HEADER GROWTH FACTOR 30-NOV-95 1HAF
TITLE HEREGULIN-ALPHA EPIDERMAL GROWTH FACTOR-LIKE DOMAIN, NMR, MINIMIZED
TITLE 2 AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEREGULIN-ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EPIDERMAL GROWTH FACTOR-LIKE DOMAIN;
COMPND 5 SYNONYM: NEU DIFFERENTIATION FACTOR (RAT), ACETYLCHOLINE RECEPTOR
COMPND 6 INDUCING ACTIVITY (CHICKEN), GLIAL GROWTH FACTOR (HUMAN), NEUREGULIN;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GROWTH FACTOR
EXPDTA SOLUTION NMR
AUTHOR N.E.JACOBSEN,N.J.SKELTON,W.J.FAIRBROTHER
REVDAT 3 23-FEB-22 1HAF 1 REMARK
REVDAT 2 24-FEB-09 1HAF 1 VERSN
REVDAT 1 11-JUL-96 1HAF 0
JRNL AUTH N.E.JACOBSEN,N.ABADI,M.X.SLIWKOWSKI,D.REILLY,N.J.SKELTON,
JRNL AUTH 2 W.J.FAIRBROTHER
JRNL TITL HIGH-RESOLUTION SOLUTION STRUCTURE OF THE EGF-LIKE DOMAIN OF
JRNL TITL 2 HEREGULIN-ALPHA.
JRNL REF BIOCHEMISTRY V. 35 3402 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8639490
JRNL DOI 10.1021/BI952626L
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.E.HOLMES,M.X.SLIWKOWSKI,R.W.AKITA,W.J.HENZEL,J.LEE,
REMARK 1 AUTH 2 J.W.PARK,D.YANSURA,N.ABADI,H.RAAB,G.D.LEWIS,ET AL.
REMARK 1 TITL IDENTIFICATION OF HEREGULIN, A SPECIFIC ACTIVATOR OF
REMARK 1 TITL 2 P185ERBB2
REMARK 1 REF SCIENCE V. 256 1205 1992
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : BIOSYM TECHNOLOGIES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HAF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173743.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 4.5
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 : 1
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 SER A 27 -57.84 -150.37
REMARK 500 SER A 30 56.54 -172.13
REMARK 500 PRO A 50 108.54 -53.72
REMARK 500 LYS A 52 -163.98 -101.72
REMARK 500 GLN A 54 73.06 -62.84
REMARK 500 ASN A 55 -41.29 -174.88
REMARK 500 GLU A 60 43.51 -80.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HAE RELATED DB: PDB
DBREF 1HAF A 1 63 UNP Q02297 NRG1_HUMAN 176 238
SEQRES 1 A 63 SER HIS LEU VAL LYS CYS ALA GLU LYS GLU LYS THR PHE
SEQRES 2 A 63 CYS VAL ASN GLY GLY GLU CYS PHE MET VAL LYS ASP LEU
SEQRES 3 A 63 SER ASN PRO SER ARG TYR LEU CYS LYS CYS GLN PRO GLY
SEQRES 4 A 63 PHE THR GLY ALA ARG CYS THR GLU ASN VAL PRO MET LYS
SEQRES 5 A 63 VAL GLN ASN GLN GLU LYS ALA GLU GLU LEU TYR
HELIX 1 1 GLU A 8 PHE A 13 1 6
SHEET 1 A 3 HIS A 2 LYS A 5 0
SHEET 2 A 3 GLU A 19 LYS A 24 -1 N LYS A 24 O HIS A 2
SHEET 3 A 3 TYR A 32 LYS A 35 -1 N LYS A 35 O GLU A 19
SSBOND 1 CYS A 6 CYS A 20 1555 1555 2.06
SSBOND 2 CYS A 14 CYS A 34 1555 1555 2.05
SSBOND 3 CYS A 36 CYS A 45 1555 1555 2.04
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
(ATOM LINES ARE NOT SHOWN.)
END