Header list of 1b4g.pdb file
Complete list - 16 20 Bytes
HEADER POTASSIUM CHANNEL 22-DEC-98 1B4G TITLE CONTROL OF K+ CHANNEL GATING BY PROTEIN PHOSPHORYLATION: STRUCTURAL TITLE 2 SWITCHES OF THE INACTIVATION GATE, NMR, 22 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: POTASSIUM CHANNEL; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: INACTIVATION DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: SER 8 IS PHOSPHORLYATED SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 4 ORGANISM_COMMON: HUMAN; SOURCE 5 ORGANISM_TAXID: 9606 KEYWDS POTASSIUM CHANNEL, INACTIVATION GATE, PHOSPHORYLATION EXPDTA SOLUTION NMR NUMMDL 22 AUTHOR C.ANTZ,T.BAUER,H.KALBACHER,R.FRANK,M.COVARRUBIAS,H.R.KALBITZER, AUTHOR 2 J.P.RUPPERSBERG,T.BAUKROWITZ,B.FAKLER REVDAT 4 16-FEB-22 1B4G 1 REMARK LINK REVDAT 3 19-MAY-10 1B4G 1 DBREF SOURCE REVDAT 2 24-FEB-09 1B4G 1 VERSN REVDAT 1 27-APR-99 1B4G 0 JRNL AUTH C.ANTZ,T.BAUER,H.KALBACHER,R.FRANK,M.COVARRUBIAS, JRNL AUTH 2 H.R.KALBITZER,J.P.RUPPERSBERG,T.BAUKROWITZ,B.FAKLER JRNL TITL CONTROL OF K+ CHANNEL GATING BY PROTEIN PHOSPHORYLATION: JRNL TITL 2 STRUCTURAL SWITCHES OF THE INACTIVATION GATE. JRNL REF NAT.STRUCT.BIOL. V. 6 146 1999 JRNL REFN ISSN 1072-8368 JRNL PMID 10048926 JRNL DOI 10.1038/5833 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.8 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1B4G 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_1000171472. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 283 REMARK 210 PH : 3.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OG SER A 21 HZ2 LYS A 22 1.48 REMARK 500 HZ2 LYS A 18 OG1 THR A 23 1.50 REMARK 500 HZ2 LYS A 14 O GLY A 16 1.53 REMARK 500 HZ3 LYS A 18 OE2 GLU A 27 1.57 REMARK 500 HZ3 LYS A 26 OXT ALA A 30 1.58 REMARK 500 REMARK 500 REMARK: NULL 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 SER A 4 17.20 56.73 REMARK 500 1 VAL A 7 -77.84 -77.33 REMARK 500 1 SEP A 8 -47.36 -169.43 REMARK 500 1 SER A 9 115.63 64.02 REMARK 500 1 TYR A 10 165.78 58.16 REMARK 500 1 ARG A 11 -143.79 -72.02 REMARK 500 1 GLU A 28 -159.67 -76.66 REMARK 500 2 SER A 4 -35.36 75.02 REMARK 500 2 SER A 9 121.10 64.86 REMARK 500 2 TYR A 10 174.18 53.83 REMARK 500 2 ARG A 11 -137.59 -84.70 REMARK 500 2 ARG A 13 65.80 -112.51 REMARK 500 2 LYS A 22 48.33 -89.35 REMARK 500 2 LEU A 25 -173.27 58.62 REMARK 500 3 SER A 4 99.66 63.72 REMARK 500 3 VAL A 7 -137.35 -87.01 REMARK 500 3 SER A 9 121.26 63.52 REMARK 500 3 TYR A 10 175.74 52.40 REMARK 500 3 ARG A 11 -157.82 -68.37 REMARK 500 3 SER A 21 -148.88 57.66 REMARK 500 3 LYS A 22 63.84 -117.48 REMARK 500 3 THR A 23 32.15 -152.35 REMARK 500 3 CYS A 24 -64.29 -159.52 REMARK 500 3 LYS A 26 79.60 18.17 REMARK 500 4 SER A 4 -71.61 -111.35 REMARK 500 4 CYS A 6 154.14 66.48 REMARK 500 4 SEP A 8 -59.88 -169.23 REMARK 500 4 SER A 9 113.21 60.76 REMARK 500 4 TYR A 10 179.72 48.29 REMARK 500 4 ARG A 11 -153.40 -73.32 REMARK 500 4 LEU A 25 -169.29 -112.82 REMARK 500 4 LYS