HEADER TRANSFERASE 07-FEB-94 1TKA
TITLE SPECIFICITY OF COENZYME BINDING IN THIAMIN DIPHOSPHATE DEPENDENT
TITLE 2 ENZYMES: CRYSTAL STRUCTURES OF YEAST TRANSKETOLASE IN COMPLEX WITH
TITLE 3 ANALOGS OF THIAMIN DIPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSKETOLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.2.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SCHNEIDER,S.KOENIG
REVDAT 4 14-FEB-24 1TKA 1 REMARK LINK
REVDAT 3 24-FEB-09 1TKA 1 VERSN
REVDAT 2 01-APR-03 1TKA 1 JRNL
REVDAT 1 30-NOV-94 1TKA 0
JRNL AUTH S.KONIG,A.SCHELLENBERGER,H.NEEF,G.SCHNEIDER
JRNL TITL SPECIFICITY OF COENZYME BINDING IN THIAMIN
JRNL TITL 2 DIPHOSPHATE-DEPENDENT ENZYMES. CRYSTAL STRUCTURES OF YEAST
JRNL TITL 3 TRANSKETOLASE IN COMPLEX WITH ANALOGS OF THIAMIN
JRNL TITL 4 DIPHOSPHATE.
JRNL REF J.BIOL.CHEM. V. 269 10879 1994
JRNL REFN ISSN 0021-9258
JRNL PMID 8144674
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.NIKKOLA,Y.LINDQVIST,G.SCHNEIDER
REMARK 1 TITL REFINED STRUCTURE OF TRANSKETOLASE FROM SACCHAROMYCES
REMARK 1 TITL 2 CEREVISIAE AT 2.0 ANGSTROM RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 238 387 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.SUNDSTROM,Y.LINDQVIST,G.SCHNEIDER,U.HELLMAN,H.RONNE
REMARK 1 TITL YEAST TKL1 GENE ENCODES A TRANSKETOLASE THAT IS REQUIRED FOR
REMARK 1 TITL 2 EFFICIENT GLYCOLYSIS AND BIOSYNTHESIS OF AROMATIC AMINO
REMARK 1 TITL 3 ACIDS
REMARK 1 REF J.BIOL.CHEM. V. 268 24346 1993
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH Y.LINDQVIST,G.SCHNEIDER,U.ERMLER,M.SUNDSTROM
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF TRANSKETOLASE, A THIAMINE
REMARK 1 TITL 2 DIPHOSPHATE DEPENDENT ENZYME, AT 2.5 ANGSTROMS RESOLUTION
REMARK 1 REF EMBO J. V. 11 2373 1992
REMARK 1 REFN ISSN 0261-4189
REMARK 1 REFERENCE 4
REMARK 1 AUTH G.SCHNEIDER,M.SUNDSTROM,Y.LINDQVIST
REMARK 1 TITL PRELIMINARY CRYSTALLOGRAPHIC DATA FOR TRANSKETOLASE FROM
REMARK 1 TITL 2 YEAST
REMARK 1 REF J.BIOL.CHEM. V. 264 21619 1989
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 28444
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 SET) : 0.158
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 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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 10396
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 0
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 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) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 3.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 1TKA 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_1000176710.
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 (%): 47.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
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 38.15000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.45000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.65000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.45000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.15000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.65000
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 300 REMARK: THE TRANSFORMATION PRESENTED ON MTRIX RECORDS BELOW WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO
REMARK 300 CHAIN *A*.
