HEADER LYASE 14-MAR-02 1L6W
TITLE FRUCTOSE-6-PHOSPHATE ALDOLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRUCTOSE-6-PHOSPHATE ALDOLASE 1;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 EC: 4.1.2.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: FSA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PUC18FSA
KEYWDS ALPHA-BETA BARREL, DOMAIN SWAPPING, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.THORELL,M.SCHUERMANN,G.A.SPRENGER,G.SCHNEIDER
REVDAT 5 07-MAR-18 1L6W 1 REMARK
REVDAT 4 13-JUL-11 1L6W 1 VERSN
REVDAT 3 24-FEB-09 1L6W 1 VERSN
REVDAT 2 01-APR-03 1L6W 1 JRNL
REVDAT 1 12-JUN-02 1L6W 0
JRNL AUTH S.THORELL,M.SCHURMANN,G.A.SPRENGER,G.SCHNEIDER
JRNL TITL CRYSTAL STRUCTURE OF DECAMERIC FRUCTOSE-6-PHOSPHATE ALDOLASE
JRNL TITL 2 FROM ESCHERICHIA COLI REVEALS INTER-SUBUNIT HELIX SWAPPING
JRNL TITL 3 AS A STRUCTURAL BASIS FOR ASSEMBLY DIFFERENCES IN THE
JRNL TITL 4 TRANSALDOLASE FAMILY.
JRNL REF J.MOL.BIOL. V. 319 161 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12051943
JRNL DOI 10.1016/S0022-2836(02)00258-9
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.SCHUERMANN,G.A.SPRENGER
REMARK 1 TITL FRUCTOSE-6-PHOSPHATE ALDOLASE IS A NOVEL CLASS I ALDOLASE
REMARK 1 TITL 2 FROM ESCHERICHIA COLI AND IS RELATED TO A NOVEL GROUP OF
REMARK 1 TITL 3 BACTERIAL TRANSALDOLASES
REMARK 1 REF J.BIOL.CHEM. V. 276 11055 2000
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.M008061200
REMARK 2
REMARK 2 RESOLUTION. 1.93 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) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 200173
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10079
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.93
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 23678
REMARK 3 BIN R VALUE (WORKING SET) : 0.2020
REMARK 3 BIN FREE R VALUE : 0.2310
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1295
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 : 16130
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 1479
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.21000
REMARK 3 B22 (A**2) : -0.84000
REMARK 3 B33 (A**2) : -1.36000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.06
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.11
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : 0.920 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.340 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.010 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.810 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.41
REMARK 3 BSOL : 60.05
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 1L6W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015700.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-00
REMARK 200 TEMPERATURE (KELVIN) : 107
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 200177
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 19.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.03800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 46.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.12500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 18.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIR
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, SODIUM ACETATE, GLYCEROL, PH
REMARK 280 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
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 57.74500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 91.81000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.47000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 91.81000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 57.74500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.47000
