Header list of 1iij.pdb file
Complete list - 23 20 Bytes
HEADER SIGNALING PROTEIN 23-APR-01 1IIJ
TITLE SOLUTION STRUCTURE OF THE NEU/ERBB-2 MEMBRANE SPANNING SEGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ERBB-2 RECEPTOR PROTEIN-TYROSINE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TRANSMEMBRANE DOMAIN, RESIDUES 650-684;
COMPND 5 EC: 2.7.1.112;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THIS
SOURCE 4 SEQUENCE OCCURS NATURALLY IN RATTUS NORVEGICUS (RAT).
KEYWDS ALPHA-HELIX-PI-BULGE-ALPHA-HELIX, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 5
AUTHOR M.GOETZ,C.CARLOTTI,F.BONTEMS,E.J.DUFOURC
REVDAT 5 23-FEB-22 1IIJ 1 REMARK
REVDAT 4 24-FEB-09 1IIJ 1 VERSN
REVDAT 3 24-FEB-04 1IIJ 1 CRYST1
REVDAT 2 01-APR-03 1IIJ 1 JRNL
REVDAT 1 27-JUN-01 1IIJ 0
JRNL AUTH M.GOETZ,C.CARLOTTI,F.BONTEMS,E.J.DUFOURC
JRNL TITL EVIDENCE FOR AN ALPHA-HELIX --> PI-BULGE HELICITY MODULATION
JRNL TITL 2 FOR THE NEU/ERBB-2 MEMBRANE-SPANNING SEGMENT. A 1H NMR AND
JRNL TITL 3 CIRCULAR DICHROISM STUDY.
JRNL REF BIOCHEMISTRY V. 40 6534 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11371217
JRNL DOI 10.1021/BI0027938
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA, DISCOVER VER. 97.0
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS INC. (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES BASED 385 NOE RESTRAINTS,
REMARK 3 111 DIHEDRAL ANGLES
REMARK 4
REMARK 4 1IIJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013300.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : ATMOSPHERIC ATM
REMARK 210 SAMPLE CONTENTS : 1.5 MM NEU-TM35 PEPTIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D NOESY; HOHAHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DISCOVER VER. 97.0, XWINNMR
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 5
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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 GLU A 1 CD GLU A 1 OE2 0.108
REMARK 500 1 ARG A 35 C ARG A 35 OXT 0.137
REMARK 500 2 GLU A 1 CD GLU A 1 OE2 0.107
REMARK 500 2 ARG A 35 C ARG A 35 OXT 0.134
REMARK 500 3 GLU A 1 CD GLU A 1 OE2 0.107
REMARK 500 3 ARG A 35 C ARG A 35 OXT 0.135
REMARK 500 4 GLU A 1 CD GLU A 1 OE2 0.107
REMARK 500 4 ARG A 35 C ARG A 35 OXT 0.137
REMARK 500 5 GLU A 1 CD GLU A 1 OE2 0.108
REMARK 500 5 ARG A 35 C ARG A 35 OXT 0.137
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 1 ARG A 3 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 1 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 1 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 1 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ARG A 35 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 ARG A 35 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 2 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 2 ARG A 3 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 2 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 2 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 2 ARG A 35 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 2 ARG A 35 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 3 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 3 ARG A 3 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 3 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 3 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 3 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ARG A 35 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 4 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 4 ARG A 3 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 4 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 4 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 4 ARG A 34 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 4 ARG A 35 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 5 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 5 ARG A 3 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 5 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 5 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 5 ARG A 35 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 5 ARG A 35 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
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 2 ARG A 34 76.21 -106.71
REMARK 500 3 SER A 5 -64.52 -146.32
REMARK 500 3 LEU A 23 -61.36 -93.01
REMARK 500 4 VAL A 26 -73.91 -76.00
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IIJ A 1 35 UNP P06494 ERBB2_RAT 647 681
SEQRES 1 A 35 GLU GLN ARG ALA SER PRO VAL THR PHE ILE ILE ALA THR
SEQRES 2 A 35 VAL VAL GLY VAL LEU LEU PHE LEU ILE LEU VAL VAL VAL
SEQRES 3 A 35 VAL GLY ILE LEU ILE LYS ARG ARG ARG
HELIX 1 1 ARG A 3 VAL A 24 1 22
HELIX 2 2 GLY A 28 ARG A 34 1 7
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 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