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL
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 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 69 NE2 HIS A 69 CD2 -0.067
REMARK 500 HIS A 79 NE2 HIS A 79 CD2 -0.072
REMARK 500 HIS A 174 NE2 HIS A 174 CD2 -0.068
REMARK 500 HIS A 256 NE2 HIS A 256 CD2 -0.069
REMARK 500 HIS A 260 NE2 HIS A 260 CD2 -0.071
REMARK 500 HIS A 263 NE2 HIS A 263 CD2 -0.076
REMARK 500 HIS A 296 NE2 HIS A 296 CD2 -0.075
REMARK 500 HIS A 419 NE2 HIS A 419 CD2 -0.067
REMARK 500 HIS A 461 NE2 HIS A 461 CD2 -0.067
REMARK 500 HIS A 481 NE2 HIS A 481 CD2 -0.067
REMARK 500 HIS A 489 NE2 HIS A 489 CD2 -0.074
REMARK 500 GLU A 535 CD GLU A 535 OE2 0.088
REMARK 500 HIS A 628 NE2 HIS A 628 CD2 -0.073
REMARK 500 HIS B 30 NE2 HIS B 30 CD2 -0.068
REMARK 500 HIS B 69 NE2 HIS B 69 CD2 -0.070
REMARK 500 HIS B 79 NE2 HIS B 79 CD2 -0.071
REMARK 500 HIS B 174 NE2 HIS B 174 CD2 -0.069
REMARK 500 HIS B 260 NE2 HIS B 260 CD2 -0.072
REMARK 500 HIS B 263 NE2 HIS B 263 CD2 -0.074
REMARK 500 HIS B 419 NE2 HIS B 419 CD2 -0.075
REMARK 500 HIS B 461 NE2 HIS B 461 CD2 -0.069
REMARK 500 HIS B 469 NE2 HIS B 469 CD2 -0.068
REMARK 500 HIS B 481 NE2 HIS B 481 CD2 -0.068
REMARK 500 HIS B 489 NE2 HIS B 489 CD2 -0.076
REMARK 500 HIS B 628 NE2 HIS B 628 CD2 -0.069
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 45 CD1 - CG - CD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TRP A 45 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 49 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 TRP A 57 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP A 57 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 62 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 VAL A 71 CB - CA - C ANGL. DEV. = -13.6 DEGREES
REMARK 500 TYR A 83 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 94 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 94 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 CYS A 159 CA - CB - SG ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG A 206 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 TRP A 212 CD1 - CG - CD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 TRP A 212 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES
REMARK 500 GLU A 307 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 TRP A 312 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TRP A 312 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 332 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 332 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 333 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP A 342 CD1 - CG - CD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TRP A 342 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 359 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 THR A 389 N - CA - CB ANGL. DEV. = -14.2 DEGREES
