HEADER HYDROLASE 22-MAY-98 1BFN
TITLE BETA-AMYLASE/BETA-CYCLODEXTRIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-AMYLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GLYCINE MAX;
SOURCE 3 ORGANISM_COMMON: SOYBEAN;
SOURCE 4 ORGANISM_TAXID: 3847;
SOURCE 5 ORGAN: SEED;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, BETA-AMYLASE, BETA-CYCLODEXTRIN, RECOMBINANT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ADACHI,B.MIKAMI,T.KATSUBE,S.UTSUMI
REVDAT 5 07-FEB-24 1BFN 1 HETSYN
REVDAT 4 29-JUL-20 1BFN 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 24-FEB-09 1BFN 1 VERSN
REVDAT 2 18-NOV-98 1BFN 1 REMARK JRNL KEYWDS HEADER
REVDAT 1 28-OCT-98 1BFN 0
JRNL AUTH M.ADACHI,B.MIKAMI,T.KATSUBE,S.UTSUMI
JRNL TITL CRYSTAL STRUCTURE OF RECOMBINANT SOYBEAN BETA-AMYLASE
JRNL TITL 2 COMPLEXED WITH BETA-CYCLODEXTRIN.
JRNL REF J.BIOL.CHEM. V. 273 19859 1998
JRNL REFN ISSN 0021-9258
JRNL PMID 9677422
JRNL DOI 10.1074/JBC.273.31.19859
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.MIKAMI,M.DEGANO,E.J.HEHRE,J.C.SACCHETTINI
REMARK 1 TITL CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH
REMARK 1 TITL 2 BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR
REMARK 1 TITL 3 APPARENT ROLES IN CATALYSIS
REMARK 1 REF BIOCHEMISTRY V. 33 7779 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.MIKAMI,E.J.HEHRE,M.SATO,Y.KATSUBE,M.HIROSE,Y.MORITA,
REMARK 1 AUTH 2 J.C.SACCHETTINI
REMARK 1 TITL THE 2.0-A RESOLUTION STRUCTURE OF SOYBEAN BETA-AMYLASE
REMARK 1 TITL 2 COMPLEXED WITH ALPHA-CYCLODEXTRIN
REMARK 1 REF BIOCHEMISTRY V. 32 6836 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 1.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 80.7
REMARK 3 NUMBER OF REFLECTIONS : 34127
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : POSTERIORI
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3402
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.07
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3163
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE : 0.2480
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.74
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 360
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3915
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 82
REMARK 3 SOLVENT ATOMS : 318
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.30
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) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 10.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 2.890
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.110
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BFN 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_1000171698.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NOV-95
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 49% (NH4)2SO4, 0.1M NAOAC PH 5.4, 18MM
REMARK 280 2-MERCAPTOETHANOL, AT 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-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 48.26667
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 96.53333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 96.53333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 48.26667
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 119 NE2 HIS A 119 CD2 -0.068
REMARK 500 HIS A 146 NE2 HIS A 146 CD2 -0.068
REMARK 500 HIS A 226 NE2 HIS A 226 CD2 -0.067
REMARK 500 HIS A 273 NE2 HIS A 273 CD2 -0.075
REMARK 500 HIS A 308 NE2 HIS A 308 CD2 -0.072
REMARK 500 HIS A 335 NE2 HIS A 335 CD2 -0.066
REMARK 500 HIS A 442 NE2 HIS A 442 CD2 -0.067
REMARK 500 HIS A 456 NE2 HIS A 456 CD2 -0.078
REMARK 500
REMARK 500 REMARK: NULL
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 TRP A 55 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 55 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP A 56 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 56 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 TRP A 69 CD1 - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 TRP A 69 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ARG A 70 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ASP A 101 CA - C - N ANGL. DEV. = -14.2 DEGREES
