HEADER SUGAR BINDING PROTEIN 29-JUL-10 2XMP
TITLE CRYSTAL STRUCTURE OF TREHALOSE SYNTHASE TRET MUTANT E326A
TITLE 2 FROM P.HORISHIKI IN COMPLEX WITH UDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TREHALOSE-SYNTHASE TRET;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PUTATIVE UNCHARACTERIZED PROTEIN PH1035;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;
SOURCE 3 ORGANISM_TAXID: 53953;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: MC1061;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P6XHIS119
KEYWDS SUGAR BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.-N.SONG,T.-Y.JUNG,S.-M.YOON,S.-B.LEE,M.-Y.LIM,E.-J.WOO
REVDAT 2 01-JUN-11 2XMP 1 JRNL
REVDAT 1 13-OCT-10 2XMP 0
JRNL AUTH E.-J.WOO,S.RYU,H.-N.SONG,T.-Y.JUNG,S.YEON,H.LEE,B.C.PARK,
JRNL AUTH 2 K.PARK,S.-B.LEE
JRNL TITL STRUCTURAL INSIGHTS ON THE NEW MECHANISM OF
JRNL TITL 2 TREHALOSE SYNTHESIS BY TREHALOSE SYNTHASE TRET
JRNL TITL 3 FROM PYROCOCCUS HORIKOSHII.
JRNL REF J.MOL.BIOL. V. 404 247 2010
JRNL REFN ISSN 0022-2836
JRNL PMID 20888836
JRNL DOI 10.1016/J.JMB.2010.09.056
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 78598.98
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.000000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 81.6
REMARK 3 NUMBER OF REFLECTIONS : 25838
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) : 0.209
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.8
REMARK 3 FREE R VALUE TEST SET COUNT : 1246
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 65.6
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3236
REMARK 3 BIN R VALUE (WORKING SET) : 0.300
REMARK 3 BIN FREE R VALUE : 0.328
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 165
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6748
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 139
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.7
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.8
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.30
REMARK 3 B22 (A**2) : -3.71
REMARK 3 B33 (A**2) : 8.01
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 1.09
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.44
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) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.56
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.3
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.2
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.83
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) : 5.28 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 7.69 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 7.54 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 10.48 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 39.3375
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : UDP_XPLOR_PAR.TXT
REMARK 3 TOPOLOGY FILE 1 : PROTEIN_REP.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : UDP_XPLOR_PAR.TXT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 2XMP COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JUL-10.
REMARK 100 THE PDBE ID CODE IS EBI-44851.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-05
