Header list of 1bnx.pdb file
Complete list - 16 20 Bytes
HEADER ELECTRON TRANSPORT 30-JUL-98 1BNX TITLE STRUCTURAL STUDIES ON THE EFFECTS OF THE DELETION IN THE RED CELL TITLE 2 ANION EXCHANGER (BAND3, AE1) ASSOCIATED WITH SOUTH EAST ASIAN TITLE 3 OVALOCYTOSIS. COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (BAND 3); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL CYTOPLASM/FIRST MEMBRANE SPAN; COMPND 5 SYNONYM: SAO, ANION EXCHANGE PROTEIN 1; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: PEPTIDE CORRESPONDS TO THE SECTION R-389 -K-430 IN THE COMPND 9 SAO MUTANT OF HUMAN BAND 3. SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: SYNTHESIZED USING FMOC PEPTIDE STRATEGY. KEYWDS HUMAN ERYTHROCYTE ANION TRANSPORTER, TRANSMEMBRANE, SYNTHETIC KEYWDS 2 PEPTIDE, ELECTRON TRANSPORT EXPDTA SOLUTION NMR NUMMDL 21 AUTHOR E.J.CHAMBERS,G.B.BLOOMBERG,S.M.RING,M.J.A.TANNER REVDAT 5 16-FEB-22 1BNX 1 REMARK SEQADV LINK REVDAT 4 24-FEB-09 1BNX 1 VERSN REVDAT 3 01-APR-03 1BNX 1 JRNL REVDAT 2 22-DEC-99 1BNX 4 HEADER COMPND REMARK JRNL REVDAT 2 2 4 ATOM SOURCE SEQRES REVDAT 1 05-AUG-98 1BNX 0 JRNL AUTH E.J.CHAMBERS,D.ASKIN,G.B.BLOOMBERG,S.M.RING,M.J.TANNER JRNL TITL STUDIES ON THE STRUCTURE OF A TRANSMEMBRANE REGION AND A JRNL TITL 2 CYTOPLASMIC LOOP OF THE HUMAN RED CELL ANION EXCHANGER (BAND JRNL TITL 3 3, AE1). JRNL REF BIOCHEM.SOC.TRANS. V. 26 516 1998 JRNL REFN ISSN 0300-5127 JRNL PMID 9765907 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: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 EUR. J. BIOCHEM. 1994, V221, 445-454. REMARK 4 REMARK 4 1BNX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000008119. 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 : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; HOHAHA. REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : ALPHA 500 REMARK 210 SPECTROMETER MANUFACTURER : JEOL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21 REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE VIOLATIONS MORE THAN 0.05 REMARK 210 NM, NO DIHEDRAL VIOLATIONS MORE REMARK 210 THAN 5 DEGREES, REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 16 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 2D HOMONUCLEAR NMR REMARK 210 SPECTROSCOPY. 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 LEU A 30 -67.99 -90.54 REMARK 500 2 PRO A 4 -80.25 -79.90 REMARK 500 2 TYR A 17 -70.02 -72.25 REMARK 500 3 TYR A 3 80.80 -155.13 REMARK 500 3 PRO A 4 -72.08 -82.68 REMARK 500 4 TYR A 3 65.20 67.16 REMARK 500 4 PRO A 4 -79.63 -93.61 REMARK 500 4 PHE A 27 -79.58 -72.63 REMARK 500 5 TYR A 3 93.08 55.33 REMARK 500 5 PRO A 4 -76.23 -87.53 REMARK 500 5 ASP A 9 -77.96 -61.30 REMARK 500 6 