Header list of 1b4c.pdb file
Complete list - b 16 2 Bytes
HEADER METAL BINDING PROTEIN 17-DEC-98 1B4C TITLE SOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLINGS COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (S-100 PROTEIN, BETA CHAIN); COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: S100B, S100BETA; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: S100B IS A HOMODIMER OF S100BETA SUBUNITS SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 GENE: S100BETA FROM RATTUS NORVEGICUS (RAT); SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3); SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11B; SOURCE 10 OTHER_DETAILS: SEE MAIN REFERENCE KEYWDS S100BETA, S100B, DIPOLAR COUPLINGS, EF-HAND, S100 PROTEIN, CALCIUM- KEYWDS 2 BINDING PROTEIN, FOUR-HELIX BUNDLE, THREE-DIMENSIONAL STRUCTURE, KEYWDS 3 SOLUTION STRUCTURE, METAL BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 21 AUTHOR D.J.WEBER,A.C.DROHAT,N.TJANDRA,D.M.BALDISSERI REVDAT 5 16-FEB-22 1B4C 1 REMARK REVDAT 4 24-FEB-09 1B4C 1 VERSN REVDAT 3 28-JAN-00 1B4C 1 JRNL REVDAT 2 29-DEC-99 1B4C 4 HEADER COMPND REMARK JRNL REVDAT 2 2 4 ATOM SOURCE SEQRES REVDAT 1 30-DEC-98 1B4C 0 JRNL AUTH A.C.DROHAT,N.TJANDRA,D.M.BALDISSERI,D.J.WEBER JRNL TITL THE USE OF DIPOLAR COUPLINGS FOR DETERMINING THE SOLUTION JRNL TITL 2 STRUCTURE OF RAT APO-S100B(BETABETA). JRNL REF PROTEIN SCI. V. 8 800 1999 JRNL REFN ISSN 0961-8368 JRNL PMID 10211826 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.C.DROHAT,J.C.AMBURGEY,F.ABILDGAARD,M.R.STARICH, REMARK 1 AUTH 2 D.M.BALDISSERI,D.J.WEBER REMARK 1 TITL SOLUTION STRUCTURE OF RAT APO-S100B(BETA BETA) AS DETERMINED REMARK 1 TITL 2 BY NMR SPECTROSCOPY REMARK 1 REF BIOCHEMISTRY V. 35 11577 1996 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.C.AMBURGEY,F.ABILDGAARD,M.R.STARICH,S.SHAH,D.C.HILT, REMARK 1 AUTH 2 D.J.WEBER REMARK 1 TITL ==1==H, ==13==C AND ==15==N NMR ASSIGNMENTS AND SOLUTION REMARK 1 TITL 2 SECONDARY STRUCTURE OF RAT APO-S100BETA REMARK 1 REF J.BIOMOL.NMR V. 6 171 1995 REMARK 1 REFN ISSN 0925-2738 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR V3.851 V3.851 REMARK 3 AUTHORS : AXEL T. BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SEE MAIN REFERENCE REMARK 4 REMARK 4 1B4C 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_1000008303. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 25MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE MAIN REFERENCE REMARK 210 SPECTROMETER FIELD STRENGTH : 600.13 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR V3.851 V3.851 REMARK 210 METHOD USED : SEE MAIN REFERENCE REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 21 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21 REMARK 210 CONFORMERS, SELECTION CRITERIA : SEE MAIN REFERENCE REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2 REMARK 210 REMARK 