HEADER TRANSFERASE 11-SEP-07 2R8P
TITLE TRANSKETOLASE FROM E. COLI IN COMPLEX WITH SUBSTRATE D-FRUCTOSE-6-
TITLE 2 PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSKETOLASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TK 1;
COMPND 5 EC: 2.2.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 GENE: TKTA, TKT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS REACTION INTERMEDIATE, CALCIUM, METAL-BINDING, THIAMINE
KEYWDS 2 PYROPHOSPHATE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.WILLE,P.ASZTALOS,M.S.WEISS,K.TITTMANN
REVDAT 4 21-FEB-24 2R8P 1 REMARK SEQADV LINK
REVDAT 3 25-OCT-17 2R8P 1 REMARK
REVDAT 2 24-FEB-09 2R8P 1 VERSN
REVDAT 1 11-DEC-07 2R8P 0
JRNL AUTH P.ASZTALOS,C.PARTHIER,R.GOLBIK,M.KLEINSCHMIDT,G.HUBNER,
JRNL AUTH 2 M.S.WEISS,R.FRIEDEMANN,G.WILLE,K.TITTMANN
JRNL TITL STRAIN AND NEAR ATTACK CONFORMERS IN ENZYMIC THIAMIN
JRNL TITL 2 CATALYSIS: X-RAY CRYSTALLOGRAPHIC SNAPSHOTS OF BACTERIAL
JRNL TITL 3 TRANSKETOLASE IN COVALENT COMPLEX WITH DONOR KETOSES
JRNL TITL 4 XYLULOSE 5-PHOSPHATE AND FRUCTOSE 6-PHOSPHATE, AND IN
JRNL TITL 5 NONCOVALENT COMPLEX WITH ACCEPTOR ALDOSE RIBOSE 5-PHOSPHATE.
JRNL REF BIOCHEMISTRY V. 46 12037 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17914867
JRNL DOI 10.1021/BI700844M
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 147003
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 + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.500
REMARK 3 FREE R VALUE TEST SET COUNT : 2182
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10442
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.1970
REMARK 3 BIN FREE R VALUE SET COUNT : 162
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10188
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 122
REMARK 3 SOLVENT ATOMS : 953
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.01000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.087
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.083
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.369
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10563 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14317 ; 1.347 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1332 ; 5.696 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 473 ;34.775 ;24.207
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1693 ;11.837 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 57 ;18.246 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1529 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8079 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5285 ; 0.193 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 7212 ; 0.304 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 