Header list of 1pjd.pdb file
Complete list - 27 202 Bytes
HEADER MEMBRANE PROTEIN 02-JUN-03 1PJD
TITLE STRUCTURE AND TOPOLOGY OF A PEPTIDE SEGMENT OF THE 6TH TRANSMEMBRANE
TITLE 2 DOMAIN OF THE SACCHAROMYCES CEREVISIAE ALPHA-FACTOR RECEPTOR IN
TITLE 3 PHOSPHOLIPID BILAYERS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHEROMONE ALPHA FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN A PORTION OF THE
SOURCE 4 6TH TRANSMEMBRANE DOMAIN OF THE ALPHA FACTOR RECEPTOR OF
SOURCE 5 SACCHAROMYCES CEREVISIAE. 15N SELECTIVELY LABELED FMOC-LEU, -ALA, -
SOURCE 6 PHE, -VAL, -ILE WERE USED.
KEYWDS ALPHA HELIX, MEMBRANE PROTEIN
EXPDTA SOLID-STATE NMR
AUTHOR K.G.VALENTINE,S.-F.LIU,F.M.MARASSI,G.VEGLIA,A.A.NEVZOROV,S.J.OPELLA,
AUTHOR 2 F.-X.DING,S.-H.WANG,B.ARSHAVA,J.M.BECKER,F.NAIDER
REVDAT 3 27-OCT-21 1PJD 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1PJD 1 VERSN
REVDAT 1 16-SEP-03 1PJD 0
JRNL AUTH K.G.VALENTINE,S.-F.LIU,F.M.MARASSI,G.VEGLIA,S.J.OPELLA,
JRNL AUTH 2 F.-X.DING,S.-H.WANG,B.ARSHAVA,J.M.BECKER,F.NAIDER
JRNL TITL STRUCTURE AND TOPOLOGY OF A PEPTIDE SEGMENT OF THE 6TH
JRNL TITL 2 TRANSMEMBRANE DOMAIN OF THE SACCHAROMYCES CEREVISIAE
JRNL TITL 3 ALPHA-FACTOR RECEPTOR IN PHOSPHOLIPID BILAYERS
JRNL REF BIOPOLYMERS V. 59 243 2001
JRNL REFN ISSN 0006-3525
JRNL PMID 11473349
JRNL DOI 10.1002/1097-0282(20011005)59:4<243::AID-BIP1021>3.0.CO;2-H
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 97, SRUCTURAL FITTING 1.0
REMARK 3 AUTHORS : ACCELRYS (FELIX), NEVZOROV, OPELLA (SRUCTURAL
REMARK 3 FITTING)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THIS STRUCTURE WAS CALCULATED BY USING
REMARK 3 A STRUCTURAL FITTING ALGORITHM THAT FINDS TORSION ANGLES BETWEEN
REMARK 3 CONSECUTIVE RESIDUES BASED ON THEIR NMR FREQUENCIES.
REMARK 4
REMARK 4 1PJD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019358.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : ALIGNED SAMPLE ON GLASS PLATES
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : PISEMA
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : MAGNEX
REMARK 210 SPECTROMETER MANUFACTURER : HOME-BUILT
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SRUCTURAL FITTING 1.0
REMARK 210 METHOD USED : DIRECT STRUCTURAL FITTING OF 2D
REMARK 210 SOLID-STATE NMR SPECTRA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: PISEMA: POLARIZATION INVERSION SPIN EXCHANGE AT THE MAGIC
REMARK 210 ANGLE
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID-
REMARK 215 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 215 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 215 ON THESE RECORDS ARE MEANINGLESS.
REMARK 217
REMARK 217 SOLID STATE NMR STUDY
REMARK 217 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID
REMARK 217 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 217 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 217 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 ALA A 1
REMARK 465 GLN A 2
REMARK 465 LYS A 18
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 LEU A 13 H SER A 16 1.55
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 VAL A 6 -31.46 -35.12
REMARK 500 ILE A 9 -31.11 -35.21
REMARK 500 ALA A 14 -18.93 -45.67
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1PJD A 1 18 UNP P06842 STE2_YEAST 252 269
SEQADV 1PJD ALA A 1 UNP P06842 CYS 252 ENGINEERED MUTATION
SEQRES 1 A 18 ALA GLN SER LEU LEU VAL PRO SER ILE ILE PHE ILE LEU
SEQRES 2 A 18 ALA TYR SER LEU LYS
HELIX 1 1 LEU A 4 ALA A 14 1 11
HELIX 2 2 TYR A 15 LEU A 17 5 3
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
Complete list - 27 202 Bytes