HEADER TRANSFERASE 25-SEP-00 1FWY
TITLE CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE
TITLE 2 URIDYLTRANSFERASE BOUND TO UDP-GLCNAC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: TRUNCATED FORM AFTER R331;
COMPND 5 SYNONYM: N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE;
COMPND 6 EC: 2.7.7.23;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET-22B
KEYWDS ACETYLTRANSFERASE, BIFUNCTIONAL, CRYSTALLOGRAPHY, DRUG
KEYWDS 2 DESIGN, PYROPHOSPHORYLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.BROWN,F.POMPEO,S.DIXON,D.MENGIN-LECREULX,C.CAMBILLAU,
AUTHOR 2 Y.BOURNE
REVDAT 2 24-FEB-09 1FWY 1 VERSN
REVDAT 1 18-OCT-00 1FWY 0
JRNL AUTH K.BROWN,F.POMPEO,S.DIXON,D.MENGIN-LECREULX,
JRNL AUTH 2 C.CAMBILLAU,Y.BOURNE
JRNL TITL CRYSTAL STRUCTURE OF THE BIFUNCTIONAL
JRNL TITL 2 N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE
JRNL TITL 3 FROM ESCHERICHIA COLI: A PARADIGM FOR THE RELATED
JRNL TITL 4 PYROPHOSPHORYLASE SUPERFAMILY.
JRNL REF EMBO J. V. 18 4096 1999
JRNL REFN ISSN 0261-4189
JRNL PMID 10428949
JRNL DOI 10.1093/EMBOJ/18.15.4096
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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) (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 40
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.253
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 : 4975
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 106
REMARK 3 SOLVENT ATOMS : 233
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) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.65
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1FWY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-00.
REMARK 100 THE RCSB ID CODE IS RCSB011971.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.1000
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3-1.5 M AMMONIUM SULFATE, 0.1 M
REMARK 280 MES, 4% ACETONE (V/V), PH 6.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 70.39000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.63969
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 81.54333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 70.39000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 40.63969
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 81.54333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 70.39000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 40.63969
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 81.54333
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 70.39000
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 40.63969
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 81.54333
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 70.39000
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 40.63969
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 81.54333
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 70.39000
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 40.63969
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 81.54333
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 81.27937
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 163.08667
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 81.27937
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 163.08667
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 81.27937
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 163.08667
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 81.27937
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 163.08667
