Header list of 1gk5.pdb file
Complete list - 28 20 Bytes
HEADER GROWTH FACTOR 08-AUG-01 1GK5
TITLE SOLUTION STRUCTURE THE MEGF/TGFALPHA44-50 CHIMERIC GROWTH FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRO-EPIDERMAL GROWTH FACTOR,PROTRANSFORMING GROWTH FACTOR
COMPND 3 ALPHA;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 977-1018,UNP RESIDUES 83-89;
COMPND 6 SYNONYM: EGF;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: THE PROTEIN IS A CHIMERA OF EPIDERMAL GROWTH FACTOR
COMPND 9 RESIDUES 977-1018 AND HUMAN TRANSFORMING GROWTH FACTOR ALPHA RESIDUES
COMPND 10 83-89,THE PROTEIN IS A CHIMERA OF EPIDERMAL GROWTH FACTOR RESIDUES
COMPND 11 977-1018 AND HUMAN TRANSFORMING GROWTH FACTOR ALPHA RESIDUES 83-89
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE, HUMAN;
SOURCE 4 ORGANISM_TAXID: 10090, 9606;
SOURCE 5 GENE: EGF, TGFA;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: PICHIA PASTORIS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PPIC9
KEYWDS GROWTH FACTOR, EGF GROWTH FACTOR, CHIMERIC
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR S.G.CHAMBERLIN,L.BRENNAN,S.M.PUDDICOMBE,D.E.DAVIES,D.L.TURNER
REVDAT 3 28-MAR-18 1GK5 1 COMPND SOURCE DBREF
REVDAT 2 24-FEB-09 1GK5 1 VERSN
REVDAT 1 08-AUG-02 1GK5 0
JRNL AUTH S.CHAMBERLIN,L.BRENNAN,S.PUDDICOMBE,D.DAVIES,D.TURNER
JRNL TITL SOLUTION STRUCTURE OF THE MEGF/TGFALPHA44-50 CHIMERIC GROWTH
JRNL TITL 2 FACTOR.
JRNL REF EUR.J.BIOCHEM. V. 268 6247 2001
JRNL REFN ISSN 0014-2956
JRNL PMID 11733021
JRNL DOI 10.1046/J.0014-2956.2001.02581.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.M.PUDDICOMBE,L.WOOD,S.G.CHAMBERLIN,D.E.DAVIES
REMARK 1 TITL THE INTERACTION OF AN EPIDERMAL GROWTH FACTOR/ TRANSFORMING
REMARK 1 TITL 2 GROWTH FACTOR ALPHA TAIL CHIMERA WITH THE HUMAN EPIDERMAL
REMARK 1 TITL 3 GROWTH FACTOR RECEPTOR REVEALS UNEXPECTED COMPLEXITIES
REMARK 1 REF J.BIOL.CHEM. V. 271 30392 1996
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 8940002
REMARK 1 DOI 10.1074/JBC.271.48.30392
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : INDYANA
REMARK 3 AUTHORS : BRENNAN L, TURNER DL, MESSIAS AM, TEODORO ML,
REMARK 3 LEGALL J, SANTOS H, XAVIER AX.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GK5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1290008426.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-1H-NOESY 2D-1H-TOCSY 2D-1H
REMARK 210 -COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : VXR500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : INDYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS WITH
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HG SER A 25 H LEU A 26 1.03
REMARK 500 HG SER A 28 H TYR A 29 1.30
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 11 65.22 77.15
REMARK 500 1 ASN A 16 86.28 45.49
REMARK 500 1 SER A 25 -83.33 -63.67
REMARK 500 1 SER A 38 -32.19 -152.19
REMARK 500 1 CYS A 42 27.72 43.93
REMARK 500 1 ASP A 46 53.20 -113.21
REMARK 500 2 TYR A 3 -42.21 -169.46
REMARK 500 2 CYS A 6 170.04 -55.13
REMARK 500 2 ASP A 11 57.97 77.77
REMARK 500 2 ASN A 16 85.72 44.63
REMARK 500 2 SER A 25 -83.17 -62.03
REMARK 500 2 SER A 38 -23.20 -151.19
REMARK 500 2 CYS A 42 28.13 46.54
REMARK 500 2 ASP A 46 54.11 -109.52
REMARK 500 3 ASP A 11 65.38 77.15
REMARK 500 3 ASN A 16 85.58 44.20
REMARK 500 3 SER A 25 -82.39 -64.25
REMARK 500 3 SER A 38 -34.13 -148.50
REMARK 500 3 ASP A 40 119.63 -38.65
REMARK 500 3 CYS A 42 29.21 44.84
REMARK 500 3 HIS A 44 94.57 -55.93
REMARK 500 4 SER A 2 -26.04 -171.23
REMARK 500 4 TYR A 3 60.99 -169.96
REMARK 500 4 ASP A 11 83.45 77.09
REMARK 500 4 ASN A 16 84.64 43.85
REMARK 500 4 SER A 25 -81.75 -67.42
REMARK 500 4 ASP A 46 52.04 -146.56
REMARK 500 4 LEU A 48 -61.03 -147.85
REMARK 500 5 SER A 2 -22.73 175.37
REMARK 500 5 ASP A 11 57.38 76.86
REMARK 500 5 ASN A 16 86.91 45.87
REMARK 500 5 SER A 25 -83.11 -62.31
REMARK 500 5 SER A 38 -154.03 -139.35
REMARK 500 5 CYS A 42 22.63 42.42
REMARK 500 5 HIS A 44 91.95 -56.56
REMARK 500 5 ASP A 46 52.40 -140.89
REMARK 500 6 ASP A 11 64.31 77.34
REMARK 500 6 ASN A 16 89.12 49.33
REMARK 500 6 MET A 21 97.48 -166.33
REMARK 500 6 SER A 25 -76.42 -66.00
REMARK 500 6 SER A 38 -157.53 -143.40
REMARK 500 6 ASP A 40 108.43 -58.21
REMARK 500 6 HIS A 44 96.18 -65.55
REMARK 500 6 ASP A 46 53.09 -143.03
REMARK 500 6 LEU A 47 28.64 -77.42
REMARK 500 6 LEU A 48 96.67 62.13
REMARK 500 7 SER A 2 27.85 -171.79
REMARK 500 7 ASP A 11 56.63 77.10
REMARK 500 7 ASN A 16 86.39 46.73
REMARK 500 7 SER A 25 -83.25 -64.16
REMARK 500
REMARK 500 THIS ENTRY HAS 76 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5120 RELATED DB: BMRB
DBREF 1GK5 A 1 42 UNP P01132 EGF_MOUSE 977 1018
DBREF 1GK5 A 43 49 UNP P01135 TGFA_HUMAN 83 89
SEQRES 1 A 49 ASN SER TYR PRO GLY CYS PRO SER SER TYR ASP GLY TYR
SEQRES 2 A 49 CYS LEU ASN GLY GLY VAL CYS MET HIS ILE GLU SER LEU
SEQRES 3 A 49 ASP SER TYR THR CYS ASN CYS VAL ILE GLY TYR SER GLY
SEQRES 4 A 49 ASP ARG CYS GLU HIS ALA ASP LEU LEU ALA
HELIX 1 1 GLY A 39 GLU A 43 5 5
SHEET 1 AA 2 VAL A 19 ILE A 23 0
SHEET 2 AA 2 SER A 28 ASN A 32 -1 O SER A 28 N ILE A 23
SSBOND 1 CYS A 6 CYS A 20 1555 1555 2.01
SSBOND 2 CYS A 14 CYS A 31 1555 1555 2.02
SSBOND 3 CYS A 33 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 - 28 20 Bytes