A 26 43.45 -98.89 REMARK 500 4 MET A 29 -161.19 -103.05 REMARK 500 5 CYS A 6 156.55 69.00 REMARK 500 5 SER A 9 -161.47 62.53 REMARK 500 5 LYS A 14 55.49 -68.49 REMARK 500 5 LYS A 22 54.84 -119.90 REMARK 500 6 SEP A 8 -58.13 -126.60 REMARK 500 6 SER A 9 111.62 62.95 REMARK 500 6 TYR A 10 -161.92 35.93 REMARK 500 6 ARG A 11 -146.74 -85.17 REMARK 500 7 VAL A 7 -146.49 -111.28 REMARK 500 7 SER A 9 116.49 63.32 REMARK 500 7 TYR A 10 172.94 54.64 REMARK 500 7 ARG A 11 -157.51 -70.15 REMARK 500 7 ARG A 13 78.08 -118.89 REMARK 500 7 ASN A 17 -158.22 -136.61 REMARK 500 7 SER A 21 -152.24 56.92 REMARK 500 7 LEU A 25 -161.98 -74.63 REMARK 500 7 MET A 29 -157.09 -103.36 REMARK 500 REMARK 500 THIS ENTRY HAS 177 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 11 0.32 SIDE CHAIN REMARK 500 1 ARG A 13 0.31 SIDE CHAIN REMARK 500 2 ARG A 11 0.30 SIDE CHAIN REMARK 500 2 ARG A 13 0.32 SIDE CHAIN REMARK 500 3 ARG A 11 0.32 SIDE CHAIN REMARK 500 3 ARG A 13 0.29 SIDE CHAIN REMARK 500 4 ARG A 11 0.32 SIDE CHAIN REMARK 500 4 ARG A 13 0.31 SIDE CHAIN REMARK 500 5 ARG A 11 0.26 SIDE CHAIN REMARK 500 5 ARG A 13 0.21 SIDE CHAIN REMARK 500 6 ARG A 11 0.29 SIDE CHAIN REMARK 500 6 ARG A 13 0.31 SIDE CHAIN REMARK 500 7 ARG A 11 0.29 SIDE CHAIN REMARK 500 7 ARG A 13 0.27 SIDE CHAIN REMARK 500 8 ARG A 11 0.32 SIDE CHAIN REMARK 500 8 ARG A 13 0.26 SIDE CHAIN REMARK 500 9 ARG A 11 0.30 SIDE CHAIN REMARK 500 9 ARG A 13 0.31 SIDE CHAIN REMARK 500 10 ARG A 11 0.32 SIDE CHAIN REMARK 500 10 ARG A 13 0.30 SIDE CHAIN REMARK 500 11 ARG A 11 0.31 SIDE CHAIN REMARK 500 11 ARG A 13 0.30 SIDE CHAIN REMARK 500 12 ARG A 11 0.30 SIDE CHAIN REMARK 500 12 ARG A 13 0.31 SIDE CHAIN REMARK 500 13 ARG A 11 0.31 SIDE CHAIN REMARK 500 13 ARG A 13 0.30 SIDE CHAIN REMARK 500 14 ARG A 11 0.28 SIDE CHAIN REMARK 500 14 ARG A 13 0.32 SIDE CHAIN REMARK 500 15 ARG A 11 0.32 SIDE CHAIN REMARK 500 15 ARG A 13 0.21 SIDE CHAIN REMARK 500 16 ARG A 11 0.32 SIDE CHAIN REMARK 500 16 ARG A 13 0.32 SIDE CHAIN REMARK 500 17 ARG A 11 0.29 SIDE CHAIN REMARK 500 17 ARG A 13 0.28 SIDE CHAIN REMARK 500 18 ARG A 11 0.29 SIDE CHAIN REMARK 500 18 ARG A 13 0.28 SIDE CHAIN REMARK 500 19 ARG A 11 0.31 SIDE CHAIN REMARK 500 19 ARG A 13 0.32 SIDE CHAIN REMARK 500 20 ARG A 11 0.32 SIDE CHAIN REMARK 500 20 ARG A 13 0.31 SIDE CHAIN REMARK 500 21 ARG A 11 0.30 SIDE CHAIN REMARK 500 21 ARG A 13 0.30 SIDE CHAIN REMARK 500 22 ARG A 11 0.31 SIDE CHAIN REMARK 500 22 ARG A 13 0.31 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1B4G A 1 30 UNP Q03721 KCNC4_HUMAN 1 30 SEQRES 1 A 30 MET ILE SER SER VAL CYS VAL SEP SER TYR ARG GLY ARG SEQRES 2 A 30 LYS SER GLY ASN LYS PRO PRO SER LYS THR CYS LEU LYS SEQRES 3 A 30 GLU GLU MET ALA MODRES 1B4G SEP A 8 SER PHOSPHOSERINE HET SEP A 8 15 HETNAM SEP PHOSPHOSERINE HETSYN SEP PHOSPHONOSERINE FORMUL 1 SEP C3 H8 N O6 P LINK C VAL A 7 N SEP A 8 1555 1555 1.31 LINK C SEP A 8 N SER A 9 1555 1555 1.32 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