HEADER BINDING PROTEINS 15-NOV-91 1APB
TITLE A PRO TO GLY MUTATION IN THE HINGE OF THE ARABINOSE-BINDING PROTEIN
TITLE 2 ENHANCES BINDING AND ALTERS SPECIFICITY: SUGAR-BINDING AND
TITLE 3 CRYSTALLOGRAPHIC STUDIES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: L-ARABINOSE-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS BINDING PROTEINS
EXPDTA X-RAY DIFFRACTION
AUTHOR P.S.VERMERSCH,J.J.G.TESMER,F.A.QUIOCHO
REVDAT 6 07-FEB-24 1APB 1 HETSYN
REVDAT 5 29-JUL-20 1APB 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 LINK SITE ATOM
REVDAT 4 24-FEB-09 1APB 1 VERSN
REVDAT 3 17-MAY-05 1APB 1 REMARK
REVDAT 2 01-APR-03 1APB 1 JRNL
REVDAT 1 15-JAN-92 1APB 0
JRNL AUTH P.S.VERMERSCH,J.J.TESMER,D.D.LEMON,F.A.QUIOCHO
JRNL TITL A PRO TO GLY MUTATION IN THE HINGE OF THE ARABINOSE-BINDING
JRNL TITL 2 PROTEIN ENHANCES BINDING AND ALTERS SPECIFICITY.
JRNL TITL 3 SUGAR-BINDING AND CRYSTALLOGRAPHIC STUDIES.
JRNL REF J.BIOL.CHEM. V. 265 16592 1990
JRNL REFN ISSN 0021-9258
JRNL PMID 2204627
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.A.QUIOCHO,D.K.WILSON,N.K.VYAS
REMARK 1 TITL SUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY
REMARK 1 TITL 2 BOUND WATER MOLECULES
REMARK 1 REF NATURE V. 340 404 1989
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.A.QUIOCHO,N.K.VYAS
REMARK 1 TITL NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN
REMARK 1 REF NATURE V. 310 381 1984
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 3
REMARK 1 AUTH B.MAO,M.R.PEAR,J.A.MCCAMMON,F.A.QUIOCHO
REMARK 1 TITL HINGE-BENDING IN L-ARABINOSE-BINDING PROTEIN. THE
REMARK 1 TITL 2 "VENUS'S-FLYTRAP" MODEL
REMARK 1 REF J.BIOL.CHEM. V. 257 1131 1982
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 4
REMARK 1 AUTH G.L.GILLILAND,F.A.QUIOCHO
REMARK 1 TITL STRUCTURE OF THE L-ARABINOSE-BINDING PROTEIN FROM
REMARK 1 TITL 2 ESCHERICHIA COLI AT 2.4 ANGSTROMS RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 146 341 1981
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 5
REMARK 1 AUTH M.E.NEWCOMER,G.L.GILLIAND,F.A.QUIOCHO
REMARK 1 TITL L-ARABINOSE-BINDING PROTEIN-SUGAR COMPLEX AT 2.4 ANGSTROMS
REMARK 1 TITL 2 RESOLUTION. STEREOCHEMISTRY AND EVIDENCE FOR A STRUCTURAL
REMARK 1 TITL 3 CHANGE
REMARK 1 REF J.BIOL.CHEM. V. 256 13213 1981
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 6
REMARK 1 AUTH M.E.NEWCOMER,B.A.LEWIS,F.A.QUIOCHO
REMARK 1 TITL THE RADIUS OF GYRATION OF L-ARABINOSE-BINDING PROTEIN
REMARK 1 TITL 2 DECREASES UPON BINDING OF LIGAND
REMARK 1 REF J.BIOL.CHEM. V. 256 13218 1981
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 7
REMARK 1 AUTH D.M.MILLER /III,M.E.NEWCOMER,F.A.QUIOCHO
REMARK 1 TITL THE THIOL GROUP OF THE L-ARABINOSE-BINDING PROTEIN.
REMARK 1 TITL 2 CHROMOPHORIC LABELING AND CHEMICAL IDENTIFICATION OF THE
REMARK 1 TITL 3 SUGAR-BINDING SITE
REMARK 1 REF J.BIOL.CHEM. V. 254 7521 1979
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 8
REMARK 1 AUTH M.E.NEWCOMER,D.M.MILLER /III,F.A.QUIOCHO
REMARK 1 TITL LOCATION OF THE SUGAR-BINDING SITE OF L-ARABINOSE-BINDING
REMARK 1 TITL 2 PROTEIN. SUGAR DERIVATIVE SYNTHESES, SUGAR BINDING
REMARK 1 TITL 3 SPECIFICITY, AND DIFFERENCE FOURIER ANALYSES
REMARK 1 REF J.BIOL.CHEM. V. 254 7529 1979
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 9
REMARK 1 AUTH F.A.QUIOCHO,G.L.GILLILAND,G.N.PHILLIPS JR.
