HEADER HYDROLASE(O-GLYCOSYL) 25-JAN-94 1BYC
TITLE CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE
TITLE 2 AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN
TITLE 3 CATALYSIS
CAVEAT 1BYC ASN A 6 HAS WRONG CHIRALITY AT ATOM CA THR A 256 HAS WRONG
CAVEAT 2 1BYC CHIRALITY AT ATOM CB
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
KEYWDS HYDROLASE(O-GLYCOSYL)
EXPDTA X-RAY DIFFRACTION
AUTHOR B.MIKAMI,M.DEGANO,E.J.HEHRE,J.C.SACCHETTINI
REVDAT 9 07-FEB-24 1BYC 1 HETSYN LINK
REVDAT 8 29-JUL-20 1BYC 1 CAVEAT COMPND REMARK HETNAM
REVDAT 8 2 1 LINK SITE ATOM
REVDAT 7 14-AUG-19 1BYC 1 REMARK
REVDAT 6 17-JUL-19 1BYC 1 REMARK LINK
REVDAT 5 25-AUG-09 1BYC 1 SOURCE
REVDAT 4 21-JUL-09 1BYC 1 HETATM
REVDAT 3 24-FEB-09 1BYC 1 VERSN
REVDAT 2 01-APR-03 1BYC 1 JRNL
REVDAT 1 31-JUL-94 1BYC 0
JRNL AUTH B.MIKAMI,M.DEGANO,E.J.HEHRE,J.C.SACCHETTINI
JRNL TITL CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH
JRNL TITL 2 BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR
JRNL TITL 3 APPARENT ROLES IN CATALYSIS.
JRNL REF BIOCHEMISTRY V. 33 7779 1994
JRNL REFN ISSN 0006-2960
JRNL PMID 8011643
JRNL DOI 10.1021/BI00191A005
REMARK 1
REMARK 1 REFERENCE 1
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-ANGSTROMS RESOLUTION STRUCTURE OF SOYBEAN
REMARK 1 TITL 2 BETA-AMYLASE COMPLEXED WITH ALPHA-CYCLODEXTRIN
REMARK 1 REF BIOCHEMISTRY V. 32 6836 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 9.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 42972
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3925
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 332
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BYC 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_1000172147.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
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) : NULL
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
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 48.06667
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 96.13333
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 96.13333
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 48.06667
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLY A 495 CA C O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NE ARG A 202 O ASN A 239 2.00
REMARK 500
REMARK 500 REMARK: NULL
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 GLU A 30 CD GLU A 30 OE2 0.067
REMARK 500 GLU A 37 CD GLU A 37 OE2 0.105
REMARK 500 GLU A 60 CD GLU A 60 OE2 0.078
REMARK 500 GLU A 116 CD GLU A 116 OE2 0.075
REMARK 500 GLU A 163 CD GLU A 163 OE1 0.080
REMARK 500 GLU A 170 CD GLU A 170 OE1 0.108
REMARK 500 GLU A 205 CD GLU A 205 OE1 0.068
REMARK 500 GLU A 228 CD GLU A 228 OE2 0.086
REMARK 500 GLU A 257 CD GLU A 257 OE2 0.106
REMARK 500 GLU A 306 CD GLU A 306 OE2 0.118
REMARK 500 ARG A 347 NE ARG A 347 CZ 0.104
REMARK 500 GLU A 350 CD GLU A 350 OE1 0.080
REMARK 500 GLU A 471 CD GLU A 471 OE2 0.075
REMARK 500 GLU A 475 CD GLU A 475 OE1 0.086
REMARK 500 GLU A 488 CD GLU A 488 OE2 0.073
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 GLY A 21 C - N - CA ANGL. DEV. = -12.8 DEGREES
REMARK 500 ASP A 31 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 31 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP A 33 CB - CG - OD1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP A 68 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 68 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 130 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 148 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP A 156 CB - CG - OD1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP A 156 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 162 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 202 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP A 216 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP A 216 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP A 233 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP A 233 CB - CG - OD2 ANGL. DEV. = -9.4 DEGREES