825 ; 0.102 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 10 ; 0.144 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 48 ; 0.138 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.147 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 6789 ; 0.588 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10501 ; 0.896 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4339 ; 1.700 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3814 ; 2.678 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2R8P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-07.
REMARK 100 THE DEPOSITION ID IS D_1000044564.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8423
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 147102
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 40.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.51800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, GLYCEROL, PH 7.9, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 281K
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 45.10700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.67250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.93150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.67250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.10700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.93150
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10450 ANGSTROM**2
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 MET A 1
REMARK 465 HIS A 664
REMARK 465 HIS A 665
REMARK 465 HIS A 666
REMARK 465 HIS A 667
REMARK 465 HIS A 668
REMARK 465 HIS A 669
REMARK 465 MET B 1
REMARK 465 HIS B 668
REMARK 465 HIS B 669
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 113 -168.88 -115.77
REMARK 500 ASP A 146 87.91 -164.01
REMARK 500 TRP A 196 -2.81 -141.40
REMARK 500 ASN A 403 15.10 -145.11
REMARK 500 HIS A 461 60.91 61.19
REMARK 500 VAL A 476 -55.12 -134.37
REMARK 500 THR B 113 -168.97 -118.65
REMARK 500 ASP B 146 89.50 -166.75
REMARK 500 TRP B 196 -2.83 -145.65
REMARK 500 LEU B 372 76.28 -119.14
REMARK 500 ASN B 403 13.75 -142.46
REMARK 500 HIS B 461 62.06 63.07
REMARK 500 VAL B 476 -56.14 -132.55
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 670 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 155 OD2
REMARK 620 2 ASN A 185 OD1 86.8
REMARK 620 3 ILE A 187 O 93.3 89.4
REMARK 620 4 T6F A 671 O1A 96.0 174.5 95.2
REMARK 620 5 T6F A 671 O2B 167.4 91.4 99.2 84.8
REMARK 620 6 HOH A 677 O 83.9 90.3 177.2 85.4 83.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 670 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 155 OD2
REMARK 620 2 ASN B 185 OD1 85.7
REMARK 620 3 ILE B 187 O 93.5 90.3
REMARK 620 4 T6F B 671 O1A 95.8 173.2 96.2