REMARK 200 TEMPERATURE (KELVIN) : 297
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2399
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26469
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.50
REMARK 200 RESOLUTION RANGE LOW (A) : 2.59
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 80.9
REMARK 200 DATA REDUNDANCY : 3.9
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 30.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.1
REMARK 200 R MERGE FOR SHELL (I) : 0.29
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.85
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350,0.2M MGCL2,0.1M
REMARK 280 SODIUM HEPES BUFFER,5MM UDP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 31.50850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLU 326 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLU 326 TO ALA
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 LYS A 2
REMARK 465 GLY A 416
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 GLY B 416
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLY A 415 CA C O
REMARK 470 GLY B 415 CA C O
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 ARG A 67 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG A 67 NE - CZ - NH1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG A 67 NE - CZ - NH2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG A 116 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 116 NE - CZ - NH2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG A 170 CD - NE - CZ ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG A 170 NE - CZ - NH1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 170 NE - CZ - NH2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG B 67 CD - NE - CZ ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG B 67 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG B 67 NE - CZ - NH2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG B 116 CD - NE - CZ ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG B 116 NE - CZ - NH1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG B 116 NE - CZ - NH2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 170 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG B 170 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG B 170 NE - CZ - NH2 ANGL. DEV. = -6.3 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 7 -32.91 58.09
REMARK 500 PHE A 9 113.10 -161.53
REMARK 500 LYS A 13 46.39 -93.24
REMARK 500 THR A 49 147.94 167.58
REMARK 500 PHE A 51 -96.70 -105.14
REMARK 500 SER A 68 5.57 -62.55
REMARK 500 GLU A 72 66.74 -69.64
REMARK 500 GLN A 96 57.74 -99.38
REMARK 500 GLU A 99 32.47 -83.78
REMARK 500 ASP A 134 166.68 60.95
REMARK 500 ILE A 141 -18.63 -48.44
REMARK 500 PRO A 184 54.37 -65.21
REMARK 500 GLU A 185 -23.76 -148.96
REMARK 500 GLU A 190 -6.23 -56.45
REMARK 500 SER A 238 158.14 175.93
REMARK 500 PRO A 261 -8.58 -48.36
REMARK 500 ASP A 274 45.33 -104.76
REMARK 500 GLU A 291 41.65 -84.43
REMARK 500 TYR A 293 21.88 -76.43
REMARK 500 GLN A 321 77.84 -157.52
REMARK 500 MET A 322 48.27 -91.84
REMARK 500 HIS A 379 71.00 -114.06
REMARK 500 SER A 413 27.81 -140.74
REMARK 500 ARG B 14 126.09 -30.43
