Header list of 1ldl.pdb file
Complete list - 23 20 Bytes
HEADER BINDING PROTEIN 20-MAR-95 1LDL TITLE THREE-DIMENSIONAL STRUCTURE OF A CYSTEINE-RICH REPEAT FROM THE LOW- TITLE 2 DENSITY LIPOPROTEIN RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: LOW-DENSITY LIPOPROTEIN RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: LIGAND-BINDING DOMAIN, FIRST REPEAT; COMPND 5 SYNONYM: LB1; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: HUMAN; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-2T; SOURCE 9 EXPRESSION_SYSTEM_GENE: HUMAN KEYWDS LDL RECEPTOR CYSTEINE-RICH REPEAT, BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR N.L.DALY,M.J.SCANLON,P.A.KROON,R.SMITH REVDAT 3 23-FEB-22 1LDL 1 REMARK SEQADV REVDAT 2 24-FEB-09 1LDL 1 VERSN REVDAT 1 08-MAR-96 1LDL 0 JRNL AUTH N.L.DALY,M.J.SCANLON,J.T.DJORDJEVIC,P.A.KROON,R.SMITH JRNL TITL THREE-DIMENSIONAL STRUCTURE OF A CYSTEINE-RICH REPEAT FROM JRNL TITL 2 THE LOW-DENSITY LIPOPROTEIN RECEPTOR. JRNL REF PROC.NATL.ACAD.SCI.USA V. 92 6334 1995 JRNL REFN ISSN 0027-8424 JRNL PMID 7603991 JRNL DOI 10.1073/PNAS.92.14.6334 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.BIERI,J.T.DJORDJEVIC,N.L.DALY,R.SMITH,P.A.KROON REMARK 1 TITL DISULFIDE BRIDGES OF A CYSTEINE-RICH REPEAT OF THE LDL REMARK 1 TITL 2 RECEPTOR LIGAND-BINDING DOMAIN REMARK 1 REF BIOCHEMISTRY V. 34 13059 1995 REMARK 1 REFN ISSN 0006-2960 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 1LDL 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_1000174668. 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 : 10 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-10 REMARK 465 RES C SSSEQI REMARK 465 GLY A -1 REMARK 465 SER A 0 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 VAL A 2 -42.39 -168.56 REMARK 500 1 ASN A 9 66.40 -105.28 REMARK 500 1 CYS A 13 172.67 -57.85 REMARK 500 1 CYS A 25 60.49 37.14 REMARK 500 1 SER A 28 30.63 -160.88 REMARK 500 1 CYS A 31 30.99 -88.37 REMARK 500 1 ASP A 33 -63.87 -174.43 REMARK 500 1 SER A 35 13.58 -151.56 REMARK 500 1 SER A 38 99.87 -58.41 REMARK 500 1 CYS A 42 -68.29 -103.79 REMARK 500 1 LEU A 43 -89.91 49.45 REMARK 500 1 VAL A 45 -66.26 -145.42 REMARK 500 2 VAL A 2 162.75 59.88 REMARK 500 2 CYS A 25 75.97 57.62 REMARK 500 2 ASP A 26 -43.91 -135.88 REMARK 500 2 ASP A 33 -64.35 -108.47 REMARK 500 2 SER A 35 50.64 -151.77 REMARK 500 2 CYS A 42 56.69 -103.67 REMARK 500 3 ASP A 4 102.26 59.13 REMARK 500 3 ARG A 5 -172.86 -62.35 REMARK 500 3 CYS A 6 -179.29 -61.24 REMARK 500 3 ASN A 9 -67.19 82.45 REMARK 500 3 GLU A 10 -164.11 49.64 REMARK 500 3 CYS A 25 73.02 58.21 REMARK 500 3 ASP A 26 -41.32 -130.95 REMARK 500 3 ALA A 29 96.95 -56.04 REMARK 500 3 GLU A 30 -75.82 -90.02 REMARK 500 3 CYS A 31 27.63 33.21 REMARK 500 3 GLN A 32 28.12 44.55 REMARK 500 3 ASP A 33 -67.74 -174.54 REMARK 500 3 SER A 35 -28.44 -152.75 REMARK 500 3 SER A 44 103.98 60.15 REMARK 500 4 GLU A 7 -169.21 -115.78 REMARK 500 4 ASN A 9 73.82 58.34 REMARK 500 4 ASP A 26 29.92 -143.38 REMARK 500 4 ASP A 33 -65.78 -168.96 REMARK 500 4 SER A 35 31.36 -151.45 REMARK 500 5 ARG A 8 -163.79 64.72 REMARK 500 5 ASN A 9 42.49 -98.74 REMARK 500 5 GLU A 10 -172.61 -57.46 REMARK 500 5 CYS A 13 -178.52 -67.40 REMARK 500 5 CYS A 25 75.26 58.28 REMARK 500 5 ASP A 26 -43.26 -138.20 REMARK 500 5 ALA A 29 77.42 59.43 REMARK 500 5 CYS A 31 45.60 -83.85 REMARK 500 5 GLN A 32 28.18 49.31 REMARK 500 5 ASP A 33 -41.97 -177.41 REMARK 500 5 SER A 35 18.36 -152.60 REMARK 500 5 SER A 44 -177.25 -172.29 REMARK 500 6 VAL A 2 -65.50 -127.26 REMARK 500 REMARK 500 THIS ENTRY HAS 100 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 0.32 SIDE CHAIN REMARK 500 1 ARG A 8 0.31 SIDE CHAIN REMARK 500 2 ARG A 5 0.31 SIDE CHAIN REMARK 500 2 ARG A 8 0.22 SIDE CHAIN REMARK 500 3 ARG A 5 0.27 SIDE CHAIN REMARK 500 3 ARG A 8 0.32 SIDE CHAIN REMARK 500 4 ARG A 5 0.27 SIDE CHAIN REMARK 500 4 ARG A 8 0.21 SIDE CHAIN REMARK 500 5 ARG A 5 0.22 SIDE CHAIN REMARK 500 5 ARG A 8 0.31 SIDE CHAIN REMARK 500 6 ARG A 5 0.31 SIDE CHAIN REMARK 500 6 ARG A 8 0.29 SIDE CHAIN REMARK 500 7 ARG A 5 0.21 SIDE CHAIN REMARK 500 7 ARG A 8 0.22 SIDE CHAIN REMARK 500 8 ARG A 5 0.27 SIDE CHAIN REMARK 500 8 ARG A 8 0.28 SIDE CHAIN REMARK 500 9 ARG A 5 0.28 SIDE CHAIN REMARK 500 9 ARG A 8 0.31 SIDE CHAIN REMARK 500 10 ARG A 5 0.31 SIDE CHAIN REMARK 500 10 ARG A 8 0.29 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1LDL A -1 46 UNP P01130 LDLR_HUMAN 20 67 SEQADV 1LDL SER A 0 UNP P01130 THR 21 CONFLICT SEQRES 1 A 48 GLY SER ALA VAL GLY ASP ARG CYS GLU ARG ASN GLU PHE SEQRES 2 A 48 GLN CYS GLN ASP GLY LYS CYS ILE SER TYR LYS TRP VAL SEQRES 3 A 48 CYS ASP GLY SER ALA GLU CYS GLN ASP GLY SER ASP GLU SEQRES 4 A 48 SER GLN GLU THR CYS LEU SER VAL THR HELIX 1 1 TYR A 21 TRP A 23 5 3 SHEET 1 A 2 GLU A 10 GLN A 12 0 SHEET 2 A 2 CYS A 18 SER A 20 -1 N ILE A 19 O PHE A 11 SSBOND 1 CYS A 6 CYS A 18 1555 1555 2.02 SSBOND 2 CYS A 13 CYS A 31 1555 1555 2.02 SSBOND 3 CYS A 25 CYS A 42 1555 1555 2.02 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