Header list of 1ocp.pdb file
Complete list - b 23 2 Bytes
HEADER DNA BINDING PROTEIN 21-FEB-95 1OCP TITLE SOLUTION STRUCTURE OF OCT3 POU-HOMEODOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: OCT-3; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: T7 GENE 1 UNDER CONTROL OF THE; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: LAC; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PAR2113; SOURCE 11 EXPRESSION_SYSTEM_GENE: T7 GENE 1 UNDER CONTROL OF THE LAC UV5 SOURCE 12 PROMOTER KEYWDS DNA-BINDING PROTEIN, DNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR E.H.MORITA,F.HAYASHI,M.SHIRAKAWA,Y.KYOGOKU REVDAT 3 23-FEB-22 1OCP 1 KEYWDS REMARK REVDAT 2 24-FEB-09 1OCP 1 VERSN REVDAT 1 15-SEP-95 1OCP 0 JRNL AUTH E.H.MORITA,M.SHIRAKAWA,F.HAYASHI,M.IMAGAWA,Y.KYOGOKU JRNL TITL STRUCTURE OF THE OCT-3 POU-HOMEODOMAIN IN SOLUTION, AS JRNL TITL 2 DETERMINED BY TRIPLE RESONANCE HETERONUCLEAR JRNL TITL 3 MULTIDIMENSIONAL NMR SPECTROSCOPY JRNL REF PROTEIN SCI. V. 4 729 1995 JRNL REFN ISSN 0961-8368 JRNL PMID 7613470 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH E.H.MORITA,M.SHIRAKAWA,F.HAYASHI,K.IMAGAWA,Y.KYOGOKU REMARK 1 TITL SECONDARY STRUCTURE OF THE OCT-3 POU HOMEODOMAIN AS REMARK 1 TITL 2 DETERMINED BY 1H-15N NMR SPECTROSCOPY REMARK 1 REF FEBS LETT. V. 321 107 1993 REMARK 1 REFN ISSN 0014-5793 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1OCP 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_1000175431. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL 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 : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: NULL 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 GLU A 2 50.57 -99.28 REMARK 500 1 VAL A 5 26.73 -149.44 REMARK 500 1 GLN A 6 52.32 -146.21 REMARK 500 1 ARG A 10 -70.07 -156.81 REMARK 500 1 SER A 14 31.57 -153.95 REMARK 500 1 ILE A 15 71.45 -151.04 REMARK 500 1 GLN A 61 58.51 -115.83 REMARK 500 2 THR A 3 34.79 -99.42 REMARK 500 2 LEU A 4 37.65 -143.62 REMARK 500 2 GLN A 6 79.52 -109.14 REMARK 500 2 ALA A 7 -166.88 -63.78 REMARK 500 2 LYS A 9 26.46 -155.82 REMARK 500 2 LYS A 11 -164.79 -160.25 REMARK 500 2 ARG A 12 39.66 -99.05 REMARK 500 2 GLN A 61 63.20 -109.96 REMARK 500 2 LYS A 64 -47.47 -150.11 REMARK 500 3 GLU A 2 -44.04 -139.81 REMARK 500 3 GLN A 6 26.15 -149.30 REMARK 500 3 ARG A 10 60.63 -102.70 REMARK 500 3 PRO A 31 32.88 -87.35 REMARK 500 3 LYS A 64 32.72 -96.64 REMARK 500 3 ARG A 65 -45.57 -135.57 REMARK 500 4 THR A 3 -71.68 -97.75 REMARK 500 4 VAL A 5 49.57 -142.64 REMARK 500 4 LYS A 9 38.93 -149.59 REMARK 500 4 ARG A 10 77.96 -155.85 REMARK 500 4 GLN A 61 58.94 -117.71 REMARK 500 4 ARG A 65 29.98 -159.87 REMARK 500 4 SER A 66 -75.95 -156.80 REMARK 500 5 GLU A 2 31.00 -142.25 REMARK 500 5 ALA A 7 -176.16 -66.81 REMARK 500 5 ARG A 8 35.02 -160.61 REMARK 500 5 LYS A 9 42.36 -155.52 REMARK 500 5 LYS A 11 41.45 -90.93 REMARK 500 5 ARG A 12 13.71 -142.40 REMARK 500 5 SER A 14 32.12 -146.85 REMARK 500 5 LYS A 64 -62.90 -92.95 REMARK 500 5 SER A 66 71.43 -158.15 REMARK 500 6 GLU A 2 62.83 -100.10 REMARK 500 6 VAL A 5 -46.02 -134.76 REMARK 500 6 ALA A 7 -175.84 -65.80 REMARK 500 6 LYS A 9 -63.48 -160.11 REMARK 500 6 ARG A 10 -58.23 -160.74 REMARK 500 6 ARG A 12 39.63 -160.28 REMARK 500 6 SER A 14 28.70 -158.74 REMARK 500 6 ILE A 15 79.24 -154.59 REMARK 500 6 GLN A 61 57.42 -117.32 REMARK 500 7 ARG A 8 29.31 -160.36 