Header list of 1x9b.pdb file
Complete list - 31 20 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 20-AUG-04 1X9B TITLE SOLUTION NMR STRUCTURE OF PROTEIN TA0354 FROM THERMOPLASMA TITLE 2 ACIDOPHILUM. ONTARIO CENTER FOR STRUCTURAL PROTEOMICS TARGET TITLE 3 TA0354_69_121; NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET TAT38. COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL MEMBRANE PROTEIN TA0354_69_121; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 69-212; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: THERMOPLASMA ACIDOPHILUM; SOURCE 3 ORGANISM_TAXID: 2303; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B KEYWDS ALPHA PROTEIN, STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, KEYWDS 2 PSI, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, ONTARIO CENTER KEYWDS 3 FOR STRUCTURAL PROTEOMICS, OCSP, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR B.WU,A.YEE,Y.J.HUANG,T.A.RAMELOT,A.SEMESI,A.LEMAK,A.EDWARD,M.KENNEDY, AUTHOR 2 G.T.MONTELIONE,C.H.ARROWSMITH,NORTHEAST STRUCTURAL GENOMICS AUTHOR 3 CONSORTIUM (NESG),ONTARIO CENTRE FOR STRUCTURAL PROTEOMICS (OCSP) REVDAT 3 31-JAN-18 1X9B 1 AUTHOR REMARK REVDAT 2 24-FEB-09 1X9B 1 VERSN REVDAT 1 14-DEC-04 1X9B 0 JRNL AUTH B.WU,A.YEE,Y.J.HUANG,T.A.RAMELOT,A.SEMESI,A.LEMAK,A.EDWARD, JRNL AUTH 2 M.KENNEDY,G.T.MONTELIONE,C.H.ARROWSMITH JRNL TITL SOLUTION STRUCTURE OF HYPOTHETICAL MEMBRANE PROTEIN JRNL TITL 2 TA0354_69_121 FROM THERMOPLASMA ACIDOPHILUM JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2.1, CNS 1.0 REMARK 3 AUTHORS : DELAGLIO,F. (NMRPIPE), BRUNGER, A.T. ET AL. (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 1131 NOE-DERIVED DISTANCE CONSTRAINTS REMARK 3 AND 142 TORSION ANGLE CONSTRAINTS REMARK 4 REMARK 4 1X9B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-04. REMARK 100 THE DEPOSITION ID IS D_1000030101. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 450 MM NACL, 25 MM PHOSPHATE REMARK 210 BUFFER REMARK 210 PRESSURE : AMBINET REMARK 210 SAMPLE CONTENTS : 1 MM TA0354, U-15N,13C; 450 MM REMARK 210 NACL, 25 MM NA2PO4, 1 MM REMARK 210 BENZAMIDINE, 1XINHIBITOR REMARK 210 COOKTAIL, 0.01% NAN3, 95% H2O, 5% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 4D_13C- REMARK 210 SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : AUTOSTRUCTURE 2.0 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 56 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 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 51 -66.50 175.36 REMARK 500 1 VAL A 52 68.94 26.46 REMARK 500 3 SER A 4 -49.80 73.28 REMARK 500 4 SER A 4 120.15 68.84 REMARK 500 4 LYS A 18 -72.45 -57.12 REMARK 500 5 ASN A 2 -178.54 61.01 REMARK 500 5 ASN A 14 -78.44 -52.65 REMARK 500 5 SER A 15 77.54 -150.72 REMARK 500 5 LYS A 51 -40.12 71.66 REMARK 500 5 VAL A 52 96.78 61.65 REMARK 500 6 SER A 15 73.20 -161.06 REMARK 500 7 LYS A 18 -71.09 -63.80 REMARK 500 8 ASN A 2 106.95 66.21 REMARK 500 9 ASN A 2 -92.58 58.97 REMARK 500 10 SER A 15 70.57 46.85 REMARK 500 10 PRO A 16 -158.11 -100.08 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6291 RELATED DB: BMRB REMARK 900 RELATED ID: TAT38 RELATED DB: TARGETDB DBREF 1X9B A 1 53 UNP Q9HL76 Q9HL76_THEAC 69 121 SEQRES 1 A 53 ARG ASN LEU SER ASP ARG ALA LYS PHE GLU SER MET ILE SEQRES 2 A 53 ASN SER PRO SER LYS SER VAL PHE VAL ARG ASN LEU ASN SEQRES 3 A 53 GLU LEU GLU ALA LEU ALA VAL ARG LEU GLY LYS SER TYR SEQRES 4 A 53 ARG ILE GLN LEU ASP GLN ALA LYS GLU LYS TRP LYS VAL SEQRES 5 A 53 LYS HELIX 1 1 SER A 4 SER A 15 1 12 HELIX 2 2 SER A 17 GLY A 36 1 20 HELIX 3 3 LYS A 37 LYS A 51 1 15 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 - 31 20 Bytes