REMARK 620 5 T6F B 671 O2B 167.1 92.9 99.3 84.1
REMARK 620 6 HOH B 703 O 82.8 87.4 175.8 86.2 84.4
REMARK 620 N 1 2 3 4 5
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 670
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 670
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T6F A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T6F B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 674
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 675
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 676
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 677
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 678
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 679
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QGD RELATED DB: PDB
REMARK 900 ENZYME WITHOUT SUBSTRATE
REMARK 900 RELATED ID: 2R5N RELATED DB: PDB
REMARK 900 RELATED ID: 2R8O RELATED DB: PDB
DBREF 2R8P A 1 663 UNP P27302 TKT1_ECOLI 1 663
DBREF 2R8P B 1 663 UNP P27302 TKT1_ECOLI 1 663
SEQADV 2R8P HIS A 664 UNP P27302 EXPRESSION TAG
SEQADV 2R8P HIS A 665 UNP P27302 EXPRESSION TAG
SEQADV 2R8P HIS A 666 UNP P27302 EXPRESSION TAG
SEQADV 2R8P HIS A 667 UNP P27302 EXPRESSION TAG
SEQADV 2R8P HIS A 668 UNP P27302 EXPRESSION TAG
SEQADV 2R8P HIS A 669 UNP P27302 EXPRESSION TAG
SEQADV 2R8P HIS B 664 UNP P27302 EXPRESSION TAG
SEQADV 2R8P HIS B 665 UNP P27302 EXPRESSION TAG
SEQADV 2R8P HIS B 666 UNP P27302 EXPRESSION TAG
SEQADV 2R8P HIS B 667 UNP P27302 EXPRESSION TAG
SEQADV 2R8P HIS B 668 UNP P27302 EXPRESSION TAG
SEQADV 2R8P HIS B 669 UNP P27302 EXPRESSION TAG
SEQRES 1 A 669 MET SER SER ARG LYS GLU LEU ALA ASN ALA ILE ARG ALA
SEQRES 2 A 669 LEU SER MET ASP ALA VAL GLN LYS ALA LYS SER GLY HIS
SEQRES 3 A 669 PRO GLY ALA PRO MET GLY MET ALA ASP ILE ALA GLU VAL
SEQRES 4 A 669 LEU TRP ARG ASP PHE LEU LYS HIS ASN PRO GLN ASN PRO
SEQRES 5 A 669 SER TRP ALA ASP ARG ASP ARG PHE VAL LEU SER ASN GLY
SEQRES 6 A 669 HIS GLY SER MET LEU ILE TYR SER LEU LEU HIS LEU THR
SEQRES 7 A 669 GLY TYR ASP LEU PRO MET GLU GLU LEU LYS ASN PHE ARG
SEQRES 8 A 669 GLN LEU HIS SER LYS THR PRO GLY HIS PRO GLU VAL GLY
SEQRES 9 A 669 TYR THR ALA GLY VAL GLU THR THR THR GLY PRO LEU GLY
SEQRES 10 A 669 GLN GLY ILE ALA ASN ALA VAL GLY MET ALA ILE ALA GLU
SEQRES 11 A 669 LYS THR LEU ALA ALA GLN PHE ASN ARG PRO GLY HIS ASP
SEQRES 12 A 669 ILE VAL ASP HIS TYR THR TYR ALA PHE MET GLY ASP GLY
SEQRES 13 A 669 CYS MET MET GLU GLY ILE SER HIS GLU VAL CYS SER LEU
SEQRES 14 A 669 ALA GLY THR LEU LYS LEU GLY LYS LEU ILE ALA PHE TYR
SEQRES 15 A 669 ASP ASP ASN GLY ILE SER ILE ASP GLY HIS VAL GLU GLY
SEQRES 16 A 669 TRP PHE THR ASP ASP THR ALA MET ARG PHE GLU ALA TYR
SEQRES 17 A 669 GLY TRP HIS VAL ILE ARG ASP ILE ASP GLY HIS ASP ALA
