Header list of 1ax3.pdb file
Complete list - b 16 2 Bytes
HEADER PHOSPHOTRANSFERASE SYSTEM 25-OCT-97 1AX3
TITLE SOLUTION NMR STRUCTURE OF B. SUBTILIS IIAGLC, 16 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSE PERMEASE IIA DOMAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: A DOMAIN;
COMPND 5 SYNONYM: IIAGLC;
COMPND 6 EC: 2.7.1.69;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: MZ1;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PRE
KEYWDS PHOSPHOTRANSFERASE SYSTEM, SUGAR TRANSPORT, TRANSFERASE,
KEYWDS 2 PHOSPHORYLATION, TRANSMEMBRANE
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR Y.CHEN,D.A.CASE,J.REIZER,M.H.SAIER JUNIOR,P.E.WRIGHT
REVDAT 4 16-FEB-22 1AX3 1 REMARK
REVDAT 3 24-FEB-09 1AX3 1 VERSN
REVDAT 2 01-APR-03 1AX3 1 JRNL
REVDAT 1 17-JUN-98 1AX3 0
JRNL AUTH Y.CHEN,D.A.CASE,J.REIZER,M.H.SAIER JR.,P.E.WRIGHT
JRNL TITL HIGH-RESOLUTION SOLUTION STRUCTURE OF BACILLUS SUBTILIS
JRNL TITL 2 IIAGLC.
JRNL REF PROTEINS V. 31 258 1998
JRNL REFN ISSN 0887-3585
JRNL PMID 9593197
JRNL DOI 10.1002/(SICI)1097-0134(19980515)31:3<258::AID-PROT3>3.3.CO;
JRNL DOI 2 2-Q
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,
REMARK 3 FERGUSON,SEIBEL,SINGH,WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 PAPER.
REMARK 4
REMARK 4 1AX3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171362.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.87
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; TOCSY; HMQC-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500; AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DISGEO, AMBER
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND
REMARK 210 LOWEST AMBER ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: PON
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: PHOSPHORYLATION SITE.
DBREF 1AX3 A 1 162 UNP P20166 PTG3C_BACSU 1 162
SEQRES 1 A 162 MET ILE ALA GLU PRO LEU GLN ASN GLU ILE GLY GLU GLU
SEQRES 2 A 162 VAL PHE VAL SER PRO ILE THR GLY GLU ILE HIS PRO ILE
SEQRES 3 A 162 THR ASP VAL PRO ASP GLN VAL PHE SER GLY LYS MET MET
SEQRES 4 A 162 GLY ASP GLY PHE ALA ILE LEU PRO SER GLU GLY ILE VAL
SEQRES 5 A 162 VAL SER PRO VAL ARG GLY LYS ILE LEU ASN VAL PHE PRO
SEQRES 6 A 162 THR LYS HIS ALA ILE GLY LEU GLN SER ASP GLY GLY ARG
SEQRES 7 A 162 GLU ILE LEU ILE HIS PHE GLY ILE ASP THR VAL SER LEU
SEQRES 8 A 162 LYS GLY GLU GLY PHE THR SER PHE VAL SER GLU GLY ASP
SEQRES 9 A 162 ARG VAL GLU PRO GLY GLN LYS LEU LEU GLU VAL ASP LEU
SEQRES 10 A 162 ASP ALA VAL LYS PRO ASN VAL PRO SER LEU MET THR PRO
SEQRES 11 A 162 ILE VAL PHE THR ASN LEU ALA GLU GLY GLU THR VAL SER
SEQRES 12 A 162 ILE LYS ALA SER GLY SER VAL ASN ARG GLU GLN GLU ASP
SEQRES 13 A 162 ILE VAL LYS ILE GLU LYS
HELIX 1 1 ILE A 26 ASP A 28 5 3
HELIX 2 2 GLN A 32 SER A 35 1 4
HELIX 3 3 LEU A 117 ASN A 123 1 7
HELIX 4 4 LEU A 136 GLU A 138 5 3
SHEET 1 A 6 GLY A 21 PRO A 25 0
SHEET 2 A 6 ASP A 41 PRO A 47 -1 N LEU A 46 O GLU A 22
SHEET 3 A 6 MET A 128 PHE A 133 -1 N PHE A 133 O ASP A 41
SHEET 4 A 6 GLU A 79 HIS A 83 -1 N LEU A 81 O VAL A 132
SHEET 5 A 6 ALA A 69 GLN A 73 -1 N LEU A 72 O ILE A 80
SHEET 6 A 6 LYS A 59 ASN A 62 -1 N ASN A 62 O GLY A 71
SHEET 1 B 2 PHE A 96 SER A 98 0
SHEET 2 B 2 LEU A 113 VAL A 115 -1 N GLU A 114 O THR A 97
SHEET 1 C 2 THR A 141 ILE A 144 0
SHEET 2 C 2 VAL A 158 GLU A 161 -1 N GLU A 161 O THR A 141
SITE 1 PON 1 HIS A 83
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 - b 16 2 Bytes