REMARK 500 TRP A 110 CD1 - CG - CD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TRP A 110 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 130 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 130 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 148 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 162 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 TRP A 198 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP A 198 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 TRP A 229 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP A 229 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP A 265 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TRP A 265 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP A 301 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 TRP A 302 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 TRP A 302 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 322 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 330 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 330 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG A 334 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 334 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 347 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 TRP A 371 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP A 371 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG A 385 NE - CZ - NH1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG A 385 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 LEU A 419 CA - C - N ANGL. DEV. = -23.4 DEGREES
REMARK 500 LEU A 419 O - C - N ANGL. DEV. = 13.4 DEGREES
REMARK 500 ARG A 420 CA - CB - CG ANGL. DEV. = -14.2 DEGREES
REMARK 500 TRP A 485 CD1 - CG - CD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TRP A 485 CB - CG - CD1 ANGL. DEV. = -8.6 DEGREES
REMARK 500 TRP A 485 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 GLY A 495 N - CA - C ANGL. DEV. = 15.6 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 GLU A 60 40.65 -105.82
REMARK 500 PHE A 92 30.14 -96.93
REMARK 500 ALA A 184 18.80 57.75
REMARK 500 PRO A 201 53.41 -109.56
REMARK 500 GLN A 207 55.06 -119.68
REMARK 500 ARG A 420 129.71 67.95
REMARK 500 ASP A 494 101.66 78.68
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BFN A 1 495 UNP P10538 AMYB_SOYBN 1 495
SEQADV 1BFN LEU A 76 UNP P10538 PHE 76 CLONING ARTIFACT
SEQADV 1BFN GLY A 202 UNP P10538 ARG 202 VARIANT
SEQADV 1BFN ARG A 399 UNP P10538 LYS 399 VARIANT
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 ASP 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 LYS PRO SER ALA PRO LYS ILE
SEQRES 37 A 495 PRO ILE GLU VAL LEU LEU GLU ALA THR LYS PRO THR LEU
SEQRES 38 A 495 PRO PHE PRO TRP LEU PRO GLU THR ASP MET LYS VAL ASP
SEQRES 39 A 495 GLY
HET GLC B 1 11
HET GLC B 2 11
HET GLC B 3 11
HET GLC B 4 11
HET GLC B 5 11
HET GLC B 6 11
HET GLC B 7 11
HET SO4 A 503 5
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 2 GLC 7(C6 H12 O6)
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *318(H2 O)
HELIX 1 1 MET A 7 ASN A 10 5 4
HELIX 2 2 PRO A 32 ALA A 44 1 13
HELIX 3 3 TRP A 56 ILE A 59 1 4
HELIX 4 4 ARG A 70 GLU A 81 1 12
HELIX 5 5 GLN A 109 SER A 117 1 9
HELIX 6 6 HIS A 119 ILE A 121 5 3
HELIX 7 7 VAL A 137 VAL A 139 5 3
HELIX 8 8 ALA A 150 ASN A 164 1 15
HELIX 9 9 SER A 166 GLU A 170 1 5
HELIX 10 10 PRO A 183 GLY A 185 5 3
HELIX 11 11 GLN A 194 GLN A 196 5 3
HELIX 12 12 LYS A 211 ARG A 223 1 13
HELIX 13 13 PRO A 242 SER A 244 5 3
HELIX 14 14 THR A 253 VAL A 255 5 3
HELIX 15 15 GLU A 257 ALA A 284 1 28
HELIX 16 16 ALA A 309 ALA A 314 1 6
HELIX 17 17 ARG A 326 HIS A 335 1 10
HELIX 18 18 ASP A 348 GLU A 350 5 3
HELIX 19 19 SER A 353 ALA A 355 5 3
HELIX 20 20 PRO A 359 ARG A 372 1 14
HELIX 21 21 ALA A 388 ALA A 398 1 11
HELIX 22 22 LYS A 428 MET A 441 1 14
HELIX 23 23 PRO A 451 TYR A 454 5 4
HELIX 24 24 ILE A 470 THR A 477 1 8
SHEET 1 A 9 VAL A 416 TYR A 418 0
SHEET 2 A 9 VAL A 14 MET A 17 1 N TYR A 15 O VAL A 416
SHEET 3 A 9 GLY A 49 TRP A 55 1 N GLY A 49 O VAL A 16
SHEET 4 A 9 THR A 85 SER A 91 1 N THR A 85 O VAL A 50
SHEET 5 A 9 ILE A 174 VAL A 179 1 N ILE A 175 O LEU A 86
SHEET 6 A 9 LYS A 291 LYS A 295 1 N LYS A 291 O ILE A 177
SHEET 7 A 9 ILE A 338 PHE A 341 1 N ILE A 338 O ILE A 294
SHEET 8 A 9 ARG A 376 GLU A 380 1 N ARG A 376 O LEU A 339
SHEET 9 A 9 GLY A 415 THR A 417 1 N GLY A 415 O GLY A 379
SHEET 1 B 2 PHE A 122 THR A 124 0
SHEET 2 B 2 ARG A 130 LEU A 135 -1 N TYR A 134 O TYR A 123
LINK O4 GLC B 1 C1 GLC B 2 1555 1555 1.45
LINK C1 GLC B 1 O4 GLC B 7 1555 1555 1.47
LINK O4 GLC B 2 C1 GLC B 3 1555 1555 1.46
LINK O4 GLC B 3 C1 GLC B 4 1555 1555 1.45
LINK O4 GLC B 4 C1 GLC B 5 1555 1555 1.43
LINK O4 GLC B 5 C1 GLC B 6 1555 1555 1.43
LINK O4 GLC B 6 C1 GLC B 7 1555 1555 1.45
CISPEP 1 PHE A 200 PRO A 201 0 2.45
CRYST1 86.030 86.030 144.800 90.00 90.00 120.00 P 31 2 1 6
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 0.011624 0.006711 0.000000 0.00000
SCALE2 0.000000 0.013422 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006906 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
