Header list of 1xv7.pdb file
Complete list - 24 20 Bytes
HEADER METAL TRANSPORT 27-OCT-04 1XV7
TITLE SOLUTION STRUCTURE OF ANTIMICROBIAL AND ENDOTOXIN-NEUTRALIZING PEPTIDE
TITLE 2 LF11 IN DPC MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LACTOFERRIN-BASED SYNTHETIC PEPTIDE FQWQRNIRKVR;
COMPND 3 CHAIN: A;
COMPND 4 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
KEYWDS LOOP, HYDROPHOBIC CORE, METAL TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 7
AUTHOR B.JAPELJ,P.PRISTOVSEK,A.MAJERLE,R.JERALA
REVDAT 4 24-JUN-20 1XV7 1 SOURCE REMARK DBREF LINK
REVDAT 3 24-FEB-09 1XV7 1 VERSN
REVDAT 2 03-MAY-05 1XV7 1 JRNL
REVDAT 1 22-MAR-05 1XV7 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, DYANA 1.5
REMARK 3 AUTHORS : GUNTERT,P., BRAUN,W., WUTHRICH,K. (DYANA),
REMARK 3 GUNTERT,P., BRAUN,W., WUTHRICH,K. (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XV7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1000030801.
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 : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM LF11; 240MM DPC-D38, 20MM
REMARK 210 SODIUM PHOSPHATE BUFFER (PH 5.5),
REMARK 210 92% H20, 8% D20
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
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 7
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 1 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 1 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 2 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 3 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 3 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 4 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 4 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 5 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 5 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 5 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 6 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 6 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 6 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 7 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 7 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 7 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
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 ASN A 6 93.69 60.74
REMARK 500 1 VAL A 10 -57.25 -166.14
REMARK 500 2 GLN A 2 44.21 -85.47
REMARK 500 2 GLN A 4 -60.95 -159.82
REMARK 500 2 ARG A 5 17.70 54.77
REMARK 500 2 ILE A 7 -87.94 -82.88
REMARK 500 2 ARG A 8 68.45 -167.81
REMARK 500 3 GLN A 2 70.09 60.07
REMARK 500 3 ARG A 5 94.24 71.70
REMARK 500 3 ASN A 6 77.26 67.96
REMARK 500 3 ARG A 8 58.74 -98.44
REMARK 500 3 VAL A 10 99.97 74.67
REMARK 500 4 TRP A 3 -161.25 69.48
REMARK 500 4 ASN A 6 44.62 -103.31
REMARK 500 4 ARG A 8 60.50 -153.42
REMARK 500 5 ILE A 7 -75.99 -63.61
REMARK 500 6 GLN A 4 -74.21 -119.33
REMARK 500 6 ASN A 6 75.20 -162.19
REMARK 500 6 VAL A 10 -60.47 -156.74
REMARK 500 7 GLN A 2 78.16 -103.30
REMARK 500 7 ILE A 7 -70.58 -131.85
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
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XV4 RELATED DB: PDB
REMARK 900 PEPTIDE LF11 IN SDS MICELLES
DBREF 1XV7 A 1 12 PDB 1XV7 1XV7 1 12
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 1 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