Header list of 3mef.pdb file
Complete list - r 25 2 Bytes
HEADER GENE REGULATION 09-OCT-98 3MEF TITLE MAJOR COLD-SHOCK PROTEIN FROM ESCHERICHIA COLI SOLUTION NMR STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (COLD-SHOCK PROTEIN A); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FULL LENGTH PROTEIN; COMPND 5 SYNONYM: CSPA, CS7.4; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 469008; SOURCE 4 STRAIN: BL21(DE3); SOURCE 5 GENE: U60035; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11-CSPA; SOURCE 11 EXPRESSION_SYSTEM_GENE: U60035; SOURCE 12 OTHER_DETAILS: PCR-GENERATED GENE KEYWDS COLD-SHOCK PROTEIN, TRANSCRIPTION REGULATION, SINGLE-STRANDED RNA/DNA KEYWDS 2 BINDING, OB FOLD, GREEK-KEY TOPOLOGY, RNA CHAPERONE, AROMATIC-BASE KEYWDS 3 STACKING INTERACTIONS, GENE REGULATION EXPDTA SOLUTION NMR NUMMDL 16 AUTHOR W.FENG,R.TEJERO,G.T.MONTELIONE REVDAT 5 13-JUL-11 3MEF 1 VERSN REVDAT 4 24-FEB-09 3MEF 1 VERSN REVDAT 3 01-APR-03 3MEF 1 JRNL REVDAT 2 22-DEC-99 3MEF 4 HEADER COMPND REMARK JRNL REVDAT 2 2 4 ATOM SOURCE SEQRES REVDAT 1 14-OCT-98 3MEF 0 SPRSDE 14-OCT-98 3MEF 1MEF JRNL AUTH W.FENG,R.TEJERO,D.E.ZIMMERMAN,M.INOUYE,G.T.MONTELIONE JRNL TITL SOLUTION NMR STRUCTURE AND BACKBONE DYNAMICS OF THE MAJOR JRNL TITL 2 COLD-SHOCK PROTEIN (CSPA) FROM ESCHERICHIA COLI: EVIDENCE JRNL TITL 3 FOR CONFORMATIONAL DYNAMICS IN THE SINGLE-STRANDED JRNL TITL 4 RNA-BINDING SITE. JRNL REF BIOCHEMISTRY V. 37 10881 1998 JRNL REFN ISSN 0006-2960 JRNL PMID 9692981 JRNL DOI 10.1021/BI980269J REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.NEWKIRK,W.FENG,W.JIANG,R.TEJERO,S.D.EMERSON,M.INOUYE, REMARK 1 AUTH 2 G.T.MONTELIONE REMARK 1 TITL SOLUTION NMR STRUCTURE OF THE MAJOR COLD SHOCK PROTEIN REMARK 1 TITL 2 (CSPA) FROM ESCHERICHIA COLI: IDENTIFICATION OF A BINDING REMARK 1 TITL 3 EPITOPE FOR DNA REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 91 5114 1994 REMARK 1 REFN ISSN 0027-8424 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DIANA REMARK 3 AUTHORS : WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION REMARK 4 REMARK 4 3MEF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-99. REMARK 100 THE RCSB ID CODE IS RCSB008057. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 50 MILLIMOLAR SODIUM PHOSPHATE REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D PFG-[15N]HSQC; 3D PFG-HNCO; REMARK 210 3D PFG-(HA)CA(CO)NH; 3D PFG- REMARK 210 HA(CA)(CO)NH; 3D PFG-HA(CA)NH; 3D REMARK 210 PFG-CBCANH; 3D PFG-CBCA(CO)NH; 3D REMARK 210 PFG- (HA)CANH; 3D PFG-HCCNH- REMARK 210 TOCSY; 3D PFG-HCC(CO)NH-TOCSY; 2D REMARK 210 CT PFG-[13C 2D HSQC-TOCSY; 2D 2QF REMARK 210 -COSY; 2D NOESY; 2D TOCSY; 3D PFG REMARK 210 -15N-EDITED NOESY; 2D HSQC-J REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITY 500 REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DIANA REMARK 210 METHOD USED : CONSTRAINT-VIOLATION REMARK 210 MINIMIZATION IN DIHEDRAL ANGLE REMARK 210 SPACE REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 500 