Header list of 1y9x.pdb file
Complete list - t 20 2 Bytes
HEADER DNA BINDING PROTEIN 16-DEC-04 1Y9X TITLE SOLUTION STRUCTURE OF ARCHAEON DNA-BINDING PROTEIN SSH10B COMPND MOL_ID: 1; COMPND 2 MOLECULE: DNA/RNA-BINDING PROTEIN ALBA 1; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: SSH10B; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE; SOURCE 3 ORGANISM_TAXID: 2286; SOURCE 4 GENE: ALBA1, SSH10B; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A KEYWDS DNA BINDING, ARCHAEA, DNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR Q.CUI,Y.TONG,J.WANG REVDAT 5 20-OCT-21 1Y9X 1 REMARK SEQADV REVDAT 4 09-JUN-09 1Y9X 1 REVDAT REVDAT 3 24-FEB-09 1Y9X 1 VERSN REVDAT 2 16-DEC-08 1Y9X 1 JRNL REVDAT 1 21-JUN-05 1Y9X 0 JRNL AUTH X.FANG,Q.CUI,Y.TONG,Y.FENG,L.SHAN,L.HUANG,J.WANG JRNL TITL A STABILIZING ALPHA/BETA-HYDROPHOBIC CORE GREATLY JRNL TITL 2 CONTRIBUTES TO HYPERTHERMOSTABILITY OF ARCHAEAL JRNL TITL 3 [P62A]SSH10B. JRNL REF BIOCHEMISTRY V. 47 11212 2008 JRNL REFN ISSN 0006-2960 JRNL PMID 18821773 JRNL DOI 10.1021/BI8007593 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1, CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON, REMARK 3 WARREN (CNS), BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE, REMARK 3 JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1Y9X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-04. REMARK 100 THE DEPOSITION ID IS D_1000031300. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : 20MM KCL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.5MM SSH10B U-95% 13C, U-98% REMARK 210 15N; 20MM ACETATE BUFFER;20MM REMARK 210 KCL; 90%H2O,10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER 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 : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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: 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 ARG A 59 -65.89 -137.10 REMARK 500 1 SER B 3 -73.14 -78.84 REMARK 500 1 ARG B 59 -68.01 -131.97 REMARK 500 1 ALA B 62 -63.36 -100.21 REMARK 500 2 THR A 5 96.88 66.36 REMARK 500 2 LYS A 16 -41.08 -155.07 REMARK 500 2 ARG A 44 -7.28 58.66 REMARK 500 2 ASP A 63 -65.00 -95.05 REMARK 500 2 GLN A 80 -38.96 175.90 REMARK 500 2 ASP A 81 -156.51 -123.47 REMARK 500 2 SER B 2 -168.80 -115.92 REMARK 500 2 SER B 9 -78.49 -114.61 REMARK 500 2 LYS B 16 -43.08 -161.89 REMARK 500 2 ARG B 44 -3.81 56.35 REMARK 500 2 GLN B 80 -38.38 174.04 REMARK 500 2 ASP B 81 -158.84 -122.44 REMARK 500 3 THR A 7 76.41 51.51 REMARK 500 3 PRO A 8 -75.86 -83.71 REMARK 500 3 SER A 9 14.90 -150.14 REMARK 500 3 LYS A 16 -65.05 -157.60 REMARK 500 3 PHE A 60 -70.12 -117.56 REMARK 500 3 GLN A 80 -82.37 -163.38 REMARK 500 3 ASP A 81 -80.03 -112.19 REMARK 500 3 LYS B 16 -65.40 -159.72 REMARK 500 3 PHE B 60 -71.56 -118.66 REMARK 500 3 ILE B 65 119.29 -160.71 REMARK 500 3 GLN B 80 -77.67 -153.42 REMARK 500 3 ASP B 81 -76.37 -120.17 REMARK 500 4 SER A 2 -52.09 -127.00 REMARK 500 4 ASN A 58 -56.02 -128.67 REMARK 500 4 PHE A 60 -63.21 -97.96 REMARK 