Header list of 1kco.pdb file
Complete list - 23 20 Bytes
HEADER PROTEIN BINDING 09-NOV-01 1KCO
TITLE STRUCTURE OF E131 ZETA PEPTIDE, A POTENT ANTAGONIST OF THE HIGH-
TITLE 2 AFFINITY IGE RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E131 ZETA PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SOLID-PHASE PEPTIDE SYNTHESIS OF A NOVEL PEPTIDE
SOURCE 4 BASED ON A NAIVE PHAGE-PEPTIDE LIBRARY THAT WAS SORTED FOR BINDING
SOURCE 5 TO THE HIGH-AFFINITY IGE RECEPTOR
KEYWDS DISULFIDE-BONDED, HELICAL, "ZETA" STRUCTURE, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.R.NAKAMURA,M.E.REYNOLDS,Y.M.CHEN,M.A.STAROVASNIK,H.B.LOWMAN
REVDAT 3 23-FEB-22 1KCO 1 REMARK LINK
REVDAT 2 24-FEB-09 1KCO 1 VERSN
REVDAT 1 06-MAR-02 1KCO 0
JRNL AUTH G.R.NAKAMURA,M.E.REYNOLDS,Y.M.CHEN,M.A.STAROVASNIK,
JRNL AUTH 2 H.B.LOWMAN
JRNL TITL STABLE "ZETA" PEPTIDES THAT ACT AS POTENT ANTAGONISTS OF THE
JRNL TITL 2 HIGH-AFFINITY IGE RECEPTOR.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 1303 2002
JRNL REFN ISSN 0027-8424
JRNL PMID 11830661
JRNL DOI 10.1073/PNAS.022635599
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, DISCOVER 98.0
REMARK 3 AUTHORS : BRUKER, INC. (XWINNMR), MOLECULAR SIMULATIONS,
REMARK 3 INC. (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 143
REMARK 3 NOE-DERIVED DISTANCE RESTRAINTS AND
REMARK 3 24 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1KCO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014816.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM E131 PEPTIDE, PH 6.0, 0.1
REMARK 210 MM NAN3, 0.1 MM DSS 85%H2O/7%D2O/
REMARK 210 8%ACETONITRILE-D3; 1 MM E131
REMARK 210 PEPTIDE, PH 6.0, 0.1 MM NAN3,
REMARK 210 0.1 MM DSS
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 2D TOCSY; 2D
REMARK 210 ROESY; 2D COSY-35
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98.0, DGII 98.0
REMARK 210 METHOD USED : HYBRID DISTANCE
REMARK 210 GEOMETRY/SIMULATED ANNEALING,
REMARK 210 THEN FURTHER REFINED BY
REMARK 210 RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING
REMARK 210 STANDARD 2D HOMONUCLEAR TECHNIQUES. 3JHNHA WERE OBTAINED BY
REMARK 210 FITTING LORENTZIAN LINES TO THE ANTIPHASE DOUBLETS OF HN-HA PEAKS
REMARK 210 IN A 2QF-COSY SPECTRUM PROCESSED TO HIGH DIGITAL RESOLUTION IN F2.
REMARK 210 3JHAHB WERE EXTRACTED FROM A COSY-35 SPECTRUM ACQUIRED IN D2O
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 2 TYR A 20 41.28 -99.31
REMARK 500 3 TYR A 20 65.96 -105.51
REMARK 500 5 GLU A 9 -61.50 -108.65
REMARK 500 5 TYR A 20 -55.02 -140.11
REMARK 500 7 GLN A 2 -60.25 -143.75
REMARK 500 9 LEU A 14 -15.88 -154.38
REMARK 500 10 TYR A 8 34.76 -99.70
REMARK 500 11 TYR A 20 -53.67 -134.43
REMARK 500 13 TYR A 20 33.33 -99.94
REMARK 500 14 TYR A 8 57.52 -99.53
REMARK 500 15 LEU A 14 -13.24 -151.35
REMARK 500 17 GLN A 2 20.77 -144.38
REMARK 500 19 GLU A 13 46.38 -96.84
REMARK 500 20 TYR A 8 59.65 -98.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 22
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KCN RELATED DB: PDB
REMARK 900 'STRUCTURE OF E109 ZETA PEPTIDE, AN ANTAGONIST OF THE HIGH-AFFINITY
REMARK 900 IGE RECEPTOR'
DBREF 1KCO A 1 22 PDB 1KCO 1KCO 1 22
SEQRES 1 A 22 VAL GLN CYS PRO HIS PHE CYS TYR GLU LEU ASP TYR GLU
SEQRES 2 A 22 LEU CYS PRO ASP VAL CYS TYR VAL NH2
HET NH2 A 22 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 PRO A 4 GLU A 9 5 6
HELIX 2 2 PRO A 16 TYR A 20 5 5
SSBOND 1 CYS A 3 CYS A 19 1555 1555 2.05
SSBOND 2 CYS A 7 CYS A 15 1555 1555 2.04
LINK C VAL A 21 N NH2 A 22 1555 1555 1.34
SITE 1 AC1 2 VAL A 18 VAL A 21
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 - 23 20 Bytes