Header list of 1m4e.pdb file
Complete list - 23 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 02-JUL-02 1M4E
TITLE SOLUTION STRUCTURE OF HEPCIDIN-20
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPCIDIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HEPCIDIN-20 (RESIDUES 65-84);
COMPND 5 SYNONYM: LIVER-EXPRESSED ANTIMICROBIAL PEPTIDE, LEAP-1, PUTATIVE
COMPND 6 LIVER TUMOR REGRESSOR, PLTR, HEPC20;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE SEQUENCE OF THE PROTEIN IS NATURALLY FOUND IN
SOURCE 4 HOMO SAPIENS. THE PROTEIN WAS CHEMICALLY SYNTHESIZED.
KEYWDS STRAND-LOOP-STRAND, BETA-SHEET, HAIRPIN LOOP, ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.N.HUNTER,D.B.FULTON,T.GANZ,H.J.VOGEL
REVDAT 3 23-FEB-22 1M4E 1 REMARK
REVDAT 2 24-FEB-09 1M4E 1 VERSN
REVDAT 1 06-NOV-02 1M4E 0
JRNL AUTH H.N.HUNTER,D.B.FULTON,T.GANZ,H.J.VOGEL
JRNL TITL THE SOLUTION STRUCTURE OF HUMAN HEPCIDIN, A PEPTIDE HORMONE
JRNL TITL 2 WITH ANTIMICROBIAL ACTIVITY THAT IS INVOLVED IN IRON UPTAKE
JRNL TITL 3 AND HEREDITARY HEMOCHROMATOSIS.
JRNL REF J.BIOL.CHEM. V. 277 37597 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12138110
JRNL DOI 10.1074/JBC.M205305200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER ET AL (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 285 NOE-DERIVED DISTANCE CONSTRAINTS,
REMARK 3 17 DIHEDRAL ANGLE RESTRAINTS, 5 DISTANCE RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1M4E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000016583.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.78MM HEPCIDIN-20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 13C-HSQC;
REMARK 210 DIFFUSION
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.1, NMRPIPE 3.4
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, MATRIX RELAXATION,
REMARK 210 TORSION ANGLE DYNAMICS
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: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 ILE A 3 96.45 -69.98
REMARK 500 1 PHE A 4 106.07 -50.34
REMARK 500 1 CYS A 9 -56.35 -129.28
REMARK 500 1 HIS A 10 -137.96 -73.35
REMARK 500 1 CYS A 18 55.08 -90.15
REMARK 500 2 PHE A 4 93.14 -45.18
REMARK 500 2 CYS A 9 -55.45 -129.04
REMARK 500 2 HIS A 10 -137.17 -81.88
REMARK 500 2 CYS A 18 51.37 -102.60
REMARK 500 3 PHE A 4 91.61 -43.96
REMARK 500 3 CYS A 9 -54.72 -129.14
REMARK 500 3 HIS A 10 -136.88 -80.04
REMARK 500 4 PHE A 4 99.33 -44.52
REMARK 500 4 CYS A 9 -54.97 -129.37
REMARK 500 4 HIS A 10 -135.66 -75.81
REMARK 500 5 ILE A 3 96.64 -68.92
REMARK 500 5 PHE A 4 99.69 -49.68
REMARK 500 5 CYS A 6 59.85 -90.39
REMARK 500 5 CYS A 9 -55.87 -128.71
REMARK 500 5 HIS A 10 -132.30 -77.37
REMARK 500 5 CYS A 18 49.75 -105.76
REMARK 500 6 PHE A 4 93.24 -44.26
REMARK 500 6 CYS A 9 -52.78 -128.93
REMARK 500 6 HIS A 10 -142.01 -73.46
REMARK 500 6 CYS A 18 52.03 -98.79
REMARK 500 6 LYS A 19 56.87 -110.67
REMARK 500 7 PHE A 4 106.12 -46.34
REMARK 500 7 CYS A 9 -58.08 -129.46
REMARK 500 7 HIS A 10 -128.88 -75.80
REMARK 500 8 PHE A 4 102.79 -50.27
REMARK 500 8 CYS A 6 58.14 -91.18
REMARK 500 8 CYS A 9 -64.82 -129.21
REMARK 500 8 HIS A 10 -122.76 -84.07
REMARK 500 9 PHE A 4 98.99 -50.89
REMARK 500 9 CYS A 9 -57.13 -129.60
REMARK 500 9 HIS A 10 -130.45 -79.63
REMARK 500 9 LYS A 19 -45.09 -29.86
REMARK 500 10 PHE A 4 105.46 -47.52
REMARK 500 10 CYS A 9 -66.23 -128.64
REMARK 500 10 HIS A 10 -52.95 -120.84
REMARK 500 11 PHE A 4 104.89 -50.54
REMARK 500 11 CYS A 9 -56.63 -129.23
REMARK 500 11 HIS A 10 -137.15 -74.64
REMARK 500 11 LYS A 19 135.19 -32.08
REMARK 500 12 ILE A 3 97.39 -66.85
REMARK 500 12 PHE A 4 104.65 -49.74
REMARK 500 12 CYS A 9 -54.31 -128.96
REMARK 500 12 HIS A 10 -138.57 -75.26
REMARK 500 13 ILE A 3 98.52 -61.56
REMARK 500 13 PHE A 4 94.66 -53.09
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: 1M4F RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF HEPCIDIN-25
DBREF 1M4E A 1 20 UNP P81172 HEPC_HUMAN 65 84
SEQRES 1 A 20 ILE CYS ILE PHE CYS CYS GLY CYS CYS HIS ARG SER LYS
SEQRES 2 A 20 CYS GLY MET CYS CYS LYS THR
SHEET 1 A 2 ILE A 3 CYS A 6 0
SHEET 2 A 2 CYS A 14 CYS A 17 -1 O GLY A 15 N CYS A 5
SSBOND 1 CYS A 2 CYS A 18 1555 1555 2.03
SSBOND 2 CYS A 5 CYS A 17 1555 1555 2.03
SSBOND 3 CYS A 6 CYS A 14 1555 1555 2.03
SSBOND 4 CYS A 8 CYS A 9 1555 1555 2.09
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