Header list of 2fcg.pdb file
Complete list - 9 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 12-DEC-05 2FCG TITLE SOLUTION STRUCTURE OF THE C-TERMINAL FRAGMENT OF HUMAN LL-37 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIBACTERIAL PROTEIN FALL-39, CORE PEPTIDE; COMPND 3 CHAIN: F; COMPND 4 FRAGMENT: RESIDUES 146-170; 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 146-170 OF HUMAN SOURCE 4 FALL-39 KEYWDS LL-37; HOST DEFENSE PEPTIDE; ANTIMICROBIAL PEPTIDE, ANTIMICROBIAL KEYWDS 2 PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR G.WANG,X.LI REVDAT 3 09-MAR-22 2FCG 1 REMARK REVDAT 2 17-FEB-09 2FCG 1 AUTHOR VERSN REVDAT 1 23-MAY-06 2FCG 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 : CD SCHWIETERS, J KUSZEWSKI, N TJANDRA, GM CLORE REMARK 3 (XPLOR-NIH), CORNILESCU, FRANK DELAGLIO, AD BAX REMARK 3 (TALOS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2FCG 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_1000035713. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 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 1.0, NMRPIPE 2.1 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY 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 310 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: F 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 MODELS 1-20 REMARK 470 RES CSSEQI ATOMS REMARK 470 SER F 37 O 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 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 GLU F 16 -67.49 -147.90 REMARK 500 1 PRO F 33 173.98 -43.67 REMARK 500 1 THR F 35 71.91 43.85 REMARK 500 2 GLU F 16 -150.96 -84.74 REMARK 500 2 LEU F 31 -75.65 -66.24 REMARK 500 2 VAL F 32 71.68 53.57 REMARK 500 2 THR F 35 43.11 -175.47 REMARK 500 2 GLU F 36 -129.87 61.82 REMARK 500 3 LYS F 15 151.70 58.17 REMARK 500 3 ARG F 34 -153.19 -84.94 REMARK 500 3 THR F 35 -105.77 -78.68 REMARK 500 3 GLU F 36 -77.78 -103.29 REMARK 500 4 LEU F 31 4.49 -68.58 REMARK 500 4 VAL F 32 102.35 51.73 REMARK 500 4 PRO F 33 -92.80 -79.71 REMARK 500 4 THR F 35 85.91 37.47 REMARK 500 5 LYS F 15 -146.06 67.26 REMARK 500 5 GLU F 16 -38.95 68.16 REMARK 500 5 LEU F 31 27.11 -72.65 REMARK 500 5 GLU F 36 97.03 59.35 REMARK 500 6 LYS F 15 -119.62 -141.32 REMARK 500 6 GLU F 16 -87.63 54.07 REMARK 500 7 LYS F 15 -91.66 36.14 REMARK 500 7 GLU F 16 98.83 46.16 REMARK 500 7 ARG F 34 44.92 -96.91 REMARK 500 8 LYS F 15 173.61 -53.03 REMARK 500 8 VAL F 32 76.31 42.92 REMARK 500 8 ARG F 34 177.82 49.80 REMARK 500 8 THR F 35 -62.78 -98.73 REMARK 500 9 LEU F 31 -93.20 -62.85 REMARK 500 9 VAL F 32 75.00 26.68 REMARK 500 9 ARG F 34 141.14 -39.30 REMARK 500 9 THR F 35 64.83 -159.40 REMARK 500 10 LYS F 15 -152.00 44.00 REMARK 500 10 GLU F 16 -32.21 71.84 REMARK 500 10 ARG F 34 99.02 40.85 REMARK 500 10 THR F 35 40.32 -76.33 REMARK 500 11 LEU F 31 -127.71 -63.33 REMARK 500 11 PRO F 33 175.05 -49.70 REMARK 500 11 ARG F 34 142.58 -173.36 REMARK 500 11 THR F 35 -105.43 -75.73 REMARK 500 12 PRO F 33 -95.31 -73.15 REMARK 500 12 ARG F 34 34.68 -149.11 REMARK 500 12 GLU F 36 -168.19 -172.99 REMARK 500 13 GLU F 16 -45.50 -177.25 REMARK 500 13 VAL F 32 102.39 -37.65 REMARK 500 13 PRO F 33 -95.36 -82.72 REMARK 500 13 ARG F 34 44.11 -171.65 REMARK 500 13 THR F 35 70.54 46.86 REMARK 500 13 GLU F 36 -106.15 -64.42 REMARK 500 REMARK 500 THIS ENTRY HAS 78 RAMACHANDRAN OUTLIERS. 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: 2FBU RELATED DB: PDB DBREF 2FCG F 13 37 UNP P49913 FAL39_HUMAN 146 170 SEQRES 1 F 25 ILE GLY LYS GLU PHE LYS ARG ILE VAL GLN ARG ILE LYS SEQRES 2 F 25 ASP PHE LEU ARG ASN LEU VAL PRO ARG THR GLU SER HELIX 1 1 GLU F 16 LEU F 31 1 16 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