C 182 GLU C 186 5 5
HELIX 59 59 PRO C 193 GLY C 197 5 5
HELIX 60 60 ASP C 210 ALA C 224 1 15
HELIX 61 61 VAL C 241 THR C 245 5 5
HELIX 62 62 GLY C 252 VAL C 255 5 4
HELIX 63 63 THR C 256 PHE C 285 1 30
HELIX 64 64 HIS C 308 GLY C 315 1 8
HELIX 65 65 TYR C 325 ARG C 334 1 10
HELIX 66 66 ARG C 347 GLN C 351 5 5
HELIX 67 67 PRO C 352 LYS C 356 5 5
HELIX 68 68 GLY C 358 GLU C 373 1 16
HELIX 69 69 ASP C 387 ARG C 399 1 13
HELIX 70 70 SER C 422 GLN C 427 1 6
HELIX 71 71 GLN C 427 HIS C 442 1 16
HELIX 72 72 ASN C 450 ASN C 455 5 6
HELIX 73 73 PRO C 469 GLU C 475 1 7
HELIX 74 74 ALA C 476 LYS C 478 5 3
HELIX 75 75 ASN D 6 TYR D 11 5 6
HELIX 76 76 ASP D 31 ALA D 45 1 15
HELIX 77 77 TRP D 56 GLU D 60 1 5
HELIX 78 78 TRP D 69 CYS D 82 1 14
HELIX 79 79 PRO D 108 ASN D 118 1 11
HELIX 80 80 VAL D 137 ASP D 140 5 4
HELIX 81 81 THR D 149 MET D 165 1 17
HELIX 82 82 MET D 165 SER D 171 1 7
HELIX 83 83 GLY D 182 GLU D 186 5 5
HELIX 84 84 PRO D 193 GLY D 197 5 5
HELIX 85 85 ASP D 210 ALA D 224 1 15
HELIX 86 86 VAL D 241 THR D 245 5 5
HELIX 87 87 GLY D 252 VAL D 255 5 4
HELIX 88 88 THR D 256 PHE D 285 1 30
HELIX 89 89 HIS D 308 GLY D 315 1 8
HELIX 90 90 TYR D 325 ARG D 334 1 10
HELIX 91 91 ARG D 347 GLN D 351 5 5
HELIX 92 92 PRO D 352 LYS D 356 5 5
HELIX 93 93 GLY D 358 GLU D 373 1 16
HELIX 94 94 ASP D 387 ARG D 399 1 13
HELIX 95 95 GLN D 427 HIS D 442 1 16
HELIX 96 96 ASN D 450 ASN D 455 5 6
HELIX 97 97 PRO D 469 LEU D 474 1 6
HELIX 98 98 GLU D 475 LYS D 478 5 4
SHEET 1 A 9 VAL A 14 MET A 17 0
SHEET 2 A 9 GLY A 49 TRP A 55 1 O MET A 51 N VAL A 16
SHEET 3 A 9 THR A 85 SER A 91 1 O ILE A 89 N VAL A 54
SHEET 4 A 9 ILE A 174 VAL A 179 1 O GLU A 178 N MET A 90
SHEET 5 A 9 LYS A 291 LYS A 295 1 O LYS A 291 N ILE A 177
SHEET 6 A 9 ILE A 338 PHE A 341 1 O ASN A 340 N ILE A 294
SHEET 7 A 9 VAL A 377 GLU A 380 1 O ALA A 378 N PHE A 341
SHEET 8 A 9 VAL A 416 TYR A 418 1 O THR A 417 N GLY A 379
SHEET 9 A 9 VAL A 14 MET A 17 1 N TYR A 15 O VAL A 416
SHEET 1 B 2 PHE A 122 THR A 124 0
SHEET 2 B 2 ARG A 130 LEU A 135 -1 O ASN A 131 N TYR A 123
SHEET 1 C 9 VAL B 14 MET B 17 0
SHEET 2 C 9 GLY B 49 TRP B 55 1 O GLY B 49 N VAL B 16
SHEET 3 C 9 THR B 85 SER B 91 1 O ILE B 89 N VAL B 54
SHEET 4 C 9 ILE B 174 VAL B 179 1 O GLU B 178 N MET B 90
SHEET 5 C 9 LYS B 291 LYS B 295 1 O LYS B 291 N ILE B 177
SHEET 6 C 9 ILE B 338 PHE B 341 1 O ASN B 340 N ILE B 294
SHEET 7 C 9 VAL B 377 GLU B 380 1 O ALA B 378 N PHE B 341
SHEET 8 C 9 GLY B 415 TYR B 418 1 O THR B 417 N GLY B 379
SHEET 9 C 9 VAL B 14 MET B 17 1 N TYR B 15 O TYR B 418
SHEET 1 D 2 PHE B 122 THR B 124 0
SHEET 2 D 2 ARG B 130 LEU B 135 -1 O ASN B 131 N TYR B 123
SHEET 1 E 9 VAL C 14 MET C 17 0
SHEET 2 E 9 GLY C 49 TRP C 55 1 O MET C 51 N VAL C 16
