Header list of 1bw5.pdb file
Complete list - b 16 2 Bytes
HEADER DNA BINDING PROTEIN 29-SEP-98 1BW5 TITLE THE NMR SOLUTION STRUCTURE OF THE HOMEODOMAIN OF THE RAT INSULIN GENE TITLE 2 ENHANCER PROTEIN ISL-1, 50 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: INSULIN GENE ENHANCER PROTEIN ISL-1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ISL-1HD SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 ORGAN: PANCREAS KEYWDS DNA-BINDING PROTEIN, HOMEODOMAIN, LIM DOMAIN, DNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 50 AUTHOR J.H.IPPEL,G.LARSSON,G.BEHRAVAN,J.ZDUNEK,M.LUNDQVIST,J.SCHLEUCHER,P.- AUTHOR 2 O.LYCKSELL,S.S.WIJMENGA REVDAT 4 16-FEB-22 1BW5 1 KEYWDS REMARK SEQADV REVDAT 3 24-FEB-09 1BW5 1 VERSN REVDAT 2 01-APR-03 1BW5 1 JRNL REVDAT 1 15-JUN-99 1BW5 0 JRNL AUTH H.IPPEL,G.LARSSON,G.BEHRAVAN,J.ZDUNEK,M.LUNDQVIST, JRNL AUTH 2 J.SCHLEUCHER,P.O.LYCKSELL,S.WIJMENGA JRNL TITL THE SOLUTION STRUCTURE OF THE HOMEODOMAIN OF THE RAT JRNL TITL 2 INSULIN-GENE ENHANCER PROTEIN ISL-1. COMPARISON WITH OTHER JRNL TITL 3 HOMEODOMAINS. JRNL REF J.MOL.BIOL. V. 288 689 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 10329173 JRNL DOI 10.1006/JMBI.1999.2718 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.H.IPPEL,G.LARSSON,G.BEHRAVAN,M.LUNDQVIST,P.O.LYCKSELL, REMARK 1 AUTH 2 J.SCHLEUCHER,J.ZDUNEK,S.S.WIJMENGA REMARK 1 TITL 1H, 13C AND 15N ASSIGNMENT OF THE ISL-1 HOMEODOMAIN REMARK 1 REF J.BIOMOL.NMR V. 12 357 1998 REMARK 1 REFN ISSN 0925-2738 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1BW5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000172119. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 281 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 50 MM NA+ REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-EDITED NOESY; 15N-EDITED REMARK 210 TOCSY; 13C-EDITED NOESY; TRIPLE REMARK 210 RESONANCE EXPERIMENTS REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : BRUKER UXNMR UXNMR, XEASY, X REMARK 210 -PLOR REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 50 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW RESTRAINT ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 3D-EDITED NOESY AND REMARK 210 TRIPLE RESONANCE SPECTRA ON UNIFORMLY LABELLED 15N AND UNIFORMLY REMARK 210 LABELLED 13C, 15N SAMPLES OF ISL-1HD. 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 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 ARG A 5 -178.20 -54.91 REMARK 500 1 LYS A 13 -70.83 -68.23 REMARK 500 1 LEU A 31 -82.39 -65.14 REMARK 500 1 ASP A 58 57.12 -67.58 REMARK 500 1 LYS A 60 -44.21 -140.43 REMARK 500 1 ARG A 61 86.81 -63.09 REMARK 500 1 SER A 62 34.73 -162.05 REMARK 500 1 MET A 65 136.03 62.60 REMARK 500 2 LYS A 2 -75.37 -64.98 REMARK 500 2 VAL A 6 104.80 39.47 REMARK 500 2 ARG A 7 63.38 -159.45 REMARK 500 2 LYS A 13 -77.14 -68.75 REMARK 500 2 ASP A 29 -154.92 -165.31 REMARK 500 2 LEU A 31 -81.95 -67.72 REMARK 500 2 GLN A 52 -83.65 -50.33 REMARK 500 2 ARG A 55 -70.94 -51.14 REMARK 500 2 ASP A 58 -161.38 -62.75 REMARK 500 2 LYS A 59 -105.33 41.50 REMARK 500 2 LYS A 60 92.59 -63.16 REMARK 500 2 ARG A 61 -156.69 -94.23 REMARK 500 2 SER A 62 38.83 -173.17 REMARK 500 2 ILE A 63 -64.34 -100.60 REMARK 500 2 MET A 64 55.01 -157.53 REMARK 500 2 MET A 65 158.48 58.62 REMARK 500 3 LYS A 2 167.25 52.38 REMARK 500 3 THR A 3 -158.38 55.97 REMARK 500 3 VAL A 6 103.12 -51.82 REMARK 500 3 THR A 8 -157.08 -92.15 REMARK 500 3 VAL A 9 12.09 -142.30 REMARK 500 3 LYS A 