Header list of 1tle.pdb file
Complete list - 2 20 Bytes
HEADER GLYCOPROTEIN 26-JAN-96 1TLE
TITLE LE (LAMININ-TYPE EGF-LIKE) MODULE GIII4 IN SOLUTION AT PH 3.5 AND 290
TITLE 2 K, NMR, 14 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LAMININ;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: NIDOGEN BINDING LE MODULE OF THE LAMININ GAMMA1 CHAIN,
COMPND 5 MODULE GIII4;
COMPND 6 SYNONYM: LAMININ-TYPE EGF-LIKE;
COMPND 7 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 TISSUE: BASEMENT MEMBRANE;
SOURCE 6 GENE: LAMC1;
SOURCE 7 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCEP4;
SOURCE 11 EXPRESSION_SYSTEM_GENE: LAMC1
KEYWDS GLYCOPROTEIN, EXTRACELLULAR MATRIX PROTEIN, NIDOGEN BINDING, LE-
KEYWDS 2 MODULE
EXPDTA SOLUTION NMR
NUMMDL 14
AUTHOR R.BAUMGARTNER,M.CZISCH,U.MAYER,E.P.SCHL,R.HUBER,R.TIMPL,T.A.HOLAK
REVDAT 3 02-MAR-22 1TLE 1 REMARK
REVDAT 2 24-FEB-09 1TLE 1 VERSN
REVDAT 1 12-FEB-97 1TLE 0
JRNL AUTH R.BAUMGARTNER,M.CZISCH,U.MAYER,E.POSCHL,R.HUBER,R.TIMPL,
JRNL AUTH 2 T.A.HOLAK
JRNL TITL STRUCTURE OF THE NIDOGEN BINDING LE MODULE OF THE LAMININ
JRNL TITL 2 GAMMA1 CHAIN IN SOLUTION.
JRNL REF J.MOL.BIOL. V. 257 658 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8648631
JRNL DOI 10.1006/JMBI.1996.0192
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.POSCHL,J.W.FOX,D.BLOCK,U.MAYER,R.TIMPL
REMARK 1 TITL TWO NON-CONTIGUOUS REGIONS CONTRIBUTE TO NIDOGEN BINDING TO
REMARK 1 TITL 2 A SINGLE EGF-LIKE MOTIF OF THE LAMININ GAMMA 1 CHAIN
REMARK 1 REF EMBO J. V. 13 3741 1994
REMARK 1 REFN ISSN 0261-4189
REMARK 1 REFERENCE 2
REMARK 1 AUTH U.MAYER,R.NISCHT,E.POSCHL,K.MANN,K.FUKUDA,M.GERL,Y.YAMADA,
REMARK 1 AUTH 2 R.TIMPL
REMARK 1 TITL A SINGLE EGF-LIKE MOTIF OF LAMININ IS RESPONSIBLE FOR HIGH
REMARK 1 TITL 2 AFFINITY NIDOGEN BINDING
REMARK 1 REF EMBO J. V. 12 1879 1993
REMARK 1 REFN ISSN 0261-4189
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 1TLE 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_1000176717.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 290
REMARK 210 PH : 3.5
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 : 14
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 CYS A 5 157.19 178.90
REMARK 500 1 ASN A 6 170.41 -54.09
REMARK 500 1 TYR A 29 77.73 -64.58
REMARK 500 1 ASN A 30 48.87 26.00
REMARK 500 1 CYS A 36 27.23 49.74
REMARK 500 1 LYS A 55 -130.69 -71.85
REMARK 500 2 PRO A 2 -90.87 -78.23
REMARK 500 2 GLN A 4 89.28 -55.97
REMARK 500 2 ASP A 7 -74.72 81.88
REMARK 500 2 ALA A 13 -171.88 -54.36
REMARK 500 2 ASN A 16 16.43 52.22
REMARK 500 2 LYS A 26 67.21 -154.02
REMARK 500 2 ILE A 28 -62.87 -104.13
REMARK 500 2 TYR A 29 73.07 -69.70
REMARK 500 2 ASN A 30 59.13 27.48
REMARK 500 2 ALA A 32 -168.70 -119.43
REMARK 500 2 LYS A 55 -105.97 -59.27
REMARK 500 2 LYS A 57 153.19 163.63
REMARK 500 3 CYS A 3 -178.06 61.78
REMARK 500 3 GLN A 4 127.92 179.76
REMARK 500 3 ASN A 6 -165.35 -164.59
REMARK 500 3 ASP A 7 -84.07 66.40
REMARK 500 3 ASN A 8 63.45 -115.73
REMARK 500 3 ASN A 16 28.43 38.85
REMARK 500 3 ASN A 30 63.79 33.63
REMARK 500 3 LYS A 55 -105.61 -59.30
REMARK 500 3 LYS A 57 172.19 170.36
REMARK 500 4 PRO A 2 -94.79 -75.41
REMARK 500 4 CYS A 3 -91.89 35.46
REMARK 500 4 CYS A 5 -143.87 -110.59
REMARK 500 4 ASN A 6 -176.22 -52.09
REMARK 500 4 ASN A 16 -29.29 -38.22
