Header list of 1lre.pdb file
Complete list - b 23 2 Bytes
HEADER CELL SURFACE PROTEIN 08-MAY-97 1LRE
TITLE RECEPTOR ASSOCIATED PROTEIN (RAP) DOMAIN 1, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR-ASSOCIATED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, DOMAIN 1, RESIDUES 17 - 97;
COMPND 5 SYNONYM: RAP, LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN,
COMPND 6 ALPHA=2=MACROGLOBULIN RECEPTOR ASSOCIATED PROTEIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PT=7=H=6=UB
KEYWDS ALPHA2-MACROGLOBULIN RECEPTOR ASSOCIATED PROTEIN, LOW DENSITY
KEYWDS 2 LIPOPROTEIN RECEPTOR FAMILY ASSOCIATED PROTEIN, LDLR FAMILY
KEYWDS 3 ASSOCIATED PROTEIN, HELIX BUNDLE, CELL SURFACE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.R.NIELSEN,F.M.POULSEN
REVDAT 3 23-FEB-22 1LRE 1 REMARK
REVDAT 2 24-FEB-09 1LRE 1 VERSN
REVDAT 1 20-AUG-97 1LRE 0
JRNL AUTH P.R.NIELSEN,L.ELLGAARD,M.ETZERODT,H.C.THOGERSEN,F.M.POULSEN
JRNL TITL THE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF
JRNL TITL 2 ALPHA2-MACROGLOBULIN RECEPTOR-ASSOCIATED PROTEIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 94 7521 1997
JRNL REFN ISSN 0027-8424
JRNL PMID 9207124
JRNL DOI 10.1073/PNAS.94.14.7521
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.R.NIELSEN,L.ELLGAARD,P.H.JENSEN,H.C.THOEGERSEN,F.M.POULSEN
REMARK 1 TITL ALPHA2-MACROGLOBULIN RECEPTOR ASSOCIATED PROTEINS CONSIST OF
REMARK 1 TITL 2 THREE DOMAINS WITH SIMILAR STRUCTURAL MOTIFS. THE 1H, 15N,
REMARK 1 TITL 3 AND 13C CHEMICAL SHIFT ASSIGNMENTS AND SECONDARY STRUCTURE
REMARK 1 TITL 4 OF THE TRUNCATED N-TERMINAL DOMAIN OF HUMAN RAP
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.ELLGAARD,T.L.HOLTET,P.R.NIELSEN,M.ETZERODT,J.GLIEMANN,
REMARK 1 AUTH 2 H.C.THOGERSEN
REMARK 1 TITL DISSECTION OF THE DOMAIN ARCHITECTURE OF THE
REMARK 1 TITL 2 ALPHA2MACROGLOBULIN-RECEPTOR-ASSOCIATED PROTEIN
REMARK 1 REF EUR.J.BIOCHEM. V. 244 544 1997
REMARK 1 REFN ISSN 0014-2956
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 1LRE 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_1000174805.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.4
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 : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : DG, MD
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
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 19 -33.02 -38.54
REMARK 500 1 LEU A 37 159.58 -46.42
REMARK 500 1 LEU A 62 -73.09 -56.72
REMARK 500 1 ASP A 68 40.00 -82.71
REMARK 500 1 ASP A 91 46.25 -162.06
REMARK 500 2 GLU A 69 -33.87 -36.49
REMARK 500 2 LYS A 94 -71.98 -165.14
REMARK 500 2 ASP A 95 145.30 62.53
REMARK 500 2 ALA A 96 89.11 40.98
REMARK 500 3 LYS A 94 25.14 -166.96
REMARK 500 4 LEU A 28 -76.37 -61.01
REMARK 500 4 LEU A 62 -74.54 -56.81
REMARK 500 4 LYS A 93 39.18 175.90
REMARK 500 4 LYS A 94 34.78 -178.42
REMARK 500 4 ASP A 95 49.60 -97.64
REMARK 500 4 ALA A 96 -81.55 -125.13
REMARK 500 5 LEU A 37 154.43 -48.66
REMARK 500 5 LEU A 62 -74.12 -54.03
REMARK 500 5 LYS A 94 -108.61 -169.47
REMARK 500 5 ASP A 95 167.68 57.70
REMARK 500 5 ALA A 96 -36.55 79.44
REMARK 500 6 GLU A 18 131.23 59.52
REMARK 500 6 PHE A 20 -168.42 -111.84
REMARK 500 6 LEU A 28 -73.87 -62.28
REMARK 500 6 HIS A 36 35.95 34.35
REMARK 500 6 LEU A 62 -70.49 -53.69
REMARK 500 6 LYS A 93 158.61 59.25
REMARK 500 6 LYS A 94 -71.21 -156.43
REMARK 500 6 ASP A 95 86.82 58.84
REMARK 500 7 GLU A 18 137.59 60.40