13 -86.37 -71.99 REMARK 500 3 ASP A 29 -154.83 -161.99 REMARK 500 3 LEU A 31 -81.98 -66.26 REMARK 500 3 GLN A 52 -71.02 -53.55 REMARK 500 3 LYS A 59 -78.94 -170.75 REMARK 500 3 LYS A 60 -87.48 -63.59 REMARK 500 3 ARG A 61 80.61 51.32 REMARK 500 4 THR A 3 -79.30 -130.55 REMARK 500 4 ARG A 5 -157.13 -135.92 REMARK 500 4 ARG A 7 29.18 -157.45 REMARK 500 4 VAL A 9 22.31 -140.77 REMARK 500 4 LYS A 13 -77.16 -67.63 REMARK 500 4 ASN A 25 101.77 -160.53 REMARK 500 4 ARG A 27 74.63 -151.89 REMARK 500 4 LEU A 31 -81.03 -65.21 REMARK 500 4 LYS A 59 -70.43 -174.86 REMARK 500 4 MET A 64 -49.96 -132.72 REMARK 500 5 ARG A 5 -177.95 -55.75 REMARK 500 5 PRO A 28 -178.53 -66.86 REMARK 500 5 LEU A 31 -81.16 -65.26 REMARK 500 5 LYS A 59 -93.89 29.09 REMARK 500 REMARK 500 THIS ENTRY HAS 511 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 5 0.21 SIDE CHAIN REMARK 500 1 ARG A 7 0.20 SIDE CHAIN REMARK 500 1 ARG A 19 0.31 SIDE CHAIN REMARK 500 1 ARG A 27 0.29 SIDE CHAIN REMARK 500 1 ARG A 45 0.22 SIDE CHAIN REMARK 500 1 ARG A 48 0.30 SIDE CHAIN REMARK 500 1 ARG A 55 0.16 SIDE CHAIN REMARK 500 1 ARG A 61 0.31 SIDE CHAIN REMARK 500 2 ARG A 5 0.27 SIDE CHAIN REMARK 500 2 ARG A 7 0.22 SIDE CHAIN REMARK 500 2 ARG A 19 0.31 SIDE CHAIN REMARK 500 2 ARG A 27 0.26 SIDE CHAIN REMARK 500 2 ARG A 45 0.27 SIDE CHAIN REMARK 500 2 ARG A 48 0.32 SIDE CHAIN REMARK 500 2 ARG A 55 0.24 SIDE CHAIN REMARK 500 2 ARG A 61 0.29 SIDE CHAIN REMARK 500 3 ARG A 5 0.32 SIDE CHAIN REMARK 500 3 ARG A 7 0.27 SIDE CHAIN REMARK 500 3 ARG A 19 0.31 SIDE CHAIN REMARK 500 3 ARG A 27 0.30 SIDE CHAIN REMARK 500 3 ARG A 45 0.10 SIDE CHAIN REMARK 500 3 ARG A 48 0.17 SIDE CHAIN REMARK 500 3 ARG A 55 0.32 SIDE CHAIN REMARK 500 3 ARG A 61 0.29 SIDE CHAIN REMARK 500 4 ARG A 5 0.32 SIDE CHAIN REMARK 500 4 ARG A 7 0.27 SIDE CHAIN REMARK 500 4 ARG A 19 0.23 SIDE CHAIN REMARK 500 4 ARG A 27 0.27 SIDE CHAIN REMARK 500 4 ARG A 45 0.25 SIDE CHAIN REMARK 500 4 ARG A 48 0.17 SIDE CHAIN REMARK 500 4 ARG A 55 0.28 SIDE CHAIN REMARK 500 4 ARG A 61 0.22 SIDE CHAIN REMARK 500 5 ARG A 5 0.26 SIDE CHAIN REMARK 500 5 ARG A 7 0.31 SIDE CHAIN REMARK 500 5 ARG A 19 0.20 SIDE CHAIN REMARK 500 5 ARG A 27 0.20 SIDE CHAIN REMARK 500 5 ARG A 45 0.20 SIDE CHAIN REMARK 500 5 ARG A 48 0.28 SIDE CHAIN REMARK 500 5 ARG A 55 0.29 SIDE CHAIN REMARK 500 5 ARG A 61 0.30 SIDE CHAIN REMARK 500 6 ARG A 5 0.28 SIDE CHAIN REMARK 500 6 ARG A 7 0.32 SIDE CHAIN REMARK 500 6 ARG A 19 0.32 SIDE CHAIN REMARK 500 6 ARG A 27 0.21 SIDE CHAIN REMARK 500 6 ARG A 45 0.32 SIDE CHAIN REMARK 500 6 ARG A 48 0.24 SIDE CHAIN REMARK 500 6 ARG A 55 0.32 SIDE CHAIN REMARK 500 6 ARG A 61 0.29 SIDE CHAIN REMARK 500 7 ARG A 5 0.29 SIDE CHAIN REMARK 500 7 ARG A 7 0.22 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 396 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1BW5 A 2 66 UNP P50480 ISL2_RAT 191 255 SEQADV 1BW5 ARG A 61 UNP P50480 LYS 250 CONFLICT SEQADV 1BW5 MET A 64 UNP P50480 LEU 253 CONFLICT SEQRES 1 A 66 MET LYS THR THR ARG VAL ARG THR VAL LEU ASN GLU LYS SEQRES 2 A 66 GLN LEU HIS THR LEU ARG THR CYS TYR ALA ALA ASN PRO SEQRES 3 A 66 ARG PRO ASP ALA LEU MET LYS GLU GLN LEU VAL GLU MET SEQRES 4 A 66 THR GLY LEU SER PRO ARG VAL ILE ARG VAL TRP PHE GLN SEQRES 5 A 66 ASN LYS ARG CYS LYS ASP LYS LYS ARG SER ILE MET MET SEQRES 6 A 66 LYS HELIX 1 H1 GLU A 12 ALA A 23 1 12 HELIX 2 H2 ALA A 30 THR A 40 1 11 HELIX 3 H3 PRO A 44 LYS A 57 1 14 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 - b 16 2 Bytes