Header list of 1d9l.pdb file
Complete list - 16 20 Bytes
HEADER MEMBRANE PROTEIN 28-OCT-99 1D9L
TITLE SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2 HYBRID PEPTIDE
TITLE 2 ANALOGUE(P1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CECROPIN A(1-8)-MAGAININ 2 HYBRID PEPTIDE ANALOGUE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS, HYALOPHORA CECROPIA;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG, CECROPIA MOTH;
SOURCE 4 ORGANISM_TAXID: 8355,7123;
SOURCE 5 STRAIN: ,;
SOURCE 6 CELLULAR_LOCATION: MEMBRANE
KEYWDS HELIX-HELIX, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.OH,Y.KIM
REVDAT 4 16-FEB-22 1D9L 1 REMARK LINK
REVDAT 3 24-FEB-09 1D9L 1 VERSN
REVDAT 2 27-MAR-00 1D9L 1 JRNL
REVDAT 1 12-NOV-99 1D9L 0
JRNL AUTH D.OH,S.Y.SHIN,J.H.KANG,K.S.HAHM,K.L.KIM,Y.KIM
JRNL TITL NMR STRUCTURAL CHARACTERIZATION OF CECROPIN A(1-8) -
JRNL TITL 2 MAGAININ 2(1-12) AND CECROPIN A (1-8) - MELITTIN (1-12)
JRNL TITL 3 HYBRID PEPTIDES.
JRNL REF J.PEPT.RES. V. 53 578 1999
JRNL REFN ISSN 1397-002X
JRNL PMID 10424354
JRNL DOI 10.1034/J.1399-3011.1999.00067.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1D9L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000009915.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 298
REMARK 210 PH : 4.29; 4.29
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 2MM PEPTIDE; 90MM DPC MICELLES;
REMARK 210 90% H2O, 10% D2O; 2MM PEPTIDE;
REMARK 210 90MM DPC MICELLES; D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 95.0
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY
REMARK 210 -DYNAMICAL SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
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 : NULL
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: 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 TRP A 2 -158.59 -161.63
REMARK 500 1 LYS A 3 114.08 -163.90
REMARK 500 2 TRP A 2 -161.44 46.46
REMARK 500 4 LYS A 3 76.63 -160.27
REMARK 500 4 LYS A 15 -104.69 -85.04
REMARK 500 4 LYS A 16 -162.14 -56.72
REMARK 500 5 TRP A 2 -92.01 -113.19
REMARK 500 5 LYS A 3 -100.88 -140.34
REMARK 500 6 TRP A 2 -69.16 -109.23
REMARK 500 6 HIS A 12 -41.34 -132.21
REMARK 500 6 LYS A 15 -98.69 -64.40
REMARK 500 7 TRP A 2 -92.57 -158.10
REMARK 500 7 LYS A 15 158.70 -49.59
REMARK 500 8 LYS A 15 -157.12 -61.94
REMARK 500 8 LYS A 16 48.48 -83.09
REMARK 500 9 TRP A 2 -144.40 63.88
REMARK 500 9 LYS A 3 -154.09 -140.08
REMARK 500 9 LYS A 16 -159.02 -70.45
REMARK 500 10 TRP A 2 -154.74 -81.15
REMARK 500 10 LYS A 3 -107.24 -71.57
REMARK 500 10 LYS A 15 170.67 -54.01
REMARK 500 11 TRP A 2 -152.87 -82.12
REMARK 500 11 LYS A 15 -162.26 -55.67
REMARK 500 12 TRP A 2 161.04 58.26
REMARK 500 12 LYS A 15 -179.59 -49.33
REMARK 500 13 LYS A 3 34.61 -89.04
REMARK 500 15 TRP A 2 -141.28 -82.28
REMARK 500 15 LYS A 16 98.70 -53.67
REMARK 500 16 LYS A 3 -71.27 -103.18
REMARK 500 17 TRP A 2 -60.32 66.81
REMARK 500 17 LYS A 3 -166.26 -68.48
REMARK 500 17 LYS A 16 -167.04 -64.28
REMARK 500 18 TRP A 2 98.95 -48.87
REMARK 500 18 LYS A 3 11.91 -146.03
REMARK 500 19 TRP A 2 -102.31 -165.24
REMARK 500 19 LYS A 3 15.06 -149.86
REMARK 500 19 LYS A 16 -144.36 -61.20
REMARK 500 20 LYS A 15 -145.46 -69.51
REMARK 500 20 LYS A 16 175.10 -47.21
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 18
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D9J RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2 HYBRID PEPTIDE
REMARK 900 ANALOGUE ( DELETION GIG SEQUENCE FROM CA-MA)
REMARK 900 RELATED ID: 1D9M RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID
REMARK 900 PEPTIDE ANALOGUE (SUBSTITUTION GIG SEQUENCE OF CA-MA TO PRO)
REMARK 900 RELATED ID: 1D9O RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID
REMARK 900 PEPTIDE ANALOGUE (SUBSTITUTION GIG SEQUENCE OF CA-MA TO PRO)
REMARK 900 RELATED ID: 1D9P RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID
REMARK 900 PEPTIDE ANALOGUE (SUBSTITUTION TRP2 OF CA-MA TO LEU)
DBREF 1D9L A 1 8 UNP P01507 CECA_HYACE 27 34
DBREF 1D9L A 9 17 UNP P11006 MAGA_XENLA 224 232
SEQRES 1 A 18 LYS TRP LYS LEU PHE LYS LYS ILE LYS PHE LEU HIS SER
SEQRES 2 A 18 ALA LYS LYS PHE NH2
HET NH2 A 18 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 LEU A 4 ALA A 14 1 11
LINK C PHE A 17 N NH2 A 18 1555 1555 1.31
SITE 1 AC1 2 LYS A 16 PHE A 17
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 - 16 20 Bytes