REMARK 500 ASP A 234 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ASP A 240 CB - CG - OD1 ANGL. DEV. = -8.5 DEGREES
REMARK 500 ASP A 240 CB - CG - OD2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 ASP A 279 CB - CG - OD1 ANGL. DEV. = -8.3 DEGREES
REMARK 500 ASP A 279 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 THR A 313 N - CA - CB ANGL. DEV. = 22.6 DEGREES
REMARK 500 ASP A 321 CB - CG - OD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP A 321 CB - CG - OD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG A 322 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP A 323 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 347 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ASP A 348 CB - CG - OD1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP A 354 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 372 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 420 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP A 424 CB - CG - OD1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ASP A 424 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP A 444 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 446 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP A 490 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP A 494 CB - CG - OD1 ANGL. DEV. = -6.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 66 75.65 -102.40
REMARK 500 PHE A 92 30.65 -93.62
REMARK 500 ASP A 101 88.85 -66.23
REMARK 500 TYR A 134 147.02 -173.84
REMARK 500 PHE A 145 76.96 -103.55
REMARK 500 ALA A 184 14.64 56.71
REMARK 500 TRP A 198 137.20 -22.10
REMARK 500 PHE A 200 -102.29 -25.67
REMARK 500 PRO A 201 32.23 -67.45
REMARK 500 THR A 313 -58.71 103.26
REMARK 500 SER A 349 2.05 -69.50
REMARK 500 ARG A 420 140.21 77.15
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 TYR A 11 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BYC A 1 495 UNP P10538 AMYB_SOYBN 1 495
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 PHE 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 ARG 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 LYS 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 BGC B 1 12
HET GLC B 2 11
HET GLC B 3 11
HET GLC B 4 11
HET SO4 A 860 5
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE 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 3(C6 H12 O6)
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *332(H2 O)
HELIX 1 A1 PRO A 32 ALA A 45 1 14
HELIX 2 A2 ARG A 70 GLU A 81 1 12
HELIX 3 A3 GLN A 109 SER A 117 1 9
HELIX 4 A4 ALA A 150 GLU A 170 1 21
HELIX 5 A5 LYS A 211 ALA A 224 1 14
HELIX 6 A6 LYS A 258 ALA A 284 1 27
HELIX 7 A7 ALA A 309 THR A 313 1 5
HELIX 8 A8 TYR A 325 ARG A 334 1 10
HELIX 9 A9 PRO A 359 GLU A 373 1 15
HELIX 10 A10 ASP A 387 LYS A 399 1 13
HELIX 11 A11 GLN A 427 HIS A 442 1 16
HELIX 12 A12 PRO A 469 GLU A 475 1 7
SHEET 1 S1 8 PRO A 13 LEU A 20 0
SHEET 2 S1 8 GLY A 49 TRP A 55 1 O MET A 51 N LEU A 18
SHEET 3 S1 8 THR A 85 SER A 91 1 O GLN A 87 N VAL A 52
SHEET 4 S1 8 ASP A 176 LEU A 181 1 O ASP A 176 N ALA A 88
SHEET 5 S1 8 VAL A 290 VAL A 296 1 O LYS A 291 N ILE A 177
SHEET 6 S1 8 ALA A 337 CYS A 343 1 O ILE A 338 N ILE A 294
SHEET 7 S1 8 ILE A 375 ASN A 381 1 O ALA A 378 N PHE A 341
SHEET 8 S1 8 GLY A 415 LEU A 419 1 N THR A 417 O GLY A 379
LINK O4 BGC B 1 C1 GLC B 2 1555 1555 1.62
LINK O4 GLC B 2 C1 GLC B 3 1555 1555 1.42
LINK O4 GLC B 3 C1 GLC B 4 1555 1555 1.42
CRYST1 86.200 86.200 144.200 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 0.011601 0.006698 0.000000 0.00000
SCALE2 0.000000 0.013396 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006935 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