REMARK 500 TRP A 391 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP A 391 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 413 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 TYR A 448 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 454 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 454 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 TRP A 465 CD1 - CG - CD2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 TRP A 465 CB - CG - CD1 ANGL. DEV. = -8.3 DEGREES
REMARK 500 TRP A 465 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 TRP A 465 CE2 - CD2 - CG ANGL. DEV. = -6.5 DEGREES
REMARK 500 TRP A 465 CG - CD2 - CE3 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG A 491 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 TRP A 499 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP A 499 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 500 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 584 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 TRP A 623 CD1 - CG - CD2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 TRP A 623 CG - CD1 - NE1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 TRP A 623 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG A 659 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 659 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG B 16 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 VAL B 20 CG1 - CB - CG2 ANGL. DEV. = -12.6 DEGREES
REMARK 500 TRP B 45 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP B 45 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 87 ANGLE DEVIATIONS.
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 THR A 5 -162.94 -117.73
REMARK 500 THR A 100 63.30 -117.20
REMARK 500 PHE A 106 -45.19 -29.98
REMARK 500 ASP A 148 21.28 -158.49
REMARK 500 LYS A 188 -3.72 53.44
REMARK 500 SER A 198 -40.78 -143.34
REMARK 500 ASN A 219 77.51 -114.41
REMARK 500 SER A 237 63.64 -56.40
REMARK 500 TYR A 252 124.30 -35.78
REMARK 500 ILE A 301 -55.41 -125.74
REMARK 500 GLU A 393 31.57 -85.43
REMARK 500 PRO A 400 -50.31 -13.29
REMARK 500 PRO A 462 54.42 -69.44
REMARK 500 SER A 471 -174.28 -175.22
REMARK 500 ASP A 503 -172.61 -174.25
REMARK 500 ASN A 554 81.14 72.07
REMARK 500 LEU A 606 79.15 -113.36
REMARK 500 VAL A 617 44.25 -84.12
REMARK 500 SER B 28 126.90 -177.31
REMARK 500 VAL B 71 -30.17 -36.28
REMARK 500 ARG B 94 11.98 49.84
REMARK 500 THR B 100 68.40 -114.40
REMARK 500 PRO B 109 107.79 -47.61
REMARK 500 ASP B 148 8.09 -168.14
REMARK 500 LYS B 188 11.12 58.70
REMARK 500 SER B 198 -52.02 -155.03
REMARK 500 ASN B 219 77.71 -119.20
REMARK 500 SER B 237 73.57 -67.49
REMARK 500 PRO B 290 126.03 -39.02
REMARK 500 ILE B 301 -57.52 -131.13
REMARK 500 GLU B 393 34.71 -84.42
REMARK 500 TYR B 407 0.82 -69.10
REMARK 500 ILE B 484 -78.02 -129.44
REMARK 500 ASN B 495 62.27 65.56
REMARK 500 PRO B 521 177.12 -59.83
REMARK 500 LEU B 588 75.12 -110.65
REMARK 500 VAL B 617 44.44 -76.83
