Header list of 2a7y.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 06-JUL-05 2A7Y TITLE SOLUTION STRUCTURE OF THE CONSERVED HYPOTHETICAL PROTEIN RV2302 FROM TITLE 2 THE BACTERIUM MYCOBACTERIUM TUBERCULOSIS COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN RV2302/MT2359; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS; SOURCE 3 ORGANISM_TAXID: 1773; SOURCE 4 GENE: RV2302; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21PRO; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B KEYWDS ANTI-PARALLEL BETA SHEET, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE KEYWDS 2 INITIATIVE, TB STRUCTURAL GENOMICS CONSORTIUM, TBSGC, UNKNOWN KEYWDS 3 FUNCTION EXPDTA SOLUTION NMR NUMMDL 25 AUTHOR G.W.BUCHKO,C.-Y.KIM,T.C.TERWILLIGER,M.A.KENNEDY,TB STRUCTURAL AUTHOR 2 GENOMICS CONSORTIUM (TBSGC) REVDAT 4 09-MAR-22 2A7Y 1 REMARK REVDAT 3 24-FEB-09 2A7Y 1 VERSN REVDAT 2 08-AUG-06 2A7Y 1 JRNL REVDAT 1 23-AUG-05 2A7Y 0 JRNL AUTH G.W.BUCHKO,C.Y.KIM,T.C.TERWILLIGER,M.A.KENNEDY JRNL TITL SOLUTION STRUCTURE OF THE CONSERVED HYPOTHETICAL PROTEIN JRNL TITL 2 RV2302 FROM MYCOBACTERIUM TUBERCULOSIS. JRNL REF J.BACTERIOL. V. 188 5993 2006 JRNL REFN ISSN 0021-9193 JRNL PMID 16885468 JRNL DOI 10.1128/JB.00460-06 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1, CNS 1.1 REMARK 3 AUTHORS : WARREN, NILGES, KUSZEWSKI, CLORE & BRUNGER (CNS), REMARK 3 WARREN, NILGES, KUSZEWSKI, CLORE & BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: FINAL SET OF STRUCTURES WERE REFINED REMARK 3 WITH EXPLICIT WATER. REMARK 4 REMARK 4 2A7Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-05. REMARK 100 THE DEPOSITION ID IS D_1000033600. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.1 REMARK 210 IONIC STRENGTH : 100 MM KCL, 20 MM POTASSIUM REMARK 210 PHOSPHATE REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : ~ 2 MM PROTEIN; UNIFORMILY 15N- REMARK 210 AND 13C-LABELED; 100 MM KCL, 20 REMARK 210 MM POTASSIUM PHOSPHATE, 2.0 MM REMARK 210 DITHIOTHREITOL, PH 7.1, 90% H2O, REMARK 210 10%D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 4D_13C- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 98 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 55 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 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: TYPICAL SUITE OF BACKBONE ASSIGNMENT EXPERIMENTS COLLECTED REMARK 210 AND ANALYZED. 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-25 REMARK 465 RES C SSSEQI REMARK 465 GLY A -2 REMARK 465 SER A -1 REMARK 465 HIS A 0 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 12 138.38 78.53 REMARK 500 1 THR A 16 84.57 75.61 REMARK 500 1 GLU A 17 -60.13 -152.53 REMARK 500 1 ASP A 20 -166.06 -109.44 REMARK 500 1 GLN A 21 85.46 40.33 REMARK 500 1 ARG A 29 32.30 -88.83 REMARK 500 1 ASP A 32 -70.84 -130.53 REMARK 500 1 ASN A 44 -64.22 -100.01 REMARK 500 1 THR A 48 -179.95 -175.18 REMARK 500 1 THR A 60 -169.78 -119.31 REMARK 500 1 ALA A 65 -73.77 -56.86 REMARK 500 2 THR A 14 4.88 -68.85 REMARK 500 2 GLN A 21 128.16 149.61 REMARK 500 2 ARG A 29 55.03 -110.36 REMARK 500 2 SER A 54 -167.94 -79.30 REMARK 500 2 ALA A 56 158.62 73.41 REMARK 500 2 THR A 60 -163.43 -124.46 REMARK 500 2 ALA A 65 -73.30 -56.93 REMARK 500 2 LYS A 69 -77.48 -56.95 REMARK 500 3 GLU A 17 32.37 -76.41 REMARK 500 3 GLN A 21 96.87 64.61 REMARK 500 3 ARG A 29 33.10 -98.46 REMARK 500 3 SER A 30 -90.86 -122.79 REMARK 500 3 ALA A 31 -66.45 176.00 REMARK 500 3 THR A 60 -164.52 -122.72 REMARK 500 3 ALA A 65 -76.43 -61.46 REMARK 500 4 GLN A 21 90.60 53.48 REMARK 500 4 ASP A 55 -60.56 70.88 REMARK 500 4 ALA A 56 132.14 51.95 REMARK 500 4 THR A 