HEADER NUCLEOTIDYL TRANSFERASE 09-JUN-95 1HXP
TITLE NUCLEOTIDE TRANSFERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEXOSE-1-PHOSPHATE URIDYLYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ALPHA-D-GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE;
COMPND 5 EC: 2.7.7.10;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE-UMP/UDP
COMPND 8 COMPLEX
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 CELL_LINE: BL21;
SOURCE 5 GENE: GALT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) (PLYSS);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTZ18ROT;
SOURCE 11 EXPRESSION_SYSTEM_GENE: GALT;
SOURCE 12 OTHER_DETAILS: PET VECTOR SYSTEM
KEYWDS METALLOENZYME, GALACTOSEMIA, NUCLEOTIDYL TRANSFERASE, COMPLEX (SERINE
KEYWDS 2 PROTEASE-INHIBITOR)
EXPDTA X-RAY DIFFRACTION
AUTHOR J.E.WEDEKIND,P.A.FREY,I.RAYMENT
REVDAT 3 29-NOV-17 1HXP 1 HELIX
REVDAT 2 24-FEB-09 1HXP 1 VERSN
REVDAT 1 08-NOV-96 1HXP 0
JRNL AUTH J.E.WEDEKIND,P.A.FREY,I.RAYMENT
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF GALACTOSE-1-PHOSPHATE
JRNL TITL 2 URIDYLYLTRANSFERASE FROM ESCHERICHIA COLI AT 1.8 A
JRNL TITL 3 RESOLUTION.
JRNL REF BIOCHEMISTRY V. 34 11049 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7669762
JRNL DOI 10.1021/BI00035A010
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.J.RUZICKA,J.E.WEDEKIND,J.KIM,I.RAYMENT,P.A.FREY
REMARK 1 TITL GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE FROM ESCHERICHIA
REMARK 1 TITL 2 COLI, A ZINC AND IRON METALLOENZYME
REMARK 1 REF BIOCHEMISTRY V. 34 5610 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.E.WEDEKIND,P.A.FREY,I.RAYMENT
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF
REMARK 1 TITL 2 GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE FROM ESCHERICHIA
REMARK 1 TITL 3 COLI
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 50 329 1994
REMARK 1 REFN ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 68553
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : NULL
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
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5354
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 469
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : 24.300
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.015 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.254 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.006 ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : 0.006 ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : 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 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 DESPITE THE PRESENCE OF THE NUCLEOTIDE PHOSPHATE(S) THE
REMARK 3 LOOP REGION ADJACENT TO THE ACTIVE SITE FROM GLY 159
REMARK 3 THROUGH ASN 162 EXHIBITS UNUSUALLY HIGH TEMPERATURE
REMARK 3 FACTORS.
REMARK 4
REMARK 4 1HXP 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_1000174068.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 1993
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : XSCALIBRE
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 : 2.000
REMARK 200 R MERGE (I) : 0.05300
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NUMBER OF OBSERVED REFLECTIONS = 169713
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 29.30000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 108.60000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.30000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 108.60000
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 CRYSTALLOGRAPHICALLY INDEPENDENT UNIT IS ONE DIMER OF
REMARK 300 CHEMICALLY IDENTICAL SUBUNITS.
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: 9320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 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 400
REMARK 400 COMPOUND
REMARK 400 THIS ENTRY REPRESENTS THE STRUCTURE OF
REMARK 400 GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE COMPLEXED WITH
REMARK 400 UMP AND UDP. ATTENUATION OR DEFICIENCY OF THIS ENZYME
REMARK 400 RESULTS IN GALACTOSEMIA.
REMARK 400
REMARK 400 THE PRESENT POSITION OF THE NUCLEOTIDE ALPHA PHOSPHORUS
REMARK 400 PRECLUDES THE ABILITY OF THE NUCLEOPHILE HIS 166 TO REACT.
REMARK 400 THIS INACTIVE CONFORMATION HAS BEEN ADOPTED DUE TO THE
REMARK 400 COVALENT MODIFICATION OF CYSTEINE 160 BY 2-MERCAPTOETHANOL.
REMARK 400
REMARK 400 THE TURN CONTAINING CYS 52 AND CYS 55 OF THE ZINC BINDING
REMARK 400 MOTIF RESEMBLES THE RUBREDOXIN KNUCKLE.