SEQRES 18 A 669 ALA SER ILE LYS ARG ALA VAL GLU GLU ALA ARG ALA VAL
SEQRES 19 A 669 THR ASP LYS PRO SER LEU LEU MET CYS LYS THR ILE ILE
SEQRES 20 A 669 GLY PHE GLY SER PRO ASN LYS ALA GLY THR HIS ASP SER
SEQRES 21 A 669 HIS GLY ALA PRO LEU GLY ASP ALA GLU ILE ALA LEU THR
SEQRES 22 A 669 ARG GLU GLN LEU GLY TRP LYS TYR ALA PRO PHE GLU ILE
SEQRES 23 A 669 PRO SER GLU ILE TYR ALA GLN TRP ASP ALA LYS GLU ALA
SEQRES 24 A 669 GLY GLN ALA LYS GLU SER ALA TRP ASN GLU LYS PHE ALA
SEQRES 25 A 669 ALA TYR ALA LYS ALA TYR PRO GLN GLU ALA ALA GLU PHE
SEQRES 26 A 669 THR ARG ARG MET LYS GLY GLU MET PRO SER ASP PHE ASP
SEQRES 27 A 669 ALA LYS ALA LYS GLU PHE ILE ALA LYS LEU GLN ALA ASN
SEQRES 28 A 669 PRO ALA LYS ILE ALA SER ARG LYS ALA SER GLN ASN ALA
SEQRES 29 A 669 ILE GLU ALA PHE GLY PRO LEU LEU PRO GLU PHE LEU GLY
SEQRES 30 A 669 GLY SER ALA ASP LEU ALA PRO SER ASN LEU THR LEU TRP
SEQRES 31 A 669 SER GLY SER LYS ALA ILE ASN GLU ASP ALA ALA GLY ASN
SEQRES 32 A 669 TYR ILE HIS TYR GLY VAL ARG GLU PHE GLY MET THR ALA
SEQRES 33 A 669 ILE ALA ASN GLY ILE SER LEU HIS GLY GLY PHE LEU PRO
SEQRES 34 A 669 TYR THR SER THR PHE LEU MET PHE VAL GLU TYR ALA ARG
SEQRES 35 A 669 ASN ALA VAL ARG MET ALA ALA LEU MET LYS GLN ARG GLN
SEQRES 36 A 669 VAL MET VAL TYR THR HIS ASP SER ILE GLY LEU GLY GLU
SEQRES 37 A 669 ASP GLY PRO THR HIS GLN PRO VAL GLU GLN VAL ALA SER
SEQRES 38 A 669 LEU ARG VAL THR PRO ASN MET SER THR TRP ARG PRO CYS
SEQRES 39 A 669 ASP GLN VAL GLU SER ALA VAL ALA TRP LYS TYR GLY VAL
SEQRES 40 A 669 GLU ARG GLN ASP GLY PRO THR ALA LEU ILE LEU SER ARG
SEQRES 41 A 669 GLN ASN LEU ALA GLN GLN GLU ARG THR GLU GLU GLN LEU
SEQRES 42 A 669 ALA ASN ILE ALA ARG GLY GLY TYR VAL LEU LYS ASP CYS
SEQRES 43 A 669 ALA GLY GLN PRO GLU LEU ILE PHE ILE ALA THR GLY SER
SEQRES 44 A 669 GLU VAL GLU LEU ALA VAL ALA ALA TYR GLU LYS LEU THR
SEQRES 45 A 669 ALA GLU GLY VAL LYS ALA ARG VAL VAL SER MET PRO SER
SEQRES 46 A 669 THR ASP ALA PHE ASP LYS GLN ASP ALA ALA TYR ARG GLU
SEQRES 47 A 669 SER VAL LEU PRO LYS ALA VAL THR ALA ARG VAL ALA VAL
SEQRES 48 A 669 GLU ALA GLY ILE ALA ASP TYR TRP TYR LYS TYR VAL GLY
SEQRES 49 A 669 LEU ASN GLY ALA ILE VAL GLY MET THR THR PHE GLY GLU
SEQRES 50 A 669 SER ALA PRO ALA GLU LEU LEU PHE GLU GLU PHE GLY PHE
SEQRES 51 A 669 THR VAL ASP ASN VAL VAL ALA LYS ALA LYS GLU LEU LEU
SEQRES 52 A 669 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 669 MET SER SER ARG LYS GLU LEU ALA ASN ALA ILE ARG ALA
SEQRES 2 B 669 LEU SER MET ASP ALA VAL GLN LYS ALA LYS SER GLY HIS
SEQRES 3 B 669 PRO GLY ALA PRO MET GLY MET ALA ASP ILE ALA GLU VAL
SEQRES 4 B 669 LEU TRP ARG ASP PHE LEU LYS HIS ASN PRO GLN ASN PRO
SEQRES 5 B 669 SER TRP ALA ASP ARG ASP ARG PHE VAL LEU SER ASN GLY