REMARK 1 TITL THE 2.8-ANGSTROMS RESOLUTION STRUCTURE OF THE
REMARK 1 TITL 2 L-ARABINOSE-BINDING PROTEIN FROM ESCHERICHIA COLI
REMARK 1 REF J.BIOL.CHEM. V. 252 5142 1977
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 10
REMARK 1 AUTH G.N.PHILLIPS JR.,V.K.MAHAJAN,A.K.Q.SIU,F.A.QUIOCHO
REMARK 1 TITL STRUCTURE OF L-ARABINOSE-BINDING PROTEIN FROM ESCHERICHIA
REMARK 1 TITL 2 COLI AT 5 ANGSTROMS RESOLUTION AND PRELIMINARY RESULTS AT
REMARK 1 TITL 3 3.5 ANGSTROMS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 73 2186 1976
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 1.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 24421
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : NULL
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 FIT/AGREEMENT OF MODEL WITH ALL DATA.
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 : 2313
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 168
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.004 ; 0.005
REMARK 3 ANGLE DISTANCE (A) : 0.011 ; 0.010
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.017 ; 0.010
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.032 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.085 ; 0.050
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.622 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.298 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.781 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.477 ; 3.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1APB 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_1000171091.
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 27.73000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.92000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.91000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.92000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.73000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.91000
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
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 GLU A 1
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 ASN A 2 CB CG OD1 ND2
REMARK 470 LYS A 306 CB CG CD CE NZ
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 ND2 ASN A 269 O HOH A 380 2.06
REMARK 500 CD GLU A 296 O HOH A 406 2.11
REMARK 500 OE1 GLU A 14 O HOH A 328 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 373 O HOH A 469 4466 1.69
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 ASP A 89 -65.41 78.40
REMARK 500 ASN A 177 57.61 -91.80
REMARK 500 ASN A 232 -50.71 141.05
REMARK 500 LYS A 273 22.50 -149.15
REMARK 500 ASP A 274 49.22 31.59
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 A 128 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 SER A 241 10.46
REMARK 500 GLU A 296 14.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 SINCE IT HAS BEEN SHOWN THAT ABP CAN BIND EITHER ALPHA OR
REMARK 600 BETA ANOMERS OF D-FUCOSE WITH ALMOST EQUAL AFFINITY, BOTH
REMARK 600 ARE PROVIDED IN THE SAME SITE.
DBREF 1APB A 1 306 UNP P02924 ARAF_ECOLI 24 329
SEQADV 1APB GLY A 254 UNP P02924 PRO 277 CONFLICT
SEQRES 1 A 306 GLU ASN LEU LYS LEU GLY PHE LEU VAL LYS GLN PRO GLU