REMARK 500 7 LEU A 28 -75.59 -64.40
REMARK 500 7 LEU A 37 166.72 -43.92
REMARK 500 7 LYS A 63 -71.20 -51.93
REMARK 500 7 LEU A 64 -29.30 -37.07
REMARK 500 7 LYS A 94 39.01 -168.05
REMARK 500 8 LEU A 37 159.80 -46.22
REMARK 500 8 LEU A 64 -32.55 -39.31
REMARK 500 8 ASP A 91 36.65 -173.02
REMARK 500 8 LYS A 94 -114.55 -167.53
REMARK 500 8 ASP A 95 -141.63 54.22
REMARK 500 8 ALA A 96 -66.57 -166.84
REMARK 500 9 LEU A 37 162.61 -43.28
REMARK 500 9 LYS A 94 -32.07 -177.12
REMARK 500 10 LEU A 37 168.89 -45.89
REMARK 500 10 GLU A 69 -35.81 -35.33
REMARK 500 10 ASP A 91 57.58 -147.63
REMARK 500 10 LYS A 93 72.69 45.43
REMARK 500 10 LYS A 94 -22.37 166.32
REMARK 500 10 ASP A 95 172.38 -44.75
REMARK 500 10 ALA A 96 100.21 61.74
REMARK 500
REMARK 500 THIS ENTRY HAS 113 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 21 0.31 SIDE CHAIN
REMARK 500 1 ARG A 34 0.13 SIDE CHAIN
REMARK 500 1 ARG A 41 0.29 SIDE CHAIN
REMARK 500 1 ARG A 54 0.17 SIDE CHAIN
REMARK 500 1 ARG A 76 0.32 SIDE CHAIN
REMARK 500 1 ARG A 79 0.30 SIDE CHAIN
REMARK 500 1 ARG A 97 0.31 SIDE CHAIN
REMARK 500 2 ARG A 21 0.32 SIDE CHAIN
REMARK 500 2 ARG A 34 0.20 SIDE CHAIN
REMARK 500 2 ARG A 41 0.21 SIDE CHAIN
REMARK 500 2 ARG A 54 0.21 SIDE CHAIN
REMARK 500 2 ARG A 76 0.09 SIDE CHAIN
REMARK 500 2 ARG A 79 0.32 SIDE CHAIN
REMARK 500 2 ARG A 97 0.17 SIDE CHAIN
REMARK 500 3 ARG A 21 0.32 SIDE CHAIN
REMARK 500 3 ARG A 34 0.24 SIDE CHAIN
REMARK 500 3 ARG A 41 0.31 SIDE CHAIN
REMARK 500 3 ARG A 54 0.26 SIDE CHAIN
REMARK 500 3 ARG A 76 0.31 SIDE CHAIN
REMARK 500 3 ARG A 79 0.20 SIDE CHAIN
REMARK 500 3 ARG A 97 0.30 SIDE CHAIN
REMARK 500 4 ARG A 21 0.30 SIDE CHAIN
REMARK 500 4 ARG A 34 0.30 SIDE CHAIN
REMARK 500 4 ARG A 41 0.29 SIDE CHAIN
REMARK 500 4 ARG A 54 0.21 SIDE CHAIN
REMARK 500 4 ARG A 76 0.30 SIDE CHAIN
REMARK 500 4 ARG A 79 0.18 SIDE CHAIN
REMARK 500 4 ARG A 97 0.29 SIDE CHAIN
REMARK 500 5 ARG A 21 0.28 SIDE CHAIN
REMARK 500 5 ARG A 34 0.32 SIDE CHAIN
REMARK 500 5 ARG A 41 0.31 SIDE CHAIN
REMARK 500 5 ARG A 76 0.14 SIDE CHAIN
REMARK 500 5 ARG A 79 0.28 SIDE CHAIN
REMARK 500 5 ARG A 97 0.32 SIDE CHAIN
REMARK 500 6 ARG A 21 0.30 SIDE CHAIN
REMARK 500 6 ARG A 34 0.31 SIDE CHAIN
REMARK 500 6 ARG A 41 0.32 SIDE CHAIN
REMARK 500 6 ARG A 54 0.17 SIDE CHAIN
REMARK 500 6 ARG A 76 0.12 SIDE CHAIN
REMARK 500 6 ARG A 79 0.25 SIDE CHAIN
REMARK 500 6 ARG A 97 0.32 SIDE CHAIN
REMARK 500 7 ARG A 21 0.28 SIDE CHAIN
REMARK 500 7 ARG A 34 0.32 SIDE CHAIN
REMARK 500 7 ARG A 41 0.20 SIDE CHAIN
REMARK 500 7 ARG A 54 0.29 SIDE CHAIN
REMARK 500 7 ARG A 76 0.17 SIDE CHAIN
REMARK 500 7 ARG A 79 0.32 SIDE CHAIN
REMARK 500 7 ARG A 97 0.29 SIDE CHAIN
REMARK 500 8 ARG A 21 0.31 SIDE CHAIN
REMARK 500 8 ARG A 34 0.27 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 135 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1LRE A 17 97 UNP P30533 AMRP_HUMAN 51 131
SEQRES 1 A 81 GLY GLU GLU PHE ARG MET GLU LYS LEU ASN GLN LEU TRP
SEQRES 2 A 81 GLU LYS ALA GLN ARG LEU HIS LEU PRO PRO VAL ARG LEU
SEQRES 3 A 81 ALA GLU LEU HIS ALA ASP LEU LYS ILE GLN GLU ARG ASP
SEQRES 4 A 81 GLU LEU ALA TRP LYS LYS LEU LYS LEU ASP GLY LEU ASP
SEQRES 5 A 81 GLU ASP GLY GLU LYS GLU ALA ARG LEU ILE ARG ASN LEU
SEQRES 6 A 81 ASN VAL ILE LEU ALA LYS TYR GLY LEU ASP GLY LYS LYS
SEQRES 7 A 81 ASP ALA ARG
HELIX 1 1 GLU A 23 ARG A 34 1 12
HELIX 2 2 PRO A 39 ASP A 65 1 27
HELIX 3 3 LYS A 73 TYR A 88 1 16
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