Header list of 1iwc.pdb file
Complete list - 23 20 Bytes
HEADER HYDROLASE 02-MAY-02 1IWC
TITLE TFE-INDUDED STRUCTURE OF THE N-TERMINAL DOMAIN OF PIG GASTRIC H/K-
TITLE 2 ATPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GASTRIC H/K-ATPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 SYNONYM: POTASSIUM-TRANSPORTING ATPASE ALPHA CHAIN 1;
COMPND 6 EC: 3.6.3.10;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE WAS SYNTHESIZED. THIS SEQUENCE CONTAINS
SOURCE 4 THE N-TERMINAL DOMAIN OF PIG GASTRIC H/K-ATPASE
KEYWDS TFE-INDUCED STRUCTURE, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR N.FUJITANI,M.KANAGAWA,T.AIZAWA,T.OHKUBO,S.KAYA,M.DEMURA,K.KAWANO,
AUTHOR 2 K.TANIGUCHI,K.NITTA
REVDAT 4 23-FEB-22 1IWC 1 REMARK
REVDAT 3 24-FEB-09 1IWC 1 VERSN
REVDAT 2 24-JUN-03 1IWC 1 JRNL
REVDAT 1 27-NOV-02 1IWC 0
JRNL AUTH N.FUJITANI,M.KANAGAWA,T.AIZAWA,T.OHKUBO,S.KAYA,M.DEMURA,
JRNL AUTH 2 K.KAWANO,S.NISHIMURA,K.TANIGUCHI,K.NITTA
JRNL TITL STRUCTURE DETERMINATION AND CONFORMATIONAL CHANGE INDUCED BY
JRNL TITL 2 TYROSINE PHOSPHORYLATION OF THE N-TERMINAL DOMAIN OF THE
JRNL TITL 3 ALPHA-CHAIN OF PIG GASTRIC H+/K+-ATPASE
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 300 223 2003
JRNL REFN ISSN 0006-291X
JRNL PMID 12480547
JRNL DOI 10.1016/S0006-291X(02)02794-8
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IWC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-MAY-02.
REMARK 100 THE DEPOSITION ID IS D_1000005336.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM PEPTIDE CONTAINING OF THE N
REMARK 210 -TERMINAL FRAGMENT OF PIG
REMARK 210 GASTRIC H/K-ATPASE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, XEASY 1.3.13
REMARK 210 METHOD USED : DISTANCE GEOMETRY-SIMULATED
REMARK 210 ANNEALING WITH THE STANDARD
REMARK 210 PROTOCOL OF XPLOR
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 13
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 ALA A 4 42.28 -155.58
REMARK 500 1 LEU A 14 -75.23 -81.03
REMARK 500 1 PRO A 16 -87.31 -78.01
REMARK 500 1 ASP A 21 65.89 -152.28
REMARK 500 1 MET A 22 -50.01 174.49
REMARK 500 1 ALA A 31 -66.57 -101.95
REMARK 500 1 ARG A 33 98.18 -66.91
REMARK 500 2 LEU A 14 -76.29 -79.33
REMARK 500 2 PRO A 18 -81.17 -78.23
REMARK 500 2 ASP A 21 35.70 -89.84
REMARK 500 2 ALA A 23 -30.28 175.17
REMARK 500 2 LYS A 30 86.82 62.00
REMARK 500 2 ARG A 33 -68.25 -142.74
REMARK 500 3 LYS A 3 -4.43 78.24
REMARK 500 3 PRO A 16 -71.94 -77.87
REMARK 500 3 SER A 19 52.01 -95.68
REMARK 500 3 ASP A 21 74.45 -114.98
REMARK 500 3 ALA A 23 -43.68 -176.25
REMARK 500 3 LYS A 30 37.92 -91.66
REMARK 500 3 ALA A 31 -87.75 -114.68
REMARK 500 4 TYR A 7 -72.68 -63.13
REMARK 500 4 SER A 19 126.38 65.20
REMARK 500 4 LYS A 30 68.90 -100.61
REMARK 500 5 LYS A 3 -5.42 78.59
REMARK 500 5 PRO A 18 -70.15 -78.20
REMARK 500 5 ALA A 23 12.66 -142.80
REMARK 500 5 LYS A 30 54.87 -172.90
REMARK 500 5 ALA A 31 -62.28 -122.04
REMARK 500 6 LYS A 3 -71.54 -140.84
REMARK 500 6 GLU A 5 -79.94 -54.41
REMARK 500 6 ASP A 21 13.15 -147.01
REMARK 500 6 MET A 22 -32.12 176.16
REMARK 500 6 ARG A 33 70.65 -100.15
REMARK 500 7 LYS A 3 -52.77 -159.09
REMARK 500 7 ALA A 4 -54.79 -171.07
REMARK 500 7 PRO A 16 -80.14 -77.54
REMARK 500 7 ASP A 21 47.02 -95.57
REMARK 500 7 MET A 22 -79.51 -124.36
REMARK 500 8 LYS A 3 -82.79 -132.74
REMARK 500 8 TYR A 7 -70.27 -68.24
REMARK 500 8 SER A 19 58.85 -153.49
REMARK 500 8 ASP A 21 25.25 44.09
REMARK 500 8 MET A 22 46.53 39.81
REMARK 500 8 ALA A 23 -32.93 163.06
REMARK 500 8 LYS A 30 105.43 -179.92
REMARK 500 8 ALA A 31 -44.16 -143.05
REMARK 500 9 PRO A 16 -90.94 -77.95
REMARK 500 9 SER A 19 -53.58 163.84
REMARK 500 9 ASP A 21 53.64 -93.87
REMARK 500 9 MET A 22 42.49 -105.64
REMARK 500
REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 33 0.21 SIDE CHAIN
REMARK 500 2 ARG A 33 0.29 SIDE CHAIN
REMARK 500 3 ARG A 33 0.32 SIDE CHAIN
REMARK 500 4 ARG A 33 0.15 SIDE CHAIN
REMARK 500 5 ARG A 33 0.21 SIDE CHAIN
REMARK 500 6 ARG A 33 0.26 SIDE CHAIN
REMARK 500 7 ARG A 33 0.21 SIDE CHAIN
REMARK 500 8 ARG A 33 0.26 SIDE CHAIN
REMARK 500 9 ARG A 33 0.12 SIDE CHAIN
REMARK 500 10 ARG A 33 0.23 SIDE CHAIN
REMARK 500 11 ARG A 33 0.28 SIDE CHAIN
REMARK 500 12 ARG A 33 0.30 SIDE CHAIN
REMARK 500 13 ARG A 33 0.22 SIDE CHAIN
REMARK 500 14 ARG A 33 0.25 SIDE CHAIN
REMARK 500 15 ARG A 33 0.21 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IWF RELATED DB: PDB
REMARK 900 1IWF CONTAINS SOLUTION STRUCTURE OF THE SAME PORTEIN
DBREF 1IWC A 1 34 UNP P19156 ATP4A_PIG 0 33
SEQRES 1 A 34 MET GLY LYS ALA GLU ASN TYR GLU LEU TYR GLN VAL GLU
SEQRES 2 A 34 LEU GLY PRO GLY PRO SER GLY ASP MET ALA ALA LYS MET
SEQRES 3 A 34 SER LYS LYS LYS ALA GLY ARG GLY
HELIX 1 1 ALA A 4 GLY A 15 1 12
HELIX 2 2 ALA A 23 LYS A 30 1 8
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