Header list of 1o53.pdb file
Complete list - 23 20 Bytes
HEADER TRANSFERASE 11-AUG-03 1O53 TITLE SOLUTION STRUCTURE OF THE N-TERMINAL MEMBRANE ANCHOR OF E. COLI ENZYME TITLE 2 IIA(GLUCOSE) COMPND MOL_ID: 1; COMPND 2 MOLECULE: PTS SYSTEM, GLUCOSE-SPECIFIC IIA COMPONENT; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL MEMBRANE ANCHOR, RESIDUES 1-15 OF ENZYME COMPND 5 IIA(GLUCOSE); COMPND 6 SYNONYM: EIIA-GLC, GLUCOSE-PERMEASE IIA COMPONENT, PHOSPHOTRANSFERASE COMPND 7 ENZYME II, A COMPONENT, EIII-GLC; COMPND 8 EC: 2.7.1.69; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS SYNTHESIZED USING THE SOLID-PHASE SOURCE 4 METHOD AND PURIFIED BY HPLC. THE SEQUENCE OF THE PEPTIDE IS SOURCE 5 NATURALLY FOUND IN ESCHERICHIA COLI (BACTERIA). KEYWDS AMPHIPATHIC HELIX, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR G.WANG,P.A.KEIFER,A.PETERKOFSKY REVDAT 3 23-FEB-22 1O53 1 REMARK REVDAT 2 24-FEB-09 1O53 1 VERSN REVDAT 1 19-AUG-03 1O53 0 SPRSDE 19-AUG-03 1O53 1O0Z JRNL AUTH G.WANG,P.A.KEIFER,A.PETERKOFSKY JRNL TITL SOLUTION STRUCTURE OF THE N-TERMINAL AMPHITROPIC DOMAIN OF JRNL TITL 2 ESCHERICHIA COLI GLUCOSE-SPECIFIC ENZYME IIA IN JRNL TITL 3 MEMBRANE-MIMETIC MICELLES JRNL REF PROTEIN SCI. V. 12 1087 2003 JRNL REFN ISSN 0961-8368 JRNL PMID 12717030 JRNL DOI 10.1110/PS.0301503 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE/NMRDRAW 2.1 REMARK 3 AUTHORS : DELAGLIO, F. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON 146 DISTANCES DERIVED FROM THE NOESY REMARK 3 SPECTRA. REMARK 3 NO DIHEDRAL ANGLES OR HYDROGEN-BOND RESTRAINTS WERE APPLIED. REMARK 4 REMARK 4 1O53 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-03. REMARK 100 THE DEPOSITION ID IS D_1000001813. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 5.4 REMARK 210 IONIC STRENGTH : NO BUFFER REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : NATURAL ABUNDANCE SYNTHETIC REMARK 210 PEPTIDE 5 MM PEPTIDE AND 50 MM REMARK 210 DIHEXANOYL PHOSPHATIDYLGLYCEROL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY, TOCSY, DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : PIPP 1.0, XPLOR-NIH 1.06, MOLMOL REMARK 210 2K.1 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE VIOLATIONS GREATER THAN REMARK 210 0.20 A; RMS DIFFERENCE FOR BOND REMARK 210 DEVIATIONS FROM IDEALITY LESS REMARK 210 THAN 0.01 A; RMS DIFFERENCE FOR REMARK 210 ANGLE DEVIATIONS FROM IDEALITY REMARK 210 LESS THAN 2 DEGREES; STRUCTURES REMARK 210 WITH THE LOWEREST ENERGIES IN REMARK 210 THE ENSEMBLE; STRUCTURES MOST REMARK 210 RESEMBLE THE AVERAGE STRUCTURE. REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D REMARK 210 HOMONUCLEAR NMR TECHNIQUES. 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: CLOSE CONTACTS 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 H2 GLY A 1 H LEU A 2 1.32 REMARK 500 O PHE A 3 H LYS A 7 1.45 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 1 LEU A 2 -86.51 -154.99 REMARK 500 1 ASP A 12 -92.65 -174.25 REMARK 500 1 ASP A 13 -2.01 60.39 REMARK 500 1 LYS A 14 101.33 -172.69 REMARK 500 2 LEU A 2 -96.87 -75.73 REMARK 500 2 ASP A 13 34.91 -78.29 REMARK 500 2 LYS A 14 -107.30 37.20 REMARK 500 3 LEU A 2 -78.94 -159.80 REMARK 500 3 ASP A 12 71.31 -153.72 REMARK 500 3 LYS A 14 90.52 31.01 REMARK 500 4 LEU A 2 -97.68 -137.99 REMARK 500 4 PHE A 3 -47.01 -21.46 REMARK 500 4 ASP A 4 -36.85 -39.85 REMARK 500 4 ASP A 12 -92.12 -97.35 REMARK 500 4 LYS A 14 148.33 58.59 REMARK 500 5 LEU A 2 -98.11 -137.31 REMARK 500 5 PHE A 3 -47.43 -20.67 REMARK 500 5 SER A 11 31.27 -89.94 REMARK 500 5 ASP A 13 -103.91 -95.39 REMARK 500 6 LEU A 2 -88.32 -88.86 REMARK 500 6 SER A 11 48.61 -89.37 REMARK 500 6 ASP A 12 20.92 -172.27 REMARK 500 7 LEU A 2 -87.81 -164.12 REMARK 500 7 SER A 11 3.97 -66.17 REMARK 500 7 ASP A 13 46.09 -78.97 REMARK 500 8 LEU A 2 -90.36 -109.48 REMARK 500 8 LYS A 14 -78.38 57.88 REMARK 500 9 LEU A 2 -85.90 -172.32 REMARK 500 9 ASP A 12 16.25 -158.57 REMARK 500 10 LEU A 2 -86.00 -82.66 REMARK 500 10 LYS A 14 52.97 -102.99 REMARK 500 11 LEU A 2 -84.92 -82.42 REMARK 500 12 LEU A 2 -87.07 -162.20 REMARK 500 12 SER A 11 40.86 -82.94 REMARK 500 12 ASP A 12 -5.54 -146.22 REMARK 500 12 ASP A 13 87.32 -167.22 REMARK 500 12 LYS A 14 167.26 -48.99 REMARK 500 13 LEU A 2 -91.45 -141.16 REMARK 500 13 SER A 11 30.93 -90.53 REMARK 500 13 ASP A 12 33.17 -161.63 REMARK 500 13 ASP A 13 -95.50 -56.85 REMARK 500 14 LEU A 2 -83.69 -90.79 REMARK 500 14 SER A 11 4.98 -67.34 REMARK 500 15 LEU A 2 -84.56 -95.38 REMARK 500 15 ASP A 12 24.85 -170.82 REMARK 500 15 ASP A 13 -36.42 -157.83 REMARK 500 16 LEU A 2 -87.45 -92.63 REMARK 500 16 SER A 11 30.01 -81.43 REMARK 500 16 ASP A 12 -20.48 -157.10 REMARK 500 16 ASP A 13 99.05 -176.73 REMARK 500 REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1GGR RELATED DB: PDB REMARK 900 HPR-IIA COMPLEX REMARK 900 RELATED ID: 2F3G RELATED DB: PDB REMARK 900 X-RAY STRUCTURE OF IIA DBREF 1O53 A 1 15 UNP P08837 PTGA_ECOLI 1 15 SEQRES 1 A 15 GLY LEU PHE ASP LYS LEU LYS SER LEU VAL SER ASP ASP SEQRES 2 A 15 LYS LYS HELIX 1 1 LEU A 2 SER A 11 1 10 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 - 23 20 Bytes