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 GLN A 37
REMARK 465 GLU A 38
REMARK 465 THR A 39
REMARK 465 PRO A 40
REMARK 465 ALA A 41
REMARK 465 LYS A 42
REMARK 465 GLN A 43
REMARK 465 MET B 1
REMARK 465 ALA B 29
REMARK 465 LYS B 30
REMARK 465 ARG B 31
REMARK 465 PRO B 32
REMARK 465 TRP B 33
REMARK 465 GLU B 34
REMARK 465 GLY B 35
REMARK 465 ALA B 36
REMARK 465 GLN B 37
REMARK 465 GLU B 38
REMARK 465 THR B 39
REMARK 465 PRO B 40
REMARK 465 ALA B 41
REMARK 465 LYS B 42
REMARK 465 GLN B 43
REMARK 465 VAL B 44
REMARK 465 GLY B 347
REMARK 465 VAL B 348
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 THR A 2 OG1 CG2
REMARK 470 HIS A 27 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 30 CG CD CE NZ
REMARK 470 GLU A 34 CG CD OE1 OE2
REMARK 470 VAL A 44 CG1 CG2
REMARK 470 HIS A 93 CG ND1 CD2 CE1 NE2
REMARK 470 THR B 2 OG1 CG2
REMARK 470 GLN B 3 CG CD OE1 NE2
REMARK 470 HIS B 27 CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 514 O HOH A 569 2.18
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 CYS A 99 CB - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG A 103 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 181 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 VAL A 223 N - CA - C ANGL. DEV. = -21.5 DEGREES
REMARK 500 ARG A 243 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 243 NE - CZ - NH2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG A 336 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 344 NE - CZ - NH1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 344 NE - CZ - NH2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG B 28 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP B 64 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP B 85 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG B 98 NE - CZ - NH2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG B 107 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 GLU B 180 OE1 - CD - OE2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ASP B 183 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG B 184 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 VAL B 223 N - CA - C ANGL. DEV. = -20.8 DEGREES
REMARK 500 ASP B 249 CB - CG - OD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ARG B 252 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 265 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 265 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 MET B 318 CG - SD - CE ANGL. DEV. = -11.5 DEGREES
REMARK 500 GLU B 321 OE1 - CD - OE2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 ARG B 324 NE - CZ - NH1 ANGL. DEV. = 3.0 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 PRO A 6 -6.12 -53.03
REMARK 500 LEU A 304 -51.59 -130.24
REMARK 500 VAL A 314 -169.50 -126.87
REMARK 500 ALA A 320 -70.77 -138.83
REMARK 500 PRO B 6 -16.84 -38.31
REMARK 500 LEU B 304 -54.28 -125.31
REMARK 500 THR B 308 -33.37 -130.96
REMARK 500 ALA B 320 -74.64 -140.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE NUCLEOTIDE BINDS PERPENDICULARLY TO STRANDS B(ETA)-3,
REMARK 600 B(ETA)-6, B(ETA)-7 AND B(ETA)-8 OF THE HALF-BARREL.
REMARK 600
REMARK 600 THE IRON BINDING SITE HAS BEEN IDENTIFIED BY ITS ANOMALOUS
REMARK 600 DISPERSION SIGNAL.
REMARK 600
REMARK 600 THE METAL COMPOSITION OF THIS ENZYME HAS BEEN REPORTED IN
REMARK 600 RUZICKA ET AL., 1995. MOST LIKELY THE IRON SITE CONTAINS
REMARK 600 A MIXTURE OF ZINC AND IRON. THERE IS NO CONFORMATIONAL
REMARK 600 DISORDER. THE OCCUPANCY OF IRON HAS BEEN MODELED AS UNITY
REMARK 600 AT THE FRN SITE.
REMARK 600
REMARK 600 THE OXIDATION STATE OF THE ZINC OF (II) IS MOST LIKELY.
REMARK 600 THE IRON SITE IS LIKELY TO BE PREDOMINANTLY IN THE (III)
REMARK 600 STATE.