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: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 41380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 69600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -317.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: 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 LEU F 163 CG LEU F 163 CD2 -0.344
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 PRO F 158 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 LEU F 163 CB - CG - CD2 ANGL. DEV. = 21.0 DEGREES
REMARK 500 PRO G 158 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO I 158 C - N - CA ANGL. DEV. = 9.1 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 LYS A 36 -26.43 72.21
REMARK 500 ALA A 157 62.07 -156.15
REMARK 500 SER A 166 89.43 72.62
REMARK 500 LYS B 36 -11.24 76.37
REMARK 500 ALA B 157 62.38 -155.35
REMARK 500 SER B 166 89.93 72.53
REMARK 500 LYS C 36 -11.41 69.23
REMARK 500 ALA C 157 62.17 -155.08
REMARK 500 SER C 166 89.28 73.15
REMARK 500 LYS D 36 -14.35 72.48
REMARK 500 ALA D 157 63.16 -154.19
REMARK 500 SER D 166 90.73 71.28
REMARK 500 LYS E 36 -6.95 66.25
REMARK 500 ALA E 157 61.99 -155.36
REMARK 500 SER E 166 89.48 72.55
REMARK 500 LYS F 36 -20.92 68.31
REMARK 500 ALA F 157 62.23 -155.69
REMARK 500 SER F 166 89.41 72.67
REMARK 500 LYS G 36 -21.27 70.77
REMARK 500 ALA G 157 62.32 -155.64
REMARK 500 SER G 166 90.10 72.32
REMARK 500 LYS H 36 -22.21 72.75
REMARK 500 ALA H 157 62.28 -155.58
REMARK 500 SER H 166 89.73 72.51
REMARK 500 LYS I 36 -23.24 69.17
REMARK 500 ALA I 157 62.23 -155.44
REMARK 500 SER I 166 89.62 73.04
REMARK 500 LYS J 36 -21.40 72.90
REMARK 500 ALA J 157 62.71 -155.41
REMARK 500 SER J 166 89.50 73.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 GOL A 250
REMARK 615 GOL B 250
REMARK 615 GOL C 250
REMARK 615 GOL D 250
REMARK 615 GOL E 250
REMARK 615 GOL F 250
REMARK 615 GOL G 250
REMARK 615 GOL H 250
REMARK 615 GOL I 250
REMARK 615 GOL J 250
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL I 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL J 250
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ONR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B
REMARK 900 RELATED ID: 1UCW RELATED DB: PDB
REMARK 900 COMPLEX OF ESCHERICHIA COLI TRANSALDOLASE B WITH THE REDUCED SCHIFF-
REMARK 900 BASE INTERMEDIATE
REMARK 900 RELATED ID: 1F05 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE
REMARK 900 RELATED ID: 1I2O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT E96A
REMARK 900 RELATED ID: 1I2P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT D17A
REMARK 900 RELATED ID: 1I2Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT T156A
DBREF 1L6W A 1 220 UNP P78055 FSAA_ECOLI 1 220
DBREF 1L6W B 1 220 UNP P78055 FSAA_ECOLI 1 220
DBREF 1L6W C 1 220 UNP P78055 FSAA_ECOLI 1 220
DBREF 1L6W D 1 220 UNP P78055 FSAA_ECOLI 1 220
DBREF 1L6W E 1 220 UNP P78055 FSAA_ECOLI 1 220
DBREF 1L6W F 1 220 UNP P78055 FSAA_ECOLI 1 220
DBREF 1L6W G 1 220 UNP P78055 FSAA_ECOLI 1 220
DBREF 1L6W H 1 220 UNP P78055 FSAA_ECOLI 1 220
DBREF 1L6W I 1 220 UNP P78055 FSAA_ECOLI 1 220
DBREF 1L6W J 1 220 UNP P78055 FSAA_ECOLI 1 220
SEQRES 1 A 220 MET GLU LEU TYR LEU ASP THR SER ASP VAL VAL ALA VAL
SEQRES 2 A 220 LYS ALA LEU SER ARG ILE PHE PRO LEU ALA GLY VAL THR
SEQRES 3 A 220 THR ASN PRO SER ILE ILE ALA ALA GLY LYS LYS PRO LEU
SEQRES 4 A 220 ASP VAL VAL LEU PRO GLN LEU HIS GLU ALA MET GLY GLY
SEQRES 5 A 220 GLN GLY ARG LEU PHE ALA GLN VAL MET ALA THR THR ALA
SEQRES 6 A 220 GLU GLY MET VAL ASN ASP ALA LEU LYS LEU ARG SER ILE