REMARK 500 TYR B 626 -47.57 -148.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 682 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 157 OD1
REMARK 620 2 ASN A 187 OD1 77.8
REMARK 620 3 ASN A 187 ND2 121.4 45.2
REMARK 620 4 ILE A 189 O 88.2 88.7 100.8
REMARK 620 5 N3T A 681 O1B 144.1 103.3 61.4 127.5
REMARK 620 6 N3T A 681 O3A 126.9 145.9 102.7 112.7 42.6
REMARK 620 7 N3T A 681 O2A 82.2 158.8 150.3 97.5 88.9 48.2
REMARK 620 8 N3T A 681 O2B 155.8 121.5 81.3 78.6 51.4 45.0 79.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 682 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 157 OD2
REMARK 620 2 ASN B 187 OD1 74.6
REMARK 620 3 ASN B 187 ND2 118.1 44.0
REMARK 620 4 ILE B 189 O 84.2 92.3 102.1
REMARK 620 5 N3T B 681 O2B 149.0 98.0 57.6 126.6
REMARK 620 6 N3T B 681 O3B 161.1 121.9 79.7 85.7 45.0
REMARK 620 7 N3T B 681 O3A 133.3 138.6 98.6 117.0 41.4 41.2
REMARK 620 8 N3T B 681 O2A 91.9 163.9 146.5 95.1 89.1 73.1 47.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N3T A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N3T B 681
DBREF 1TKA A 3 680 UNP P23254 TKT1_YEAST 2 679
DBREF 1TKA B 3 680 UNP P23254 TKT1_YEAST 2 679
SEQRES 1 A 678 GLN PHE THR ASP ILE ASP LYS LEU ALA VAL SER THR ILE
SEQRES 2 A 678 ARG ILE LEU ALA VAL ASP THR VAL SER LYS ALA ASN SER
SEQRES 3 A 678 GLY HIS PRO GLY ALA PRO LEU GLY MET ALA PRO ALA ALA
SEQRES 4 A 678 HIS VAL LEU TRP SER GLN MET ARG MET ASN PRO THR ASN
SEQRES 5 A 678 PRO ASP TRP ILE ASN ARG ASP ARG PHE VAL LEU SER ASN
SEQRES 6 A 678 GLY HIS ALA VAL ALA LEU LEU TYR SER MET LEU HIS LEU
SEQRES 7 A 678 THR GLY TYR ASP LEU SER ILE GLU ASP LEU LYS GLN PHE
SEQRES 8 A 678 ARG GLN LEU GLY SER ARG THR PRO GLY HIS PRO GLU PHE
SEQRES 9 A 678 GLU LEU PRO GLY VAL GLU VAL THR THR GLY PRO LEU GLY
SEQRES 10 A 678 GLN GLY ILE SER ASN ALA VAL GLY MET ALA MET ALA GLN
SEQRES 11 A 678 ALA ASN LEU ALA ALA THR TYR ASN LYS PRO GLY PHE THR
SEQRES 12 A 678 LEU SER ASP ASN TYR THR TYR VAL PHE LEU GLY ASP GLY
SEQRES 13 A 678 CYS LEU GLN GLU GLY ILE SER SER GLU ALA SER SER LEU
SEQRES 14 A 678 ALA GLY HIS LEU LYS LEU GLY ASN LEU ILE ALA ILE TYR
SEQRES 15 A 678 ASP ASP ASN LYS ILE THR ILE ASP GLY ALA THR SER ILE
SEQRES 16 A 678 SER PHE ASP GLU ASP VAL ALA LYS ARG TYR GLU ALA TYR
SEQRES 17 A 678 GLY TRP GLU VAL LEU TYR VAL GLU ASN GLY ASN GLU ASP
SEQRES 18 A 678 LEU ALA GLY ILE ALA LYS ALA ILE ALA GLN ALA LYS LEU
SEQRES 19 A 678 SER LYS ASP LYS PRO THR LEU ILE LYS MET THR THR THR
SEQRES 20 A 678 ILE GLY TYR GLY SER LEU HIS ALA GLY SER HIS SER VAL
SEQRES 21 A 678 HIS GLY ALA PRO LEU LYS ALA ASP ASP VAL LYS GLN LEU
SEQRES 22 A 678 LYS SER LYS PHE GLY PHE ASN PRO ASP LYS SER PHE VAL
SEQRES 23 A 678 VAL PRO GLN GLU VAL TYR ASP HIS TYR GLN LYS THR ILE
SEQRES 24 A 678 LEU LYS PRO GLY VAL GLU ALA ASN ASN LYS TRP ASN LYS
SEQRES 25 A 678 LEU PHE SER GLU TYR GLN LYS LYS PHE PRO GLU LEU GLY
SEQRES 26 A 678 ALA GLU LEU ALA ARG ARG LEU SER GLY GLN LEU PRO ALA
SEQRES 27 A 678 ASN TRP GLU SER LYS LEU PRO THR TYR THR ALA LYS ASP