SHEET 3 E 9 THR C 85 SER C 91 1 O GLN C 87 N VAL C 50
SHEET 4 E 9 ILE C 174 VAL C 179 1 O GLU C 178 N MET C 90
SHEET 5 E 9 LYS C 291 LYS C 295 1 O LYS C 291 N ILE C 177
SHEET 6 E 9 ILE C 338 PHE C 341 1 O ASN C 340 N ILE C 294
SHEET 7 E 9 VAL C 377 GLU C 380 1 O ALA C 378 N PHE C 341
SHEET 8 E 9 VAL C 416 TYR C 418 1 O THR C 417 N GLY C 379
SHEET 9 E 9 VAL C 14 MET C 17 1 N TYR C 15 O TYR C 418
SHEET 1 F 2 PHE C 122 THR C 124 0
SHEET 2 F 2 ARG C 130 LEU C 135 -1 O ASN C 131 N TYR C 123
SHEET 1 G 9 VAL D 14 MET D 17 0
SHEET 2 G 9 GLY D 49 TRP D 55 1 O MET D 51 N VAL D 16
SHEET 3 G 9 THR D 85 SER D 91 1 O ILE D 89 N VAL D 54
SHEET 4 G 9 ILE D 174 VAL D 179 1 O GLU D 178 N MET D 90
SHEET 5 G 9 LYS D 291 LYS D 295 1 O LYS D 291 N ILE D 177
SHEET 6 G 9 ILE D 338 PHE D 341 1 O ASN D 340 N ILE D 294
SHEET 7 G 9 VAL D 377 GLU D 380 1 O ALA D 378 N PHE D 341
SHEET 8 G 9 GLY D 415 TYR D 418 1 O THR D 417 N GLY D 379
SHEET 9 G 9 VAL D 14 MET D 17 1 N TYR D 15 O TYR D 418
SHEET 1 H 2 PHE D 122 THR D 124 0
SHEET 2 H 2 ARG D 130 LEU D 135 -1 O ASN D 131 N TYR D 123
CISPEP 1 PHE A 200 PRO A 201 0 0.25
CISPEP 2 LEU A 419 ARG A 420 0 0.39
CISPEP 3 PHE B 200 PRO B 201 0 -0.60
CISPEP 4 LEU B 419 ARG B 420 0 0.48
CISPEP 5 PHE C 200 PRO C 201 0 0.22
CISPEP 6 LEU C 419 ARG C 420 0 0.55
CISPEP 7 PHE D 200 PRO D 201 0 -0.28
CISPEP 8 LEU D 419 ARG D 420 0 0.82
SITE 1 AC1 3 TYR A 67 SER A 160 ASN A 164
SITE 1 AC2 2 SER B 160 ASN B 164
SITE 1 AC3 2 SER C 160 ASN C 164
SITE 1 AC4 2 SER D 160 ASN D 164
SITE 1 AC5 3 ASP A 234 HOH A1357 HIS B 146
SITE 1 AC6 5 HIS A 146 HOH A1134 ASP B 234 GLY B 246
SITE 2 AC6 5 HOH B 819
SITE 1 AC7 4 GLY C 246 HIS D 146 HOH D1172 HOH D1490
SITE 1 AC8 3 HIS C 146 ASP D 234 HOH D1445
SITE 1 AC9 3 ARG A 347 SER A 349 HOH A1151
SITE 1 BC1 4 ARG B 347 SER B 349 HOH B 537 HOH B1425
SITE 1 BC2 3 ARG C 347 SER C 349 HOH C 785
SITE 1 BC3 3 ARG D 347 SER D 349 HOH D 739
SITE 1 BC4 6 LYS A 291 ARG A 376 PHE A 414 ASN A 455
SITE 2 BC4 6 HIS A 456 ALA A 457
SITE 1 BC5 5 LYS B 291 ARG B 376 ASN B 455 HIS B 456
SITE 2 BC5 5 ALA B 457
SITE 1 BC6 5 LYS C 291 ARG C 376 PHE C 414 ASN C 455
SITE 2 BC6 5 ALA C 457
SITE 1 BC7 4 ARG D 376 PHE D 414 ASN D 455 ALA D 457
SITE 1 BC8 4 ASP A 387 ALA A 388 THR A 389 HOH A 606
SITE 1 BC9 4 ASP B 387 ALA B 388 THR B 389 HOH B 648
SITE 1 CC1 4 ASP C 387 ALA C 388 THR C 389 HOH C 787
SITE 1 CC2 4 ASP D 387 ALA D 388 THR D 389 HOH D 704
CRYST1 75.463 78.801 88.560 89.92 90.21 89.90 P 1 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 0.013251 -0.000023 0.000048 0.00000
SCALE2 0.000000 0.012690 -0.000018 0.00000
SCALE3 0.000000 0.000000 0.011292 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