SEQRES 7 A 220 ILE ALA ASP ILE VAL VAL LYS VAL PRO VAL THR ALA GLU
SEQRES 8 A 220 GLY LEU ALA ALA ILE LYS MET LEU LYS ALA GLU GLY ILE
SEQRES 9 A 220 PRO THR LEU GLY THR ALA VAL TYR GLY ALA ALA GLN GLY
SEQRES 10 A 220 LEU LEU SER ALA LEU ALA GLY ALA GLU TYR VAL ALA PRO
SEQRES 11 A 220 TYR VAL ASN ARG ILE ASP ALA GLN GLY GLY SER GLY ILE
SEQRES 12 A 220 GLN THR VAL THR ASP LEU HIS GLN LEU LEU LYS MET HIS
SEQRES 13 A 220 ALA PRO GLN ALA LYS VAL LEU ALA ALA SER PHE LYS THR
SEQRES 14 A 220 PRO ARG GLN ALA LEU ASP CYS LEU LEU ALA GLY CYS GLU
SEQRES 15 A 220 SER ILE THR LEU PRO LEU ASP VAL ALA GLN GLN MET ILE
SEQRES 16 A 220 SER TYR PRO ALA VAL ASP ALA ALA VAL ALA LYS PHE GLU
SEQRES 17 A 220 GLN ASP TRP GLN GLY ALA PHE GLY ARG THR SER ILE
SEQRES 1 B 220 MET GLU LEU TYR LEU ASP THR SER ASP VAL VAL ALA VAL
SEQRES 2 B 220 LYS ALA LEU SER ARG ILE PHE PRO LEU ALA GLY VAL THR
SEQRES 3 B 220 THR ASN PRO SER ILE ILE ALA ALA GLY LYS LYS PRO LEU
SEQRES 4 B 220 ASP VAL VAL LEU PRO GLN LEU HIS GLU ALA MET GLY GLY
SEQRES 5 B 220 GLN GLY ARG LEU PHE ALA GLN VAL MET ALA THR THR ALA
SEQRES 6 B 220 GLU GLY MET VAL ASN ASP ALA LEU LYS LEU ARG SER ILE
SEQRES 7 B 220 ILE ALA ASP ILE VAL VAL LYS VAL PRO VAL THR ALA GLU
SEQRES 8 B 220 GLY LEU ALA ALA ILE LYS MET LEU LYS ALA GLU GLY ILE
SEQRES 9 B 220 PRO THR LEU GLY THR ALA VAL TYR GLY ALA ALA GLN GLY
SEQRES 10 B 220 LEU LEU SER ALA LEU ALA GLY ALA GLU TYR VAL ALA PRO
SEQRES 11 B 220 TYR VAL ASN ARG ILE ASP ALA GLN GLY GLY SER GLY ILE
SEQRES 12 B 220 GLN THR VAL THR ASP LEU HIS GLN LEU LEU LYS MET HIS
SEQRES 13 B 220 ALA PRO GLN ALA LYS VAL LEU ALA ALA SER PHE LYS THR
SEQRES 14 B 220 PRO ARG GLN ALA LEU ASP CYS LEU LEU ALA GLY CYS GLU
SEQRES 15 B 220 SER ILE THR LEU PRO LEU ASP VAL ALA GLN GLN MET ILE
SEQRES 16 B 220 SER TYR PRO ALA VAL ASP ALA ALA VAL ALA LYS PHE GLU
SEQRES 17 B 220 GLN ASP TRP GLN GLY ALA PHE GLY ARG THR SER ILE
SEQRES 1 C 220 MET GLU LEU TYR LEU ASP THR SER ASP VAL VAL ALA VAL
SEQRES 2 C 220 LYS ALA LEU SER ARG ILE PHE PRO LEU ALA GLY VAL THR
SEQRES 3 C 220 THR ASN PRO SER ILE ILE ALA ALA GLY LYS LYS PRO LEU
SEQRES 4 C 220 ASP VAL VAL LEU PRO GLN LEU HIS GLU ALA MET GLY GLY
SEQRES 5 C 220 GLN GLY ARG LEU PHE ALA GLN VAL MET ALA THR THR ALA
SEQRES 6 C 220 GLU GLY MET VAL ASN ASP ALA LEU LYS LEU ARG SER ILE
SEQRES 7 C 220 ILE ALA ASP ILE VAL VAL LYS VAL PRO VAL THR ALA GLU
SEQRES 8 C 220 GLY LEU ALA ALA ILE LYS MET LEU LYS ALA GLU GLY ILE
SEQRES 9 C 220 PRO THR LEU GLY THR ALA VAL TYR GLY ALA ALA GLN GLY
SEQRES 10 C 220 LEU LEU SER ALA LEU ALA GLY ALA GLU TYR VAL ALA PRO
SEQRES 11 C 220 TYR VAL ASN ARG ILE ASP ALA GLN GLY GLY SER GLY ILE
SEQRES 12 C 220 GLN THR VAL THR ASP LEU HIS GLN LEU LEU LYS MET HIS
SEQRES 13 C 220 ALA PRO GLN ALA LYS VAL LEU ALA ALA SER PHE LYS THR
SEQRES 14 C 220 PRO ARG GLN ALA LEU ASP CYS LEU LEU ALA GLY CYS GLU
SEQRES 15 C 220 SER ILE THR LEU PRO LEU ASP VAL ALA GLN GLN MET ILE
SEQRES 16 C 220 SER TYR PRO ALA VAL ASP ALA ALA VAL ALA LYS PHE GLU
SEQRES 17 C 220 GLN ASP TRP GLN GLY ALA PHE GLY ARG THR SER ILE
SEQRES 1 D 220 MET GLU LEU TYR LEU ASP THR SER ASP VAL VAL ALA VAL
SEQRES 2 D 220 LYS ALA LEU SER ARG ILE PHE PRO LEU ALA GLY VAL THR
SEQRES 3 D 220 THR ASN PRO SER ILE ILE ALA ALA GLY LYS LYS PRO LEU
SEQRES 4 D 220 ASP VAL VAL LEU PRO GLN LEU HIS GLU ALA MET GLY GLY
SEQRES 5 D 220 GLN GLY ARG LEU PHE ALA GLN VAL MET ALA THR THR ALA
SEQRES 6 D 220 GLU GLY MET VAL ASN ASP ALA LEU LYS LEU ARG SER ILE
SEQRES 7 D 220 ILE ALA ASP ILE VAL VAL LYS VAL PRO VAL THR ALA GLU
SEQRES 8 D 220 GLY LEU ALA ALA ILE LYS MET LEU LYS ALA GLU GLY ILE