SEQRES 28 A 678 SER ALA VAL ALA THR ARG LYS LEU SER GLU THR VAL LEU
SEQRES 29 A 678 GLU ASP VAL TYR ASN GLN LEU PRO GLU LEU ILE GLY GLY
SEQRES 30 A 678 SER ALA ASP LEU THR PRO SER ASN LEU THR ARG TRP LYS
SEQRES 31 A 678 GLU ALA LEU ASP PHE GLN PRO PRO SER SER GLY SER GLY
SEQRES 32 A 678 ASN TYR SER GLY ARG TYR ILE ARG TYR GLY ILE ARG GLU
SEQRES 33 A 678 HIS ALA MET GLY ALA ILE MET ASN GLY ILE SER ALA PHE
SEQRES 34 A 678 GLY ALA ASN TYR LYS PRO TYR GLY GLY THR PHE LEU ASN
SEQRES 35 A 678 PHE VAL SER TYR ALA ALA GLY ALA VAL ARG LEU SER ALA
SEQRES 36 A 678 LEU SER GLY HIS PRO VAL ILE TRP VAL ALA THR HIS ASP
SEQRES 37 A 678 SER ILE GLY VAL GLY GLU ASP GLY PRO THR HIS GLN PRO
SEQRES 38 A 678 ILE GLU THR LEU ALA HIS PHE ARG SER LEU PRO ASN ILE
SEQRES 39 A 678 GLN VAL TRP ARG PRO ALA ASP GLY ASN GLU VAL SER ALA
SEQRES 40 A 678 ALA TYR LYS ASN SER LEU GLU SER LYS HIS THR PRO SER
SEQRES 41 A 678 ILE ILE ALA LEU SER ARG GLN ASN LEU PRO GLN LEU GLU
SEQRES 42 A 678 GLY SER SER ILE GLU SER ALA SER LYS GLY GLY TYR VAL
SEQRES 43 A 678 LEU GLN ASP VAL ALA ASN PRO ASP ILE ILE LEU VAL ALA
SEQRES 44 A 678 THR GLY SER GLU VAL SER LEU SER VAL GLU ALA ALA LYS
SEQRES 45 A 678 THR LEU ALA ALA LYS ASN ILE LYS ALA ARG VAL VAL SER
SEQRES 46 A 678 LEU PRO ASP PHE PHE THR PHE ASP LYS GLN PRO LEU GLU
SEQRES 47 A 678 TYR ARG LEU SER VAL LEU PRO ASP ASN VAL PRO ILE MET
SEQRES 48 A 678 SER VAL GLU VAL LEU ALA THR THR CYS TRP GLY LYS TYR
SEQRES 49 A 678 ALA HIS GLN SER PHE GLY ILE ASP ARG PHE GLY ALA SER
SEQRES 50 A 678 GLY LYS ALA PRO GLU VAL PHE LYS PHE PHE GLY PHE THR
SEQRES 51 A 678 PRO GLU GLY VAL ALA GLU ARG ALA GLN LYS THR ILE ALA
SEQRES 52 A 678 PHE TYR LYS GLY ASP LYS LEU ILE SER PRO LEU LYS LYS
SEQRES 53 A 678 ALA PHE
SEQRES 1 B 678 GLN PHE THR ASP ILE ASP LYS LEU ALA VAL SER THR ILE
SEQRES 2 B 678 ARG ILE LEU ALA VAL ASP THR VAL SER LYS ALA ASN SER
SEQRES 3 B 678 GLY HIS PRO GLY ALA PRO LEU GLY MET ALA PRO ALA ALA
SEQRES 4 B 678 HIS VAL LEU TRP SER GLN MET ARG MET ASN PRO THR ASN
SEQRES 5 B 678 PRO ASP TRP ILE ASN ARG ASP ARG PHE VAL LEU SER ASN
SEQRES 6 B 678 GLY HIS ALA VAL ALA LEU LEU TYR SER MET LEU HIS LEU
SEQRES 7 B 678 THR GLY TYR ASP LEU SER ILE GLU ASP LEU LYS GLN PHE
SEQRES 8 B 678 ARG GLN LEU GLY SER ARG THR PRO GLY HIS PRO GLU PHE
SEQRES 9 B 678 GLU LEU PRO GLY VAL GLU VAL THR THR GLY PRO LEU GLY
SEQRES 10 B 678 GLN GLY ILE SER ASN ALA VAL GLY MET ALA MET ALA GLN
SEQRES 11 B 678 ALA ASN LEU ALA ALA THR TYR ASN LYS PRO GLY PHE THR
SEQRES 12 B 678 LEU SER ASP ASN TYR THR TYR VAL PHE LEU GLY ASP GLY
SEQRES 13 B 678 CYS LEU GLN GLU GLY ILE SER SER GLU ALA SER SER LEU
SEQRES 14 B 678 ALA GLY HIS LEU LYS LEU GLY ASN LEU ILE ALA ILE TYR
SEQRES 15 B 678 ASP ASP ASN LYS ILE THR ILE ASP GLY ALA THR SER ILE
SEQRES 16 B 678 SER PHE ASP GLU ASP VAL ALA LYS ARG TYR GLU ALA TYR
SEQRES 17 B 678 GLY TRP GLU VAL LEU TYR VAL GLU ASN GLY ASN GLU ASP
SEQRES 18 B 678 LEU ALA GLY ILE ALA LYS ALA ILE ALA GLN ALA LYS LEU