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 ZN A 350 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 52 SG
REMARK 620 2 CYS A 55 SG 114.5
REMARK 620 3 HIS A 115 ND1 109.2 105.8
REMARK 620 4 HIS A 164 ND1 118.4 105.4 102.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 351 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 182 OE1
REMARK 620 2 GLU A 182 OE2 61.0
REMARK 620 3 HIS A 281 ND1 89.8 104.7
REMARK 620 4 HIS A 296 NE2 88.3 126.6 118.8
REMARK 620 5 HIS A 298 NE2 164.9 105.0 100.0 96.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 349 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 52 SG
REMARK 620 2 CYS B 55 SG 115.7
REMARK 620 3 HIS B 115 ND1 103.4 106.0
REMARK 620 4 HIS B 164 ND1 115.9 109.7 104.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 350 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 182 OE1
REMARK 620 2 GLU B 182 OE2 61.1
REMARK 620 3 HIS B 281 ND1 90.4 108.2
REMARK 620 4 HIS B 296 NE2 85.6 126.0 113.5
REMARK 620 5 HIS B 298 NE2 167.2 106.4 96.4 101.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: NUC
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NUCLEOTIDE BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: NU2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NUCLEOTIDE BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZNC
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ZINC BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZN2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ZINC BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: FRN
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: IRON BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: FR2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: IRON BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 349
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 352
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 353
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U5P A 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 351
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP B 352
DBREF 1HXP A 1 348 UNP P09148 GAL7_ECOLI 1 348
DBREF 1HXP B 1 348 UNP P09148 GAL7_ECOLI 1 348
SEQADV 1HXP GLU A 34 UNP P09148 GLN 34 CONFLICT
SEQADV 1HXP GLU B 34 UNP P09148 GLN 34 CONFLICT
SEQRES 1 A 348 MET THR GLN PHE ASN PRO VAL ASP HIS PRO HIS ARG ARG
SEQRES 2 A 348 TYR ASN PRO LEU THR GLY GLN TRP ILE LEU VAL SER PRO
SEQRES 3 A 348 HIS ARG ALA LYS ARG PRO TRP GLU GLY ALA GLN GLU THR
SEQRES 4 A 348 PRO ALA LYS GLN VAL LEU PRO ALA HIS ASP PRO ASP CYS
SEQRES 5 A 348 PHE LEU CYS ALA GLY ASN VAL ARG VAL THR GLY ASP LYS
SEQRES 6 A 348 ASN PRO ASP TYR THR GLY THR TYR VAL PHE THR ASN ASP