SEQRES 9 D 220 PRO THR LEU GLY THR ALA VAL TYR GLY ALA ALA GLN GLY
SEQRES 10 D 220 LEU LEU SER ALA LEU ALA GLY ALA GLU TYR VAL ALA PRO
SEQRES 11 D 220 TYR VAL ASN ARG ILE ASP ALA GLN GLY GLY SER GLY ILE
SEQRES 12 D 220 GLN THR VAL THR ASP LEU HIS GLN LEU LEU LYS MET HIS
SEQRES 13 D 220 ALA PRO GLN ALA LYS VAL LEU ALA ALA SER PHE LYS THR
SEQRES 14 D 220 PRO ARG GLN ALA LEU ASP CYS LEU LEU ALA GLY CYS GLU
SEQRES 15 D 220 SER ILE THR LEU PRO LEU ASP VAL ALA GLN GLN MET ILE
SEQRES 16 D 220 SER TYR PRO ALA VAL ASP ALA ALA VAL ALA LYS PHE GLU
SEQRES 17 D 220 GLN ASP TRP GLN GLY ALA PHE GLY ARG THR SER ILE
SEQRES 1 E 220 MET GLU LEU TYR LEU ASP THR SER ASP VAL VAL ALA VAL
SEQRES 2 E 220 LYS ALA LEU SER ARG ILE PHE PRO LEU ALA GLY VAL THR
SEQRES 3 E 220 THR ASN PRO SER ILE ILE ALA ALA GLY LYS LYS PRO LEU
SEQRES 4 E 220 ASP VAL VAL LEU PRO GLN LEU HIS GLU ALA MET GLY GLY
SEQRES 5 E 220 GLN GLY ARG LEU PHE ALA GLN VAL MET ALA THR THR ALA
SEQRES 6 E 220 GLU GLY MET VAL ASN ASP ALA LEU LYS LEU ARG SER ILE
SEQRES 7 E 220 ILE ALA ASP ILE VAL VAL LYS VAL PRO VAL THR ALA GLU
SEQRES 8 E 220 GLY LEU ALA ALA ILE LYS MET LEU LYS ALA GLU GLY ILE
SEQRES 9 E 220 PRO THR LEU GLY THR ALA VAL TYR GLY ALA ALA GLN GLY
SEQRES 10 E 220 LEU LEU SER ALA LEU ALA GLY ALA GLU TYR VAL ALA PRO
SEQRES 11 E 220 TYR VAL ASN ARG ILE ASP ALA GLN GLY GLY SER GLY ILE
SEQRES 12 E 220 GLN THR VAL THR ASP LEU HIS GLN LEU LEU LYS MET HIS
SEQRES 13 E 220 ALA PRO GLN ALA LYS VAL LEU ALA ALA SER PHE LYS THR
SEQRES 14 E 220 PRO ARG GLN ALA LEU ASP CYS LEU LEU ALA GLY CYS GLU
SEQRES 15 E 220 SER ILE THR LEU PRO LEU ASP VAL ALA GLN GLN MET ILE
SEQRES 16 E 220 SER TYR PRO ALA VAL ASP ALA ALA VAL ALA LYS PHE GLU
SEQRES 17 E 220 GLN ASP TRP GLN GLY ALA PHE GLY ARG THR SER ILE
SEQRES 1 F 220 MET GLU LEU TYR LEU ASP THR SER ASP VAL VAL ALA VAL
SEQRES 2 F 220 LYS ALA LEU SER ARG ILE PHE PRO LEU ALA GLY VAL THR
SEQRES 3 F 220 THR ASN PRO SER ILE ILE ALA ALA GLY LYS LYS PRO LEU
SEQRES 4 F 220 ASP VAL VAL LEU PRO GLN LEU HIS GLU ALA MET GLY GLY
SEQRES 5 F 220 GLN GLY ARG LEU PHE ALA GLN VAL MET ALA THR THR ALA
SEQRES 6 F 220 GLU GLY MET VAL ASN ASP ALA LEU LYS LEU ARG SER ILE
SEQRES 7 F 220 ILE ALA ASP ILE VAL VAL LYS VAL PRO VAL THR ALA GLU
SEQRES 8 F 220 GLY LEU ALA ALA ILE LYS MET LEU LYS ALA GLU GLY ILE
SEQRES 9 F 220 PRO THR LEU GLY THR ALA VAL TYR GLY ALA ALA GLN GLY
SEQRES 10 F 220 LEU LEU SER ALA LEU ALA GLY ALA GLU TYR VAL ALA PRO
SEQRES 11 F 220 TYR VAL ASN ARG ILE ASP ALA GLN GLY GLY SER GLY ILE
SEQRES 12 F 220 GLN THR VAL THR ASP LEU HIS GLN LEU LEU LYS MET HIS
SEQRES 13 F 220 ALA PRO GLN ALA LYS VAL LEU ALA ALA SER PHE LYS THR
SEQRES 14 F 220 PRO ARG GLN ALA LEU ASP CYS LEU LEU ALA GLY CYS GLU
SEQRES 15 F 220 SER ILE THR LEU PRO LEU ASP VAL ALA GLN GLN MET ILE
SEQRES 16 F 220 SER TYR PRO ALA VAL ASP ALA ALA VAL ALA LYS PHE GLU
SEQRES 17 F 220 GLN ASP TRP GLN GLY ALA PHE GLY ARG THR SER ILE
SEQRES 1 G 220 MET GLU LEU TYR LEU ASP THR SER ASP VAL VAL ALA VAL
SEQRES 2 G 220 LYS ALA LEU SER ARG ILE PHE PRO LEU ALA GLY VAL THR
SEQRES 3 G 220 THR ASN PRO SER ILE ILE ALA ALA GLY LYS LYS PRO LEU
SEQRES 4 G 220 ASP VAL VAL LEU PRO GLN LEU HIS GLU ALA MET GLY GLY
SEQRES 5 G 220 GLN GLY ARG LEU PHE ALA GLN VAL MET ALA THR THR ALA
SEQRES 6 G 220 GLU GLY MET VAL ASN ASP ALA LEU LYS LEU ARG SER ILE
SEQRES 7 G 220 ILE ALA ASP ILE VAL VAL LYS VAL PRO VAL THR ALA GLU
SEQRES 8 G 220 GLY LEU ALA ALA ILE LYS MET LEU LYS ALA GLU GLY ILE
SEQRES 9 G 220 PRO THR LEU GLY THR ALA VAL TYR GLY ALA ALA GLN GLY
SEQRES 10 G 220 LEU LEU SER ALA LEU ALA GLY ALA GLU TYR VAL ALA PRO
SEQRES 11 G 220 TYR VAL ASN ARG ILE ASP ALA GLN GLY GLY SER GLY ILE
