HEADER TRANSFERASE 22-NOV-00 1G95
TITLE CRYSTAL STRUCTURE OF S.PNEUMONIAE GLMU, APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GLMU, UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE;
COMPND 5 EC: 2.7.7.23;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 1313;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLMU, ACETYLTRANSFERASE, URIDYLTRANSFERASE PYROPHOSPHORYLASE, LEFT-
KEYWDS 2 HANDED BETA-SHEET HELIX, TRIMER, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KOSTREWA,A.D'ARCY,M.KAMBER
REVDAT 5 07-FEB-24 1G95 1 REMARK
REVDAT 4 13-JUL-11 1G95 1 VERSN
REVDAT 3 24-FEB-09 1G95 1 VERSN
REVDAT 2 01-APR-03 1G95 1 JRNL
REVDAT 1 22-MAY-01 1G95 0
JRNL AUTH D.KOSTREWA,A.D'ARCY,B.TAKACS,M.KAMBER
JRNL TITL CRYSTAL STRUCTURES OF STREPTOCOCCUS PNEUMONIAE
JRNL TITL 2 N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE, GLMU, IN
JRNL TITL 3 APO FORM AT 2.33 A RESOLUTION AND IN COMPLEX WITH
JRNL TITL 4 UDP-N-ACETYLGLUCOSAMINE AND MG(2+) AT 1.96 A RESOLUTION.
JRNL REF J.MOL.BIOL. V. 305 279 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11124906
JRNL DOI 10.1006/JMBI.2000.4296
REMARK 2
REMARK 2 RESOLUTION. 2.33 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) : 2.33
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) (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 20576
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE-R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.303
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1039
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.33
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1889
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE : 0.3500
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 118
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 : 3358
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 276
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.36400
REMARK 3 B22 (A**2) : -8.36400
REMARK 3 B33 (A**2) : 16.72800
REMARK 3 B12 (A**2) : -1.04800
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.20
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) : 0.45
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.31
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.100
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.500 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.800 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.800 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.300 ; 6.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : BULK SOLVENT MASK
REMARK 3 KSOL : 0.26
REMARK 3 BSOL : 23.50
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.PARAM
REMARK 3 PARAMETER FILE 2 : ROCHE.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ROCHE.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 BULK SOLVENT CORRECTION WITH ELECTRON DENSITY = 0.26 E/A**3, B-
REMARK 3 FACTOR = 23.5 A**2.
REMARK 3 THE FOLLOWING AMINO ACID RESIDUES WERE NOT VISIBLE IN THE
REMARK 3 ELECTRON DENSITY MAPS: 188-193, 453-459.
REMARK 3 THE ELECTRON DENSITY MAPS OF THE FOLLOWING AMINO ACID
REMARK 3 RESIDUES WERE OF RELATIVELY POOR QUALITY: 2, 10-12, 51-94,
REMARK 3 145-149, 154-164, 179-187, 194-197, 439-441, 447-452.
REMARK 3 THE WATER MOLECULES ARE
REMARK 3 ORDERED WITH ASCENDING B-FACTORS.
REMARK 4
REMARK 4 1G95 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-00.