210 REMARK: SEE MAIN REFERENCE 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 O SER B 78 H THR B 82 1.53 REMARK 500 O SER A 78 H THR A 82 1.53 REMARK 500 O GLU B 49 H VAL B 52 1.59 REMARK 500 O GLU A 49 H VAL A 52 1.59 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 GLU A 21 -45.19 -146.49 REMARK 500 1 GLU A 46 55.59 -90.48 REMARK 500 1 LYS A 48 -46.26 -143.05 REMARK 500 1 GLU B 21 -45.16 -146.46 REMARK 500 1 GLU B 46 55.68 -90.57 REMARK 500 1 LYS B 48 -46.20 -143.01 REMARK 500 1 GLU B 62 40.03 -101.95 REMARK 500 2 SER A 18 59.00 -100.10 REMARK 500 2 GLU A 21 -47.85 -144.97 REMARK 500 2 HIS A 25 39.43 -99.07 REMARK 500 2 GLU A 62 39.82 -98.58 REMARK 500 2 HIS A 85 177.56 -49.86 REMARK 500 2 GLU A 86 100.10 -45.23 REMARK 500 2 HIS A 90 35.44 -75.18 REMARK 500 2 SER B 18 59.04 -100.07 REMARK 500 2 GLU B 21 -47.82 -144.93 REMARK 500 2 HIS B 25 39.37 -99.09 REMARK 500 2 GLU B 62 39.92 -98.62 REMARK 500 2 HIS B 85 177.61 -49.90 REMARK 500 2 GLU B 86 100.09 -45.24 REMARK 500 2 HIS B 90 35.38 -75.19 REMARK 500 3 SER A 18 58.48 -97.35 REMARK 500 3 GLU A 21 -44.91 -147.29 REMARK 500 3 GLU A 62 41.62 -102.30 REMARK 500 3 HIS A 85 175.23 -49.02 REMARK 500 3 GLU A 86 101.51 -43.89 REMARK 500 3 GLU A 89 49.22 -94.04 REMARK 500 3 HIS A 90 81.60 -59.09 REMARK 500 3 SER B 18 58.51 -97.30 REMARK 500 3 GLU B 21 -44.82 -147.38 REMARK 500 3 GLU B 62 41.62 -102.34 REMARK 500 3 HIS B 85 175.20 -48.89 REMARK 500 3 GLU B 86 101.53 -43.87 REMARK 500 3 GLU B 89 49.18 -94.00 REMARK 500 3 HIS B 90 81.66 -59.10 REMARK 500 4 SER A 18 59.78 -99.12 REMARK 500 4 GLU A 21 -46.12 -146.35 REMARK 500 4 HIS A 85 174.27 -47.91 REMARK 500 4 GLU A 86 99.81 -47.45 REMARK 500 4 GLU A 89 55.27 -103.31 REMARK 500 4 HIS A 90 67.62 -67.00 REMARK 500 4 SER B 18 59.83 -99.10 REMARK 500 4 GLU B 21 -46.15 -146.27 REMARK 500 4 HIS B 85 174.34 -47.91 REMARK 500 4 GLU B 86 99.82 -47.55 REMARK 500 4 GLU B 89 55.15 -103.22 REMARK 500 4 HIS B 90 67.57 -66.99 REMARK 500 5 GLU A 21 -45.14 -148.79 REMARK 500 5 LYS A 48 -50.71 -139.76 REMARK 500 5 GLU A 62 41.52 -101.40 REMARK 500 REMARK 500 THIS ENTRY HAS 236 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 20 0.32 SIDE CHAIN REMARK 500 1 ARG B 20 0.32 SIDE CHAIN REMARK 500 2 ARG A 20 0.29 SIDE CHAIN REMARK 500 2 ARG B 20 0.29 SIDE CHAIN REMARK 500 3 ARG A 20 0.27 SIDE CHAIN REMARK 500 3 ARG B 20 0.26 SIDE CHAIN REMARK 500 4 ARG A 20 0.29 SIDE CHAIN REMARK 500 4 ARG B 20 0.29 SIDE CHAIN REMARK 500 5 ARG A 20 0.18 SIDE CHAIN REMARK 500 5 ARG B 20 0.18 SIDE CHAIN REMARK 500 6 ARG A 20 0.30 SIDE CHAIN REMARK 500 6 ARG B 20 0.30 SIDE CHAIN REMARK 500 7 ARG A 20 0.31 SIDE CHAIN REMARK 500 7 ARG B 20 0.31 SIDE CHAIN REMARK 500 8 ARG A 20 0.20 SIDE CHAIN REMARK 500 8 ARG B 20 0.20 SIDE CHAIN REMARK 500 9 ARG A 20 0.30 SIDE CHAIN REMARK 500 9 ARG B 20 0.30 SIDE CHAIN REMARK 500 10 ARG A 20 0.31 SIDE CHAIN REMARK 