Header list of 1kcn.pdb file
Complete list - 23 20 Bytes
HEADER PROTEIN BINDING 09-NOV-01 1KCN TITLE STRUCTURE OF E109 ZETA PEPTIDE, AN ANTAGONIST OF THE HIGH-AFFINITY IGE TITLE 2 RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: E109 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 1KCN 1 REMARK LINK REVDAT 2 24-FEB-09 1KCN 1 VERSN REVDAT 1 06-MAR-02 1KCN 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 101 REMARK 3 NOE-DERIVED DISTANCE RESTRAINTS, REMARK 3 18 DIHEDRAL ANGLE RESTRAINTS, AND 12 DISTANT REMARK 3 RESTRAINTS FROM 6 HYDROGEN BONDS. REMARK 4 REMARK 4 1KCN 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_1000014815. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 288 REMARK 210 PH : 5.4 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM E109 PEPTIDE, 92% H2O/8% REMARK 210 D2O, PH 5.4, 0.1 MM NAN3, 0.1 MM REMARK 210 DSS; 2MM E109 PEPTIDE, 100% D2O, REMARK 210 PH 5.4, 0.1 MM NAN3, 0.1 MM DSS REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 2D TOCSY; 2D REMARK 210 COSY-35; 2D ROESY 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 REMARK 210 IN A 2QF-COSY SPECTRUM PROCESSED TO HIGH DIGITAL RESOLUTION IN F2. REMARK 210 3JHAHB WERE EXTRACTED FROM A COSY-35 REMARK 210 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 1 LYS A 12 -65.55 -138.10 REMARK 500 1 ALA A 13 115.58 -160.03 REMARK 500 1 LEU A 14 44.15 -153.06 REMARK 500 3 LEU A 2 46.17 -153.47 REMARK 500 3 LYS A 12 70.77 -162.43 REMARK 500 4 ALA A 13 42.62 -144.91 REMARK 500 6 TYR A 8 -57.01 -137.99 REMARK 500 6 ALA A 13 73.03 -160.64 REMARK 500 6 LEU A 14 43.36 -151.92 REMARK 500 8 CYS A 7 24.06 -77.17 REMARK 500 8 TYR A 8 -55.56 -148.77 REMARK 500 8 ALA A 13 53.05 -144.13 REMARK 500 9 ALA A 13 37.71 -140.73 REMARK 500 10 ALA A 13 39.63 -81.32 REMARK 500 11 LEU A 14 59.91 -90.99 REMARK 500 12 LYS A 12 -99.26 -119.30 REMARK 500 13 LEU A 14 54.09 -108.07 REMARK 500 14 LYS A 12 78.22 -161.41 REMARK 500 14 ALA A 13 43.57 -80.57 REMARK 500 16 LEU A 14 55.04 -101.99 REMARK 500 18 ALA A 13 42.54 -74.31 REMARK 500 19 LEU A 14 33.05 -163.18 REMARK 500 20 LEU A 14 -28.75 -153.90 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: 1KCO RELATED DB: PDB REMARK 900 'STRUCTURE OF E131 ZETA PEPTIDE, A POTENT ANTAGONIST OF THE HIGH- REMARK 900 AFFINITY IGE RECEPTOR' DBREF 1KCN A 1 22 PDB 1KCN 1KCN 1 22 SEQRES 1 A 22 ALA LEU CYS PRO ALA VAL CYS TYR VAL GLY GLY LYS ALA 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 TYR A 8 5 5 HELIX 2 2 PRO A 16 VAL A 21 1 6 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 TYR A 20 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