REMARK 100 THE DEPOSITION ID IS D_1000012388.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-APR-98
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.873
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20586
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.330
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.18800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS/TRIS, 0.2 M AMMONIUM
REMARK 280 SULFATE, 25 % PEG 3350, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 47.45500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 27.39816
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 93.31333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 47.45500
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 27.39816
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 93.31333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 47.45500
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 27.39816
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 93.31333
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 47.45500
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 27.39816
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 93.31333
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 47.45500
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 27.39816
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 93.31333
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 47.45500
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 27.39816
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 93.31333
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 54.79631
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 186.62667
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 54.79631
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 186.62667
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 54.79631
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 186.62667
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 54.79631
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 186.62667
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 54.79631
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 186.62667
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 54.79631
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 186.62667
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 BIOLOGICAL ASSEMBLY IS A TRIMER GENERATED
REMARK 300 FROM THE MONOMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS:
REMARK 300 -Y+1, X-Y, Z
REMARK 300 AND
REMARK 300 -X+Y+1, -X+1, Z
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 11130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL
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 94.91000
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 47.45500
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 82.19447
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 ASN A 188
REMARK 465 THR A 189
REMARK 465 ASN A 190
REMARK 465 ASN A 191
REMARK 465 ALA A 192
REMARK 465 GLN A 193
REMARK 465 PRO A 453
REMARK 465 HIS A 454
REMARK 465 HIS A 455
REMARK 465 PRO A 456
REMARK 465 LYS A 457
REMARK 465 ASN A 458
REMARK 465 GLN A 459
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 PRO A 104 C - N - CA ANGL. DEV. = 9.6 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 ALA A 9 64.34 -153.84