REMARK 500 THR B 49 148.49 167.84
REMARK 500 PHE B 51 -96.18 -104.76
REMARK 500 SER B 68 4.84 -62.72
REMARK 500 GLU B 72 66.07 -69.32
REMARK 500 GLN B 96 57.84 -99.39
REMARK 500 GLU B 99 33.14 -83.72
REMARK 500 ASP B 134 166.45 60.46
REMARK 500 ILE B 141 -17.79 -48.79
REMARK 500 PRO B 184 54.70 -64.42
REMARK 500 GLU B 185 -23.70 -149.62
REMARK 500 GLU B 190 -6.05 -56.70
REMARK 500 PRO B 201 -167.74 -71.14
REMARK 500 PRO B 205 -6.83 -55.47
REMARK 500 SER B 238 157.95 177.35
REMARK 500 PRO B 261 -8.34 -49.20
REMARK 500 ASP B 274 45.56 -104.38
REMARK 500 GLU B 291 41.79 -84.68
REMARK 500 TYR B 293 20.06 -74.47
REMARK 500 GLN B 321 76.39 -158.64
REMARK 500 MET B 322 47.99 -90.28
REMARK 500 HIS B 379 69.58 -113.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP A7517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP B7517
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2X6Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TREHALOSE SYNTHASE TRET
REMARK 900 FROM P.HORIKOSHI
REMARK 900 RELATED ID: 2X6R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TREHALOSE SYNTHASE TRET
REMARK 900 FROM P.HORIKOSHI PRODUCED BY SOAKING IN
REMARK 900 TREHALOSE
REMARK 900 RELATED ID: 2XA1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TREHALOSE SYNTHASE TRET
REMARK 900 FROM P.HORIKOSHII (SELENO DERIVATIVE)
DBREF 2XMP A 1 416 UNP O58762 O58762_PYRHO 1 416
DBREF 2XMP B 1 416 UNP O58762 O58762_PYRHO 1 416
SEQADV 2XMP ALA A 326 UNP O58762 GLU 326 ENGINEERED MUTATION
SEQADV 2XMP VAL A 372 UNP O58762 LYS 372 CONFLICT
SEQADV 2XMP ALA B 326 UNP O58762 GLU 326 ENGINEERED MUTATION
SEQADV 2XMP VAL B 372 UNP O58762 LYS 372 CONFLICT
SEQRES 1 A 416 MET LYS MET TYR GLU VAL LYS GLU PHE SER SER GLY LYS
SEQRES 2 A 416 ARG LYS LEU GLU ASP TYR LYS SER ILE ILE GLY GLU GLU
SEQRES 3 A 416 GLU VAL SER LYS ILE GLN GLU LYS ALA GLU LYS LEU LYS
SEQRES 4 A 416 GLY ARG SER PHE VAL HIS VAL ASN SER THR SER PHE GLY
SEQRES 5 A 416 GLY GLY VAL ALA GLU ILE LEU HIS SER LEU VAL PRO LEU
SEQRES 6 A 416 LEU ARG SER ILE GLY ILE GLU ALA ARG TRP PHE VAL ILE
SEQRES 7 A 416 GLU GLY PRO THR GLU PHE PHE ASN VAL THR LYS THR PHE
SEQRES 8 A 416 HIS ASN ALA LEU GLN GLY ASN GLU SER LEU LYS LEU THR
SEQRES 9 A 416 GLU GLU MET LYS GLU LEU TYR LEU ASN VAL ASN ARG GLU
SEQRES 10 A 416 ASN SER LYS PHE ILE ASP LEU SER SER PHE ASP TYR VAL
SEQRES 11 A 416 LEU VAL HIS ASP PRO GLN PRO ALA ALA LEU ILE GLU PHE
SEQRES 12 A 416 TYR GLU LYS LYS SER PRO TRP LEU TRP ARG CYS HIS ILE
SEQRES 13 A 416 ASP LEU SER SER PRO ASN ARG GLU PHE TRP GLU PHE LEU
SEQRES 14 A 416 ARG ARG PHE VAL GLU LYS TYR ASP ARG TYR ILE PHE HIS
SEQRES 15 A 416 LEU PRO GLU TYR VAL GLN PRO GLU LEU ASP ARG ASN LYS
SEQRES 16 A 416 ALA VAL ILE MET PRO PRO SER ILE ASP PRO LEU SER GLU
SEQRES 17 A 416 LYS ASN VAL GLU LEU LYS GLN THR GLU ILE LEU ARG ILE
SEQRES 18 A 416 LEU GLU ARG PHE ASP VAL ASP PRO GLU LYS PRO ILE ILE
SEQRES 19 A 416 THR GLN VAL SER ARG PHE ASP PRO TRP LYS GLY ILE PHE
SEQRES 20 A 416 ASP VAL ILE GLU ILE TYR ARG LYS VAL LYS GLU LYS ILE
SEQRES 21 A 416 PRO GLY VAL GLN LEU LEU LEU VAL GLY VAL MET ALA HIS
SEQRES 22 A 416 ASP ASP PRO GLU GLY TRP ILE TYR PHE GLU LYS THR LEU
