Header list of 1omq.pdb file
Complete list - 23 20 Bytes
HEADER DNA BINDING PROTEIN 26-FEB-03 1OMQ
TITLE STRUCTURE OF PENETRATIN IN BICELLAR SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMEOTIC ANTENNAPEDIA PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL FRAGMENT;
COMPND 5 SYNONYM: PENETRATIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THE PEPTIDE IS NATURALLY FOUND IN DROSOPHILA MELANOGASTER (FRUIT
SOURCE 5 FLY). THE PEPTIDE WAS OBTAINED FROM NEOSYSTEM INC. AND USED WITHOUT
SOURCE 6 FURTHER PURIFICATION.
KEYWDS UNSTRUCTURED AT THE TERMINALS, ALPHA HELICAL IN THE MIDDLE, DNA
KEYWDS 2 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.LINDBERG,H.BIVERSTAHL,A.GRASLUND,L.MALER
REVDAT 3 23-FEB-22 1OMQ 1 REMARK
REVDAT 2 24-FEB-09 1OMQ 1 VERSN
REVDAT 1 29-JUL-03 1OMQ 0
JRNL AUTH M.LINDBERG,H.BIVERSTAHL,A.GRASLUND,L.MALER
JRNL TITL STRUCTURE AND POSITIONING COMPARISON OF TWO VARIANTS OF
JRNL TITL 2 PENETRATIN IN TWO DIFFERENT MEMBRANE MIMICKING SYSTEMS BY
JRNL TITL 3 NMR
JRNL REF EUR.J.BIOCHEM. V. 270 3055 2003
JRNL REFN ISSN 0014-2956
JRNL PMID 12846839
JRNL DOI 10.1046/J.1432-1033.2003.03685.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, DYANA 1.5
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER, HERRMANN (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: A TOTAL OF 129 DISTANCE CONSTRAINTS
REMARK 3 WHERE IDENTIFIED, MOSTLY SEQUENTIAL AND MEDIUM RANGE NOES (40
REMARK 3 INTRA-RESIDUE, 54 SEQUENTIAL AND 35 MEDIUM RANGE NOES)
REMARK 4
REMARK 4 1OMQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018449.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 50MM KCL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 3MM PENETRATIN, 50 MM KCL; 15%
REMARK 210 W/V (DMPC+DMPG)/DHPC BICELLAR
REMARK 210 SOLUTION WITH Q=0.5 AND 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000.1, DYANA 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
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: STRUCTURE WAS DETERMINED BY STANDARD 2D HOMONUCLEAR
REMARK 210 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 O ILE A 47 HD21 ASN A 51 1.59
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 LYS A 57 107.81 -40.69
REMARK 500 2 GLN A 44 24.42 -149.94
REMARK 500 3 TRP A 56 71.74 -104.31
REMARK 500 4 ARG A 53 68.36 -115.00
REMARK 500 4 MET A 54 -26.36 161.05
REMARK 500 4 TRP A 56 66.43 -114.59
REMARK 500 5 GLN A 44 37.27 39.26
REMARK 500 5 MET A 54 58.23 38.71
REMARK 500 8 ARG A 53 57.63 -92.11
REMARK 500 8 MET A 54 -26.27 161.00
REMARK 500 9 GLN A 44 34.01 -96.74
REMARK 500 10 LYS A 57 109.95 -46.37
REMARK 500 11 GLN A 44 -34.05 174.59
REMARK 500 11 LYS A 55 56.12 -119.54
REMARK 500 11 TRP A 56 -47.13 -162.43
REMARK 500 12 GLN A 44 19.28 -148.22
REMARK 500 12 MET A 54 -44.59 -144.09
REMARK 500 12 LYS A 57 -162.39 47.61
REMARK 500 13 GLN A 44 20.78 -150.45
REMARK 500 13 LYS A 55 -45.84 -157.05
REMARK 500 14 GLN A 44 19.77 -147.06
REMARK 500 14 TRP A 56 -49.01 -133.00
REMARK 500 15 GLN A 44 28.40 -156.40
REMARK 500 15 ARG A 53 63.92 -105.84
REMARK 500 15 MET A 54 -28.82 165.47
REMARK 500 15 LYS A 57 -179.83 179.54
REMARK 500 16 LYS A 57 -75.79 70.60
REMARK 500 17 GLN A 44 29.30 39.90
REMARK 500 17 LYS A 57 119.29 64.37
REMARK 500 18 LYS A 57 170.20 64.98
REMARK 500 19 GLN A 44 -149.65 -147.62
REMARK 500 19 ILE A 45 31.38 39.95
REMARK 500 19 LYS A 46 -39.10 -164.04
REMARK 500 20 GLN A 44 -13.66 86.42
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1OMQ A 43 58 UNP P02833 ANTP_DROME 339 354
SEQRES 1 A 16 ARG GLN ILE LYS ILE TRP PHE GLN ASN ARG ARG MET LYS
SEQRES 2 A 16 TRP LYS LYS
HELIX 1 1 TRP A 48 LYS A 57 1 10
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