SEQRES 7 A 348 PHE ALA ALA LEU MET SER ASP THR PRO ASP ALA PRO GLU
SEQRES 8 A 348 SER HIS ASP PRO LEU MET ARG CYS GLN SER ALA ARG GLY
SEQRES 9 A 348 THR SER ARG VAL ILE CYS PHE SER PRO ASP HIS SER LYS
SEQRES 10 A 348 THR LEU PRO GLU LEU SER VAL ALA ALA LEU THR GLU ILE
SEQRES 11 A 348 VAL LYS THR TRP GLN GLU GLN THR ALA GLU LEU GLY LYS
SEQRES 12 A 348 THR TYR PRO TRP VAL GLN VAL PHE GLU ASN LYS GLY ALA
SEQRES 13 A 348 ALA MET GLY CYS SER ASN PRO HIS PRO HIS GLY GLN ILE
SEQRES 14 A 348 TRP ALA ASN SER PHE LEU PRO ASN GLU ALA GLU ARG GLU
SEQRES 15 A 348 ASP ARG LEU GLN LYS GLU TYR PHE ALA GLU GLN LYS SER
SEQRES 16 A 348 PRO MET LEU VAL ASP TYR VAL GLN ARG GLU LEU ALA ASP
SEQRES 17 A 348 GLY SER ARG THR VAL VAL GLU THR GLU HIS TRP LEU ALA
SEQRES 18 A 348 VAL VAL PRO TYR TRP ALA ALA TRP PRO PHE GLU THR LEU
SEQRES 19 A 348 LEU LEU PRO LYS ALA HIS VAL LEU ARG ILE THR ASP LEU
SEQRES 20 A 348 THR ASP ALA GLN ARG SER ASP LEU ALA LEU ALA LEU LYS
SEQRES 21 A 348 LYS LEU THR SER ARG TYR ASP ASN LEU PHE GLN CYS SER
SEQRES 22 A 348 PHE PRO TYR SER MET GLY TRP HIS GLY ALA PRO PHE ASN
SEQRES 23 A 348 GLY GLU GLU ASN GLN HIS TRP GLN LEU HIS ALA HIS PHE
SEQRES 24 A 348 TYR PRO PRO LEU LEU ARG SER ALA THR VAL ARG LYS PHE
SEQRES 25 A 348 MET VAL GLY TYR GLU MET LEU ALA GLU THR GLN ARG ASP
SEQRES 26 A 348 LEU THR ALA GLU GLN ALA ALA GLU ARG LEU ARG ALA VAL
SEQRES 27 A 348 SER ASP ILE HIS PHE ARG GLU SER GLY VAL
SEQRES 1 B 348 MET THR GLN PHE ASN PRO VAL ASP HIS PRO HIS ARG ARG
SEQRES 2 B 348 TYR ASN PRO LEU THR GLY GLN TRP ILE LEU VAL SER PRO
SEQRES 3 B 348 HIS ARG ALA LYS ARG PRO TRP GLU GLY ALA GLN GLU THR
SEQRES 4 B 348 PRO ALA LYS GLN VAL LEU PRO ALA HIS ASP PRO ASP CYS
SEQRES 5 B 348 PHE LEU CYS ALA GLY ASN VAL ARG VAL THR GLY ASP LYS
SEQRES 6 B 348 ASN PRO ASP TYR THR GLY THR TYR VAL PHE THR ASN ASP
SEQRES 7 B 348 PHE ALA ALA LEU MET SER ASP THR PRO ASP ALA PRO GLU
SEQRES 8 B 348 SER HIS ASP PRO LEU MET ARG CYS GLN SER ALA ARG GLY
SEQRES 9 B 348 THR SER ARG VAL ILE CYS PHE SER PRO ASP HIS SER LYS
SEQRES 10 B 348 THR LEU PRO GLU LEU SER VAL ALA ALA LEU THR GLU ILE
SEQRES 11 B 348 VAL LYS THR TRP GLN GLU GLN THR ALA GLU LEU GLY LYS
SEQRES 12 B 348 THR TYR PRO TRP VAL GLN VAL PHE GLU ASN LYS GLY ALA
SEQRES 13 B 348 ALA MET GLY CYS SER ASN PRO HIS PRO HIS GLY GLN ILE
SEQRES 14 B 348 TRP ALA ASN SER PHE LEU PRO ASN GLU ALA GLU ARG GLU
SEQRES 15 B 348 ASP ARG LEU GLN LYS GLU TYR PHE ALA GLU GLN LYS SER
SEQRES 16 B 348 PRO MET LEU VAL ASP TYR VAL GLN ARG GLU LEU ALA ASP
SEQRES 17 B 348 GLY SER ARG THR VAL VAL GLU THR GLU HIS TRP LEU ALA
SEQRES 18 B 348 VAL VAL PRO TYR TRP ALA ALA TRP PRO PHE GLU THR LEU
SEQRES 19 B 348 LEU LEU PRO LYS ALA HIS VAL LEU ARG ILE THR ASP LEU