SEQRES 6 B 669 HIS GLY SER MET LEU ILE TYR SER LEU LEU HIS LEU THR
SEQRES 7 B 669 GLY TYR ASP LEU PRO MET GLU GLU LEU LYS ASN PHE ARG
SEQRES 8 B 669 GLN LEU HIS SER LYS THR PRO GLY HIS PRO GLU VAL GLY
SEQRES 9 B 669 TYR THR ALA GLY VAL GLU THR THR THR GLY PRO LEU GLY
SEQRES 10 B 669 GLN GLY ILE ALA ASN ALA VAL GLY MET ALA ILE ALA GLU
SEQRES 11 B 669 LYS THR LEU ALA ALA GLN PHE ASN ARG PRO GLY HIS ASP
SEQRES 12 B 669 ILE VAL ASP HIS TYR THR TYR ALA PHE MET GLY ASP GLY
SEQRES 13 B 669 CYS MET MET GLU GLY ILE SER HIS GLU VAL CYS SER LEU
SEQRES 14 B 669 ALA GLY THR LEU LYS LEU GLY LYS LEU ILE ALA PHE TYR
SEQRES 15 B 669 ASP ASP ASN GLY ILE SER ILE ASP GLY HIS VAL GLU GLY
SEQRES 16 B 669 TRP PHE THR ASP ASP THR ALA MET ARG PHE GLU ALA TYR
SEQRES 17 B 669 GLY TRP HIS VAL ILE ARG ASP ILE ASP GLY HIS ASP ALA
SEQRES 18 B 669 ALA SER ILE LYS ARG ALA VAL GLU GLU ALA ARG ALA VAL
SEQRES 19 B 669 THR ASP LYS PRO SER LEU LEU MET CYS LYS THR ILE ILE
SEQRES 20 B 669 GLY PHE GLY SER PRO ASN LYS ALA GLY THR HIS ASP SER
SEQRES 21 B 669 HIS GLY ALA PRO LEU GLY ASP ALA GLU ILE ALA LEU THR
SEQRES 22 B 669 ARG GLU GLN LEU GLY TRP LYS TYR ALA PRO PHE GLU ILE
SEQRES 23 B 669 PRO SER GLU ILE TYR ALA GLN TRP ASP ALA LYS GLU ALA
SEQRES 24 B 669 GLY GLN ALA LYS GLU SER ALA TRP ASN GLU LYS PHE ALA
SEQRES 25 B 669 ALA TYR ALA LYS ALA TYR PRO GLN GLU ALA ALA GLU PHE
SEQRES 26 B 669 THR ARG ARG MET LYS GLY GLU MET PRO SER ASP PHE ASP
SEQRES 27 B 669 ALA LYS ALA LYS GLU PHE ILE ALA LYS LEU GLN ALA ASN
SEQRES 28 B 669 PRO ALA LYS ILE ALA SER ARG LYS ALA SER GLN ASN ALA
SEQRES 29 B 669 ILE GLU ALA PHE GLY PRO LEU LEU PRO GLU PHE LEU GLY
SEQRES 30 B 669 GLY SER ALA ASP LEU ALA PRO SER ASN LEU THR LEU TRP
SEQRES 31 B 669 SER GLY SER LYS ALA ILE ASN GLU ASP ALA ALA GLY ASN
SEQRES 32 B 669 TYR ILE HIS TYR GLY VAL ARG GLU PHE GLY MET THR ALA
SEQRES 33 B 669 ILE ALA ASN GLY ILE SER LEU HIS GLY GLY PHE LEU PRO
SEQRES 34 B 669 TYR THR SER THR PHE LEU MET PHE VAL GLU TYR ALA ARG
SEQRES 35 B 669 ASN ALA VAL ARG MET ALA ALA LEU MET LYS GLN ARG GLN
SEQRES 36 B 669 VAL MET VAL TYR THR HIS ASP SER ILE GLY LEU GLY GLU
SEQRES 37 B 669 ASP GLY PRO THR HIS GLN PRO VAL GLU GLN VAL ALA SER
SEQRES 38 B 669 LEU ARG VAL THR PRO ASN MET SER THR TRP ARG PRO CYS
SEQRES 39 B 669 ASP GLN VAL GLU SER ALA VAL ALA TRP LYS TYR GLY VAL
SEQRES 40 B 669 GLU ARG GLN ASP GLY PRO THR ALA LEU ILE LEU SER ARG
SEQRES 41 B 669 GLN ASN LEU ALA GLN GLN GLU ARG THR GLU GLU GLN LEU
SEQRES 42 B 669 ALA ASN ILE ALA ARG GLY GLY TYR VAL LEU LYS ASP CYS
SEQRES 43 B 669 ALA GLY GLN PRO GLU LEU ILE PHE ILE ALA THR GLY SER
SEQRES 44 B 669 GLU VAL GLU LEU ALA VAL ALA ALA TYR GLU LYS LEU THR
SEQRES 45 B 669 ALA GLU GLY VAL LYS ALA ARG VAL VAL SER MET PRO SER