SEQRES 12 G 220 GLN THR VAL THR ASP LEU HIS GLN LEU LEU LYS MET HIS
SEQRES 13 G 220 ALA PRO GLN ALA LYS VAL LEU ALA ALA SER PHE LYS THR
SEQRES 14 G 220 PRO ARG GLN ALA LEU ASP CYS LEU LEU ALA GLY CYS GLU
SEQRES 15 G 220 SER ILE THR LEU PRO LEU ASP VAL ALA GLN GLN MET ILE
SEQRES 16 G 220 SER TYR PRO ALA VAL ASP ALA ALA VAL ALA LYS PHE GLU
SEQRES 17 G 220 GLN ASP TRP GLN GLY ALA PHE GLY ARG THR SER ILE
SEQRES 1 H 220 MET GLU LEU TYR LEU ASP THR SER ASP VAL VAL ALA VAL
SEQRES 2 H 220 LYS ALA LEU SER ARG ILE PHE PRO LEU ALA GLY VAL THR
SEQRES 3 H 220 THR ASN PRO SER ILE ILE ALA ALA GLY LYS LYS PRO LEU
SEQRES 4 H 220 ASP VAL VAL LEU PRO GLN LEU HIS GLU ALA MET GLY GLY
SEQRES 5 H 220 GLN GLY ARG LEU PHE ALA GLN VAL MET ALA THR THR ALA
SEQRES 6 H 220 GLU GLY MET VAL ASN ASP ALA LEU LYS LEU ARG SER ILE
SEQRES 7 H 220 ILE ALA ASP ILE VAL VAL LYS VAL PRO VAL THR ALA GLU
SEQRES 8 H 220 GLY LEU ALA ALA ILE LYS MET LEU LYS ALA GLU GLY ILE
SEQRES 9 H 220 PRO THR LEU GLY THR ALA VAL TYR GLY ALA ALA GLN GLY
SEQRES 10 H 220 LEU LEU SER ALA LEU ALA GLY ALA GLU TYR VAL ALA PRO
SEQRES 11 H 220 TYR VAL ASN ARG ILE ASP ALA GLN GLY GLY SER GLY ILE
SEQRES 12 H 220 GLN THR VAL THR ASP LEU HIS GLN LEU LEU LYS MET HIS
SEQRES 13 H 220 ALA PRO GLN ALA LYS VAL LEU ALA ALA SER PHE LYS THR
SEQRES 14 H 220 PRO ARG GLN ALA LEU ASP CYS LEU LEU ALA GLY CYS GLU
SEQRES 15 H 220 SER ILE THR LEU PRO LEU ASP VAL ALA GLN GLN MET ILE
SEQRES 16 H 220 SER TYR PRO ALA VAL ASP ALA ALA VAL ALA LYS PHE GLU
SEQRES 17 H 220 GLN ASP TRP GLN GLY ALA PHE GLY ARG THR SER ILE
SEQRES 1 I 220 MET GLU LEU TYR LEU ASP THR SER ASP VAL VAL ALA VAL
SEQRES 2 I 220 LYS ALA LEU SER ARG ILE PHE PRO LEU ALA GLY VAL THR
SEQRES 3 I 220 THR ASN PRO SER ILE ILE ALA ALA GLY LYS LYS PRO LEU
SEQRES 4 I 220 ASP VAL VAL LEU PRO GLN LEU HIS GLU ALA MET GLY GLY
SEQRES 5 I 220 GLN GLY ARG LEU PHE ALA GLN VAL MET ALA THR THR ALA
SEQRES 6 I 220 GLU GLY MET VAL ASN ASP ALA LEU LYS LEU ARG SER ILE
SEQRES 7 I 220 ILE ALA ASP ILE VAL VAL LYS VAL PRO VAL THR ALA GLU
SEQRES 8 I 220 GLY LEU ALA ALA ILE LYS MET LEU LYS ALA GLU GLY ILE
SEQRES 9 I 220 PRO THR LEU GLY THR ALA VAL TYR GLY ALA ALA GLN GLY
SEQRES 10 I 220 LEU LEU SER ALA LEU ALA GLY ALA GLU TYR VAL ALA PRO
SEQRES 11 I 220 TYR VAL ASN ARG ILE ASP ALA GLN GLY GLY SER GLY ILE
SEQRES 12 I 220 GLN THR VAL THR ASP LEU HIS GLN LEU LEU LYS MET HIS
SEQRES 13 I 220 ALA PRO GLN ALA LYS VAL LEU ALA ALA SER PHE LYS THR
SEQRES 14 I 220 PRO ARG GLN ALA LEU ASP CYS LEU LEU ALA GLY CYS GLU
SEQRES 15 I 220 SER ILE THR LEU PRO LEU ASP VAL ALA GLN GLN MET ILE
SEQRES 16 I 220 SER TYR PRO ALA VAL ASP ALA ALA VAL ALA LYS PHE GLU
SEQRES 17 I 220 GLN ASP TRP GLN GLY ALA PHE GLY ARG THR SER ILE
SEQRES 1 J 220 MET GLU LEU TYR LEU ASP THR SER ASP VAL VAL ALA VAL
SEQRES 2 J 220 LYS ALA LEU SER ARG ILE PHE PRO LEU ALA GLY VAL THR
SEQRES 3 J 220 THR ASN PRO SER ILE ILE ALA ALA GLY LYS LYS PRO LEU
SEQRES 4 J 220 ASP VAL VAL LEU PRO GLN LEU HIS GLU ALA MET GLY GLY
SEQRES 5 J 220 GLN GLY ARG LEU PHE ALA GLN VAL MET ALA THR THR ALA
SEQRES 6 J 220 GLU GLY MET VAL ASN ASP ALA LEU LYS LEU ARG SER ILE
SEQRES 7 J 220 ILE ALA ASP ILE VAL VAL LYS VAL PRO VAL THR ALA GLU
SEQRES 8 J 220 GLY LEU ALA ALA ILE LYS MET LEU LYS ALA GLU GLY ILE
SEQRES 9 J 220 PRO THR LEU GLY THR ALA VAL TYR GLY ALA ALA GLN GLY
SEQRES 10 J 220 LEU LEU SER ALA LEU ALA GLY ALA GLU TYR VAL ALA PRO
SEQRES 11 J 220 TYR VAL ASN ARG ILE ASP ALA GLN GLY GLY SER GLY ILE
SEQRES 12 J 220 GLN THR VAL THR ASP LEU HIS GLN LEU LEU LYS MET HIS
SEQRES 13 J 220 ALA PRO GLN ALA LYS VAL LEU ALA ALA SER PHE LYS THR
SEQRES 14 J 220 PRO ARG GLN ALA LEU ASP CYS LEU LEU ALA GLY CYS GLU