REMARK 500 GLN A 44 70.69 34.43
REMARK 500 SER A 73 -76.16 -50.58
REMARK 500 ALA A 125 115.65 -161.61
REMARK 500 ARG A 143 -161.18 -120.68
REMARK 500 GLN A 155 49.75 -80.09
REMARK 500 LYS A 156 -22.90 -140.48
REMARK 500 GLU A 289 -0.77 67.41
REMARK 500 ASN A 311 58.05 37.50
REMARK 500 GLU A 316 64.54 28.52
REMARK 500 ALA A 320 -173.82 -66.32
REMARK 500 GLN A 340 18.60 59.58
REMARK 500 LEU A 363 62.70 24.19
REMARK 500 LYS A 389 -59.56 -167.12
REMARK 500 ASN A 417 18.44 59.96
REMARK 500 ARG A 439 -160.32 -124.03
REMARK 500 GLU A 447 18.53 47.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G97 RELATED DB: PDB
REMARK 900 1G97 CONTAINS THE SAME PROTEIN WITH THE BOUND PRODUCT UDP-N-
REMARK 900 ACETYLGLUCOSAMINE AND MG2+
DBREF 1G95 A 1 459 UNP Q97R46 Q97R46_STRPN 1 459
SEQRES 1 A 459 MET SER ASN PHE ALA ILE ILE LEU ALA ALA GLY LYS GLY
SEQRES 2 A 459 THR ARG MET LYS SER ASP LEU PRO LYS VAL LEU HIS LYS
SEQRES 3 A 459 VAL ALA GLY ILE SER MET LEU GLU HIS VAL PHE ARG SER
SEQRES 4 A 459 VAL GLY ALA ILE GLN PRO GLU LYS THR VAL THR VAL VAL
SEQRES 5 A 459 GLY HIS LYS ALA GLU LEU VAL GLU GLU VAL LEU ALA GLY
SEQRES 6 A 459 GLN THR GLU PHE VAL THR GLN SER GLU GLN LEU GLY THR
SEQRES 7 A 459 GLY HIS ALA VAL MET MET THR GLU PRO ILE LEU GLU GLY
SEQRES 8 A 459 LEU SER GLY HIS THR LEU VAL ILE ALA GLY ASP THR PRO
SEQRES 9 A 459 LEU ILE THR GLY GLU SER LEU LYS ASN LEU ILE ASP PHE
SEQRES 10 A 459 HIS ILE ASN HIS LYS ASN VAL ALA THR ILE LEU THR ALA
SEQRES 11 A 459 GLU THR ASP ASN PRO PHE GLY TYR GLY ARG ILE VAL ARG
SEQRES 12 A 459 ASN ASP ASN ALA GLU VAL LEU ARG ILE VAL GLU GLN LYS
SEQRES 13 A 459 ASP ALA THR ASP PHE GLU LYS GLN ILE LYS GLU ILE ASN
SEQRES 14 A 459 THR GLY THR TYR VAL PHE ASP ASN GLU ARG LEU PHE GLU
SEQRES 15 A 459 ALA LEU LYS ASN ILE ASN THR ASN ASN ALA GLN GLY GLU
SEQRES 16 A 459 TYR TYR ILE THR ASP VAL ILE GLY ILE PHE ARG GLU THR
SEQRES 17 A 459 GLY GLU LYS VAL GLY ALA TYR THR LEU LYS ASP PHE ASP
SEQRES 18 A 459 GLU SER LEU GLY VAL ASN ASP ARG VAL ALA LEU ALA THR
SEQRES 19 A 459 ALA GLU SER VAL MET ARG ARG ARG ILE ASN HIS LYS HIS
SEQRES 20 A 459 MET VAL ASN GLY VAL SER PHE VAL ASN PRO GLU ALA THR
SEQRES 21 A 459 TYR ILE ASP ILE ASP VAL GLU ILE ALA SER GLU VAL GLN
SEQRES 22 A 459 ILE GLU ALA ASN VAL THR LEU LYS GLY GLN THR LYS ILE
SEQRES 23 A 459 GLY ALA GLU THR VAL LEU THR ASN GLY THR TYR VAL VAL
SEQRES 24 A 459 ASP SER THR ILE GLY ALA GLY ALA VAL ILE THR ASN SER
SEQRES 25 A 459 MET ILE GLU GLU SER SER VAL ALA ASP GLY VAL ILE VAL
SEQRES 26 A 459 GLY PRO TYR ALA HIS ILE ARG PRO ASN SER SER LEU GLY
SEQRES 27 A 459 ALA GLN VAL HIS ILE GLY ASN PHE VAL GLU VAL LYS GLY
SEQRES 28 A 459 SER SER ILE GLY GLU ASN THR LYS ALA GLY HIS LEU THR
SEQRES 29 A 459 TYR ILE GLY ASN CYS GLU VAL GLY SER ASN VAL ASN PHE
SEQRES 30 A 459 GLY ALA GLY THR ILE THR VAL ASN TYR ASP GLY LYS ASN
SEQRES 31 A 459 LYS TYR LYS THR VAL ILE GLY ASN ASN VAL PHE VAL GLY
SEQRES 32 A 459 SER ASN SER THR ILE ILE ALA PRO VAL GLU LEU GLY ASP
SEQRES 33 A 459 ASN SER LEU VAL GLY ALA GLY SER THR ILE THR LYS ASP
SEQRES 34 A 459 VAL PRO ALA ASP ALA ILE ALA ILE GLY ARG GLY ARG GLN
SEQRES 35 A 459 ILE ASN LYS ASP GLU TYR ALA THR ARG LEU PRO HIS HIS
SEQRES 36 A 459 PRO LYS ASN GLN
FORMUL 2 HOH *276(H2 O)