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 81.27937
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 163.08667
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 81.27937
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 163.08667
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TRIMER EITHER FROM CHAIN A
REMARK 300 OR B
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: TRIMERIC
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 BIOMT1 2 -0.500000 -0.866025 0.000000 140.78000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 70.39000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 121.91906
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 140.78000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 70.39000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 121.91906
REMARK 350 BIOMT3 3 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 LEU A 2
REMARK 465 PHE A 329
REMARK 465 ALA A 330
REMARK 465 ARG A 331
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 GLY B 327
REMARK 465 PRO B 328
REMARK 465 PHE B 329
REMARK 465 ALA B 330
REMARK 465 ARG B 331
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 CYS A 307 CA - CB - SG ANGL. DEV. = 8.7 DEGREES
REMARK 500 CYS B 307 CA - CB - SG ANGL. DEV. = 6.9 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 LEU A 80 41.80 -103.68
REMARK 500 PRO A 91 -19.93 -46.22
REMARK 500 GLU A 208 1.87 -67.87
REMARK 500 ASP A 256 103.32 -164.67
REMARK 500 ASN B 4 164.66 -44.06
REMARK 500 ARG B 18 6.87 -69.71
REMARK 500 GLU B 208 1.50 -67.86
REMARK 500 ASP B 256 100.98 -160.43
REMARK 500 ASN B 300 65.64 34.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 312 0.09 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 687 DISTANCE = 5.46 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 951
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 952
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 953
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 954
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UD1 A 501
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UD1 B 502
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 901
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 902
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FXJ RELATED DB: PDB
REMARK 900 1FXJ IS CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-
REMARK 900 PHOSPHATE URIDYLTRANSFERASE
DBREF 1FWY A 1 331 UNP P0ACC7 GLMU_ECOLI 1 331
DBREF 1FWY B 1 331 UNP P0ACC7 GLMU_ECOLI 1 331
SEQRES 1 A 331 MET LEU ASN ASN ALA MET SER VAL VAL ILE LEU ALA ALA
SEQRES 2 A 331 GLY LYS GLY THR ARG MET TYR SER ASP LEU PRO LYS VAL
SEQRES 3 A 331 LEU HIS THR LEU ALA GLY LYS ALA MET VAL GLN HIS VAL
SEQRES 4 A 331 ILE ASP ALA ALA ASN GLU LEU GLY ALA ALA HIS VAL HIS
SEQRES 5 A 331 LEU VAL TYR GLY HIS GLY GLY ASP LEU LEU LYS GLN ALA
SEQRES 6 A 331 LEU LYS ASP ASP ASN LEU ASN TRP VAL LEU GLN ALA GLU
SEQRES 7 A 331 GLN LEU GLY THR GLY HIS ALA MET GLN GLN ALA ALA PRO
SEQRES 8 A 331 PHE PHE ALA ASP ASP GLU ASP ILE LEU MET LEU TYR GLY
SEQRES 9 A 331 ASP VAL PRO LEU ILE SER VAL GLU THR LEU GLN ARG LEU
SEQRES 10 A 331 ARG ASP ALA LYS PRO GLN GLY GLY ILE GLY LEU LEU THR
SEQRES 11 A 331 VAL LYS LEU ASP ASP PRO THR GLY TYR GLY ARG ILE THR
SEQRES 12 A 331 ARG GLU ASN GLY LYS VAL THR GLY ILE VAL GLU HIS LYS
SEQRES 13 A 331 ASP ALA THR ASP GLU GLN ARG GLN ILE GLN GLU ILE ASN
SEQRES 14 A 331 THR GLY ILE LEU ILE ALA ASN GLY ALA ASP MET LYS ARG
SEQRES 15 A 331 TRP LEU ALA LYS LEU THR ASN ASN ASN ALA GLN GLY GLU