SEQRES 19 B 678 SER LYS ASP LYS PRO THR LEU ILE LYS MET THR THR THR
SEQRES 20 B 678 ILE GLY TYR GLY SER LEU HIS ALA GLY SER HIS SER VAL
SEQRES 21 B 678 HIS GLY ALA PRO LEU LYS ALA ASP ASP VAL LYS GLN LEU
SEQRES 22 B 678 LYS SER LYS PHE GLY PHE ASN PRO ASP LYS SER PHE VAL
SEQRES 23 B 678 VAL PRO GLN GLU VAL TYR ASP HIS TYR GLN LYS THR ILE
SEQRES 24 B 678 LEU LYS PRO GLY VAL GLU ALA ASN ASN LYS TRP ASN LYS
SEQRES 25 B 678 LEU PHE SER GLU TYR GLN LYS LYS PHE PRO GLU LEU GLY
SEQRES 26 B 678 ALA GLU LEU ALA ARG ARG LEU SER GLY GLN LEU PRO ALA
SEQRES 27 B 678 ASN TRP GLU SER LYS LEU PRO THR TYR THR ALA LYS ASP
SEQRES 28 B 678 SER ALA VAL ALA THR ARG LYS LEU SER GLU THR VAL LEU
SEQRES 29 B 678 GLU ASP VAL TYR ASN GLN LEU PRO GLU LEU ILE GLY GLY
SEQRES 30 B 678 SER ALA ASP LEU THR PRO SER ASN LEU THR ARG TRP LYS
SEQRES 31 B 678 GLU ALA LEU ASP PHE GLN PRO PRO SER SER GLY SER GLY
SEQRES 32 B 678 ASN TYR SER GLY ARG TYR ILE ARG TYR GLY ILE ARG GLU
SEQRES 33 B 678 HIS ALA MET GLY ALA ILE MET ASN GLY ILE SER ALA PHE
SEQRES 34 B 678 GLY ALA ASN TYR LYS PRO TYR GLY GLY THR PHE LEU ASN
SEQRES 35 B 678 PHE VAL SER TYR ALA ALA GLY ALA VAL ARG LEU SER ALA
SEQRES 36 B 678 LEU SER GLY HIS PRO VAL ILE TRP VAL ALA THR HIS ASP
SEQRES 37 B 678 SER ILE GLY VAL GLY GLU ASP GLY PRO THR HIS GLN PRO
SEQRES 38 B 678 ILE GLU THR LEU ALA HIS PHE ARG SER LEU PRO ASN ILE
SEQRES 39 B 678 GLN VAL TRP ARG PRO ALA ASP GLY ASN GLU VAL SER ALA
SEQRES 40 B 678 ALA TYR LYS ASN SER LEU GLU SER LYS HIS THR PRO SER
SEQRES 41 B 678 ILE ILE ALA LEU SER ARG GLN ASN LEU PRO GLN LEU GLU
SEQRES 42 B 678 GLY SER SER ILE GLU SER ALA SER LYS GLY GLY TYR VAL
SEQRES 43 B 678 LEU GLN ASP VAL ALA ASN PRO ASP ILE ILE LEU VAL ALA
SEQRES 44 B 678 THR GLY SER GLU VAL SER LEU SER VAL GLU ALA ALA LYS
SEQRES 45 B 678 THR LEU ALA ALA LYS ASN ILE LYS ALA ARG VAL VAL SER
SEQRES 46 B 678 LEU PRO ASP PHE PHE THR PHE ASP LYS GLN PRO LEU GLU
SEQRES 47 B 678 TYR ARG LEU SER VAL LEU PRO ASP ASN VAL PRO ILE MET
SEQRES 48 B 678 SER VAL GLU VAL LEU ALA THR THR CYS TRP GLY LYS TYR
SEQRES 49 B 678 ALA HIS GLN SER PHE GLY ILE ASP ARG PHE GLY ALA SER
SEQRES 50 B 678 GLY LYS ALA PRO GLU VAL PHE LYS PHE PHE GLY PHE THR
SEQRES 51 B 678 PRO GLU GLY VAL ALA GLU ARG ALA GLN LYS THR ILE ALA
SEQRES 52 B 678 PHE TYR LYS GLY ASP LYS LEU ILE SER PRO LEU LYS LYS
SEQRES 53 B 678 ALA PHE
HET CA A 682 1
HET N3T A 681 26
HET CA B 682 1
HET N3T B 681 26
HETNAM CA CALCIUM ION
HETNAM N3T 3'-DEAZO-THIAMIN DIPHOSPHATE
FORMUL 3 CA 2(CA 2+)
FORMUL 4 N3T 2(C13 H19 N3 O7 P2 S)
HELIX 1 A1 ASP A 6 ALA A 26 1N-TERMINAL DOMAIN 21
HELIX 2 A2 GLY A 32 PRO A 39 1N-TERMINAL DOMAIN 8
HELIX 3 A3 ALA A 40 SER A 46 1N-TERMINAL DOMAIN 7
HELIX 4 A4 VAL A 71 LEU A 80 1N-TERMINAL DOMAIN 10
HELIX 5 A5 ILE A 87 LYS A 91 1N-TERMINAL DOMAIN 5
HELIX 6 A6 GLN A 120 TYR A 139 1N-TERMINAL DOMAIN 20
HELIX 7 A7 ASP A 157 GLN A 161 1N-TERMINAL DOMAIN 5
HELIX 8 A8 GLY A 163 LEU A 175 1N-TERMINAL DOMAIN 13