SEQRES 20 B 348 THR ASP ALA GLN ARG SER ASP LEU ALA LEU ALA LEU LYS
SEQRES 21 B 348 LYS LEU THR SER ARG TYR ASP ASN LEU PHE GLN CYS SER
SEQRES 22 B 348 PHE PRO TYR SER MET GLY TRP HIS GLY ALA PRO PHE ASN
SEQRES 23 B 348 GLY GLU GLU ASN GLN HIS TRP GLN LEU HIS ALA HIS PHE
SEQRES 24 B 348 TYR PRO PRO LEU LEU ARG SER ALA THR VAL ARG LYS PHE
SEQRES 25 B 348 MET VAL GLY TYR GLU MET LEU ALA GLU THR GLN ARG ASP
SEQRES 26 B 348 LEU THR ALA GLU GLN ALA ALA GLU ARG LEU ARG ALA VAL
SEQRES 27 B 348 SER ASP ILE HIS PHE ARG GLU SER GLY VAL
HET ZN A 350 1
HET FE A 351 1
HET BME A 352 4
HET BME A 353 4
HET BME A 354 4
HET U5P A 355 21
HET ZN B 349 1
HET FE B 350 1
HET BME B 351 4
HET UDP B 352 25
HETNAM ZN ZINC ION
HETNAM FE FE (III) ION
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM U5P URIDINE-5'-MONOPHOSPHATE
HETNAM UDP URIDINE-5'-DIPHOSPHATE
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 FE 2(FE 3+)
FORMUL 5 BME 4(C2 H6 O S)
FORMUL 8 U5P C9 H13 N2 O9 P
FORMUL 12 UDP C9 H14 N2 O12 P2
FORMUL 13 HOH *469(H2 O)
HELIX 1 1 VAL A 124 LEU A 141 1 18
HELIX 2 2 ASN A 177 GLN A 193 1 17
HELIX 3 3 MET A 197 ASP A 208 1 12
HELIX 4 4 ASP A 249 ASP A 267 1 19
HELIX 5 5 GLY A 315 LEU A 319 1 5
HELIX 6 6 ALA A 328 ALA A 337 1 10
HELIX 7 7 VAL B 124 LEU B 141 1 18
HELIX 8 8 ASN B 177 GLN B 193 1 17
HELIX 9 9 MET B 197 ASP B 208 1 12
HELIX 10 10 ASP B 249 ASP B 267 1 19
HELIX 11 11 GLY B 315 LEU B 319 1 5
HELIX 12 12 ALA B 328 ALA B 337 1 10
SHEET 1 A 3 GLN A 20 VAL A 24 0
SHEET 2 A 3 HIS A 11 ASN A 15 -1 N ASN A 15 O GLN A 20
SHEET 3 A 3 CYS B 99 SER B 101 -1 N GLN B 100 O ARG A 12
SHEET 1 B 9 TYR A 73 THR A 76 0
SHEET 2 B 9 GLY A 104 CYS A 110 -1 N CYS A 110 O TYR A 73
SHEET 3 B 9 HIS A 166 ASN A 172 -1 N ALA A 171 O THR A 105
SHEET 4 B 9 TRP A 147 LYS A 154 -1 N PHE A 151 O GLN A 168
SHEET 5 B 9 TYR A 276 HIS A 281 -1 N MET A 278 O GLU A 152
SHEET 6 B 9 HIS A 296 TYR A 300 -1 N TYR A 300 O SER A 277
SHEET 7 B 9 THR A 233 PRO A 237 -1 N LEU A 235 O ALA A 297
SHEET 8 B 9 TRP A 219 VAL A 222 -1 N VAL A 222 O LEU A 234
SHEET 9 B 9 THR A 212 GLU A 215 -1 N VAL A 214 O ALA A 221
SHEET 1 C 3 CYS A 99 SER A 101 0
SHEET 2 C 3 HIS B 11 ASN B 15 -1 N ARG B 12 O GLN A 100
SHEET 3 C 3 GLN B 20 VAL B 24 -1 N VAL B 24 O HIS B 11
SHEET 1 D 9 TYR B 73 THR B 76 0
SHEET 2 D 9 GLY B 104 CYS B 110 -1 N CYS B 110 O TYR B 73
SHEET 3 D 9 HIS B 166 ASN B 172 -1 N ALA B 171 O THR B 105
SHEET 4 D 9 TRP B 147 LYS B 154 -1 N PHE B 151 O GLN B 168
SHEET 5 D 9 TYR B 276 HIS B 281 -1 N MET B 278 O GLU B 152
SHEET 6 D 9 HIS B 296 TYR B 300 -1 N TYR B 300 O SER B 277
SHEET 7 D 9 THR B 233 PRO B 237 -1 N LEU B 235 O ALA B 297