SEQRES 46 B 669 THR ASP ALA PHE ASP LYS GLN ASP ALA ALA TYR ARG GLU
SEQRES 47 B 669 SER VAL LEU PRO LYS ALA VAL THR ALA ARG VAL ALA VAL
SEQRES 48 B 669 GLU ALA GLY ILE ALA ASP TYR TRP TYR LYS TYR VAL GLY
SEQRES 49 B 669 LEU ASN GLY ALA ILE VAL GLY MET THR THR PHE GLY GLU
SEQRES 50 B 669 SER ALA PRO ALA GLU LEU LEU PHE GLU GLU PHE GLY PHE
SEQRES 51 B 669 THR VAL ASP ASN VAL VAL ALA LYS ALA LYS GLU LEU LEU
SEQRES 52 B 669 HIS HIS HIS HIS HIS HIS
HET CA A 670 1
HET T6F A 671 42
HET EDO A 672 4
HET CA B 670 1
HET T6F B 671 42
HET EDO B 672 4
HET EDO B 673 4
HET EDO B 674 4
HET EDO B 675 4
HET EDO B 676 4
HET EDO B 677 4
HET EDO B 678 4
HET EDO B 679 4
HETNAM CA CALCIUM ION
HETNAM T6F 2-C-{3-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-5-(2-
HETNAM 2 T6F {[(R)-HYDROXY(PHOSPHONOOXY)PHOSPHORYL]OXY}ETHYL)-4-
HETNAM 3 T6F METHYL-1,3-THIAZOL-3-IUM-2-YL}-6-O-PHOSPHONO-D-
HETNAM 4 T6F GLUCITOL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN T6F D-FRUCTOSE-6-PHOSPHATE THIAMIN DIPHOSPHATE ADDUCT
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 CA 2(CA 2+)
FORMUL 4 T6F 2(C18 H32 N4 O16 P3 S 1+)
FORMUL 5 EDO 9(C2 H6 O2)
FORMUL 16 HOH *953(H2 O)
HELIX 1 1 SER A 3 LYS A 23 1 21
HELIX 2 2 PRO A 27 PHE A 44 1 18
HELIX 3 3 ASN A 64 HIS A 66 5 3
HELIX 4 4 GLY A 67 GLY A 79 1 13
HELIX 5 5 PRO A 83 LYS A 88 1 6
HELIX 6 6 GLY A 117 ASN A 138 1 22
HELIX 7 7 GLY A 154 GLU A 160 1 7
HELIX 8 8 GLU A 160 LEU A 173 1 14
HELIX 9 9 GLU A 194 TRP A 196 5 3
HELIX 10 10 ASP A 200 TYR A 208 1 9
HELIX 11 11 ASP A 220 VAL A 234 1 15
HELIX 12 12 THR A 257 HIS A 261 5 5
HELIX 13 13 GLY A 266 GLY A 278 1 13
HELIX 14 14 PRO A 287 ASP A 295 1 9
HELIX 15 15 ALA A 296 TYR A 318 1 23
HELIX 16 16 TYR A 318 GLY A 331 1 14
HELIX 17 17 ASP A 336 ASN A 351 1 16
HELIX 18 18 SER A 357 GLY A 369 1 13
HELIX 19 19 LEU A 382 LEU A 387 1 6
HELIX 20 20 ARG A 410 GLY A 425 1 16
HELIX 21 21 MET A 436 TYR A 440 5 5
HELIX 22 22 ALA A 441 MET A 451 1 11
HELIX 23 23 SER A 463 GLY A 467 5 5
HELIX 24 24 GLU A 477 VAL A 484 1 8
HELIX 25 25 ASP A 495 ARG A 509 1 15
HELIX 26 26 THR A 529 ILE A 536 1 8
HELIX 27 27 ALA A 537 GLY A 539 5 3
HELIX 28 28 GLU A 560 GLY A 575 1 16
HELIX 29 29 SER A 585 LYS A 591 1 7
HELIX 30 30 ASP A 593 LEU A 601 1 9
HELIX 31 31 TRP A 619 GLY A 624 1 6
HELIX 32 32 PRO A 640 PHE A 648 1 9
HELIX 33 33 THR A 651 LEU A 663 1 13
HELIX 34 34 SER B 3 LYS B 23 1 21
HELIX 35 35 PRO B 27 PHE B 44 1 18
HELIX 36 36 ASN B 64 HIS B 66 5 3
HELIX 37 37 GLY B 67 GLY B 79 1 13
HELIX 38 38 PRO B 83 ASN B 89 1 7
HELIX 39 39 GLY B 117 ASN B 138 1 22
HELIX 40 40 GLY B 154 GLU B 160 1 7
HELIX 41 41 GLU B 160 LEU B 173 1 14
HELIX 42 42 GLU B 194 TRP B 196 5 3
HELIX 43 43 ASP B 200 TYR B 208 1 9
HELIX 44 44 ASP B 220 VAL B 234 1 15