60 -164.33 -118.86 REMARK 500 4 ALA A 65 -73.21 -60.35 REMARK 500 4 ALA A 73 -73.43 -75.71 REMARK 500 5 HIS A 2 100.10 -162.08 REMARK 500 5 LYS A 12 -51.75 78.55 REMARK 500 5 THR A 15 -79.31 -152.11 REMARK 500 5 GLN A 21 101.29 63.07 REMARK 500 5 ALA A 23 -179.82 -179.01 REMARK 500 5 ARG A 29 38.78 -95.50 REMARK 500 5 THR A 60 -165.10 -119.41 REMARK 500 5 ALA A 65 -70.23 -60.04 REMARK 500 5 LYS A 69 -71.46 -56.67 REMARK 500 5 ALA A 78 22.33 -168.59 REMARK 500 6 GLN A 21 104.26 53.73 REMARK 500 6 SER A 30 -35.34 172.23 REMARK 500 6 ALA A 31 -16.44 74.63 REMARK 500 6 ASP A 55 50.95 -143.86 REMARK 500 6 THR A 60 -169.18 -116.39 REMARK 500 6 ALA A 65 -76.02 -56.98 REMARK 500 6 ALA A 78 -50.13 -129.70 REMARK 500 6 ALA A 79 131.55 67.17 REMARK 500 REMARK 500 THIS ENTRY HAS 193 RAMACHANDRAN OUTLIERS. 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 ASP A 7 TYR A 8 2 -142.01 REMARK 500 GLU A 24 ILE A 25 2 -148.20 REMARK 500 ASP A 7 TYR A 8 7 -142.19 REMARK 500 TYR A 8 LEU A 9 7 -149.73 REMARK 500 VAL A 38 VAL A 39 7 -129.29 REMARK 500 VAL A 38 VAL A 39 14 -149.19 REMARK 500 ASP A 7 TYR A 8 19 -148.18 REMARK 500 VAL A 38 VAL A 39 19 -149.45 REMARK 500 ASP A 7 TYR A 8 23 -148.48 REMARK 500 VAL A 38 VAL A 39 25 -149.56 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: RV2302 RELATED DB: TARGETDB REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE PROTEIN WAS EXPRESSED WITH THE FOLLOWING REMARK 999 HISTIDINE-TAG (MGSSHHHHHHSSGLVPRGSH-) AT THE REMARK 999 N-TERMINUS OF RV2302. FOLLOWING THROMBIN REMARK 999 CLEAVAGE GSH- REMAINED AT THE N-TERMINUS. REMARK 999 BECAUSE NO 1H-15N HSQC CROSS PEAKS WERE REMARK 999 OBSERVED FOR THESE N-TERMINAL THREE RESIDUES, REMARK 999 THESE THREE RESIDUES WERE NOT INCLUDED IN REMARK 999 THE STRUCTURE CALCULATIONS. DBREF 2A7Y A 1 80 UNP P64983 Y2302_MYCTU 1 80 SEQADV 2A7Y GLY A -2 UNP P64983 SEE REMARK 999 SEQADV 2A7Y SER A -1 UNP P64983 SEE REMARK 999 SEQADV 2A7Y HIS A 0 UNP P64983 SEE REMARK 999 SEQRES 1 A 83 GLY SER HIS MET HIS ALA LYS VAL GLY ASP TYR LEU VAL SEQRES 2 A 83 VAL LYS GLY THR THR THR GLU ARG HIS ASP GLN HIS ALA SEQRES 3 A 83 GLU ILE ILE GLU VAL ARG SER ALA ASP GLY SER PRO PRO SEQRES 4 A 83 TYR VAL VAL ARG TRP LEU VAL ASN GLY HIS GLU THR THR SEQRES 5 A 83 VAL TYR PRO GLY SER ASP ALA VAL VAL VAL THR ALA THR SEQRES 6 A 83 GLU HIS ALA GLU ALA GLU LYS ARG ALA ALA ALA ARG ALA SEQRES 7 A 83 GLY HIS ALA ALA THR HELIX 1 1 THR A 60 GLY A 76 1 17 SHEET 1 A 5 HIS A 46 VAL A 50 0 SHEET 2 A 5 TYR A 37 TRP A 41 -1 N TRP A 41 O HIS A 46 SHEET 3 A 5 ASP A 20 GLU A 27 -1 N GLU A 24 O ARG A 40 SHEET 4 A 5 ASP A 7 VAL A 11 -1 N ASP A 7 O ILE A 25 SHEET 5 A 5 VAL A 57 VAL A 59 -1 O VAL A 59 N TYR A 8 CISPEP 1 PRO A 35 PRO A 36 1 1.92 CISPEP 2 PRO A 35 PRO A 36 2 1.71 CISPEP 3 PRO A 35 PRO A 36 3 0.14 CISPEP 4 PRO A 35 PRO A 36 4 2.56 CISPEP 5 PRO A 35 PRO A 36 5 0.02 CISPEP 6 PRO A 35 PRO A 36 6 -1.53 CISPEP 7 PRO A 35 PRO A 36 7 0.28 CISPEP 8 PRO A 35 PRO A 36 8 2.45 CISPEP 9 PRO A 35 PRO A 36 9 0.99 CISPEP 10 PRO A 35 PRO A 36 10 2.20 CISPEP 11 PRO A 35 PRO A 36 11 -1.95 CISPEP 12 PRO A 35 PRO A 36 12 1.66 CISPEP 13 PRO A 35 PRO A 36 13 0.62 CISPEP 14 PRO A 35 PRO A 36 14 1.74 CISPEP 15 PRO A 35 PRO A 36 15 0.83 CISPEP 16 PRO A 35 PRO A 36 16 3.84 CISPEP 17 PRO A 35 PRO A 36 17 -1.41 CISPEP 18 PRO A 35 PRO A 36 18 1.14 CISPEP 19 PRO A 35 PRO A 36 19 3.63 CISPEP 20 PRO A 35 PRO A 36 20 -0.69 CISPEP 21 PRO A 35 PRO A 36 21 1.18 CISPEP 22 PRO A 35 PRO A 36 22 2.97 CISPEP 23 PRO A 35 PRO A 36 23 -1.41 CISPEP 24 PRO A 35 PRO A 36 24 3.55 CISPEP 25 PRO A 35 PRO A 36 25 2.34 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 9 2 Bytes