Header list of 1pe3.pdb file
Complete list - b 23 2 Bytes
HEADER CELL CYCLE 21-MAY-03 1PE3
TITLE SOLUTION STRUCTURE OF THE DISULPHIDE-LINKED DIMER OF HUMAN INTESTINAL
TITLE 2 TREFOIL FACTOR (TFF3)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TREFOIL FACTOR 3;
COMPND 3 CHAIN: 1, 2;
COMPND 4 SYNONYM: INTESTINAL TREFOIL FACTOR, HP1.B;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TFF3 OR ITF OR TFI;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS INTESTINAL TREFOIL FACTOR, ITF, TREFOIL FACTOR FAMILY, TFF3, TFF3
KEYWDS 2 DIMER, TREFOIL MOTIF, SOLUTION STRUCTURE, NMR SPECTROSCOPY, CELL
KEYWDS 3 CYCLE
EXPDTA SOLUTION NMR
NUMMDL 47
AUTHOR F.W.MUSKETT,F.E.MAY,B.R.WESTLEY,J.FEENEY
REVDAT 3 23-FEB-22 1PE3 1 REMARK
REVDAT 2 24-FEB-09 1PE3 1 VERSN
REVDAT 1 09-MAR-04 1PE3 0
JRNL AUTH F.W.MUSKETT,F.E.MAY,B.R.WESTLEY,J.FEENEY
JRNL TITL SOLUTION STRUCTURE OF THE DISULFIDE-LINKED DIMER OF HUMAN
JRNL TITL 2 INTESTINAL TREFOIL FACTOR (TFF3): THE INTERMOLECULAR
JRNL TITL 3 ORIENTATION AND INTERACTIONS ARE MARKEDLY DIFFERENT FROM
JRNL TITL 4 THOSE OF OTHER DIMERIC TREFOIL PROTEINS.
JRNL REF BIOCHEMISTRY V. 42 15139 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 14690424
JRNL DOI 10.1021/BI030182K
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUNTERT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PE3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019264.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 100MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.0MM TFF3 U-15N; 50MM PHOSPHATE
REMARK 210 BUFFER PH 6.8; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 47
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 1, 2
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 O CYS 1 31 H CYS 1 36 1.60
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 TYR 1 3 86.35 -29.96
REMARK 500 1 VAL 1 4 -47.94 -136.41
REMARK 500 1 SER 1 7 -145.60 -108.48
REMARK 500 1 ASN 1 9 -34.54 89.93
REMARK 500 1 VAL 1 13 166.43 -40.61
REMARK 500 1 ALA 1 15 52.79 85.47
REMARK 500 1 LYS 1 16 45.10 172.34
REMARK 500 1 ASP 1 17 11.11 -155.03
REMARK 500 1 ASP 1 20 88.29 34.32
REMARK 500 1 LYS 1 29 -26.85 -178.36
REMARK 500 1 ASP 1 39 -83.45 -91.12
REMARK 500 1 SER 1 40 -16.61 89.14
REMARK 500 1 CYS 1 48 103.81 -170.81
REMARK 500 1 PRO 1 51 -97.51 -75.03
REMARK 500 1 LEU 1 52 31.55 -92.37
REMARK 500 1 GLU 1 54 -27.99 -39.20
REMARK 500 1 ALA 1 55 -73.87 -41.34
REMARK 500 1 CYS 1 57 -64.03 -104.98
REMARK 500 1 GLU 2 2 49.59 -88.49
