Header list of 1egf.pdb file
Complete list - 16 20 Bytes
HEADER GROWTH FACTOR 01-OCT-91 1EGF
TITLE SOLUTION STRUCTURE OF MURINE EPIDERMAL GROWTH FACTOR DETERMINED BY NMR
TITLE 2 SPECTROSCOPY AND REFINED BY ENERGY MINIMIZATION WITH RESTRAINTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR;
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
KEYWDS GROWTH FACTOR
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR G.T.MONTELIONE,K.WUTHRICH,H.A.SCHERAGA
REVDAT 3 16-FEB-22 1EGF 1 REMARK
REVDAT 2 24-FEB-09 1EGF 1 VERSN
REVDAT 1 31-JAN-94 1EGF 0
JRNL AUTH G.T.MONTELIONE,K.WUTHRICH,A.W.BURGESS,E.C.NICE,G.WAGNER,
JRNL AUTH 2 K.D.GIBSON,H.A.SCHERAGA
JRNL TITL SOLUTION STRUCTURE OF MURINE EPIDERMAL GROWTH FACTOR
JRNL TITL 2 DETERMINED BY NMR SPECTROSCOPY AND REFINED BY ENERGY
JRNL TITL 3 MINIMIZATION WITH RESTRAINTS.
JRNL REF BIOCHEMISTRY V. 31 236 1992
JRNL REFN ISSN 0006-2960
JRNL PMID 1731873
JRNL DOI 10.1021/BI00116A033
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.T.MONTELIONE,K.WUTHRICH,H.A.SCHERAGA
REMARK 1 TITL SEQUENCE-SPECIFIC 1H NMR ASSIGNMENTS AND IDENTIFICATION OF
REMARK 1 TITL 2 SLOWLY EXCHANGING AMIDE PROTONS IN MURINE EPIDERMAL GROWTH
REMARK 1 TITL 3 FACTOR
REMARK 1 REF BIOCHEMISTRY V. 27 2235 1988
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.T.MONTELIONE,K.WUTHRICH,E.C.NICE,A.W.BURGESS,H.A.SCHERAGA
REMARK 1 TITL SOLUTION STRUCTURE OF MURINE EPIDERMAL GROWTH FACTOR:
REMARK 1 TITL 2 DETERMINATION OF THE POLYPEPTIDE BACKBONE CHAIN-FOLD BY
REMARK 1 TITL 3 NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 84 5226 1987
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 3
REMARK 1 AUTH G.T.MONTELIONE,K.WUTHRICH,E.C.NICE,A.W.BURGESS,H.A.SCHERAGA
REMARK 1 TITL IDENTIFICATION OF TWO ANTI-PARALLEL BETA-SHEET CONFORMATIONS
REMARK 1 TITL 2 IN THE SOLUTION STRUCTURE OF MURINE EPIDERMAL GROWTH FACTOR
REMARK 1 TITL 3 BY PROTON MAGNETIC RESONANCE
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 83 8594 1986
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISMAN
REMARK 3 AUTHORS : BRAUN,GO
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EGF 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_1000173044.
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 : 16
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 6 89.11 -178.07
REMARK 500 1 TYR A 10 -98.72 -92.26
REMARK 500 1 ASP A 11 88.14 153.89
REMARK 500 1 TYR A 13 -34.97 -34.48
REMARK 500 1 ASN A 16 -50.93 80.33
REMARK 500 1 LEU A 26 24.08 -158.08
REMARK 500 1 CYS A 33 -144.47 -111.32
REMARK 500 1 ILE A 35 132.51 -37.98
REMARK 500 1 SER A 38 -164.81 179.88
REMARK 500 1 ARG A 41 -87.68 -166.43
REMARK 500 1 CYS A 42 18.21 -148.89
REMARK 500 1 THR A 44 69.43 -66.21
REMARK 500 1 ARG A 45 55.83 -68.56
REMARK 500 1 LEU A 47 -114.64 -82.82
REMARK 500 1 ARG A 48 87.96 71.35
REMARK 500 1 TRP A 49 99.66 -42.82
REMARK 500 1 TRP A 50 65.05 -109.28
REMARK 500 2 CYS A 6 94.94 -168.60
REMARK 500 2 ASP A 11 80.42 58.10
REMARK 500 2 ASN A 16 56.42 21.81
REMARK 500 2 LEU A 26 22.74 -154.49
REMARK 500 2 THR A 30 -166.52 -129.84
REMARK 500 2 CYS A 33 -160.89 -64.45
REMARK 500 2 ASP A 40 -59.97 70.31
REMARK 500 2 ARG A 41 -71.30 -100.20
REMARK 500 2 CYS A 42 42.79 157.36
REMARK 500 2 ASP A 46 -148.02 -80.92
REMARK 500 2 LEU A 47 -95.26 -131.70
REMARK 500 2 ARG A 48 75.04 77.79
REMARK 500 2 TRP A 49 94.48 42.06
REMARK 500 3 CYS A 6 101.42 -179.70
REMARK 500 3 ASN A 16 -55.83 70.02