SEQRES 15 J 220 SER ILE THR LEU PRO LEU ASP VAL ALA GLN GLN MET ILE
SEQRES 16 J 220 SER TYR PRO ALA VAL ASP ALA ALA VAL ALA LYS PHE GLU
SEQRES 17 J 220 GLN ASP TRP GLN GLY ALA PHE GLY ARG THR SER ILE
HET GOL A 250 6
HET GOL B 250 6
HET GOL C 250 6
HET GOL D 250 6
HET GOL E 250 6
HET GOL F 250 6
HET GOL G 250 6
HET GOL H 250 6
HET GOL I 250 6
HET GOL J 250 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 11 GOL 10(C3 H8 O3)
FORMUL 21 HOH *1479(H2 O)
HELIX 1 1 ASP A 9 ARG A 18 1 10
HELIX 2 2 ASN A 28 LYS A 36 1 9
HELIX 3 3 PRO A 38 MET A 50 1 13
HELIX 4 4 THR A 64 ILE A 79 1 16
HELIX 5 5 THR A 89 GLY A 103 1 15
HELIX 6 6 GLY A 113 GLY A 124 1 12
HELIX 7 7 TYR A 131 GLN A 138 1 8
HELIX 8 8 SER A 141 ALA A 157 1 17
HELIX 9 9 THR A 169 ALA A 179 1 11
HELIX 10 10 PRO A 187 MET A 194 1 8
HELIX 11 11 TYR A 197 GLY A 216 1 20
HELIX 12 12 ASP B 9 ARG B 18 1 10
HELIX 13 13 ASN B 28 LYS B 36 1 9
HELIX 14 14 PRO B 38 MET B 50 1 13
HELIX 15 15 THR B 64 ILE B 79 1 16
HELIX 16 16 THR B 89 GLY B 103 1 15
HELIX 17 17 GLY B 113 ALA B 123 1 11
HELIX 18 18 TYR B 131 GLN B 138 1 8
HELIX 19 19 SER B 141 ALA B 157 1 17
HELIX 20 20 THR B 169 ALA B 179 1 11
HELIX 21 21 PRO B 187 MET B 194 1 8
HELIX 22 22 TYR B 197 GLY B 216 1 20
HELIX 23 23 ASP C 9 SER C 17 1 9
HELIX 24 24 ASN C 28 LYS C 36 1 9
HELIX 25 25 PRO C 38 MET C 50 1 13
HELIX 26 26 THR C 64 ILE C 79 1 16
HELIX 27 27 THR C 89 GLY C 103 1 15
HELIX 28 28 GLY C 113 GLY C 124 1 12
HELIX 29 29 TYR C 131 GLN C 138 1 8
HELIX 30 30 SER C 141 ALA C 157 1 17
HELIX 31 31 THR C 169 ALA C 179 1 11
HELIX 32 32 PRO C 187 MET C 194 1 8
HELIX 33 33 TYR C 197 GLY C 216 1 20
HELIX 34 34 ASP D 9 SER D 17 1 9
HELIX 35 35 ASN D 28 LYS D 36 1 9
HELIX 36 36 PRO D 38 MET D 50 1 13
HELIX 37 37 THR D 64 ILE D 79 1 16
HELIX 38 38 THR D 89 GLU D 102 1 14
HELIX 39 39 GLY D 113 GLY D 124 1 12
HELIX 40 40 TYR D 131 GLN D 138 1 8
HELIX 41 41 SER D 141 ALA D 157 1 17
HELIX 42 42 THR D 169 ALA D 179 1 11
HELIX 43 43 PRO D 187 MET D 194 1 8
HELIX 44 44 TYR D 197 GLY D 216 1 20
HELIX 45 45 ASP E 9 SER E 17 1 9
HELIX 46 46 ASN E 28 LYS E 36 1 9
HELIX 47 47 PRO E 38 MET E 50 1 13
HELIX 48 48 THR E 64 ILE E 79 1 16
HELIX 49 49 THR E 89 GLY E 103 1 15
HELIX 50 50 GLY E 113 GLY E 124 1 12
HELIX 51 51 TYR E 131 GLN E 138 1 8
HELIX 52 52 SER E 141 ALA E 157 1 17
HELIX 53 53 THR E 169 ALA E 179 1 11
HELIX 54 54 PRO E 187 MET E 194 1 8
HELIX 55 55 TYR E 197 GLY E 216 1 20
HELIX 56 56 ASP F 9 SER F 17 1 9
HELIX 57 57 ASN F 28 LYS F 36 1 9
HELIX 58 58 PRO F 38 MET F 50 1 13
HELIX 59 59 THR F 64 ILE F 79 1 16
HELIX 60 60 THR F 89 GLY F 103 1 15
HELIX 61 61 GLY F 113 GLY F 124 1 12
HELIX 62 62 TYR F 131 GLN F 138 1 8
HELIX 63 63 SER F 141 ALA F 157 1 17
HELIX 64 64 THR F 169 ALA F 179 1 11
HELIX 65 65 PRO F 187 MET F 194 1 8
HELIX 66 66 TYR F 197 GLY F 216 1 20
HELIX 67 67 ASP G 9 SER G 17 1 9
HELIX 68 68 ASN G 28 LYS G 36 1 9
HELIX 69 69 PRO G 38 MET G 50 1 13
HELIX 70 70 THR G 64 ILE G 79 1 16
HELIX 71 71 THR G 89 GLY G 103 1 15
HELIX 72 72 GLY G 113 GLY G 124 1 12
HELIX 73 73 TYR G 131 GLN G 138 1 8
HELIX 74 74 SER G 141 ALA G 157 1 17
HELIX 75 75 THR G 169 ALA G 179 1 11
HELIX 76 76 PRO G 187 MET G 194 1 8
HELIX 77 77 TYR G 197 GLY G 216 1 20
HELIX 78 78 ASP H 9 SER H 17 1 9
HELIX 79 79 ASN H 28 LYS H 36 1 9
HELIX 80 80 PRO H 38 MET H 50 1 13
HELIX 81 81 THR H 64 ILE H 79 1 16
HELIX 82 82 THR H 89 GLU H 102 1 14
HELIX 83 83 GLY H 113 GLY H 124 1 12
HELIX 84 84 TYR H 131 GLN H 138 1 8
HELIX 85 85 SER H 141 ALA H 157 1 17
HELIX 86 86 THR H 169 ALA H 179 1 11
HELIX 87 87 PRO H 187 MET H 194 1 8
HELIX 88 88 TYR H 197 GLY H 216 1 20