HELIX 1 1 GLY A 13 LYS A 17 5 5
HELIX 2 2 PRO A 21 LEU A 24 5 4
HELIX 3 3 MET A 32 GLY A 41 1 10
HELIX 4 4 ALA A 42 GLN A 44 5 3
HELIX 5 5 LYS A 55 LEU A 63 1 9
HELIX 6 6 LEU A 76 MET A 84 1 9
HELIX 7 7 THR A 85 GLU A 90 1 6
HELIX 8 8 THR A 107 HIS A 121 1 15
HELIX 9 9 PHE A 161 ILE A 165 5 5
HELIX 10 10 ASN A 177 LEU A 184 1 8
HELIX 11 11 THR A 199 THR A 208 1 10
HELIX 12 12 ASP A 219 LEU A 224 5 6
HELIX 13 13 ASP A 228 ASN A 250 1 23
HELIX 14 14 ASN A 256 THR A 260 5 5
HELIX 15 15 TYR A 448 LEU A 452 5 5
SHEET 1 A 7 GLU A 68 THR A 71 0
SHEET 2 A 7 LYS A 47 VAL A 52 1 O THR A 48 N GLU A 68
SHEET 3 A 7 ASN A 3 ALA A 9 1 O ASN A 3 N LYS A 47
SHEET 4 A 7 HIS A 95 ALA A 100 1 O HIS A 95 N PHE A 4
SHEET 5 A 7 GLU A 167 ASP A 176 -1 O TYR A 173 N VAL A 98
SHEET 6 A 7 ALA A 125 GLU A 131 -1 N THR A 126 O VAL A 174
SHEET 7 A 7 VAL A 212 LEU A 217 1 O GLY A 213 N ILE A 127
SHEET 1 B 2 LYS A 26 VAL A 27 0
SHEET 2 B 2 ILE A 30 SER A 31 -1 O ILE A 30 N VAL A 27
SHEET 1 C 2 ARG A 140 VAL A 142 0
SHEET 2 C 2 ARG A 151 VAL A 153 -1 O ARG A 151 N VAL A 142
SHEET 1 D11 ILE A 435 ALA A 436 0
SHEET 2 D11 LEU A 419 VAL A 420 1 O LEU A 419 N ALA A 436
SHEET 3 D11 PHE A 401 VAL A 402 1 O PHE A 401 N VAL A 420
SHEET 4 D11 ASN A 376 PHE A 377 1 O ASN A 376 N VAL A 402
SHEET 5 D11 LYS A 359 GLY A 367 1 O LYS A 359 N PHE A 377
SHEET 6 D11 HIS A 342 LYS A 350 1 O HIS A 342 N ALA A 360
SHEET 7 D11 ILE A 324 VAL A 325 1 O ILE A 324 N ILE A 343
SHEET 8 D11 VAL A 308 ILE A 309 1 O VAL A 308 N VAL A 325
SHEET 9 D11 VAL A 291 LEU A 292 1 O VAL A 291 N ILE A 309
SHEET 10 D11 GLN A 273 ILE A 274 1 O GLN A 273 N LEU A 292
SHEET 11 D11 SER A 253 PHE A 254 1 O SER A 253 N ILE A 274
SHEET 1 E11 ILE A 435 ALA A 436 0
SHEET 2 E11 LEU A 419 VAL A 420 1 O LEU A 419 N ALA A 436
SHEET 3 E11 PHE A 401 VAL A 402 1 O PHE A 401 N VAL A 420
SHEET 4 E11 ASN A 376 PHE A 377 1 O ASN A 376 N VAL A 402
SHEET 5 E11 LYS A 359 GLY A 367 1 O LYS A 359 N PHE A 377
SHEET 6 E11 HIS A 342 LYS A 350 1 O HIS A 342 N ALA A 360
SHEET 7 E11 HIS A 330 ILE A 331 1 N HIS A 330 O VAL A 347
SHEET 8 E11 MET A 313 GLU A 315 1 O MET A 313 N ILE A 331
SHEET 9 E11 TYR A 297 VAL A 299 1 O TYR A 297 N ILE A 314
SHEET 10 E11 THR A 279 LYS A 281 1 O THR A 279 N VAL A 298
SHEET 11 E11 TYR A 261 ILE A 262 1 O TYR A 261 N LEU A 280
SHEET 1 F 9 GLU A 267 ILE A 268 0
SHEET 2 F 9 LYS A 285 ILE A 286 1 N ILE A 286 O GLU A 267
SHEET 3 F 9 THR A 302 ILE A 303 1 N ILE A 303 O LYS A 285
SHEET 4 F 9 SER A 317 VAL A 319 1 O SER A 317 N THR A 302
SHEET 5 F 9 SER A 335 LEU A 337 1 O SER A 335 N SER A 318
SHEET 6 F 9 SER A 353 ILE A 354 1 N ILE A 354 O SER A 336
SHEET 7 F 9 CYS A 369 VAL A 371 1 O CYS A 369 N SER A 353
SHEET 8 F 9 THR A 394 ILE A 396 1 O THR A 394 N GLU A 370
SHEET 9 F 9 VAL A 412 LEU A 414 1 O VAL A 412 N VAL A 395
SHEET 1 G 3 ILE A 382 VAL A 384 0
SHEET 2 G 3 THR A 407 ILE A 409 1 O ILE A 408 N VAL A 384
SHEET 3 G 3 THR A 425 ILE A 426 1 O ILE A 426 N ILE A 409
CISPEP 1 GLY A 326 PRO A 327 0 0.03
CISPEP 2 ALA A 410 PRO A 411 0 -0.18
CRYST1 94.910 94.910 279.940 90.00 90.00 120.00 H 3 2 18
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 0.010536 0.006083 0.000000 0.00000
SCALE2 0.000000 0.012166 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003572 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