REMARK 500 7 ARG A 10 39.46 -99.26 REMARK 500 7 GLN A 61 51.48 -95.88 REMARK 500 REMARK 500 THIS ENTRY HAS 139 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 8 0.25 SIDE CHAIN REMARK 500 1 ARG A 10 0.31 SIDE CHAIN REMARK 500 1 ARG A 12 0.28 SIDE CHAIN REMARK 500 1 ARG A 18 0.23 SIDE CHAIN REMARK 500 1 ARG A 20 0.26 SIDE CHAIN REMARK 500 1 ARG A 53 0.31 SIDE CHAIN REMARK 500 1 ARG A 59 0.20 SIDE CHAIN REMARK 500 1 ARG A 60 0.27 SIDE CHAIN REMARK 500 1 ARG A 65 0.24 SIDE CHAIN REMARK 500 2 ARG A 8 0.24 SIDE CHAIN REMARK 500 2 ARG A 10 0.23 SIDE CHAIN REMARK 500 2 ARG A 12 0.30 SIDE CHAIN REMARK 500 2 ARG A 18 0.32 SIDE CHAIN REMARK 500 2 ARG A 20 0.31 SIDE CHAIN REMARK 500 2 ARG A 53 0.27 SIDE CHAIN REMARK 500 2 ARG A 59 0.22 SIDE CHAIN REMARK 500 2 ARG A 60 0.30 SIDE CHAIN REMARK 500 2 ARG A 65 0.30 SIDE CHAIN REMARK 500 3 ARG A 8 0.20 SIDE CHAIN REMARK 500 3 ARG A 10 0.31 SIDE CHAIN REMARK 500 3 ARG A 12 0.19 SIDE CHAIN REMARK 500 3 ARG A 18 0.21 SIDE CHAIN REMARK 500 3 ARG A 20 0.30 SIDE CHAIN REMARK 500 3 ARG A 53 0.27 SIDE CHAIN REMARK 500 3 ARG A 59 0.19 SIDE CHAIN REMARK 500 3 ARG A 60 0.27 SIDE CHAIN REMARK 500 3 ARG A 65 0.25 SIDE CHAIN REMARK 500 4 ARG A 8 0.29 SIDE CHAIN REMARK 500 4 ARG A 10 0.30 SIDE CHAIN REMARK 500 4 ARG A 12 0.32 SIDE CHAIN REMARK 500 4 ARG A 18 0.32 SIDE CHAIN REMARK 500 4 ARG A 20 0.27 SIDE CHAIN REMARK 500 4 ARG A 53 0.23 SIDE CHAIN REMARK 500 4 ARG A 59 0.31 SIDE CHAIN REMARK 500 4 ARG A 60 0.22 SIDE CHAIN REMARK 500 4 ARG A 65 0.31 SIDE CHAIN REMARK 500 5 ARG A 8 0.28 SIDE CHAIN REMARK 500 5 ARG A 10 0.20 SIDE CHAIN REMARK 500 5 ARG A 12 0.24 SIDE CHAIN REMARK 500 5 ARG A 18 0.24 SIDE CHAIN REMARK 500 5 ARG A 20 0.25 SIDE CHAIN REMARK 500 5 ARG A 53 0.32 SIDE CHAIN REMARK 500 5 ARG A 59 0.30 SIDE CHAIN REMARK 500 5 ARG A 60 0.31 SIDE CHAIN REMARK 500 5 ARG A 65 0.27 SIDE CHAIN REMARK 500 6 ARG A 8 0.21 SIDE CHAIN REMARK 500 6 ARG A 10 0.25 SIDE CHAIN REMARK 500 6 ARG A 12 0.30 SIDE CHAIN REMARK 500 6 ARG A 18 0.30 SIDE CHAIN REMARK 500 6 ARG A 20 0.30 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 180 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1OCP A 2 67 UNP P20263 PO5F1_MOUSE 217 282 SEQRES 1 A 67 MET GLU THR LEU VAL GLN ALA ARG LYS ARG LYS ARG THR SEQRES 2 A 67 SER ILE GLU ASN ARG VAL ARG TRP SER LEU GLU THR MET SEQRES 3 A 67 PHE LEU LYS CYS PRO LYS PRO SER LEU GLN GLN ILE THR SEQRES 4 A 67 HIS ILE ALA ASN GLN LEU GLY LEU GLU LYS ASP VAL VAL SEQRES 5 A 67 ARG VAL TRP PHE CYS ASN ARG ARG GLN LYS GLY LYS ARG SEQRES 6 A 67 SER SER HELIX 1 1 ASN A 17 PHE A 27 1 11 HELIX 2 2 LEU A 35 LEU A 45 1 11 HELIX 3 3 LYS A 49 ARG A 60 1 12 SHEET 1 B 2 ALA A 42 LEU A 45 0 SHEET 2 B 2 GLU A 16 VAL A 19 -1 N ARG A 18 O ASN A 43 SHEET 1 D 2 LYS A 32 SER A 34 0 SHEET 2 D 2 LYS A 64 SER A 66 -1 N ARG A 65 O PRO A 33 SHEET 1 E 2 PRO A 31 PRO A 33 0 SHEET 2 E 2 LYS A 9 LYS A 11 1 N LYS A 9 O LYS A 32 SHEET 1 F 2 THR A 25 PHE A 27 0 SHEET 2 F 2 THR A 39 ILE A 41 -1 N ILE A 41 O THR A 25 SHEET 1 G 2 VAL A 19 TRP A 21 0 SHEET 2 G 2 HIS A 40 ASN A 43 1 N ILE A 41 O VAL A 19 SHEET 1 H 2 VAL A 52 TRP A 55 0 SHEET 2 H 2 VAL A 54 PHE A 56 -1 N TRP A 55 O ARG A 53 SHEET 1 I 2 VAL A 54 CYS A 57 0 SHEET 2 I 2 VAL A 51 ARG A 53 1 N VAL A 51 O TRP A 55 SHEET 1 J 2 ALA A 42 LEU A 45 0 SHEET 2 J 2 SER A 14 GLU A 16 -1 N GLU A 16 O ALA A 42 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 23 2 Bytes