SHEET 8 D 9 TRP B 219 VAL B 222 -1 N VAL B 222 O LEU B 234
SHEET 9 D 9 THR B 212 GLU B 215 -1 N VAL B 214 O ALA B 221
LINK S2 BME A 352 SG CYS A 99 1555 1555 2.03
LINK S2 BME A 353 SG CYS A 160 1555 1555 2.04
LINK S2 BME A 354 SG CYS A 272 1555 1555 2.01
LINK ZN ZN A 350 SG CYS A 52 1555 1555 2.22
LINK ZN ZN A 350 SG CYS A 55 1555 1555 2.37
LINK ZN ZN A 350 ND1 HIS A 115 1555 1555 2.04
LINK ZN ZN A 350 ND1 HIS A 164 1555 1555 1.96
LINK FE FE A 351 OE1 GLU A 182 1555 1555 2.30
LINK FE FE A 351 OE2 GLU A 182 1555 1555 1.85
LINK FE FE A 351 ND1 HIS A 281 1555 1555 2.02
LINK FE FE A 351 NE2 HIS A 296 1555 1555 2.03
LINK FE FE A 351 NE2 HIS A 298 1555 1555 1.99
LINK S2 BME B 351 SG CYS B 160 1555 1555 2.03
LINK ZN ZN B 349 SG CYS B 52 1555 1555 2.30
LINK ZN ZN B 349 SG CYS B 55 1555 1555 2.30
LINK ZN ZN B 349 ND1 HIS B 115 1555 1555 2.08
LINK ZN ZN B 349 ND1 HIS B 164 1555 1555 2.00
LINK FE FE B 350 OE1 GLU B 182 1555 1555 2.26
LINK FE FE B 350 OE2 GLU B 182 1555 1555 1.95
LINK FE FE B 350 ND1 HIS B 281 1555 1555 2.01
LINK FE FE B 350 NE2 HIS B 296 1555 1555 2.11
LINK FE FE B 350 NE2 HIS B 298 1555 1555 2.01
SITE 1 NUC 9 LEU A 54 VAL A 61 PHE A 75 ASN A 77
SITE 2 NUC 9 ASP A 78 PHE A 79 VAL A 108 SER A 161
SITE 3 NUC 9 ASN A 162
SITE 1 NU2 9 LEU B 54 VAL B 61 PHE B 75 ASN B 77
SITE 2 NU2 9 ASP B 78 PHE B 79 VAL B 108 SER B 161
SITE 3 NU2 9 ASN B 162
SITE 1 ZNC 4 CYS A 52 CYS A 55 HIS A 115 HIS A 164
SITE 1 ZN2 4 CYS B 52 CYS B 55 HIS B 115 HIS B 164
SITE 1 FRN 4 GLU A 182 HIS A 281 HIS A 296 HIS A 298
SITE 1 FR2 4 GLU B 182 HIS B 281 HIS B 296 HIS B 298
SITE 1 AC1 4 CYS A 52 CYS A 55 HIS A 115 HIS A 164
SITE 1 AC2 4 GLU A 182 HIS A 281 HIS A 296 HIS A 298
SITE 1 AC3 4 CYS B 52 CYS B 55 HIS B 115 HIS B 164
SITE 1 AC4 4 GLU B 182 HIS B 281 HIS B 296 HIS B 298
SITE 1 AC5 6 CYS A 99 HOH A 567 PHE B 4 PRO B 6
SITE 2 AC5 6 HIS B 11 TYR B 225
SITE 1 AC6 3 ASN A 153 CYS A 160 GLN A 168
SITE 1 AC7 5 CYS A 272 SER A 273 PRO A 275 LEU A 303
SITE 2 AC7 5 ALA A 307
SITE 1 AC8 8 PHE A 53 ARG A 60 VAL A 61 PHE A 75
SITE 2 AC8 8 ASN A 77 ASP A 78 PHE A 79 HOH A 586
SITE 1 AC9 4 ASN B 153 CYS B 160 HIS B 166 GLN B 168
SITE 1 BC1 10 ARG A 31 ARG B 60 VAL B 61 PHE B 75
SITE 2 BC1 10 ASN B 77 ASP B 78 PHE B 79 SER B 161
SITE 3 BC1 10 ASN B 162 HOH B 355
CRYST1 58.600 217.200 69.600 90.00 90.00 90.00 P 21 21 2 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 0.017065 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004604 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014368 0.00000
MTRIX1 1 0.944110 -0.010720 0.329450 -10.37684 1
MTRIX2 1 -0.011350 -0.999940 0.000000 159.46695 1
MTRIX3 1 0.329430 -0.003740 -0.944170 66.34219 1
(ATOM LINES ARE NOT SHOWN.)
END