500 4 GLN A 80 -76.50 -144.87 REMARK 500 4 ASP A 81 -79.42 -123.24 REMARK 500 4 SER B 2 176.46 71.06 REMARK 500 4 THR B 5 82.28 52.90 REMARK 500 4 THR B 7 91.53 55.98 REMARK 500 4 ASN B 58 -57.08 -131.56 REMARK 500 4 PHE B 60 -64.03 -101.65 REMARK 500 4 GLN B 80 -84.36 -148.57 REMARK 500 4 ASP B 81 -80.27 -113.03 REMARK 500 5 SER A 2 135.49 -170.94 REMARK 500 5 GLN A 80 -73.61 -140.31 REMARK 500 5 ASP A 81 -82.14 -122.56 REMARK 500 5 SER B 3 -38.83 71.73 REMARK 500 5 ARG B 59 -66.58 -125.80 REMARK 500 5 GLN B 80 -75.38 -139.50 REMARK 500 5 ASP B 81 -79.23 -126.53 REMARK 500 6 LYS A 16 -50.95 -160.21 REMARK 500 6 PHE A 60 -57.58 -123.71 REMARK 500 6 ASP A 63 -59.70 -149.65 REMARK 500 REMARK 500 THIS ENTRY HAS 219 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 3 ARG A 95 0.08 SIDE CHAIN REMARK 500 3 ARG B 95 0.08 SIDE CHAIN REMARK 500 14 ARG B 71 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6019 RELATED DB: BMRB REMARK 900 THE CHEMICAL SHIFT ASSIGNMENTS OF SSH10B P62A MUTANT REMARK 900 RELATED ID: 5226 RELATED DB: BMRB REMARK 900 THE CHEMICAL SHIFT ASSIGNMENTS OF SSH10B PROTEIN DBREF 1Y9X A 2 97 UNP P60848 ALBA1_SULSH 1 96 DBREF 1Y9X B 2 97 UNP P60848 ALBA1_SULSH 1 96 SEQADV 1Y9X MET A 1 UNP P60848 INITIATING METHIONINE SEQADV 1Y9X ALA A 62 UNP P60848 PRO 61 ENGINEERED MUTATION SEQADV 1Y9X MET B 1 UNP P60848 INITIATING METHIONINE SEQADV 1Y9X ALA B 62 UNP P60848 PRO 61 ENGINEERED MUTATION SEQRES 1 A 97 MET SER SER GLY THR PRO THR PRO SER ASN VAL VAL LEU SEQRES 2 A 97 ILE GLY LYS LYS PRO VAL MET ASN TYR VAL LEU ALA ALA SEQRES 3 A 97 LEU THR LEU LEU ASN GLN GLY VAL SER GLU ILE VAL ILE SEQRES 4 A 97 LYS ALA ARG GLY ARG ALA ILE SER LYS ALA VAL ASP THR SEQRES 5 A 97 VAL GLU ILE VAL ARG ASN ARG PHE LEU ALA ASP LYS ILE SEQRES 6 A 97 GLU ILE LYS GLU ILE ARG VAL GLY SER GLN VAL VAL THR SEQRES 7 A 97 SER GLN ASP GLY ARG GLN SER ARG VAL SER THR ILE GLU SEQRES 8 A 97 ILE ALA ILE ARG LYS LYS SEQRES 1 B 97 MET SER SER GLY THR PRO THR PRO SER ASN VAL VAL LEU SEQRES 2 B 97 ILE GLY LYS LYS PRO VAL MET ASN TYR VAL LEU ALA ALA SEQRES 3 B 97 LEU THR LEU LEU ASN GLN GLY VAL SER GLU ILE VAL ILE SEQRES 4 B 97 LYS ALA ARG GLY ARG ALA ILE SER LYS ALA VAL ASP THR SEQRES 5 B 97 VAL GLU ILE VAL ARG ASN ARG PHE LEU ALA ASP LYS ILE SEQRES 6 B 97 GLU ILE LYS GLU ILE ARG VAL GLY SER GLN VAL VAL THR SEQRES 7 B 97 SER GLN ASP GLY ARG GLN SER ARG VAL SER THR ILE GLU SEQRES 8 B 97 ILE ALA ILE ARG LYS LYS HELIX 1 1 PRO A 18 ASN A 31 1 14 HELIX 2 2 ALA A 45 ASN A 58 1 14 HELIX 3 3 PRO B 18 ASN B 31 1 14 HELIX 4 4 ALA B 45 ASN B 58 1 14 SHEET 1 A 4 VAL A 11 LEU A 13 0 SHEET 2 A 4 GLU A 36 ARG A 42 1 O LYS A 40 N VAL A 12 SHEET 3 A 4 GLN A 84 ARG A 95 -1 O ILE A 90 N ALA A 41 SHEET 4 A 4 GLU A 66 THR A 78 -1 N GLU A 66 O ARG A 95 SHEET 1 B 4 VAL B 11 LEU B 13 0 SHEET 2 B 4 GLU B 36 ARG B 42 1 O LYS B 40 N VAL B 12 SHEET 3 B 4 GLN B 84 ARG B 95 -1 O ILE B 90 N ALA B 41 SHEET 4 B 4 GLU B 66 THR B 78 -1 N VAL B 77 O SER B 85 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 - t 20 2 Bytes