500 10 ARG B 20 0.31 SIDE CHAIN REMARK 500 11 ARG A 20 0.19 SIDE CHAIN REMARK 500 11 ARG B 20 0.19 SIDE CHAIN REMARK 500 12 ARG A 20 0.26 SIDE CHAIN REMARK 500 12 ARG B 20 0.26 SIDE CHAIN REMARK 500 13 ARG A 20 0.17 SIDE CHAIN REMARK 500 13 ARG B 20 0.17 SIDE CHAIN REMARK 500 14 ARG A 20 0.09 SIDE CHAIN REMARK 500 14 ARG B 20 0.09 SIDE CHAIN REMARK 500 16 ARG A 20 0.29 SIDE CHAIN REMARK 500 16 ARG B 20 0.29 SIDE CHAIN REMARK 500 17 ARG A 20 0.30 SIDE CHAIN REMARK 500 17 ARG B 20 0.30 SIDE CHAIN REMARK 500 18 ARG A 20 0.13 SIDE CHAIN REMARK 500 18 ARG B 20 0.13 SIDE CHAIN REMARK 500 19 ARG A 20 0.32 SIDE CHAIN REMARK 500 19 ARG B 20 0.32 SIDE CHAIN REMARK 500 20 ARG A 20 0.16 SIDE CHAIN REMARK 500 20 ARG B 20 0.16 SIDE CHAIN REMARK 500 21 ARG A 20 0.29 SIDE CHAIN REMARK 500 21 ARG B 20 0.29 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1B4C A 1 91 UNP P04631 S100B_RAT 1 91 DBREF 1B4C B 1 91 UNP P04631 S100B_RAT 1 91 SEQADV 1B4C MET A 0 UNP P04631 SEE REMARK 999 SEQADV 1B4C MET B 0 UNP P04631 SEE REMARK 999 SEQRES 1 A 92 MET SER GLU LEU GLU LYS ALA MET VAL ALA LEU ILE ASP SEQRES 2 A 92 VAL PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS SEQRES 3 A 92 LYS LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN SEQRES 4 A 92 GLU LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU SEQRES 5 A 92 VAL VAL ASP LYS VAL MET GLU THR LEU ASP GLU ASP GLY SEQRES 6 A 92 ASP GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL SEQRES 7 A 92 SER MET VAL THR THR ALA CYS HIS GLU PHE PHE GLU HIS SEQRES 8 A 92 GLU SEQRES 1 B 92 MET SER GLU LEU GLU LYS ALA MET VAL ALA LEU ILE ASP SEQRES 2 B 92 VAL PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS SEQRES 3 B 92 LYS LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN SEQRES 4 B 92 GLU LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU SEQRES 5 B 92 VAL VAL ASP LYS VAL MET GLU THR LEU ASP GLU ASP GLY SEQRES 6 B 92 ASP GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL SEQRES 7 B 92 SER MET VAL THR THR ALA CYS HIS GLU PHE PHE GLU HIS SEQRES 8 B 92 GLU HELIX 1 1A GLU A 2 GLY A 19 1 18 HELIX 2 2A LYS A 29 GLU A 39 1 11 HELIX 3 3A PHE A 43 GLU A 45 5 3 HELIX 4 4A GLN A 50 ASP A 61 1 12 HELIX 5 5A PHE A 70 ALA A 83 1 14 HELIX 6 6A SER A 41 GLU A 45 1 5 HELIX 7 7A PHE A 70 THR A 82 1 13 HELIX 8 8A PHE A 87 GLU A 89 5 3 HELIX 9 9A PHE A 70 CYS A 84 1 15 HELIX 10 10A HIS A 85 PHE A 87 5 3 HELIX 11 11A GLN A 50 GLU A 62 1 13 HELIX 12 1B GLU B 2 GLY B 19 1 18 HELIX 13 2B LYS B 29 GLU B 39 1 11 HELIX 14 3B PHE B 43 GLU B 45 5 3 HELIX 15 4B GLN B 50 ASP B 61 1 12 HELIX 16 5B PHE B 70 ALA B 83 1 14 HELIX 17 6B SER B 41 GLU B 45 1 5 HELIX 18 7B PHE B 70 THR B 82 1 13 HELIX 19 8B PHE B 87 GLU B 89 5 3 HELIX 20 9B PHE B 70 CYS B 84 1 15 HELIX 21 10B HIS B 85 PHE B 87 5 3 HELIX 22 11B GLN B 50 GLU B 62 1 13 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