Header list of 1bh7.pdb file
Complete list - 16 202 Bytes
HEADER MEMBRANE PROTEIN 16-JUN-98 1BH7 TITLE A LOW ENERGY STRUCTURE FOR THE FINAL CYTOPLASMIC LOOP OF BAND 3, NMR, TITLE 2 MINIMIZED AVERAGE STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: BAND 3; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FINAL CYTOPLASMIC LOOP; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606 KEYWDS MEMBRANE PROTEIN, CYTOPLASMIC LOOP, ANION EXCHANGE PROTEIN EXPDTA SOLUTION NMR AUTHOR D.ASKIN,G.B.BLOOMBERG,E.J.CHAMBERS,M.J.A.TANNER REVDAT 4 16-FEB-22 1BH7 1 REMARK REVDAT 3 24-FEB-09 1BH7 1 VERSN REVDAT 2 18-NOV-98 1BH7 3 ATOM SOURCE COMPND REMARK REVDAT 2 2 3 TITLE DBREF SEQADV JRNL REVDAT 2 3 3 EXPDTA REVDAT 1 04-NOV-98 1BH7 0 JRNL AUTH D.ASKIN,G.B.BLOOMBERG,E.J.CHAMBERS,M.J.TANNER JRNL TITL NMR SOLUTION STRUCTURE OF A CYTOPLASMIC SURFACE LOOP OF THE JRNL TITL 2 HUMAN RED CELL ANION TRANSPORTER, BAND 3. JRNL REF BIOCHEMISTRY V. 37 11670 1998 JRNL REFN ISSN 0006-2960 JRNL PMID 9709005 JRNL DOI 10.1021/BI973158D 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: 480 DISTANCE RESTRAINTS 10 DIHEDRAL REMARK 3 ANGLE RESTRAINTS 4 H-BONDING DISTANCE RESTRAINTS NO NOE REMARK 3 VIOLATIONS > 0.05NM NO TORSION ANGLE VIOLATIONS > 5 DEGREES REMARK 4 REMARK 4 1BH7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000171753. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 3.5 REMARK 210 IONIC STRENGTH : 12MM REMARK 210 PRESSURE : ATMOSPHERIC ATM REMARK 210 SAMPLE CONTENTS : 30% TFE-D3/H2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; HOHAHA REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : ALPHA 500MHZ REMARK 210 SPECTROMETER MANUFACTURER : JEOL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 15 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : AVERAGE STRUCTURE- ONLY THE REMARK 210 THREE STRUCTURED REGIONS WITHIN REMARK 210 THE PEPTIDE ARE GIVEN REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 2D SOLUTION-STATE NMR 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 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 LEU A 17 REMARK 465 VAL A 28 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 LEU A 11 47.20 -94.22 REMARK 500 ARG A 14 3.35 -69.80 REMARK 500 ILE A 15 -68.72 -134.98 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 ARG A 14 0.30 SIDE CHAIN REMARK 500 ARG A 33 0.30 SIDE CHAIN REMARK 500 ARG A 38 0.24 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1BH7 A 9 41 UNP P02730 B3AT_HUMAN 803 835 SEQRES 1 A 33 ILE GLN LEU PHE ASP ARG ILE LEU LEU LEU PHE LYS PRO SEQRES 2 A 33 PRO LYS TYR HIS PRO ASP VAL PRO TYR VAL LYS ARG VAL SEQRES 3 A 33 LYS THR TRP ARG MET HIS LEU HELIX 1 1 LYS A 35 MET A 39 1 5 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 - 16 202 Bytes