SEQRES 2 A 306 GLU PRO TRP PHE GLN THR GLU TRP LYS PHE ALA ASP LYS
SEQRES 3 A 306 ALA GLY LYS ASP LEU GLY PHE GLU VAL ILE LYS ILE ALA
SEQRES 4 A 306 VAL PRO ASP GLY GLU LYS THR LEU ASN ALA ILE ASP SER
SEQRES 5 A 306 LEU ALA ALA SER GLY ALA LYS GLY PHE VAL ILE CYS THR
SEQRES 6 A 306 PRO ASP PRO LYS LEU GLY SER ALA ILE VAL ALA LYS ALA
SEQRES 7 A 306 ARG GLY TYR ASP MET LYS VAL ILE ALA VAL ASP ASP GLN
SEQRES 8 A 306 PHE VAL ASN ALA LYS GLY LYS PRO MET ASP THR VAL PRO
SEQRES 9 A 306 LEU VAL MET MET ALA ALA THR LYS ILE GLY GLU ARG GLN
SEQRES 10 A 306 GLY GLN GLU LEU TYR LYS GLU MET GLN LYS ARG GLY TRP
SEQRES 11 A 306 ASP VAL LYS GLU SER ALA VAL MET ALA ILE THR ALA ASN
SEQRES 12 A 306 GLU LEU ASP THR ALA ARG ARG ARG THR THR GLY SER MET
SEQRES 13 A 306 ASP ALA LEU LYS ALA ALA GLY PHE PRO GLU LYS GLN ILE
SEQRES 14 A 306 TYR GLN VAL PRO THR LYS SER ASN ASP ILE PRO GLY ALA
SEQRES 15 A 306 PHE ASP ALA ALA ASN SER MET LEU VAL GLN HIS PRO GLU
SEQRES 16 A 306 VAL LYS HIS TRP LEU ILE VAL GLY MET ASN ASP SER THR
SEQRES 17 A 306 VAL LEU GLY GLY VAL ARG ALA THR GLU GLY GLN GLY PHE
SEQRES 18 A 306 LYS ALA ALA ASP ILE ILE GLY ILE GLY ILE ASN GLY VAL
SEQRES 19 A 306 ASP ALA VAL SER GLU LEU SER LYS ALA GLN ALA THR GLY
SEQRES 20 A 306 PHE TYR GLY SER LEU LEU GLY SER PRO ASP VAL HIS GLY
SEQRES 21 A 306 TYR LYS SER SER GLU MET LEU TYR ASN TRP VAL ALA LYS
SEQRES 22 A 306 ASP VAL GLU PRO PRO LYS PHE THR GLU VAL THR ASP VAL
SEQRES 23 A 306 VAL LEU ILE THR ARG ASP ASN PHE LYS GLU GLU LEU GLU
SEQRES 24 A 306 LYS LYS GLY LEU GLY GLY LYS
HET FCA A 307 11
HET FCB A 308 11
HETNAM FCA ALPHA-D-FUCOPYRANOSE
HETNAM FCB BETA-D-FUCOPYRANOSE
HETSYN FCA ALPHA-D-FUCOSE; 6-DEOXY-ALPHA-D-GALACTOPYRANOSE; D-
HETSYN 2 FCA FUCOSE; FUCOSE
HETSYN FCB BETA-D-FUCOSE; 6-DEOXY-BETA-D-GALACTOPYRANOSE; D-
HETSYN 2 FCB FUCOSE; FUCOSE
FORMUL 2 FCA C6 H12 O5
FORMUL 3 FCB C6 H12 O5
FORMUL 4 HOH *168(H2 O)
HELIX 1 H01 TRP A 16 ASP A 30 1 15
HELIX 2 H02 ASP A 42 GLY A 57 1 16
HELIX 3 H03 LEU A 70 TYR A 81 1 12
HELIX 4 H04 ALA A 109 GLY A 129 1 21
HELIX 5 H05 ASP A 146 ALA A 161 1 16
HELIX 6 H06 ASN A 177 GLN A 192 1 16
HELIX 7 H07 ASP A 206 GLY A 218 1 13
HELIX 8 H08 GLY A 233 SER A 241 1HAS SEGMENTS OF 3/10 HELIX 9
HELIX 9 H09 ASP A 257 LYS A 273 1 17
HELIX 10 H10 ASN A 293 LYS A 301 1HAS SEGMENTS OF 3/10 HELIX 9
SHEET 1 S1 6 GLU A 34 ALA A 39 0
SHEET 2 S1 6 LYS A 4 LYS A 10 1 N VAL A 9 O ILE A 38
SHEET 3 S1 6 LYS A 59 CYS A 64 1 N GLY A 60 O LYS A 4
SHEET 4 S1 6 LYS A 84 ASP A 89 1 N ILE A 86 O PHE A 61
SHEET 5 S1 6 PRO A 104 ALA A 109 1 O PRO A 104 N ALA A 87
SHEET 6 S1 6 THR A 281 VAL A 283 1 N VAL A 283 O MET A 107
SHEET 1 S2 6 TYR A 170 VAL A 172 0
SHEET 2 S2 6 ALA A 136 THR A 141 1 N ALA A 139 O TYR A 170
SHEET 3 S2 6 TRP A 199 MET A 204 1 N LEU A 200 O ALA A 136
SHEET 4 S2 6 ASP A 225 ASN A 232 1 N ILE A 227 O TRP A 199
SHEET 5 S2 6 GLY A 247 LEU A 253 1 N GLY A 250 O GLY A 228
SHEET 6 S2 6 VAL A 287 ARG A 291 -1 N ILE A 289 O SER A 251
CRYST1 55.460 71.820 77.840 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 0.018031 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013924 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012847 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