HELIX 89 89 ASP I 9 SER I 17 1 9
HELIX 90 90 ASN I 28 LYS I 36 1 9
HELIX 91 91 PRO I 38 MET I 50 1 13
HELIX 92 92 THR I 64 ILE I 79 1 16
HELIX 93 93 THR I 89 GLY I 103 1 15
HELIX 94 94 GLY I 113 GLY I 124 1 12
HELIX 95 95 TYR I 131 GLN I 138 1 8
HELIX 96 96 SER I 141 ALA I 157 1 17
HELIX 97 97 THR I 169 ALA I 179 1 11
HELIX 98 98 PRO I 187 MET I 194 1 8
HELIX 99 99 TYR I 197 GLY I 216 1 20
HELIX 100 100 ASP J 9 SER J 17 1 9
HELIX 101 101 ASN J 28 LYS J 36 1 9
HELIX 102 102 PRO J 38 MET J 50 1 13
HELIX 103 103 THR J 64 ILE J 79 1 16
HELIX 104 104 THR J 89 GLY J 103 1 15
HELIX 105 105 GLY J 113 GLY J 124 1 12
HELIX 106 106 TYR J 131 GLN J 138 1 8
HELIX 107 107 SER J 141 ALA J 157 1 17
HELIX 108 108 THR J 169 ALA J 179 1 11
HELIX 109 109 PRO J 187 MET J 194 1 8
HELIX 110 110 TYR J 197 GLY J 216 1 20
SHEET 1 A 9 GLU A 2 ASP A 6 0
SHEET 2 A 9 GLY A 24 THR A 26 1 O THR A 26 N LEU A 5
SHEET 3 A 9 ARG A 55 GLN A 59 1 O ARG A 55 N VAL A 25
SHEET 4 A 9 VAL A 83 PRO A 87 1 O LYS A 85 N ALA A 58
SHEET 5 A 9 THR A 106 VAL A 111 1 O LEU A 107 N VAL A 86
SHEET 6 A 9 TYR A 127 PRO A 130 1 O ALA A 129 N GLY A 108
SHEET 7 A 9 LYS A 161 ALA A 164 1 O LEU A 163 N VAL A 128
SHEET 8 A 9 SER A 183 LEU A 186 1 O THR A 185 N ALA A 164
SHEET 9 A 9 GLU A 2 ASP A 6 1 N TYR A 4 O ILE A 184
SHEET 1 B 9 GLU B 2 ASP B 6 0
SHEET 2 B 9 GLY B 24 THR B 26 1 O THR B 26 N LEU B 5
SHEET 3 B 9 ARG B 55 GLN B 59 1 O ARG B 55 N VAL B 25
SHEET 4 B 9 VAL B 83 PRO B 87 1 O LYS B 85 N ALA B 58
SHEET 5 B 9 THR B 106 VAL B 111 1 O LEU B 107 N VAL B 86
SHEET 6 B 9 TYR B 127 PRO B 130 1 O ALA B 129 N GLY B 108
SHEET 7 B 9 LYS B 161 ALA B 164 1 O LEU B 163 N VAL B 128
SHEET 8 B 9 SER B 183 LEU B 186 1 O THR B 185 N ALA B 164
SHEET 9 B 9 GLU B 2 ASP B 6 1 N TYR B 4 O ILE B 184
SHEET 1 C 9 GLU C 2 ASP C 6 0
SHEET 2 C 9 GLY C 24 THR C 26 1 O THR C 26 N LEU C 5
SHEET 3 C 9 ARG C 55 GLN C 59 1 O ARG C 55 N VAL C 25
SHEET 4 C 9 VAL C 83 PRO C 87 1 O LYS C 85 N ALA C 58
SHEET 5 C 9 THR C 106 VAL C 111 1 O LEU C 107 N VAL C 86
SHEET 6 C 9 TYR C 127 PRO C 130 1 O ALA C 129 N GLY C 108
SHEET 7 C 9 LYS C 161 ALA C 164 1 O LEU C 163 N VAL C 128
SHEET 8 C 9 SER C 183 LEU C 186 1 O THR C 185 N ALA C 164
SHEET 9 C 9 GLU C 2 ASP C 6 1 N TYR C 4 O ILE C 184
SHEET 1 D 9 GLU D 2 ASP D 6 0
SHEET 2 D 9 GLY D 24 THR D 26 1 O THR D 26 N LEU D 5
SHEET 3 D 9 ARG D 55 GLN D 59 1 O ARG D 55 N VAL D 25
SHEET 4 D 9 VAL D 83 PRO D 87 1 O LYS D 85 N ALA D 58
SHEET 5 D 9 THR D 106 VAL D 111 1 O LEU D 107 N VAL D 86
SHEET 6 D 9 TYR D 127 PRO D 130 1 O ALA D 129 N GLY D 108
SHEET 7 D 9 LYS D 161 ALA D 164 1 O LEU D 163 N VAL D 128
SHEET 8 D 9 SER D 183 LEU D 186 1 O THR D 185 N ALA D 164
SHEET 9 D 9 GLU D 2 ASP D 6 1 N TYR D 4 O ILE D 184
SHEET 1 E 9 GLU E 2 ASP E 6 0
SHEET 2 E 9 GLY E 24 THR E 26 1 O THR E 26 N LEU E 5
SHEET 3 E 9 ARG E 55 GLN E 59 1 O ARG E 55 N VAL E 25
SHEET 4 E 9 VAL E 83 PRO E 87 1 O LYS E 85 N ALA E 58
SHEET 5 E 9 THR E 106 VAL E 111 1 O LEU E 107 N VAL E 86
SHEET 6 E 9 TYR E 127 PRO E 130 1 O ALA E 129 N GLY E 108
SHEET 7 E 9 LYS E 161 ALA E 164 1 O LEU E 163 N VAL E 128
SHEET 8 E 9 SER E 183 LEU E 186 1 O THR E 185 N ALA E 164
SHEET 9 E 9 GLU E 2 ASP E 6 1 N TYR E 4 O ILE E 184
SHEET 1 F 9 GLU F 2 ASP F 6 0
SHEET 2 F 9 GLY F 24 THR F 26 1 O THR F 26 N LEU F 5
SHEET 3 F 9 ARG F 55 GLN F 59 1 O ARG F 55 N VAL F 25
SHEET 4 F 9 VAL F 83 PRO F 87 1 O LYS F 85 N ALA F 58
SHEET 5 F 9 THR F 106 VAL F 111 1 O LEU F 107 N VAL F 86
SHEET 6 F 9 TYR F 127 PRO F 130 1 O ALA F 129 N GLY F 108
SHEET 7 F 9 LYS F 161 ALA F 164 1 O LEU F 163 N VAL F 128
SHEET 8 F 9 SER F 183 LEU F 186 1 O THR F 185 N ALA F 164
SHEET 9 F 9 GLU F 2 ASP F 6 1 N TYR F 4 O ILE F 184