REMARK 500 3 GLU A 24 -174.74 46.75
REMARK 500 3 SER A 25 -33.68 83.60
REMARK 500 3 LEU A 26 12.94 -145.75
REMARK 500 3 CYS A 33 -106.67 -84.03
REMARK 500 3 SER A 38 -140.68 -177.65
REMARK 500 3 ASP A 40 -35.40 87.92
REMARK 500 3 ARG A 41 -85.93 -128.26
REMARK 500 3 CYS A 42 35.49 176.86
REMARK 500 3 ASP A 46 -91.73 -40.43
REMARK 500 3 ARG A 48 51.05 85.23
REMARK 500 3 GLU A 51 -55.52 -141.14
REMARK 500 4 CYS A 6 97.61 177.90
REMARK 500 4 ASP A 11 47.56 -105.04
REMARK 500 4 LEU A 26 21.02 -155.03
REMARK 500 4 THR A 30 -165.17 -122.27
REMARK 500 4 CYS A 33 -159.36 -76.27
REMARK 500 4 ASP A 40 -66.83 67.89
REMARK 500 4 ARG A 41 -71.77 -96.99
REMARK 500
REMARK 500 THIS ENTRY HAS 205 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 41 0.30 SIDE CHAIN
REMARK 500 1 ARG A 45 0.28 SIDE CHAIN
REMARK 500 1 ARG A 48 0.30 SIDE CHAIN
REMARK 500 1 ARG A 53 0.30 SIDE CHAIN
REMARK 500 2 ARG A 41 0.30 SIDE CHAIN
REMARK 500 2 ARG A 45 0.30 SIDE CHAIN
REMARK 500 2 ARG A 48 0.30 SIDE CHAIN
REMARK 500 2 ARG A 53 0.30 SIDE CHAIN
REMARK 500 3 ARG A 41 0.30 SIDE CHAIN
REMARK 500 3 ARG A 45 0.30 SIDE CHAIN
REMARK 500 3 ARG A 48 0.30 SIDE CHAIN
REMARK 500 3 ARG A 53 0.30 SIDE CHAIN
REMARK 500 4 ARG A 41 0.30 SIDE CHAIN
REMARK 500 4 ARG A 45 0.30 SIDE CHAIN
REMARK 500 4 ARG A 48 0.29 SIDE CHAIN
REMARK 500 4 ARG A 53 0.30 SIDE CHAIN
REMARK 500 5 ARG A 41 0.30 SIDE CHAIN
REMARK 500 5 ARG A 45 0.30 SIDE CHAIN
REMARK 500 5 ARG A 48 0.29 SIDE CHAIN
REMARK 500 5 ARG A 53 0.30 SIDE CHAIN
REMARK 500 6 ARG A 41 0.30 SIDE CHAIN
REMARK 500 6 ARG A 45 0.30 SIDE CHAIN
REMARK 500 6 ARG A 48 0.30 SIDE CHAIN
REMARK 500 6 ARG A 53 0.29 SIDE CHAIN
REMARK 500 7 ARG A 41 0.30 SIDE CHAIN
REMARK 500 7 ARG A 45 0.30 SIDE CHAIN
REMARK 500 7 ARG A 48 0.30 SIDE CHAIN
REMARK 500 7 ARG A 53 0.30 SIDE CHAIN
REMARK 500 8 ARG A 41 0.30 SIDE CHAIN
REMARK 500 8 ARG A 45 0.30 SIDE CHAIN
REMARK 500 8 ARG A 48 0.30 SIDE CHAIN
REMARK 500 8 ARG A 53 0.26 SIDE CHAIN
REMARK 500 9 ARG A 41 0.30 SIDE CHAIN
REMARK 500 9 ARG A 45 0.30 SIDE CHAIN
REMARK 500 9 ARG A 48 0.30 SIDE CHAIN
REMARK 500 9 ARG A 53 0.29 SIDE CHAIN
REMARK 500 10 ARG A 41 0.30 SIDE CHAIN
REMARK 500 10 ARG A 45 0.30 SIDE CHAIN
REMARK 500 10 ARG A 48 0.30 SIDE CHAIN
REMARK 500 10 ARG A 53 0.27 SIDE CHAIN
REMARK 500 11 ARG A 41 0.30 SIDE CHAIN
REMARK 500 11 ARG A 45 0.30 SIDE CHAIN
REMARK 500 11 ARG A 48 0.28 SIDE CHAIN
REMARK 500 11 ARG A 53 0.30 SIDE CHAIN
REMARK 500 12 ARG A 41 0.30 SIDE CHAIN
REMARK 500 12 ARG A 45 0.30 SIDE CHAIN
REMARK 500 12 ARG A 48 0.30 SIDE CHAIN
REMARK 500 12 ARG A 53 0.30 SIDE CHAIN
REMARK 500 13 ARG A 41 0.30 SIDE CHAIN
REMARK 500 13 ARG A 45 0.30 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 64 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1EGF A 1 53 UNP P01132 EGF_MOUSE 977 1029
SEQRES 1 A 53 ASN SER TYR PRO GLY CYS PRO SER SER TYR ASP GLY TYR
SEQRES 2 A 53 CYS LEU ASN GLY GLY VAL CYS MET HIS ILE GLU SER LEU
SEQRES 3 A 53 ASP SER TYR THR CYS ASN CYS VAL ILE GLY TYR SER GLY
SEQRES 4 A 53 ASP ARG CYS GLN THR ARG ASP LEU ARG TRP TRP GLU LEU
SEQRES 5 A 53 ARG
SHEET 1 A 3 SER A 2 TYR A 3 0
SHEET 2 A 3 VAL A 19 ILE A 23 -1 O HIS A 22 N TYR A 3
SHEET 3 A 3 TYR A 29 ASN A 32 -1 N THR A 30 O MET A 21
SSBOND 1 CYS A 6 CYS A 20 1555 1555 1.92
SSBOND 2 CYS A 14 CYS A 31 1555 1555 1.53
SSBOND 3 CYS A 33 CYS A 42 1555 1555 1.86
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 - 16 20 Bytes