REMARK 500 1 VAL 2 4 -50.56 -125.85
REMARK 500 1 SER 2 7 -161.65 -106.89
REMARK 500 1 ALA 2 8 85.22 -66.32
REMARK 500 1 ASN 2 9 -27.65 166.47
REMARK 500 1 VAL 2 13 167.18 -42.67
REMARK 500 1 PRO 2 14 27.84 -74.99
REMARK 500 1 ALA 2 15 72.77 49.90
REMARK 500 1 LYS 2 16 41.66 164.86
REMARK 500 1 ASP 2 17 13.20 -161.81
REMARK 500 1 ASP 2 20 86.65 33.58
REMARK 500 1 PRO 2 28 47.91 -74.96
REMARK 500 1 LYS 2 29 -17.74 -177.95
REMARK 500 1 ASP 2 39 -83.33 -81.48
REMARK 500 1 SER 2 40 -24.03 86.83
REMARK 500 1 CYS 2 48 101.16 -168.89
REMARK 500 1 LYS 2 50 67.87 -116.78
REMARK 500 1 PRO 2 51 -105.56 -75.02
REMARK 500 1 LEU 2 52 40.81 -94.30
REMARK 500 1 GLU 2 54 -28.47 -37.77
REMARK 500 1 ALA 2 55 -70.35 -30.40
REMARK 500 1 CYS 2 57 -63.55 -92.88
REMARK 500 2 GLU 1 2 -129.60 -86.95
REMARK 500 2 VAL 1 4 -57.00 -125.66
REMARK 500 2 LEU 1 6 26.56 -145.85
REMARK 500 2 PRO 1 14 29.05 -75.03
REMARK 500 2 LYS 1 16 31.33 -169.63
REMARK 500 2 ASP 1 17 16.61 -157.87
REMARK 500 2 ASP 1 20 86.41 29.84
REMARK 500 2 LYS 1 29 -21.86 177.97
REMARK 500 2 ASP 1 39 -83.61 -91.11
REMARK 500 2 SER 1 40 -17.17 88.61
REMARK 500
REMARK 500 THIS ENTRY HAS 1622 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E9T RELATED DB: PDB
REMARK 900 MONOMERIC FORM OF THE PROTEIN
DBREF 1PE3 1 1 59 UNP Q07654 TFF3_HUMAN 22 80
DBREF 1PE3 2 1 59 UNP Q07654 TFF3_HUMAN 22 80
SEQRES 1 1 59 GLU GLU TYR VAL GLY LEU SER ALA ASN GLN CYS ALA VAL
SEQRES 2 1 59 PRO ALA LYS ASP ARG VAL ASP CYS GLY TYR PRO HIS VAL
SEQRES 3 1 59 THR PRO LYS GLU CYS ASN ASN ARG GLY CYS CYS PHE ASP
SEQRES 4 1 59 SER ARG ILE PRO GLY VAL PRO TRP CYS PHE LYS PRO LEU
SEQRES 5 1 59 GLN GLU ALA GLU CYS THR PHE
SEQRES 1 2 59 GLU GLU TYR VAL GLY LEU SER ALA ASN GLN CYS ALA VAL
SEQRES 2 2 59 PRO ALA LYS ASP ARG VAL ASP CYS GLY TYR PRO HIS VAL
SEQRES 3 2 59 THR PRO LYS GLU CYS ASN ASN ARG GLY CYS CYS PHE ASP
SEQRES 4 2 59 SER ARG ILE PRO GLY VAL PRO TRP CYS PHE LYS PRO LEU
SEQRES 5 2 59 GLN GLU ALA GLU CYS THR PHE
HELIX 1 1 ASN 1 9 VAL 1 13 5 5
HELIX 2 2 GLU 1 30 GLY 1 35 1 6
HELIX 3 3 LEU 1 52 GLU 1 56 5 5
HELIX 4 4 ASN 2 9 VAL 2 13 5 5
HELIX 5 5 GLU 2 30 GLY 2 35 1 6
HELIX 6 6 LEU 2 52 GLU 2 56 5 5
SSBOND 1 CYS 1 11 CYS 1 37 1555 1555 1.87
SSBOND 2 CYS 1 21 CYS 1 36 1555 1555 1.87
SSBOND 3 CYS 1 31 CYS 1 48 1555 1555 1.82
SSBOND 4 CYS 1 57 CYS 2 57 1555 1555 1.72
SSBOND 5 CYS 2 11 CYS 2 37 1555 1555 1.97
SSBOND 6 CYS 2 21 CYS 2 36 1555 1555 2.04
SSBOND 7 CYS 2 31 CYS 2 48 1555 1555 1.92
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