SEQRES 23 A 416 ARG LYS ILE GLY GLU ASP TYR ASP VAL LYS VAL LEU THR
SEQRES 24 A 416 ASN LEU ILE GLY VAL HIS ALA ARG GLU VAL ASN ALA PHE
SEQRES 25 A 416 GLN ARG ALA SER ASP VAL ILE LEU GLN MET SER ILE ARG
SEQRES 26 A 416 ALA GLY PHE GLY LEU THR VAL THR GLU ALA MET TRP LYS
SEQRES 27 A 416 GLY LYS PRO VAL ILE GLY ARG ALA VAL GLY GLY ILE LYS
SEQRES 28 A 416 PHE GLN ILE VAL ASP GLY GLU THR GLY PHE LEU VAL ARG
SEQRES 29 A 416 ASP ALA ASN GLU ALA VAL GLU VAL VAL LEU TYR LEU LEU
SEQRES 30 A 416 LYS HIS PRO GLU VAL SER LYS GLU MET GLY ALA LYS ALA
SEQRES 31 A 416 LYS GLU ARG VAL ARG LYS ASN PHE ILE ILE THR LYS HIS
SEQRES 32 A 416 MET GLU ARG TYR LEU ASP ILE LEU ASN SER LEU GLY GLY
SEQRES 1 B 416 MET LYS MET TYR GLU VAL LYS GLU PHE SER SER GLY LYS
SEQRES 2 B 416 ARG LYS LEU GLU ASP TYR LYS SER ILE ILE GLY GLU GLU
SEQRES 3 B 416 GLU VAL SER LYS ILE GLN GLU LYS ALA GLU LYS LEU LYS
SEQRES 4 B 416 GLY ARG SER PHE VAL HIS VAL ASN SER THR SER PHE GLY
SEQRES 5 B 416 GLY GLY VAL ALA GLU ILE LEU HIS SER LEU VAL PRO LEU
SEQRES 6 B 416 LEU ARG SER ILE GLY ILE GLU ALA ARG TRP PHE VAL ILE
SEQRES 7 B 416 GLU GLY PRO THR GLU PHE PHE ASN VAL THR LYS THR PHE
SEQRES 8 B 416 HIS ASN ALA LEU GLN GLY ASN GLU SER LEU LYS LEU THR
SEQRES 9 B 416 GLU GLU MET LYS GLU LEU TYR LEU ASN VAL ASN ARG GLU
SEQRES 10 B 416 ASN SER LYS PHE ILE ASP LEU SER SER PHE ASP TYR VAL
SEQRES 11 B 416 LEU VAL HIS ASP PRO GLN PRO ALA ALA LEU ILE GLU PHE
SEQRES 12 B 416 TYR GLU LYS LYS SER PRO TRP LEU TRP ARG CYS HIS ILE
SEQRES 13 B 416 ASP LEU SER SER PRO ASN ARG GLU PHE TRP GLU PHE LEU
SEQRES 14 B 416 ARG ARG PHE VAL GLU LYS TYR ASP ARG TYR ILE PHE HIS
SEQRES 15 B 416 LEU PRO GLU TYR VAL GLN PRO GLU LEU ASP ARG ASN LYS
SEQRES 16 B 416 ALA VAL ILE MET PRO PRO SER ILE ASP PRO LEU SER GLU
SEQRES 17 B 416 LYS ASN VAL GLU LEU LYS GLN THR GLU ILE LEU ARG ILE
SEQRES 18 B 416 LEU GLU ARG PHE ASP VAL ASP PRO GLU LYS PRO ILE ILE
SEQRES 19 B 416 THR GLN VAL SER ARG PHE ASP PRO TRP LYS GLY ILE PHE
SEQRES 20 B 416 ASP VAL ILE GLU ILE TYR ARG LYS VAL LYS GLU LYS ILE
SEQRES 21 B 416 PRO GLY VAL GLN LEU LEU LEU VAL GLY VAL MET ALA HIS
SEQRES 22 B 416 ASP ASP PRO GLU GLY TRP ILE TYR PHE GLU LYS THR LEU
SEQRES 23 B 416 ARG LYS ILE GLY GLU ASP TYR ASP VAL LYS VAL LEU THR
SEQRES 24 B 416 ASN LEU ILE GLY VAL HIS ALA ARG GLU VAL ASN ALA PHE
SEQRES 25 B 416 GLN ARG ALA SER ASP VAL ILE LEU GLN MET SER ILE ARG
SEQRES 26 B 416 ALA GLY PHE GLY LEU THR VAL THR GLU ALA MET TRP LYS
SEQRES 27 B 416 GLY LYS PRO VAL ILE GLY ARG ALA VAL GLY GLY ILE LYS
SEQRES 28 B 416 PHE GLN ILE VAL ASP GLY GLU THR GLY PHE LEU VAL ARG
SEQRES 29 B 416 ASP ALA ASN GLU ALA VAL GLU VAL VAL LEU TYR LEU LEU
SEQRES 30 B 416 LYS HIS PRO GLU VAL SER LYS GLU MET GLY ALA LYS ALA
SEQRES 31 B 416 LYS GLU ARG VAL ARG LYS ASN PHE ILE ILE THR LYS HIS
SEQRES 32 B 416 MET GLU ARG TYR LEU ASP ILE LEU ASN SER LEU GLY GLY
HET UDP A7517 25
HET UDP B7517 25
HETNAM UDP URIDINE-5'-DIPHOSPHATE
FORMUL 3 UDP 2(C9 H14 N2 O12 P2)
FORMUL 4 HOH *139(H2 O)
HELIX 1 1 LYS A 15 ASP A 18 5 4
HELIX 2 2 TYR A 19 GLY A 24 1 6
HELIX 3 3 GLY A 24 ALA A 35 1 12
HELIX 4 4 GLY A 53 SER A 68 1 16
HELIX 5 5 PRO A 81 GLN A 96 1 16