HELIX 45 45 THR B 257 HIS B 261 5 5
HELIX 46 46 GLY B 266 GLY B 278 1 13
HELIX 47 47 PRO B 287 ASP B 295 1 9
HELIX 48 48 ALA B 296 TYR B 318 1 23
HELIX 49 49 TYR B 318 GLY B 331 1 14
HELIX 50 50 ASP B 336 ASN B 351 1 16
HELIX 51 51 SER B 357 GLY B 369 1 13
HELIX 52 52 LEU B 382 LEU B 387 1 6
HELIX 53 53 ARG B 410 GLY B 425 1 16
HELIX 54 54 MET B 436 TYR B 440 5 5
HELIX 55 55 ALA B 441 MET B 451 1 11
HELIX 56 56 SER B 463 GLY B 467 5 5
HELIX 57 57 GLU B 477 VAL B 484 1 8
HELIX 58 58 ASP B 495 ARG B 509 1 15
HELIX 59 59 THR B 529 ILE B 536 1 8
HELIX 60 60 ALA B 537 GLY B 539 5 3
HELIX 61 61 GLU B 560 GLU B 574 1 15
HELIX 62 62 SER B 585 GLN B 592 1 8
HELIX 63 63 ASP B 593 LEU B 601 1 9
HELIX 64 64 TRP B 619 GLY B 624 1 6
HELIX 65 65 PRO B 640 PHE B 648 1 9
HELIX 66 66 THR B 651 HIS B 667 1 17
SHEET 1 A 5 ARG A 59 LEU A 62 0
SHEET 2 A 5 THR A 149 MET A 153 1 O TYR A 150 N ARG A 59
SHEET 3 A 5 LEU A 178 ASP A 184 1 O ASP A 183 N MET A 153
SHEET 4 A 5 SER A 239 LYS A 244 1 O SER A 239 N ALA A 180
SHEET 5 A 5 HIS A 211 ASP A 217 1 N ILE A 213 O MET A 242
SHEET 1 B 2 ILE A 187 SER A 188 0
SHEET 2 B 2 GLY A 191 HIS A 192 -1 O GLY A 191 N SER A 188
SHEET 1 C 2 ILE A 355 ALA A 356 0
SHEET 2 C 2 ASN A 522 LEU A 523 -1 O LEU A 523 N ILE A 355
SHEET 1 D 6 TYR A 404 HIS A 406 0
SHEET 2 D 6 PHE A 375 SER A 379 1 N GLY A 377 O ILE A 405
SHEET 3 D 6 LEU A 428 PHE A 434 1 O LEU A 428 N LEU A 376
SHEET 4 D 6 VAL A 456 THR A 460 1 O VAL A 458 N THR A 431
SHEET 5 D 6 THR A 514 ILE A 517 1 O LEU A 516 N MET A 457
SHEET 6 D 6 SER A 489 TRP A 491 1 N SER A 489 O ALA A 515
SHEET 1 E 5 TYR A 541 LYS A 544 0
SHEET 2 E 5 ALA A 578 SER A 582 -1 O VAL A 580 N LEU A 543
SHEET 3 E 5 LEU A 552 ALA A 556 1 N PHE A 554 O VAL A 581
SHEET 4 E 5 ARG A 608 ILE A 615 1 O VAL A 609 N ILE A 553
SHEET 5 E 5 ALA A 628 MET A 632 1 O VAL A 630 N ALA A 610
SHEET 1 F 5 ARG B 59 LEU B 62 0
SHEET 2 F 5 THR B 149 MET B 153 1 O TYR B 150 N ARG B 59
SHEET 3 F 5 LEU B 178 ASP B 184 1 O PHE B 181 N ALA B 151
SHEET 4 F 5 SER B 239 LYS B 244 1 O LEU B 241 N TYR B 182
SHEET 5 F 5 HIS B 211 ASP B 217 1 N ILE B 216 O LYS B 244
SHEET 1 G 2 ILE B 187 SER B 188 0
SHEET 2 G 2 GLY B 191 HIS B 192 -1 O GLY B 191 N SER B 188
SHEET 1 H 2 ILE B 355 ALA B 356 0
SHEET 2 H 2 ASN B 522 LEU B 523 -1 O LEU B 523 N ILE B 355
SHEET 1 I 6 TYR B 404 HIS B 406 0
SHEET 2 I 6 PHE B 375 SER B 379 1 N GLY B 377 O ILE B 405
SHEET 3 I 6 LEU B 428 PHE B 434 1 O LEU B 428 N LEU B 376
SHEET 4 I 6 VAL B 456 THR B 460 1 O VAL B 458 N THR B 431
SHEET 5 I 6 THR B 514 LEU B 518 1 O LEU B 516 N MET B 457
SHEET 6 I 6 SER B 489 TRP B 491 1 N SER B 489 O ALA B 515
SHEET 1 J 5 TYR B 541 LYS B 544 0
SHEET 2 J 5 ALA B 578 SER B 582 -1 O VAL B 580 N LEU B 543