HELIX 9 A9 VAL A 203 ALA A 209 1N-TERMINAL DOMAIN 7
HELIX 10 A10 LEU A 224 LEU A 236 1N-TERMINAL DOMAIN 13
HELIX 11 A11 ALA A 269 LYS A 278 1N-TERMINAL DOMAIN 10
HELIX 12 A12 GLN A 291 PRO A 324 1N-TERMINAL DOMAIN 34
HELIX 13 A13 LEU A 326 LEU A 334 1MIDDLE DOMAIN 9
HELIX 14 A14 THR A 358 VAL A 369 1MIDDLE DOMAIN 12
HELIX 15 A15 THR A 384 ASN A 387 1MIDDLE DOMAIN 4
HELIX 16 A16 GLU A 418 PHE A 431 1MIDDLE DOMAIN 14
HELIX 17 A17 LEU A 443 VAL A 446 1MIDDLE DOMAIN 4
HELIX 18 A18 ARG A 500 ALA A 509 1MIDDLE DOMAIN 10
HELIX 19 A19 THR A 486 ARG A 491 1MIDDLE DOMAIN 6
HELIX 20 A20 GLY A 504 GLU A 516 1MIDDLE DOMAIN 13
HELIX 21 A21 ILE A 539 ALA A 542 1C-TERMINAL DOMAIN 4
HELIX 22 A22 GLU A 565 ALA A 578 1C-TERMINAL DOMAIN 14
HELIX 23 A23 PHE A 591 LYS A 596 1C-TERMINAL DOMAIN 6
HELIX 24 A24 LEU A 599 VAL A 605 1C-TERMINAL DOMAIN 7
HELIX 25 A25 ALA A 642 PHE A 649 1C-TERMINAL DOMAIN 8
HELIX 26 A26 PRO A 653 TYR A 667 1C-TERMINAL DOMAIN 15
HELIX 27 B1 ASP B 6 ALA B 26 1N-TERMINAL DOMAIN 21
HELIX 28 B2 GLY B 32 PRO B 39 1N-TERMINAL DOMAIN 8
HELIX 29 B3 ALA B 40 SER B 46 1N-TERMINAL DOMAIN 7
HELIX 30 B4 VAL B 71 LEU B 80 1N-TERMINAL DOMAIN 10
HELIX 31 B5 ILE B 87 LYS B 91 1N-TERMINAL DOMAIN 5
HELIX 32 B6 GLN B 120 TYR B 139 1N-TERMINAL DOMAIN 20
HELIX 33 B7 ASP B 157 GLN B 161 1N-TERMINAL DOMAIN 5
HELIX 34 B8 GLY B 163 LEU B 175 1N-TERMINAL DOMAIN 13
HELIX 35 B9 VAL B 203 ALA B 209 1N-TERMINAL DOMAIN 7
HELIX 36 B10 LEU B 224 LEU B 236 1N-TERMINAL DOMAIN 13
HELIX 37 B11 ALA B 269 LYS B 278 1N-TERMINAL DOMAIN 10
HELIX 38 B12 GLN B 291 PRO B 324 1N-TERMINAL DOMAIN 34
HELIX 39 B13 LEU B 326 LEU B 334 1MIDDLE DOMAIN 9
HELIX 40 B14 THR B 358 VAL B 369 1MIDDLE DOMAIN 12
HELIX 41 B15 THR B 384 ASN B 387 1MIDDLE DOMAIN 4
HELIX 42 B16 GLU B 418 PHE B 431 1MIDDLE DOMAIN 14
HELIX 43 B17 LEU B 443 VAL B 446 1MIDDLE DOMAIN 4
HELIX 44 B18 ARG B 500 ALA B 509 1MIDDLE DOMAIN 10
HELIX 45 B19 THR B 486 ARG B 491 1MIDDLE DOMAIN 6
HELIX 46 B20 GLY B 504 GLU B 516 1MIDDLE DOMAIN 13
HELIX 47 B21 ILE B 539 ALA B 542 1C-TERMINAL DOMAIN 4
HELIX 48 B22 GLU B 565 ALA B 578 1C-TERMINAL DOMAIN 14
HELIX 49 B23 PHE B 591 LYS B 596 1C-TERMINAL DOMAIN 6
HELIX 50 B24 LEU B 599 VAL B 605 1C-TERMINAL DOMAIN 7
HELIX 51 B25 ALA B 642 PHE B 649 1C-TERMINAL DOMAIN 8
HELIX 52 B26 PRO B 653 TYR B 667 1C-TERMINAL DOMAIN 15
SHEET 1 AN 5 ARG A 62 LEU A 65 0
SHEET 2 AN 5 THR A 151 ASP A 157 1 N TYR A 152 O ARG A 62
SHEET 3 AN 5 LEU A 180 ASP A 186 1 N ILE A 181 O THR A 151
SHEET 4 AN 5 THR A 242 THR A 247 1 N THR A 242 O LEU A 180
SHEET 5 AN 5 GLU A 213 VAL A 217 1 N LEU A 215 O LEU A 243
SHEET 1 AM 6 TYR A 411 ARG A 413 0
SHEET 2 AM 6 LEU A 376 SER A 380 1 O GLY A 378 N ILE A 412
SHEET 3 AM 6 LYS A 436 PHE A 442 1 N TYR A 438 O ILE A 377
SHEET 4 AM 6 ILE A 464 THR A 468 1 N VAL A 466 O GLY A 439
SHEET 5 AM 6 SER A 522 ALA A 525 1 N ILE A 524 O TRP A 465
SHEET 6 AM 6 GLN A 497 TRP A 499 1 N TRP A 499 O ILE A 523
SHEET 1 AC 5 TYR A 547 GLN A 550 0