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST VALUE OF TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURES WERE DETERMINED USING DOUBLE- AND TRIPLE- REMARK 210 RESONANCE NMR SPECTROSCOPY METHODS ON UNENRICHED, 15N-ENRICHED, REMARK 210 AND 13C,15N-ENRICHED CSPA FROM E.COLI - 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 HD1 HIS A 33 H SER A 35 1.53 REMARK 500 H GLU A 56 O ALA A 64 1.60 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 LYS A 10 -61.06 -99.35 REMARK 500 1 ASP A 24 -70.06 -51.11 REMARK 500 1 LYS A 28 -173.88 -57.84 REMARK 500 1 PHE A 34 41.18 -98.90 REMARK 500 1 ALA A 36 37.53 -170.46 REMARK 500 1 ASN A 39 42.86 -146.56 REMARK 500 1 ASP A 40 -92.30 58.89 REMARK 500 1 TYR A 42 72.74 31.16 REMARK 500 1 PHE A 53 -161.45 -169.85 REMARK 500 1 THR A 54 29.58 -154.24 REMARK 500 1 ILE A 55 83.11 34.35 REMARK 500 1 ALA A 59 -77.43 -108.42 REMARK 500 1 LYS A 60 -86.61 -100.93 REMARK 500 1 ALA A 63 101.26 175.49 REMARK 500 1 ALA A 64 -143.02 38.33 REMARK 500 2 SER A 27 -108.49 -116.76 REMARK 500 2 PHE A 34 -164.93 46.18 REMARK 500 2 SER A 35 -26.59 71.81 REMARK 500 2 GLN A 38 100.23 -36.30 REMARK 500 2 ASN A 39 -148.28 -109.97 REMARK 500 2 LYS A 43 97.92 -50.38 REMARK 500 2 SER A 44 109.01 -169.32 REMARK 500 2 LEU A 45 -139.71 -143.14 REMARK 500 2 ASP A 46 -155.24 41.98 REMARK 500 2 PHE A 53 -159.60 -153.49 REMARK 500 2 THR A 54 29.27 -151.61 REMARK 500 2 ILE A 55 86.26 36.95 REMARK 500 2 ALA A 59 -161.45 -164.48 REMARK 500 3 ASP A 24 -91.52 -51.80 REMARK 500 3 LYS A 28 -169.82 92.74 REMARK 500 3 PHE A 34 -156.44 -63.36 REMARK 500 3 SER A 35 -48.46 73.61 REMARK 500 3 GLN A 38 95.39 -67.19 REMARK 500 3 ASN A 39 121.70 175.73 REMARK 500 3 ASP A 40 -91.17 58.30 REMARK 500 3 TYR A 42 50.04 31.18 REMARK 500 3 VAL A 51 -169.53 -113.29 REMARK 500 3 PHE A 53 -157.80 -162.85 REMARK 500 3 ILE A 55 86.34 13.06 REMARK 500 3 GLU A 56 133.95 -177.34 REMARK 500 3 ALA A 59 -39.20 176.75 REMARK 500 3 ALA A 63 -159.99 175.03 REMARK 500 3 ALA A 64 -146.07 -74.52 REMARK 500 3 ASN A 66 62.36 60.13 REMARK 500 3 SER A 69 160.93 -45.30 REMARK 500 4 PHE A 12 119.71 -173.71 REMARK 500 4 PRO A 23 -165.07 -75.08 REMARK 500 4 ASP A 24 0.51 -67.24 REMARK 500 4 ASP A 25 0.84 120.52 REMARK 500 4 SER A 27 -38.29 98.77 REMARK 500 REMARK 500 THIS ENTRY HAS 285 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 3MEF A 2 70 UNP P0A9X9 CSPA_ECOLI 2 70 SEQRES 1 A 69 SER GLY LYS MET THR GLY ILE VAL LYS TRP PHE ASN ALA SEQRES 2 A 69 ASP LYS GLY PHE GLY PHE ILE THR PRO ASP ASP GLY SER SEQRES 3 A 69 LYS ASP VAL PHE VAL HIS PHE SER ALA ILE GLN ASN ASP SEQRES 4 A 69 GLY TYR LYS SER LEU ASP GLU GLY GLN LYS VAL SER PHE SEQRES 5 A 69 THR ILE GLU SER GLY ALA LYS GLY PRO ALA ALA GLY ASN SEQRES 6 A 69 VAL THR SER LEU SHEET 1 S1 1 MET A 5 ASN A 13 0 SHEET 1 S2 1 PHE A 18 THR A 22 0 SHEET 1 S3 1 VAL A 30 HIS A 33 0 SHEET 1 S4 1 LYS A 50 GLU A 56 0 SHEET 1 S5 1 ALA A 63 LEU A 70 0 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 - r 25 2 Bytes