Header list of 2fbu.pdb file
Complete list - 9 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 10-DEC-05 2FBU
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL FRAGMENT OF HUMAN LL-37
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIBACTERIAL PROTEIN FALL-39, CORE PEPTIDE;
COMPND 3 CHAIN: H;
COMPND 4 FRAGMENT: RESIDUES 134-145;
COMPND 5 SYNONYM: FALL-39 PEPTIDE ANTIBIOTIC; CATIONIC ANTIMICROBIAL PROTEIN
COMPND 6 CAP-18; HCAP-18;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SEQUENCE CORRESPONDS TO RESIDUES 134-145 OF HUMAN
SOURCE 4 FALL-39
KEYWDS LL-37; HOST DEFENSE PEPTIDE; ANTIMICROBIAL PEPTIDE; AGGREGATION;
KEYWDS 2 AROMATIC-AROMATIC INTERACTION, ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 5
AUTHOR G.WANG,X.LI
REVDAT 3 09-MAR-22 2FBU 1 REMARK
REVDAT 2 17-FEB-09 2FBU 1 AUTHOR VERSN
REVDAT 1 23-MAY-06 2FBU 0
JRNL AUTH X.LI,Y.LI,H.HAN,D.W.MILLER,G.WANG
JRNL TITL SOLUTION STRUCTURES OF HUMAN LL-37 FRAGMENTS AND NMR-BASED
JRNL TITL 2 IDENTIFICATION OF A MINIMAL MEMBRANE-TARGETING ANTIMICROBIAL
JRNL TITL 3 AND ANTICANCER REGION
JRNL REF J.AM.CHEM.SOC. V. 128 5776 2006
JRNL REFN ISSN 0002-7863
JRNL PMID 16637646
JRNL DOI 10.1021/JA0584875
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 1.0, TALOS 1999
REMARK 3 AUTHORS : GM CLORE ET AL. (XPLOR-NIH), CORNILESCU, FRANK
REMARK 3 DELAGLIO, AD BAX (TALOS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FBU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000035692.
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 : 80
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2 MM PEPTIDE AND 80 MM SDS
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY;
REMARK 210 (H1, H13) HSQC; (H1, N15) HSQC
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 : PIPP 1, NMRPIPE 2.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 5
REMARK 210 CONFORMERS, SELECTION CRITERIA : AROMATIC-AROMATIC INTERACTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: A SET OF NMR DATA WAS ALSO COLLECTED AT 298 K
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: H
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 ASP H 4 H LYS H 8 1.58
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 LEU H 2 -64.97 -161.22
REMARK 500 1 LYS H 8 132.19 -174.96
REMARK 500 1 LYS H 10 -66.99 -169.80
REMARK 500 1 GLU H 11 -118.38 -76.57
REMARK 500 2 LEU H 2 -65.08 -142.83
REMARK 500 2 LYS H 10 65.04 -168.91
REMARK 500 2 GLU H 11 -118.42 -78.69
REMARK 500 3 LYS H 8 112.98 -1.84
REMARK 500 3 LYS H 10 74.18 74.58
REMARK 500 3 GLU H 11 -111.00 -78.23
REMARK 500 4 LYS H 10 -75.38 -155.60
REMARK 500 4 GLU H 11 -151.08 -63.53
REMARK 500 5 LEU H 2 -65.05 -165.91
REMARK 500 5 LYS H 8 144.34 74.69
REMARK 500 5 LYS H 10 71.53 73.42
REMARK 500 5 GLU H 11 -132.16 -83.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VM5 RELATED DB: PDB
REMARK 900 RELATED ID: 2F3A RELATED DB: PDB
REMARK 900 RELATED ID: 2FBS RELATED DB: PDB
REMARK 900 RELATED ID: 2FCG RELATED DB: PDB
DBREF 2FBU H 1 12 UNP P49913 FAL39_HUMAN 134 145
SEQRES 1 H 12 LEU LEU GLY ASP PHE PHE ARG LYS SER LYS GLU LYS
HELIX 1 1 LEU H 2 LYS H 8 1 7
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 - 9 20 Bytes