SEQRES 16 A 331 TYR TYR ILE THR ASP ILE ILE ALA LEU ALA TYR GLN GLU
SEQRES 17 A 331 GLY ARG GLU ILE VAL ALA VAL HIS PRO GLN ARG LEU SER
SEQRES 18 A 331 GLU VAL GLU GLY VAL ASN ASN ARG LEU GLN LEU SER ARG
SEQRES 19 A 331 LEU GLU ARG VAL TYR GLN SER GLU GLN ALA GLU LYS LEU
SEQRES 20 A 331 LEU LEU ALA GLY VAL MET LEU ARG ASP PRO ALA ARG PHE
SEQRES 21 A 331 ASP LEU ARG GLY THR LEU THR HIS GLY ARG ASP VAL GLU
SEQRES 22 A 331 ILE ASP THR ASN VAL ILE ILE GLU GLY ASN VAL THR LEU
SEQRES 23 A 331 GLY HIS ARG VAL LYS ILE GLY THR GLY CYS VAL ILE LYS
SEQRES 24 A 331 ASN SER VAL ILE GLY ASP ASP CYS GLU ILE SER PRO TYR
SEQRES 25 A 331 THR VAL VAL GLU ASP ALA ASN LEU ALA ALA ALA CYS THR
SEQRES 26 A 331 ILE GLY PRO PHE ALA ARG
SEQRES 1 B 331 MET LEU ASN ASN ALA MET SER VAL VAL ILE LEU ALA ALA
SEQRES 2 B 331 GLY LYS GLY THR ARG MET TYR SER ASP LEU PRO LYS VAL
SEQRES 3 B 331 LEU HIS THR LEU ALA GLY LYS ALA MET VAL GLN HIS VAL
SEQRES 4 B 331 ILE ASP ALA ALA ASN GLU LEU GLY ALA ALA HIS VAL HIS
SEQRES 5 B 331 LEU VAL TYR GLY HIS GLY GLY ASP LEU LEU LYS GLN ALA
SEQRES 6 B 331 LEU LYS ASP ASP ASN LEU ASN TRP VAL LEU GLN ALA GLU
SEQRES 7 B 331 GLN LEU GLY THR GLY HIS ALA MET GLN GLN ALA ALA PRO
SEQRES 8 B 331 PHE PHE ALA ASP ASP GLU ASP ILE LEU MET LEU TYR GLY
SEQRES 9 B 331 ASP VAL PRO LEU ILE SER VAL GLU THR LEU GLN ARG LEU
SEQRES 10 B 331 ARG ASP ALA LYS PRO GLN GLY GLY ILE GLY LEU LEU THR
SEQRES 11 B 331 VAL LYS LEU ASP ASP PRO THR GLY TYR GLY ARG ILE THR
SEQRES 12 B 331 ARG GLU ASN GLY LYS VAL THR GLY ILE VAL GLU HIS LYS
SEQRES 13 B 331 ASP ALA THR ASP GLU GLN ARG GLN ILE GLN GLU ILE ASN
SEQRES 14 B 331 THR GLY ILE LEU ILE ALA ASN GLY ALA ASP MET LYS ARG
SEQRES 15 B 331 TRP LEU ALA LYS LEU THR ASN ASN ASN ALA GLN GLY GLU
SEQRES 16 B 331 TYR TYR ILE THR ASP ILE ILE ALA LEU ALA TYR GLN GLU
SEQRES 17 B 331 GLY ARG GLU ILE VAL ALA VAL HIS PRO GLN ARG LEU SER
SEQRES 18 B 331 GLU VAL GLU GLY VAL ASN ASN ARG LEU GLN LEU SER ARG
SEQRES 19 B 331 LEU GLU ARG VAL TYR GLN SER GLU GLN ALA GLU LYS LEU
SEQRES 20 B 331 LEU LEU ALA GLY VAL MET LEU ARG ASP PRO ALA ARG PHE
SEQRES 21 B 331 ASP LEU ARG GLY THR LEU THR HIS GLY ARG ASP VAL GLU
SEQRES 22 B 331 ILE ASP THR ASN VAL ILE ILE GLU GLY ASN VAL THR LEU
SEQRES 23 B 331 GLY HIS ARG VAL LYS ILE GLY THR GLY CYS VAL ILE LYS
SEQRES 24 B 331 ASN SER VAL ILE GLY ASP ASP CYS GLU ILE SER PRO TYR
SEQRES 25 B 331 THR VAL VAL GLU ASP ALA ASN LEU ALA ALA ALA CYS THR
SEQRES 26 B 331 ILE GLY PRO PHE ALA ARG
HET SO4 A 951 5
HET SO4 A 952 5
HET SO4 B 953 5
HET SO4 B 954 5
HET UD1 A 501 39
HET UD1 B 502 39
HET EDO A 901 4
HET EDO B 902 4
HETNAM SO4 SULFATE ION
HETNAM UD1 URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 UD1 2(C17 H27 N3 O17 P2)
FORMUL 9 EDO 2(C2 H6 O2)
FORMUL 11 HOH *233(H2 O)
HELIX 1 1 GLY A 16 TYR A 20 5 5
HELIX 2 2 PRO A 24 LEU A 27 5 4
HELIX 3 3 MET A 35 LEU A 46 1 12
HELIX 4 4 GLY A 58 LEU A 66 1 9
HELIX 5 5 GLY A 81 ALA A 90 1 10
HELIX 6 6 PRO A 91 PHE A 93 5 3
HELIX 7 7 SER A 110 LYS A 121 1 12
HELIX 8 8 GLU A 154 ALA A 158 5 5
HELIX 9 9 GLU A 161 ILE A 165 5 5
HELIX 10 10 GLY A 177 LYS A 186 1 10
HELIX 11 11 TYR A 197 THR A 199 5 3
HELIX 12 12 ASP A 200 GLU A 208 1 9
HELIX 13 13 ARG A 219 GLU A 224 5 6
HELIX 14 14 ASN A 228 ALA A 250 1 23
HELIX 15 15 GLY B 16 TYR B 20 5 5
HELIX 16 16 PRO B 24 LEU B 27 5 4
HELIX 17 17 MET B 35 GLY B 47 1 13
HELIX 18 18 GLY B 58 LEU B 66 1 9
HELIX 19 19 GLY B 81 ALA B 90 1 10
HELIX 20 20 PRO B 91 PHE B 93 5 3
HELIX 21 21 SER B 110 LYS B 121 1 12
HELIX 22 22 GLU B 154 ALA B 158 5 5
HELIX 23 23 THR B 159 GLN B 164 1 6
HELIX 24 24 GLY B 177 LYS B 186 1 10
