Header list of 1b9u.pdb file
Complete list - 16 20 Bytes
HEADER HYDROLASE 15-FEB-99 1B9U
TITLE MEMBRANE DOMAIN OF THE SUBUNIT B OF THE E.COLI ATP SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (ATP SYNTHASE);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MEMBRANE DOMAIN;
COMPND 5 EC: 3.6.1.34;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: PROTEIN SYNTHESIZED BY SOLID PHASE PEPTIDE SYNTHESIS
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SEQUENCE CORRESPONDS TO RESIDUES 1-34 OF SUBUNIT B
SOURCE 4 FROM GENE UNCF OF ESCHERICHIA COLI CYTOPLASMIC MEMBRANE
KEYWDS ATP SYNTHASE, MEMBRANE PROTEIN, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR O.DMITRIEV,P.C.JONES,W.JIANG,R.H.FILLINGAME
REVDAT 5 16-FEB-22 1B9U 1 REMARK LINK
REVDAT 4 24-FEB-09 1B9U 1 VERSN
REVDAT 3 01-APR-03 1B9U 1 JRNL
REVDAT 2 26-NOV-99 1B9U 1 DBREF
REVDAT 1 15-SEP-99 1B9U 0
JRNL AUTH O.DMITRIEV,P.C.JONES,W.JIANG,R.H.FILLINGAME
JRNL TITL STRUCTURE OF THE MEMBRANE DOMAIN OF SUBUNIT B OF THE
JRNL TITL 2 ESCHERICHIA COLI F0F1 ATP SYNTHASE.
JRNL REF J.BIOL.CHEM. V. 274 15598 1999
JRNL REFN ISSN 0021-9258
JRNL PMID 10336456
JRNL DOI 10.1074/JBC.274.22.15598
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA, DISCOVER (MSI) 1.5
REMARK 3 AUTHORS : GUENTERT ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1B9U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-99.
REMARK 100 THE DEPOSITION ID IS D_1000000491.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 50 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : CHLOROFORM/METHANOL/WATER=4/4/1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TARGET FUNCTION VALUE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: WATER SUPPESSION USING PULSED FIELD GRADIENTS
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 ASN A 4 -60.23 -26.75
REMARK 500 1 LYS A 23 -53.69 -127.76
REMARK 500 2 LEU A 3 88.47 -157.37
REMARK 500 2 LYS A 23 -45.55 -132.83
REMARK 500 3 LYS A 23 -47.98 -130.99
REMARK 500 4 LEU A 3 47.64 -81.37
REMARK 500 4 LYS A 23 -45.02 -133.82
REMARK 500 5 ASN A 4 -71.27 -167.06
REMARK 500 6 LYS A 23 -48.26 -133.00
REMARK 500 7 ASN A 4 -65.66 -22.68
REMARK 500 8 LEU A 3 87.32 -157.21
REMARK 500 8 LYS A 23 -43.81 -139.74
REMARK 500 9 LYS A 23 -45.28 -134.69
REMARK 500 10 LEU A 3 100.56 -170.55
REMARK 500 10 ASN A 4 -64.47 -27.76
REMARK 500 10 LYS A 23 -40.04 -140.20
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1B9U A 1 34 UNP P0ABA0 ATPF_ECOLI 1 34
SEQRES 1 A 34 MET ASN LEU ASN ALA THR ILE LEU GLY GLN ALA ILE ALA
SEQRES 2 A 34 PHE VAL LEU PHE VAL LEU PHE CYS MET LYS TYR VAL TRP
SEQRES 3 A 34 PRO PRO LEU MET ALA ALA ILE GMA
MODRES 1B9U GMA A 34 GLU 4-AMIDO-4-CARBAMOYL-BUTYRIC ACID
HET GMA A 34 18
HETNAM GMA 4-AMIDO-4-CARBAMOYL-BUTYRIC ACID
FORMUL 1 GMA C5 H10 N2 O3
HELIX 1 1 ASN A 4 TYR A 24 1 21
HELIX 2 2 TRP A 26 ALA A 32 1 7
LINK C ILE A 33 N GMA A 34 1555 1555 1.34
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