REMARK 500 4 LYS A 26 70.81 -165.04
REMARK 500 4 ILE A 28 -63.13 -105.47
REMARK 500 4 TYR A 29 82.86 -57.17
REMARK 500 4 ASN A 30 49.91 21.20
REMARK 500 4 ALA A 32 -162.47 -125.01
REMARK 500 4 LYS A 55 -139.70 -63.41
REMARK 500 5 GLN A 4 140.12 -172.03
REMARK 500 5 ASP A 7 -134.92 -152.59
REMARK 500 5 ALA A 13 -165.80 -78.83
REMARK 500 5 ASN A 16 25.51 45.12
REMARK 500 5 CYS A 24 107.77 -58.25
REMARK 500 5 ILE A 28 -62.05 -108.82
REMARK 500 5 ASN A 30 62.07 38.47
REMARK 500 5 ALA A 32 -164.99 -122.98
REMARK 500 5 LYS A 55 -129.75 -77.57
REMARK 500 6 CYS A 5 -135.47 -69.35
REMARK 500 6 ASN A 6 -174.02 -56.96
REMARK 500 6 ASN A 12 -72.15 -78.57
REMARK 500
REMARK 500 THIS ENTRY HAS 133 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 1 0.32 SIDE CHAIN
REMARK 500 1 ARG A 19 0.28 SIDE CHAIN
REMARK 500 1 ARG A 38 0.19 SIDE CHAIN
REMARK 500 2 ARG A 1 0.15 SIDE CHAIN
REMARK 500 2 ARG A 19 0.21 SIDE CHAIN
REMARK 500 2 ARG A 38 0.32 SIDE CHAIN
REMARK 500 3 ARG A 1 0.15 SIDE CHAIN
REMARK 500 3 ARG A 19 0.25 SIDE CHAIN
REMARK 500 3 ARG A 38 0.27 SIDE CHAIN
REMARK 500 4 ARG A 1 0.25 SIDE CHAIN
REMARK 500 4 ARG A 19 0.17 SIDE CHAIN
REMARK 500 4 ARG A 38 0.09 SIDE CHAIN
REMARK 500 5 ARG A 1 0.29 SIDE CHAIN
REMARK 500 5 ARG A 19 0.14 SIDE CHAIN
REMARK 500 5 ARG A 38 0.23 SIDE CHAIN
REMARK 500 6 ARG A 1 0.30 SIDE CHAIN
REMARK 500 6 ARG A 19 0.29 SIDE CHAIN
REMARK 500 6 ARG A 38 0.14 SIDE CHAIN
REMARK 500 7 ARG A 19 0.21 SIDE CHAIN
REMARK 500 7 ARG A 38 0.32 SIDE CHAIN
REMARK 500 8 ARG A 1 0.21 SIDE CHAIN
REMARK 500 8 ARG A 19 0.17 SIDE CHAIN
REMARK 500 8 ARG A 38 0.30 SIDE CHAIN
REMARK 500 9 ARG A 1 0.14 SIDE CHAIN
REMARK 500 9 ARG A 19 0.29 SIDE CHAIN
REMARK 500 9 ARG A 38 0.23 SIDE CHAIN
REMARK 500 10 ARG A 1 0.30 SIDE CHAIN
REMARK 500 10 ARG A 19 0.31 SIDE CHAIN
REMARK 500 10 ARG A 38 0.28 SIDE CHAIN
REMARK 500 11 ARG A 1 0.32 SIDE CHAIN
REMARK 500 11 ARG A 19 0.30 SIDE CHAIN
REMARK 500 11 ARG A 38 0.26 SIDE CHAIN
REMARK 500 12 ARG A 1 0.14 SIDE CHAIN
REMARK 500 12 ARG A 19 0.17 SIDE CHAIN
REMARK 500 12 ARG A 38 0.29 SIDE CHAIN
REMARK 500 13 ARG A 1 0.27 SIDE CHAIN
REMARK 500 13 ARG A 19 0.31 SIDE CHAIN
REMARK 500 13 ARG A 38 0.11 SIDE CHAIN
REMARK 500 14 ARG A 1 0.29 SIDE CHAIN
REMARK 500 14 ARG A 19 0.11 SIDE CHAIN
REMARK 500 14 ARG A 38 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: BIN
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: BINDING SITE TO NIDOGEN.
DBREF 1TLE A 1 58 UNP P02468 LAMC1_MOUSE 824 881
SEQRES 1 A 58 ARG PRO CYS GLN CYS ASN ASP ASN ILE ASP PRO ASN ALA
SEQRES 2 A 58 VAL GLY ASN CYS ASN ARG LEU THR GLY GLU CYS LEU LYS
SEQRES 3 A 58 CYS ILE TYR ASN THR ALA GLY PHE TYR CYS ASP ARG CYS
SEQRES 4 A 58 LYS GLU GLY PHE PHE GLY ASN PRO LEU ALA PRO ASN PRO
SEQRES 5 A 58 ALA ASP LYS CYS LYS ALA
HELIX 1 1 PRO A 52 ASP A 54 5 3
SHEET 1 A 2 THR A 31 ALA A 32 0
SHEET 2 A 2 ARG A 38 CYS A 39 -1 N ARG A 38 O ALA A 32
SHEET 1 B 2 PHE A 44 GLY A 45 0
SHEET 2 B 2 CYS A 56 LYS A 57 -1 O LYS A 57 N PHE A 44
SSBOND 1 CYS A 3 CYS A 17 1555 1555 2.02
SSBOND 2 CYS A 5 CYS A 24 1555 1555 2.02
SSBOND 3 CYS A 27 CYS A 36 1555 1555 2.02
SSBOND 4 CYS A 39 CYS A 56 1555 1555 2.02
SITE 1 BIN 7 ASN A 8 ILE A 9 ASP A 10 PRO A 11
SITE 2 BIN 7 ASN A 12 ALA A 13 VAL A 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 - 2 20 Bytes