Header list of 1u62.pdb file
Complete list - 24 20 Bytes
HEADER TRANSPORT PROTEIN 29-JUL-04 1U62
TITLE NMR STRUCTURE ANALYSIS OF THE LACTOFERRIN-BASED PEPTIDE FQWQRNIRKVR IN
TITLE 2 COMPLEX WITH LIPOPOLYSACCHARIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LACTOFERRIN-BASED PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LF11;
COMPND 5 SYNONYM: LACTOFERRIN,GROWTH-INHIBITING PROTEIN 12,TALALACTOFERRIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 OTHER_DETAILS: HUMAN LACTOFERRIN-BASED PEPTIDE FQWQRNIRKVR
KEYWDS HUMAN LACTOFERRICIN, PEPTIDE-LIPOPOLYSACCHARIDE COMPLEX, TRANFERRED
KEYWDS 2 NOE, TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 12
AUTHOR B.JAPELJ,P.PRISTOVSEK,A.MAJERLE,R.JERALA
REVDAT 4 24-JUN-20 1U62 1 COMPND SOURCE REMARK DBREF
REVDAT 4 2 1 SEQADV HET HETNAM FORMUL
REVDAT 4 3 1 LINK
REVDAT 3 24-FEB-09 1U62 1 VERSN
REVDAT 2 03-MAY-05 1U62 1 JRNL
REVDAT 1 22-MAR-05 1U62 0
JRNL AUTH B.JAPELJ,P.PRISTOVSEK,A.MAJERLE,R.JERALA
JRNL TITL STRUCTURAL ORIGIN OF ENDOTOXIN NEUTRALIZATION AND
JRNL TITL 2 ANTIMICROBIAL ACTIVITY OF A LACTOFERRIN-BASED PEPTIDE
JRNL REF J.BIOL.CHEM. V. 280 16955 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15687491
JRNL DOI 10.1074/JBC.M500266200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, DISCOVER 97
REMARK 3 AUTHORS : GUENTHERT ET AL. (DYANA), ACCELRYS INC. (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 109 MEANINGFUL NOE DISTANCE RESTRAINTS
REMARK 4
REMARK 4 1U62 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000023290.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 20
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2MM LACFOTEFFICIN; 20MM SODIUM
REMARK 210 PHOSPHATE BUFFER (PH=5.5); 95%
REMARK 210 H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
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 : SIMULATED ANNEALING IN TORSION
REMARK 210 ANGLE SPACE; ENERGY MINIMIZATION
REMARK 210 IN A TRUE FORCE FIELD
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 12
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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: 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 ASN A 6 91.53 -48.97
REMARK 500 1 ARG A 8 -73.15 -78.59
REMARK 500 2 ASN A 6 92.56 -46.22
REMARK 500 2 ARG A 8 -152.70 -77.19
REMARK 500 3 ASN A 6 92.82 -39.70
REMARK 500 4 ASN A 6 92.90 -45.33
REMARK 500 4 ARG A 8 -163.77 -74.91
REMARK 500 4 LYS A 9 171.53 -49.79
REMARK 500 5 TRP A 3 87.08 -59.70
REMARK 500 5 GLN A 4 -34.25 -37.40
REMARK 500 5 ASN A 6 72.52 -65.05
REMARK 500 6 GLN A 2 97.04 -63.75
REMARK 500 6 GLN A 4 -70.93 -56.43
REMARK 500 6 ASN A 6 81.88 -64.12
REMARK 500 6 ARG A 8 82.17 -60.19
REMARK 500 6 LYS A 9 56.73 36.41
REMARK 500 7 GLN A 2 95.81 -65.13
REMARK 500 7 GLN A 4 -79.01 -38.76
REMARK 500 7 ASN A 6 87.87 -55.50
REMARK 500 7 ARG A 8 -152.23 -58.76
REMARK 500 8 ASN A 6 72.71 -64.83
REMARK 500 8 ARG A 8 55.37 -158.00
REMARK 500 9 ASN A 6 73.25 -66.28
REMARK 500 10 ASN A 6 73.68 -64.98
REMARK 500 10 ARG A 8 -152.30 35.42
REMARK 500 11 ASN A 6 90.06 -52.63
REMARK 500 11 ARG A 8 36.32 37.79
REMARK 500 12 ASN A 6 89.15 -55.44
REMARK 500 12 ARG A 8 -170.10 -53.31
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 12
DBREF 1U62 A 1 11 UNP P02788 TRFL_HUMAN 39 49
SEQADV 1U62 ILE A 7 UNP P02788 MET 45 CONFLICT
SEQADV 1U62 NH2 A 12 UNP P02788 EXPRESSION TAG
SEQRES 1 A 12 PHE GLN TRP GLN ARG ASN ILE ARG LYS VAL ARG NH2
HET NH2 A 12 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
LINK C ARG A 11 N NH2 A 12 1555 1555 1.33
SITE 1 AC1 2 VAL A 10 ARG A 11
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 - 24 20 Bytes