SHEET 2 AC 5 ALA A 583 SER A 587 -1 N VAL A 585 O GLN A 550
SHEET 3 AC 5 ILE A 557 ALA A 561 1 N LEU A 559 O ARG A 584
SHEET 4 AC 5 ILE A 612 VAL A 615 1 N MET A 613 O ILE A 558
SHEET 5 AC 5 GLN A 629 PHE A 631 1 N PHE A 631 O SER A 614
SHEET 1 BN 5 ARG B 62 LEU B 65 0
SHEET 2 BN 5 THR B 151 ASP B 157 1 N TYR B 152 O ARG B 62
SHEET 3 BN 5 LEU B 180 ASP B 186 1 N ILE B 181 O THR B 151
SHEET 4 BN 5 THR B 242 THR B 247 1 N THR B 242 O LEU B 180
SHEET 5 BN 5 GLU B 213 VAL B 217 1 N LEU B 215 O LEU B 243
SHEET 1 BM 6 TYR B 411 ARG B 413 0
SHEET 2 BM 6 LEU B 376 SER B 380 1 O GLY B 378 N ILE B 412
SHEET 3 BM 6 LYS B 436 PHE B 442 1 N TYR B 438 O ILE B 377
SHEET 4 BM 6 ILE B 464 THR B 468 1 N VAL B 466 O GLY B 439
SHEET 5 BM 6 SER B 522 ALA B 525 1 N ILE B 524 O TRP B 465
SHEET 6 BM 6 GLN B 497 TRP B 499 1 N TRP B 499 O ILE B 523
SHEET 1 BC 5 TYR B 547 GLN B 550 0
SHEET 2 BC 5 ALA B 583 SER B 587 -1 N VAL B 585 O GLN B 550
SHEET 3 BC 5 ILE B 557 ALA B 561 1 N LEU B 559 O ARG B 584
SHEET 4 BC 5 ILE B 612 VAL B 615 1 N MET B 613 O ILE B 558
SHEET 5 BC 5 GLN B 629 PHE B 631 1 N PHE B 631 O SER B 614
LINK OD1 ASP A 157 CA CA A 682 1555 1555 2.33
LINK OD1 ASN A 187 CA CA A 682 1555 1555 1.82
LINK ND2 ASN A 187 CA CA A 682 1555 1555 3.13
LINK O ILE A 189 CA CA A 682 1555 1555 2.22
LINK O1B N3T A 681 CA CA A 682 1555 1555 1.65
LINK O3A N3T A 681 CA CA A 682 1555 1555 3.30
LINK O2A N3T A 681 CA CA A 682 1555 1555 2.09
LINK O2B N3T A 681 CA CA A 682 1555 1555 3.08
LINK OD2 ASP B 157 CA CA B 682 1555 1555 2.72
LINK OD1 ASN B 187 CA CA B 682 1555 1555 1.86
LINK ND2 ASN B 187 CA CA B 682 1555 1555 3.22
LINK O ILE B 189 CA CA B 682 1555 1555 1.83
LINK O2B N3T B 681 CA CA B 682 1555 1555 1.66
LINK O3B N3T B 681 CA CA B 682 1555 1555 3.34
LINK O3A N3T B 681 CA CA B 682 1555 1555 3.33
LINK O2A N3T B 681 CA CA B 682 1555 1555 2.28
SITE 1 AC1 4 ASP A 157 ASN A 187 ILE A 189 N3T A 681
SITE 1 AC2 4 ASP B 157 ASN B 187 ILE B 189 N3T B 681
SITE 1 AC3 22 ALA A 33 HIS A 69 GLY A 116 PRO A 117
SITE 2 AC3 22 LEU A 118 GLY A 156 ASP A 157 GLY A 158
SITE 3 AC3 22 GLU A 162 ASN A 187 ILE A 189 THR A 190
SITE 4 AC3 22 ILE A 191 ILE A 250 HIS A 263 CA A 682
SITE 5 AC3 22 ASP B 382 ILE B 416 GLU B 418 PHE B 445
SITE 6 AC3 22 TYR B 448 HIS B 481
SITE 1 AC4 19 ASP A 382 GLU A 418 PHE A 445 TYR A 448
SITE 2 AC4 19 HIS A 481 ALA B 33 HIS B 69 GLY B 116
SITE 3 AC4 19 PRO B 117 LEU B 118 ASP B 157 GLY B 158
SITE 4 AC4 19 GLU B 162 ASN B 187 ILE B 189 THR B 190
SITE 5 AC4 19 ILE B 191 HIS B 263 CA B 682
CRYST1 76.300 113.300 160.900 90.00 90.00 90.00 P 21 21 21 8
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 0.013106 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008826 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006215 0.00000
MTRIX1 1 -0.784000 0.001000 -0.621000 25.04400 1
MTRIX2 1 0.000000 -1.000000 -0.002000 132.15700 1
MTRIX3 1 -0.621000 -0.001000 0.784000 8.81300 1
(ATOM LINES ARE NOT SHOWN.)
END