PRO A 4 -77.49 -88.54 REMARK 500 7 TYR A 3 82.84 -155.89 REMARK 500 8 TYR A 3 71.87 -164.96 REMARK 500 8 LEU A 30 49.84 -89.78 REMARK 500 8 LEU A 31 -72.23 -90.38 REMARK 500 9 TYR A 3 61.90 -163.90 REMARK 500 9 PRO A 4 -77.52 -80.47 REMARK 500 9 PHE A 27 90.10 -69.02 REMARK 500 10 TYR A 3 -51.15 177.89 REMARK 500 11 TYR A 3 71.86 -159.28 REMARK 500 11 PRO A 4 -64.54 -90.73 REMARK 500 11 PHE A 27 -87.46 -60.34 REMARK 500 13 PRO A 4 -70.43 -90.26 REMARK 500 14 PRO A 4 -75.95 -82.95 REMARK 500 15 TYR A 3 -51.78 -178.39 REMARK 500 15 PRO A 4 -71.43 -88.81 REMARK 500 16 TYR A 3 82.12 -156.79 REMARK 500 16 PRO A 4 -82.34 -79.98 REMARK 500 17 TYR A 3 -52.50 173.60 REMARK 500 17 PRO A 4 -74.95 -90.18 REMARK 500 17 PHE A 27 -178.65 -67.74 REMARK 500 18 TYR A 3 92.66 56.11 REMARK 500 18 PRO A 4 -79.35 -86.41 REMARK 500 19 PRO A 4 -75.60 -89.24 REMARK 500 19 PHE A 27 -79.60 -86.00 REMARK 500 20 TYR A 3 56.70 -141.02 REMARK 500 20 PRO A 4 -78.54 -81.74 REMARK 500 21 PHE A 27 -73.49 -76.41 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 2 0.32 SIDE CHAIN REMARK 500 2 ARG A 2 0.29 SIDE CHAIN REMARK 500 3 ARG A 2 0.32 SIDE CHAIN REMARK 500 4 ARG A 2 0.31 SIDE CHAIN REMARK 500 5 ARG A 2 0.29 SIDE CHAIN REMARK 500 6 ARG A 2 0.31 SIDE CHAIN REMARK 500 7 ARG A 2 0.30 SIDE CHAIN REMARK 500 8 ARG A 2 0.28 SIDE CHAIN REMARK 500 9 ARG A 2 0.32 SIDE CHAIN REMARK 500 10 ARG A 2 0.27 SIDE CHAIN REMARK 500 11 ARG A 2 0.31 SIDE CHAIN REMARK 500 12 ARG A 2 0.24 SIDE CHAIN REMARK 500 13 ARG A 2 0.31 SIDE CHAIN REMARK 500 14 ARG A 2 0.27 SIDE CHAIN REMARK 500 15 ARG A 2 0.25 SIDE CHAIN REMARK 500 16 ARG A 2 0.31 SIDE CHAIN REMARK 500 17 ARG A 2 0.26 SIDE CHAIN REMARK 500 18 ARG A 2 0.29 SIDE CHAIN REMARK 500 19 ARG A 2 0.25 SIDE CHAIN REMARK 500 20 ARG A 2 0.23 SIDE CHAIN REMARK 500 21 ARG A 2 0.22 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE A 1 DBREF 1BNX A 2 34 UNP P02730 B3AT_HUMAN 388 429 SEQADV 1BNX A UNP P02730 ALA 399 DELETION SEQADV 1BNX A UNP P02730 PHE 400 DELETION SEQADV 1BNX A UNP P02730 SER 401 DELETION SEQADV 1BNX A UNP P02730 PRO 402 DELETION SEQADV 1BNX A UNP P02730 GLN 403 DELETION SEQADV 1BNX A UNP P02730 VAL 404 DELETION SEQADV 1BNX A UNP P02730 LEU 405 DELETION SEQADV 1BNX A UNP P02730 ALA 406 DELETION SEQADV 1BNX A UNP P02730 ALA 407 DELETION SEQRES 1 A 34 ACE ARG TYR PRO TYR TYR LEU SER ASP ILE THR ASP VAL SEQRES 2 A 34 ILE PHE ILE TYR PHE ALA ALA LEU SER PRO ALA ILE THR SEQRES 3 A 34 PHE GLY GLY LEU LEU GLY GLU LYS HET ACE A 1 6 HETNAM ACE ACETYL GROUP FORMUL 1 ACE C2 H4 O HELIX 1 1 SER A 8 THR A 26 1 19 LINK C ACE A 1 N ARG A 2 1555 1555 1.31 SITE 1 AC1 3 ARG A 2 TYR A 3 PRO A 4 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