HELIX 6 6 THR A 104 ASN A 118 1 15
HELIX 7 7 PRO A 137 PHE A 143 5 7
HELIX 8 8 ASN A 162 GLU A 174 1 13
HELIX 9 9 ASP A 192 ASN A 194 5 3
HELIX 10 10 LYS A 214 PHE A 225 1 12
HELIX 11 11 GLY A 245 ILE A 260 1 16
HELIX 12 12 ASP A 275 GLY A 290 1 16
HELIX 13 13 LEU A 301 GLY A 303 5 3
HELIX 14 14 HIS A 305 ALA A 315 1 11
HELIX 15 15 GLY A 329 LYS A 338 1 10
HELIX 16 16 VAL A 347 ILE A 354 1 8
HELIX 17 17 ASP A 365 HIS A 379 1 15
HELIX 18 18 HIS A 379 PHE A 398 1 20
HELIX 19 19 ILE A 399 ASN A 412 1 14
HELIX 20 20 LYS B 15 ASP B 18 5 4
HELIX 21 21 TYR B 19 GLY B 24 1 6
HELIX 22 22 GLY B 24 ALA B 35 1 12
HELIX 23 23 GLY B 53 SER B 68 1 16
HELIX 24 24 PRO B 81 GLN B 96 1 16
HELIX 25 25 THR B 104 ASN B 118 1 15
HELIX 26 26 PRO B 137 PHE B 143 5 7
HELIX 27 27 ASN B 162 GLU B 174 1 13
HELIX 28 28 ASP B 192 ASN B 194 5 3
HELIX 29 29 LYS B 214 PHE B 225 1 12
HELIX 30 30 GLY B 245 ILE B 260 1 16
HELIX 31 31 ASP B 275 GLY B 290 1 16
HELIX 32 32 LEU B 301 GLY B 303 5 3
HELIX 33 33 HIS B 305 ALA B 315 1 11
HELIX 34 34 GLY B 329 LYS B 338 1 10
HELIX 35 35 VAL B 347 ILE B 354 1 8
HELIX 36 36 ASP B 365 HIS B 379 1 15
HELIX 37 37 HIS B 379 PHE B 398 1 20
HELIX 38 38 ILE B 399 SER B 413 1 15
SHEET 1 AA 7 TYR A 4 GLU A 5 0
SHEET 2 AA 7 GLU A 72 VAL A 77 -1 O VAL A 77 N TYR A 4
SHEET 3 AA 7 SER A 42 ASN A 47 1 O PHE A 43 N ARG A 74
SHEET 4 AA 7 TYR A 129 HIS A 133 1 O TYR A 129 N VAL A 44
SHEET 5 AA 7 TRP A 150 ARG A 153 1 O LEU A 151 N VAL A 132
SHEET 6 AA 7 ARG A 178 PHE A 181 1 O ARG A 178 N TRP A 152
SHEET 7 AA 7 ALA A 196 ILE A 198 1 O VAL A 197 N PHE A 181
SHEET 1 AB 6 VAL A 295 THR A 299 0
SHEET 2 AB 6 GLN A 264 GLY A 269 1 O LEU A 265 N LYS A 296
SHEET 3 AB 6 ILE A 233 VAL A 237 1 O ILE A 234 N LEU A 266
SHEET 4 AB 6 VAL A 318 GLN A 321 1 O VAL A 318 N THR A 235
SHEET 5 AB 6 VAL A 342 ARG A 345 1 O ILE A 343 N GLN A 321
SHEET 6 AB 6 GLY A 360 VAL A 363 1 O PHE A 361 N GLY A 344
SHEET 1 BA 6 GLU B 72 VAL B 77 0
SHEET 2 BA 6 SER B 42 ASN B 47 1 O PHE B 43 N ARG B 74
SHEET 3 BA 6 TYR B 129 HIS B 133 1 O TYR B 129 N VAL B 44
SHEET 4 BA 6 TRP B 150 ARG B 153 1 O LEU B 151 N VAL B 132
SHEET 5 BA 6 ARG B 178 PHE B 181 1 O ARG B 178 N TRP B 152
SHEET 6 BA 6 ALA B 196 ILE B 198 1 O VAL B 197 N PHE B 181
SHEET 1 BB 6 VAL B 295 THR B 299 0
SHEET 2 BB 6 GLN B 264 GLY B 269 1 O LEU B 265 N LYS B 296
SHEET 3 BB 6 ILE B 233 VAL B 237 1 O ILE B 234 N LEU B 266
SHEET 4 BB 6 VAL B 318 GLN B 321 1 O VAL B 318 N THR B 235
SHEET 5 BB 6 VAL B 342 ARG B 345 1 O ILE B 343 N GLN B 321
SHEET 6 BB 6 GLY B 360 VAL B 363 1 O PHE B 361 N GLY B 344
SITE 1 AC1 11 LYS A 209 SER A 238 ARG A 239 LYS A 244
SITE 2 AC1 11 GLY A 269 VAL A 270 GLY A 327 PHE A 328
SITE 3 AC1 11 GLY A 329 LEU A 330 GLU A 334
SITE 1 AC2 14 LYS B 209 SER B 238 ARG B 239 LYS B 244
SITE 2 AC2 14 GLY B 269 VAL B 270 GLY B 327 PHE B 328
SITE 3 AC2 14 GLY B 329 LEU B 330 THR B 331 GLU B 334
SITE 4 AC2 14 HOH B2041 HOH B2072
CRYST1 80.874 63.017 91.107 90.00 98.84 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012365 0.000000 0.001923 0.00000
SCALE2 0.000000 0.015869 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011108 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
