Header list of 1wcj.pdb file
Complete list - 25 20 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 17-NOV-04 1WCJ TITLE CONSERVED HYPOTHETICAL PROTEIN TM0487 FROM THERMOTOGA TITLE 2 MARITIMA COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN TM0487; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 2-104; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: CONFORMER WITH THE LOWEST R.M.S.D. TO THE COMPND 7 MEAN STRUCTURE. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA; SOURCE 3 ORGANISM_TAXID: 2336; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET KEYWDS STRUCTURAL GENOMICS, UNKNOWN FUNCTION, CONTAINS PAAD KEYWDS 2 DOMAIN, SIMILAR TO PAAD PROTEIN, UNKNOWN ACTIVITY, KEYWDS 3 ALPHA/BETA FOLD, JCSG, HYPOTHETICAL PROTEIN, PSI, PROTEIN KEYWDS 4 STRUCTURE INITIATIVE, JOINT CENTER FOR STRUCTURAL GENOMICS EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR M.S.ALMEIDA,W.PETI,T.HERRMANN,K.WUTHRICH, AUTHOR 2 JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG) REVDAT 4 24-FEB-09 1WCJ 1 VERSN REVDAT 3 08-NOV-06 1WCJ 1 KEYWDS AUTHOR REVDAT 2 02-NOV-05 1WCJ 1 JRNL REVDAT 1 14-DEC-04 1WCJ 0 JRNL AUTH M.S.ALMEIDA,T.HERRMANN,W.PETI,I.A.WILSON,K.WUTHRICH JRNL TITL NMR STRUCTURE OF THE CONSERVED HYPOTHETICAL JRNL TITL 2 PROTEIN TM0487 FROM THERMOTOGA MARITIMA: JRNL TITL 3 IMPLICATIONS FOR 216 HOMOLOGOUS DUF59 PROTEINS. JRNL REF PROTEIN SCI. V. 14 2880 2005 JRNL REFN ISSN 0961-8368 JRNL PMID 16199668 JRNL DOI 10.1110/PS.051755805 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.S.ALMEIDA,W.PETI,K.WUTHRICH REMARK 1 TITL 1H-, 13C- AND 15N-NMR ASSIGNMENT OF THE CONSERVED REMARK 1 TITL 2 HYPOTHETICAL PROTEIN TM0487 FROM THERMOTOGA REMARK 1 TITL 3 MARITIMA REMARK 1 REF J.BIOMOL.NMR V. 29 453 2004 REMARK 1 REFN ISSN 0925-2738 REMARK 1 PMID 15213465 REMARK 1 DOI 10.1023/B:JNMR.0000032522.43753.F1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : OPALP REMARK 3 AUTHORS : R.KORADI,M.BILLETER,P.GUNTERT REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THIS STRUCTURE WAS ENERGY-MINIMIZED REMARK 3 IN A WATER SHELL USING THE AMBER FORCE FIELD. REMARK 4 REMARK 4 1WCJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-NOV-04. REMARK 100 THE PDBE ID CODE IS EBI-16254. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 313 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 90% H2O/10% D2O, 20 MM REMARK 210 SODIUM PHOSPHATE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N-RESOLVED REMARK 210 [1H,1H]-NOESY; REMARK 210 3D 13C-RESOLVED REMARK 210 [1H,1H]-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 900 REMARK 210 SPECTROMETER MODEL : DRX900 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : ATNOS/CANDID/DYANA REMARK 210 METHOD USED : DISTANCE GEOMETRY REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST R.M.S.D. TO THE REMARK 210 MEAN STRUCTURE REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: IT REPRESENTS THE CLOSEST CONFORMER TO THE MEAN.. REMARK 210 THE SAMPLE WAS 13C AND 15N-LABELED. 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 PRO A 1 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 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 LYS A 16 10.98 -58.10 REMARK 500 VAL A 75 64.30 -45.67 REMARK 500 TRP A 88 -93.85 -70.21 REMARK 500 THR A 89 114.39 158.64 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 CYS A 55 PRO A 56 -146.87 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1UWD RELATED DB: PDB REMARK 900 CONSERVED HYPOTHETICAL PROTEIN TM0487 FROM REMARK 900 THERMOTOGA MARITIMA REMARK 999 REMARK 999 SEQUENCE REMARK 999 MET 1 AND PRO 2 ARE NOT INCLUDED IN THESE STRUCTURES. REMARK 999 THE MET1 IS NOT PRESENT IN THE RECOMBINANT PROTEIN. DBREF 1WCJ A 1 103 UNP Q9WYV7 Q9WYV7 2 104 SEQRES 1 A 103 PRO MET SER LYS LYS VAL THR LYS GLU ASP VAL LEU ASN SEQRES 2 A 103 ALA LEU LYS ASN VAL ILE ASP PHE GLU LEU GLY LEU ASP SEQRES 3 A 103 VAL VAL SER LEU GLY LEU VAL TYR ASP ILE GLN ILE ASP SEQRES 4 A 103 ASP GLN ASN ASN VAL LYS VAL LEU MET THR MET THR THR SEQRES 5 A 103 PRO MET CYS PRO LEU ALA GLY MET ILE LEU SER ASP ALA SEQRES 6 A 103 GLU GLU ALA ILE LYS LYS ILE GLU GLY VAL ASN ASN VAL SEQRES 7 A 103 GLU VAL GLU LEU THR PHE ASP PRO PRO TRP THR PRO GLU SEQRES 8 A 103 ARG MET SER PRO GLU LEU ARG GLU LYS PHE GLY VAL HELIX 1 1 THR A 7 LYS A 16 1 10 HELIX 2 2 ASP A 26 GLY A 31 1 6 HELIX 3 3 LEU A 57 LYS A 70 1 14 HELIX 4 4 THR A 89 MET A 93 5 5 HELIX 5 5 SER A 94 GLY A 102 1 9 SHEET 1 AA 3 ASP A 35 ILE A 38 0 SHEET 2 AA 3 ASN A 43 MET A 48 -1 O LYS A 45 N GLN A 37 SHEET 3 AA 3 ASN A 77 LEU A 82 1 O ASN A 77 N VAL A 44 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 - 25 20 Bytes