HELIX 25 25 THR B 199 GLU B 208 1 10
HELIX 26 26 ARG B 219 GLU B 224 5 6
HELIX 27 27 ASN B 228 ALA B 250 1 23
HELIX 28 28 ASP B 256 ALA B 258 5 3
SHEET 1 A 7 LEU A 71 LEU A 75 0
SHEET 2 A 7 VAL A 51 TYR A 55 1 O VAL A 51 N ASN A 70
SHEET 3 A 7 MET A 6 LEU A 11 1 O VAL A 8 N HIS A 50
SHEET 4 A 7 ASP A 96 TYR A 103 1 O ASP A 96 N SER A 7
SHEET 5 A 7 GLU A 167 ASN A 176 -1 O LEU A 173 N MET A 101
SHEET 6 A 7 ILE A 126 LYS A 132 -1 N GLY A 125 O ILE A 172
SHEET 7 A 7 ILE A 212 VAL A 213 1 O VAL A 213 N LEU A 128
SHEET 1 B 2 ARG A 141 GLU A 145 0
SHEET 2 B 2 LYS A 148 VAL A 153 -1 O LYS A 148 N GLU A 145
SHEET 1 C 5 VAL A 252 ARG A 255 0
SHEET 2 C 5 VAL A 272 ASP A 275 1 O VAL A 272 N MET A 253
SHEET 3 C 5 VAL A 290 GLY A 293 1 O VAL A 290 N GLU A 273
SHEET 4 C 5 CYS A 307 SER A 310 1 O CYS A 307 N LYS A 291
SHEET 5 C 5 CYS A 324 GLY A 327 1 O CYS A 324 N GLU A 308
SHEET 1 D 4 PHE A 260 ARG A 263 0
SHEET 2 D 4 VAL A 278 GLU A 281 1 O VAL A 278 N ASP A 261
SHEET 3 D 4 CYS A 296 LYS A 299 1 O CYS A 296 N ILE A 279
SHEET 4 D 4 THR A 313 GLU A 316 1 O THR A 313 N VAL A 297
SHEET 1 E 4 LEU A 266 GLY A 269 0
SHEET 2 E 4 VAL A 284 GLY A 287 1 N VAL A 284 O THR A 265
SHEET 3 E 4 SER A 301 GLY A 304 1 N SER A 301 O ASN A 283
SHEET 4 E 4 ALA A 318 ALA A 321 1 N ALA A 318 O ASN A 300
SHEET 1 F 7 LEU B 71 LEU B 75 0
SHEET 2 F 7 VAL B 51 TYR B 55 1 O VAL B 51 N ASN B 72
SHEET 3 F 7 MET B 6 LEU B 11 1 O VAL B 8 N HIS B 52
SHEET 4 F 7 ASP B 98 TYR B 103 1 O ASP B 98 N SER B 7
SHEET 5 F 7 GLU B 167 ASN B 176 -1 O LEU B 173 N MET B 101
SHEET 6 F 7 ILE B 126 LYS B 132 -1 N GLY B 127 O ILE B 174
SHEET 7 F 7 ILE B 212 VAL B 215 1 O VAL B 213 N LEU B 128
SHEET 1 G 2 ARG B 141 GLU B 145 0
SHEET 2 G 2 LYS B 148 VAL B 153 -1 O LYS B 148 N GLU B 145
SHEET 1 H 4 VAL B 252 ARG B 255 0
SHEET 2 H 4 VAL B 272 ASP B 275 1 O VAL B 272 N MET B 253
SHEET 3 H 4 VAL B 290 GLY B 293 1 O VAL B 290 N GLU B 273
SHEET 4 H 4 CYS B 307 SER B 310 1 O CYS B 307 N LYS B 291
SHEET 1 I 4 PHE B 260 ARG B 263 0
SHEET 2 I 4 VAL B 278 GLU B 281 1 O VAL B 278 N ASP B 261
SHEET 3 I 4 CYS B 296 LYS B 299 1 O CYS B 296 N ILE B 279
SHEET 4 I 4 THR B 313 GLU B 316 1 O THR B 313 N VAL B 297
SHEET 1 J 4 LEU B 266 GLY B 269 0
SHEET 2 J 4 VAL B 284 GLY B 287 1 N VAL B 284 O THR B 265
SHEET 3 J 4 SER B 301 GLY B 304 1 N SER B 301 O ASN B 283
SHEET 4 J 4 ALA B 318 ALA B 321 1 N ALA B 318 O ASN B 300
SSBOND 1 CYS A 307 CYS A 324 1555 1555 2.10
SSBOND 2 CYS B 307 CYS B 324 1555 1555 2.07
SITE 1 AC1 6 ARG A 144 GLY A 147 LYS A 148 VAL A 149
SITE 2 AC1 6 VAL A 213 ALA A 214
SITE 1 AC2 1 GLN A 231
SITE 1 AC3 4 ARG B 144 GLY B 147 VAL B 213 ALA B 214
SITE 1 AC4 3 ASN B 227 GLN B 231 HOH B 638
SITE 1 AC5 18 LEU A 11 ALA A 13 GLY A 14 GLN A 76
SITE 2 AC5 18 GLN A 79 LEU A 80 GLY A 81 THR A 82
SITE 3 AC5 18 TYR A 103 ASP A 105 TYR A 139 GLY A 140
SITE 4 AC5 18 GLU A 154 ASN A 169 TYR A 197 ILE A 198
SITE 5 AC5 18 THR A 199 HOH A 607
SITE 1 AC6 18 LEU B 11 ALA B 13 GLY B 14 GLN B 76
SITE 2 AC6 18 GLN B 79 LEU B 80 GLY B 81 THR B 82
SITE 3 AC6 18 TYR B 103 ASP B 105 TYR B 139 GLY B 140
SITE 4 AC6 18 GLU B 154 ASN B 169 TYR B 197 THR B 199
SITE 5 AC6 18 HOH B 594 HOH B 603
SITE 1 AC7 4 TYR A 139 VAL A 223 GLU A 224 HOH A 524
SITE 1 AC8 4 TYR B 139 THR B 170 VAL B 223 HOH B 563
CRYST1 140.780 140.780 244.630 90.00 90.00 120.00 H 3 2 36
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 0.007103 0.004101 0.000000 0.00000
SCALE2 0.000000 0.008202 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004088 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
