Header list of 1e0g.pdb file
Complete list - p 25 2 Bytes
HEADER HYDROLASE 27-MAR-00 1E0G
TITLE LYSM DOMAIN FROM E.COLI MLTD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE D;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LYSM DOMAIN;
COMPND 5 EC: 4.2.2.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 4 ORGANISM_TAXID: 562
KEYWDS CELL WALL, HYDROLASE, GLYCOSIDASE, LIPOPROTEIN, OUTER MEMBRANE,
KEYWDS 2 MULTIGENE FAMILY
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.BATEMAN,M.BYCROFT
REVDAT 5 25-SEP-19 1E0G 1 COMPND SOURCE REMARK DBREF
REVDAT 4 24-FEB-09 1E0G 1 VERSN
REVDAT 3 05-NOV-03 1E0G 1 SPRSDE REMARK
REVDAT 2 06-JUN-02 1E0G 1 JRNL
REVDAT 1 21-JUN-00 1E0G 0
SPRSDE 05-NOV-03 1E0G 1E01
JRNL AUTH A.BATEMAN,M.BYCROFT
JRNL TITL THE STRUCTURE OF A LYSM DOMAIN FROM E.COLI MEMBRANE BOUND
JRNL TITL 2 LYTIC MUREIN TRANSGLYCOSYLASE D (MLTD)
JRNL REF J.MOL.BIOL. V. 299 1113 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10843862
JRNL DOI 10.1006/JMBI.2000.3778
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.K.BIRKELAND
REMARK 1 TITL CLONING, MOLECULAR CHARACTERIZATION, AND EXPRESSION OF THE
REMARK 1 TITL 2 GENES ENCODING THE LYTIC FUNCTIONS OF LACTOCOCCAL
REMARK 1 TITL 3 BACTERIOPHAGE-PHI-LC3; A DUAL LYSIS SYSTEM OF MODULAR DESIGN
REMARK 1 REF CAN.J.MICROBIOL. V. 40 658 1994
REMARK 1 REFN ISSN 0008-4166
REMARK 1 PMID 7922887
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SA FROM RANDOM COIL STARTING STRUCTURES
REMARK 4
REMARK 4 1E0G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1290004771.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED MTLD LYSM DOMAIN
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 1 PRO A 39 86.75 -69.01
REMARK 500 1 LEU A 45 55.32 -117.02
REMARK 500 1 VAL A 47 143.39 -39.57
REMARK 500 2 PRO A 39 84.53 -68.84
REMARK 500 2 LEU A 45 55.09 -115.05
REMARK 500 2 VAL A 47 141.57 -39.43
REMARK 500 3 SER A 32 -82.69 -89.68
REMARK 500 3 THR A 34 42.36 -88.20
REMARK 500 3 PRO A 39 86.30 -68.45
REMARK 500 3 LEU A 45 55.13 -110.62
REMARK 500 3 VAL A 47 144.65 -39.64
REMARK 500 4 THR A 34 32.61 -86.97
REMARK 500 4 PRO A 39 85.99 -68.69
REMARK 500 4 LEU A 45 55.53 -109.02
REMARK 500 4 VAL A 47 142.87 -37.94
REMARK 500 5 PRO A 39 85.04 -69.08
REMARK 500 5 VAL A 47 139.04 -39.59
REMARK 500 6 SER A 32 -81.92 -87.04
REMARK 500 6 THR A 34 43.78 -89.82
REMARK 500 6 PRO A 39 86.19 -69.44
REMARK 500 6 VAL A 47 140.06 -39.40
REMARK 500 7 SER A 32 -82.83 -93.13
REMARK 500 7 THR A 34 48.39 -84.37
REMARK 500 7 PRO A 39 86.83 -68.91
REMARK 500 7 LEU A 45 55.20 -110.78
REMARK 500 7 VAL A 47 142.88 -38.94
REMARK 500 8 THR A 34 32.48 -89.13
REMARK 500 8 PRO A 39 84.73 -69.10
REMARK 500 8 VAL A 47 138.15 -37.21
REMARK 500 9 THR A 34 41.08 -86.99
REMARK 500 9 PRO A 39 84.29 -69.32
REMARK 500 9 VAL A 47 143.12 -38.24
REMARK 500 10 SER A 32 -82.12 -92.31
REMARK 500 10 THR A 34 41.64 -87.12
REMARK 500 10 PRO A 39 86.39 -69.87
REMARK 500 10 LEU A 45 54.52 -117.73
REMARK 500 10 VAL A 47 137.30 -38.39
REMARK 500 11 SER A 32 -81.32 -91.00
REMARK 500 11 THR A 34 41.08 -86.22
REMARK 500 11 PRO A 39 85.59 -68.98
REMARK 500 11 LEU A 45 54.00 -115.02
REMARK 500 11 VAL A 47 137.46 -38.53
REMARK 500 12 PRO A 39 85.82 -69.29
REMARK 500 13 SER A 32 -78.72 -92.45
REMARK 500 13 THR A 34 47.06 -84.84
REMARK 500 13 PRO A 39 85.90 -69.86
REMARK 500 13 LEU A 45 54.53 -118.38
REMARK 500 13 VAL A 47 137.49 -39.00
REMARK 500 14 SER A 32 -82.53 -94.42
REMARK 500 14 THR A 34 47.57 -84.29
REMARK 500
REMARK 500 THIS ENTRY HAS 76 RAMACHANDRAN OUTLIERS.