SHEET 1 G 9 GLU G 2 ASP G 6 0
SHEET 2 G 9 GLY G 24 THR G 26 1 O THR G 26 N LEU G 5
SHEET 3 G 9 ARG G 55 GLN G 59 1 O ARG G 55 N VAL G 25
SHEET 4 G 9 VAL G 83 PRO G 87 1 O LYS G 85 N ALA G 58
SHEET 5 G 9 THR G 106 VAL G 111 1 O LEU G 107 N VAL G 86
SHEET 6 G 9 TYR G 127 PRO G 130 1 O ALA G 129 N GLY G 108
SHEET 7 G 9 LYS G 161 ALA G 164 1 O LEU G 163 N VAL G 128
SHEET 8 G 9 SER G 183 LEU G 186 1 O THR G 185 N ALA G 164
SHEET 9 G 9 GLU G 2 ASP G 6 1 N TYR G 4 O ILE G 184
SHEET 1 H 9 GLU H 2 ASP H 6 0
SHEET 2 H 9 GLY H 24 THR H 26 1 O THR H 26 N LEU H 5
SHEET 3 H 9 ARG H 55 GLN H 59 1 O ARG H 55 N VAL H 25
SHEET 4 H 9 VAL H 83 PRO H 87 1 O LYS H 85 N ALA H 58
SHEET 5 H 9 THR H 106 VAL H 111 1 O LEU H 107 N VAL H 86
SHEET 6 H 9 TYR H 127 PRO H 130 1 O ALA H 129 N GLY H 108
SHEET 7 H 9 LYS H 161 ALA H 164 1 O LEU H 163 N VAL H 128
SHEET 8 H 9 SER H 183 LEU H 186 1 O THR H 185 N ALA H 164
SHEET 9 H 9 GLU H 2 ASP H 6 1 N TYR H 4 O ILE H 184
SHEET 1 I 9 GLU I 2 ASP I 6 0
SHEET 2 I 9 GLY I 24 THR I 26 1 O THR I 26 N LEU I 5
SHEET 3 I 9 ARG I 55 GLN I 59 1 O ARG I 55 N VAL I 25
SHEET 4 I 9 VAL I 83 PRO I 87 1 O LYS I 85 N ALA I 58
SHEET 5 I 9 THR I 106 VAL I 111 1 O LEU I 107 N VAL I 86
SHEET 6 I 9 TYR I 127 PRO I 130 1 O ALA I 129 N GLY I 108
SHEET 7 I 9 LYS I 161 ALA I 164 1 O LEU I 163 N VAL I 128
SHEET 8 I 9 SER I 183 LEU I 186 1 O THR I 185 N ALA I 164
SHEET 9 I 9 GLU I 2 ASP I 6 1 N TYR I 4 O ILE I 184
SHEET 1 J 9 GLU J 2 ASP J 6 0
SHEET 2 J 9 GLY J 24 THR J 26 1 O THR J 26 N LEU J 5
SHEET 3 J 9 ARG J 55 GLN J 59 1 O ARG J 55 N VAL J 25
SHEET 4 J 9 VAL J 83 PRO J 87 1 O LYS J 85 N ALA J 58
SHEET 5 J 9 THR J 106 VAL J 111 1 O LEU J 107 N VAL J 86
SHEET 6 J 9 TYR J 127 PRO J 130 1 O ALA J 129 N GLY J 108
SHEET 7 J 9 LYS J 161 ALA J 164 1 O LEU J 163 N VAL J 128
SHEET 8 J 9 SER J 183 LEU J 186 1 O THR J 185 N ALA J 164
SHEET 9 J 9 GLU J 2 ASP J 6 1 N TYR J 4 O ILE J 184
LINK NZ LYS A 85 C1 GOL A 250 1555 1555 1.45
LINK NZ LYS B 85 C1 GOL B 250 1555 1555 1.45
LINK NZ LYS C 85 C1 GOL C 250 1555 1555 1.45
LINK NZ LYS D 85 C1 GOL D 250 1555 1555 1.46
LINK NZ LYS E 85 C1 GOL E 250 1555 1555 1.46
LINK NZ LYS F 85 C1 GOL F 250 1555 1555 1.45
LINK NZ LYS G 85 C1 GOL G 250 1555 1555 1.46
LINK NZ LYS H 85 C1 GOL H 250 1555 1555 1.46
LINK NZ LYS I 85 C1 GOL I 250 1555 1555 1.46
LINK NZ LYS J 85 C1 GOL J 250 1555 1555 1.45
SITE 1 AC1 7 ASP A 6 THR A 27 ASN A 28 LYS A 85
SITE 2 AC1 7 TYR A 131 HOH A 894 HOH A1760
SITE 1 AC2 7 ASP B 6 THR B 27 ASN B 28 LYS B 85
SITE 2 AC2 7 TYR B 131 HOH B 579 HOH B1762
SITE 1 AC3 9 ASP C 6 THR C 26 THR C 27 ASN C 28
SITE 2 AC3 9 LYS C 85 ALA C 129 TYR C 131 HOH C 636
SITE 3 AC3 9 HOH C1764
SITE 1 AC4 8 ASP D 6 THR D 27 ASN D 28 LYS D 85
SITE 2 AC4 8 TYR D 131 LEU D 163 HOH D 513 HOH D1767
SITE 1 AC5 6 ASP E 6 THR E 27 ASN E 28 LYS E 85
SITE 2 AC5 6 TYR E 131 HOH E1768
SITE 1 AC6 7 ASP F 6 THR F 27 ASN F 28 LYS F 85
SITE 2 AC6 7 TYR F 131 HOH F 663 HOH F1771
SITE 1 AC7 7 ASP G 6 THR G 27 ASN G 28 LYS G 85
SITE 2 AC7 7 TYR G 131 HOH G 614 HOH G1772
SITE 1 AC8 7 ASP H 6 THR H 27 ASN H 28 LYS H 85
SITE 2 AC8 7 TYR H 131 HOH H 769 HOH H1774
SITE 1 AC9 7 ASP I 6 THR I 27 ASN I 28 LYS I 85
SITE 2 AC9 7 TYR I 131 HOH I 615 HOH I1776
SITE 1 BC1 7 ASP J 6 THR J 27 ASN J 28 LYS J 85
SITE 2 BC1 7 TYR J 131 HOH J 514 HOH J1778
CRYST1 115.490 126.940 183.620 90.00 90.00 90.00 P 21 21 21 40
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 0.008659 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007878 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005446 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
