Header list of 2amn.pdb file
Complete list - 9 20 Bytes
HEADER ANTIMICROBIAL PROTEIN 09-AUG-05 2AMN
TITLE SOLUTION STRUCTURE OF FOWLICIDIN-1, A NOVEL CATHELICIDIN ANTIMICROBIAL
TITLE 2 PEPTIDE FROM CHICKEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATHELICIDIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN, RESIDUES 123-148;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN CHICKEN
KEYWDS LINEAR HELIX, ANTIMICROBIAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.XIAO,H.DAI,Y.R.BOMMINENI,O.PRAKASH,G.ZHANG
REVDAT 4 14-JUN-23 2AMN 1 REMARK
REVDAT 3 05-FEB-20 2AMN 1 REMARK
REVDAT 2 24-FEB-09 2AMN 1 VERSN
REVDAT 1 18-JUL-06 2AMN 0
JRNL AUTH Y.XIAO,H.DAI,Y.R.BOMMINENI,J.L.SOULAGES,Y.X.GONG,O.PRAKASH,
JRNL AUTH 2 G.ZHANG
JRNL TITL STRUCTURE-ACTIVITY RELATIONSHIPS OF FOWLICIDIN-1, A
JRNL TITL 2 CATHELICIDIN ANTIMICROBIAL PEPTIDE IN CHICKEN.
JRNL REF FEBS J. V. 273 2581 2006
JRNL REFN ISSN 1742-464X
JRNL PMID 16817888
JRNL DOI 10.1111/J.1742-4658.2006.05261.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, CNS 1.1
REMARK 3 AUTHORS : BRUNGER (CNS), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AMN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034071.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 4MM FOWLICIDIN-1, 50% H2O, 50%
REMARK 210 TFE-D6
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 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: 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 ARG A 4 111.01 -167.49
REMARK 500 1 VAL A 5 -68.61 -106.59
REMARK 500 1 TYR A 17 13.79 -147.63
REMARK 500 1 LYS A 25 41.10 -95.06
REMARK 500 2 TYR A 20 -59.96 -170.00
REMARK 500 3 VAL A 5 -62.99 -129.90
REMARK 500 3 LYS A 25 98.96 -68.75
REMARK 500 4 VAL A 2 -51.11 -129.46
REMARK 500 4 LYS A 3 78.56 59.78
REMARK 500 4 TYR A 20 -54.91 -127.51
REMARK 500 5 VAL A 2 138.51 -176.41
REMARK 500 5 ARG A 4 143.29 63.03
REMARK 500 5 VAL A 5 -163.50 -103.22
REMARK 500 5 TYR A 20 -51.05 -131.84
REMARK 500 5 LYS A 25 51.02 -107.78
REMARK 500 6 ARG A 4 -70.99 -106.51
REMARK 500 6 VAL A 5 -73.05 -149.45
REMARK 500 6 TYR A 17 -33.98 -155.41
REMARK 500 6 TYR A 20 -50.20 -129.48
REMARK 500 6 LYS A 25 92.11 -69.74
REMARK 500 7 VAL A 2 -45.15 -136.49
REMARK 500 7 TYR A 20 -54.39 -121.81
REMARK 500 8 LYS A 3 92.59 66.66
REMARK 500 8 ARG A 4 116.77 62.17
REMARK 500 8 VAL A 5 -67.93 -99.46
REMARK 500 8 ASN A 18 -43.29 -142.04
REMARK 500 8 TYR A 20 -55.34 -157.07
REMARK 500 9 VAL A 2 80.70 61.92
REMARK 500 9 LYS A 3 118.23 -173.00
REMARK 500 9 TYR A 20 -51.89 -128.46
REMARK 500 9 LYS A 25 49.89 -91.34
REMARK 500 10 TYR A 17 10.83 -143.44
REMARK 500 12 ARG A 4 149.35 62.12
REMARK 500 12 TYR A 17 -65.66 -98.31
REMARK 500 12 ARG A 21 -48.18 -146.69
REMARK 500 13 VAL A 2 -44.87 -132.84
REMARK 500 13 LYS A 3 122.50 64.09
REMARK 500 14 LYS A 3 -67.38 68.68
REMARK 500 14 TYR A 20 -55.72 -125.71
REMARK 500 14 LYS A 25 33.47 -99.89
REMARK 500 15 ARG A 4 -73.19 -96.62
REMARK 500 15 VAL A 5 -65.46 -151.99
REMARK 500 16 ARG A 4 107.88 -168.16
REMARK 500 16 TYR A 17 -51.75 -135.76
REMARK 500 16 TYR A 20 -56.86 -126.10
REMARK 500 17 LYS A 3 -69.74 -144.74
REMARK 500 18 VAL A 2 97.83 63.67
REMARK 500 18 LYS A 3 -65.32 -159.61
REMARK 500 18 ARG A 4 -168.39 55.40
REMARK 500 18 TYR A 20 -59.88 -163.34
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6835 RELATED DB: BMRB
DBREF 2AMN A 1 26 UNP Q2IAM1 Q2IAM1_CHICK 123 148
SEQRES 1 A 26 ARG VAL LYS ARG VAL TRP PRO LEU VAL ILE ARG THR VAL
SEQRES 2 A 26 ILE ALA GLY TYR ASN LEU TYR ARG ALA ILE LYS LYS LYS
HELIX 1 1 LEU A 8 ASN A 18 1 11
HELIX 2 2 TYR A 20 LYS A 25 1 6
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