SHEET 3 J 5 LEU B 552 ALA B 556 1 N PHE B 554 O ARG B 579
SHEET 4 J 5 ARG B 608 ILE B 615 1 O VAL B 609 N ILE B 555
SHEET 5 J 5 ALA B 628 MET B 632 1 O VAL B 630 N ALA B 610
LINK OD2 ASP A 155 CA CA A 670 1555 1555 2.32
LINK OD1 ASN A 185 CA CA A 670 1555 1555 2.40
LINK O ILE A 187 CA CA A 670 1555 1555 2.28
LINK CA CA A 670 O1A T6F A 671 1555 1555 2.20
LINK CA CA A 670 O2B T6F A 671 1555 1555 2.30
LINK CA CA A 670 O HOH A 677 1555 1555 2.50
LINK OD2 ASP B 155 CA CA B 670 1555 1555 2.33
LINK OD1 ASN B 185 CA CA B 670 1555 1555 2.37
LINK O ILE B 187 CA CA B 670 1555 1555 2.24
LINK CA CA B 670 O1A T6F B 671 1555 1555 2.20
LINK CA CA B 670 O2B T6F B 671 1555 1555 2.27
LINK CA CA B 670 O HOH B 703 1555 1555 2.46
SITE 1 AC1 5 ASP A 155 ASN A 185 ILE A 187 T6F A 671
SITE 2 AC1 5 HOH A 677
SITE 1 AC2 5 ASP B 155 ASN B 185 ILE B 187 T6F B 671
SITE 2 AC2 5 HOH B 703
SITE 1 AC3 32 HIS A 26 ALA A 29 HIS A 66 HIS A 100
SITE 2 AC3 32 GLY A 114 LEU A 116 ASP A 155 GLY A 156
SITE 3 AC3 32 GLU A 160 ASN A 185 ILE A 187 ILE A 189
SITE 4 AC3 32 ILE A 247 HIS A 261 CA A 670 HOH A 689
SITE 5 AC3 32 HOH A 708 HOH A 713 HOH A 736 HOH A1114
SITE 6 AC3 32 ARG B 358 ASP B 381 LEU B 382 SER B 385
SITE 7 AC3 32 GLU B 411 PHE B 434 PHE B 437 TYR B 440
SITE 8 AC3 32 HIS B 461 ASP B 469 HIS B 473 ARG B 520
SITE 1 AC4 32 ARG A 358 ASP A 381 SER A 385 GLU A 411
SITE 2 AC4 32 PHE A 434 PHE A 437 TYR A 440 HIS A 461
SITE 3 AC4 32 ASP A 469 HIS A 473 ARG A 520 HOH A 886
SITE 4 AC4 32 HIS B 26 ALA B 29 HIS B 66 HIS B 100
SITE 5 AC4 32 GLY B 114 LEU B 116 ASP B 155 GLY B 156
SITE 6 AC4 32 GLU B 160 ASN B 185 ILE B 187 ILE B 189
SITE 7 AC4 32 ILE B 247 HIS B 261 CA B 670 HOH B 706
SITE 8 AC4 32 HOH B 708 HOH B 722 HOH B1084 HOH B1111
SITE 1 AC5 6 ARG B 274 GLU B 275 TRP B 279 GLN B 592
SITE 2 AC5 6 HOH B 760 HOH B1052
SITE 1 AC6 7 ALA B 271 TYR B 505 GLU B 508 ARG B 509
SITE 2 AC6 7 EDO B 674 HOH B 732 HOH B 754
SITE 1 AC7 3 ALA B 271 GLU B 275 EDO B 673
SITE 1 AC8 5 LEU B 272 GLU B 275 ARG B 509 ASP B 511
SITE 2 AC8 5 HOH B1032
SITE 1 AC9 6 ILE A 615 ASP A 617 THR A 633 HOH A 840
SITE 2 AC9 6 ARG B 483 HOH B 840
SITE 1 BC1 6 PHE B 375 TRP B 390 SER B 393 ASN B 403
SITE 2 BC1 6 TYR B 404 TYR B 430
SITE 1 BC2 6 GLU B 6 GLY B 278 TRP B 279 LYS B 280
SITE 2 BC2 6 TYR B 281 HOH B 845
SITE 1 BC3 6 LYS B 131 THR B 172 LYS B 174 ASN B 397
SITE 2 BC3 6 HOH B 779 HOH B1023
SITE 1 BC4 5 LYS B 21 LYS B 88 GLN B 92 HOH B 743
SITE 2 BC4 5 HOH B 970
CRYST1 90.214 101.863 133.345 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 0.011085 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009817 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007499 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