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 1 ARG A 6 0.29 SIDE CHAIN
REMARK 500 1 ARG A 8 0.30 SIDE CHAIN
REMARK 500 1 ARG A 19 0.31 SIDE CHAIN
REMARK 500 1 ARG A 29 0.30 SIDE CHAIN
REMARK 500 2 ARG A 6 0.29 SIDE CHAIN
REMARK 500 2 ARG A 8 0.29 SIDE CHAIN
REMARK 500 2 ARG A 19 0.13 SIDE CHAIN
REMARK 500 2 ARG A 29 0.26 SIDE CHAIN
REMARK 500 3 ARG A 6 0.31 SIDE CHAIN
REMARK 500 3 ARG A 8 0.32 SIDE CHAIN
REMARK 500 3 ARG A 19 0.14 SIDE CHAIN
REMARK 500 3 ARG A 29 0.26 SIDE CHAIN
REMARK 500 4 ARG A 6 0.32 SIDE CHAIN
REMARK 500 4 ARG A 8 0.23 SIDE CHAIN
REMARK 500 4 ARG A 19 0.26 SIDE CHAIN
REMARK 500 4 ARG A 29 0.31 SIDE CHAIN
REMARK 500 5 ARG A 6 0.32 SIDE CHAIN
REMARK 500 5 ARG A 8 0.27 SIDE CHAIN
REMARK 500 5 ARG A 19 0.24 SIDE CHAIN
REMARK 500 5 ARG A 29 0.28 SIDE CHAIN
REMARK 500 6 ARG A 6 0.32 SIDE CHAIN
REMARK 500 6 ARG A 8 0.32 SIDE CHAIN
REMARK 500 6 ARG A 19 0.25 SIDE CHAIN
REMARK 500 6 ARG A 29 0.31 SIDE CHAIN
REMARK 500 7 ARG A 6 0.26 SIDE CHAIN
REMARK 500 7 ARG A 8 0.22 SIDE CHAIN
REMARK 500 7 ARG A 19 0.21 SIDE CHAIN
REMARK 500 7 ARG A 29 0.23 SIDE CHAIN
REMARK 500 8 ARG A 6 0.25 SIDE CHAIN
REMARK 500 8 ARG A 8 0.31 SIDE CHAIN
REMARK 500 8 ARG A 19 0.28 SIDE CHAIN
REMARK 500 8 ARG A 29 0.24 SIDE CHAIN
REMARK 500 9 ARG A 6 0.30 SIDE CHAIN
REMARK 500 9 ARG A 8 0.28 SIDE CHAIN
REMARK 500 9 ARG A 19 0.25 SIDE CHAIN
REMARK 500 9 ARG A 29 0.29 SIDE CHAIN
REMARK 500 10 ARG A 6 0.29 SIDE CHAIN
REMARK 500 10 ARG A 8 0.30 SIDE CHAIN
REMARK 500 10 ARG A 19 0.30 SIDE CHAIN
REMARK 500 10 ARG A 29 0.23 SIDE CHAIN
REMARK 500 11 ARG A 6 0.22 SIDE CHAIN
REMARK 500 11 ARG A 8 0.19 SIDE CHAIN
REMARK 500 11 ARG A 19 0.21 SIDE CHAIN
REMARK 500 11 ARG A 29 0.32 SIDE CHAIN
REMARK 500 12 ARG A 6 0.26 SIDE CHAIN
REMARK 500 12 ARG A 8 0.31 SIDE CHAIN
REMARK 500 12 ARG A 19 0.23 SIDE CHAIN
REMARK 500 12 ARG A 29 0.24 SIDE CHAIN
REMARK 500 13 ARG A 6 0.23 SIDE CHAIN
REMARK 500 13 ARG A 8 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 80 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 1E0G A 1 48 UNP A0A2Z2J5F1_ECOLX
DBREF2 1E0G A A0A2Z2J5F1 352 399
SEQRES 1 A 48 ASP SER ILE THR TYR ARG VAL ARG LYS GLY ASP SER LEU
SEQRES 2 A 48 SER SER ILE ALA LYS ARG HIS GLY VAL ASN ILE LYS ASP
SEQRES 3 A 48 VAL MET ARG TRP ASN SER ASP THR ALA ASN LEU GLN PRO
SEQRES 4 A 48 GLY ASP LYS LEU THR LEU PHE VAL LYS
HELIX 1 1 SER A 12 HIS A 20 1 9
HELIX 2 2 ASN A 23 ASN A 31 1 9
HELIX 3 3 ASP A 33 LEU A 37 5 5
SHEET 1 A 2 THR A 4 VAL A 7 0
SHEET 2 A 2 ASP A 41 THR A 44 -1 N LEU A 43 O TYR A 5
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - p 25 2 Bytes