Header list of 2fki.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 04-JAN-06 2FKI TITLE NMR STRUCTURE OF PROTEIN YJBR FROM ESCHERICHIA COLI; NORTHEAST TITLE 2 STRUCTURAL GENOMICS CONSORTIUM TARGET ER226 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN YJBR; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 GENE: YJBR; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PMGK; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21 KEYWDS NESG, ER226, GFT-NMR, ALPHA-BETA, STRUCTURAL GENOMICS, PSI, PROTEIN KEYWDS 2 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, KEYWDS 3 UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.K.SINGARAPU,G.LIU,R.XIAO,K.G.SHETTY,G.T.MONTELIONE,T.SZYPERSKI, AUTHOR 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 4 09-MAR-22 2FKI 1 REMARK SEQADV REVDAT 3 24-FEB-09 2FKI 1 VERSN REVDAT 2 24-APR-07 2FKI 1 JRNL REVDAT 1 28-FEB-06 2FKI 0 JRNL AUTH K.K.SINGARAPU,G.LIU,R.XIAO,C.BERTONATI,B.HONIG, JRNL AUTH 2 G.T.MONTELIONE,T.SZYPERSKI JRNL TITL NMR STRUCTURE OF PROTEIN YJBR FROM ESCHERICHIA COLI REVEALS JRNL TITL 2 'DOUBLE-WING' DNA BINDING MOTIF. JRNL REF PROTEINS V. 67 501 2007 JRNL REFN ISSN 0887-3585 JRNL PMID 17266124 JRNL DOI 10.1002/PROT.21297 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2.5, CYANA 2.1, CNS 1.1 REMARK 3 AUTHORS : BAX, A., DELAGLIO, F. (NMRPIPE), GUNTERT, P., ET REMARK 3 AL (CYANA), BRUNGER, A.T. ET AL (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 2100 RESTRAINTS. REMARK 4 REMARK 4 2FKI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JAN-06. REMARK 100 THE DEPOSITION ID IS D_1000035985. 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 : 100 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : U-15N, 13C; 0.02% NAN3, 10MM REMARK 210 DTT, 5MM CACL2, 100MM NACL, 20MM REMARK 210 MES, PH 6.5, 5% D2O, 95% H2O. REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : [4,3]D GFT, HNNCABCA; [4,3]D REMARK 210 GFT, CABCA(CO)NHN; [4,3]D GFT REMARK 210 ALI-HCCH; [4,3]D GFT ARO-HCCH; REMARK 210 [4,3]D GFT, HABCAB(CO)NHN; REMARK 210 SIMULTANEOUS HETERONUCLEAR REMARK 210 RESOLVED [1H, 1H]-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.3.13, DYANA 1.5, REMARK 210 AUTOSTRUCTURE 2.0.0 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING MOLECULAR DYNAMICS REMARK 210 TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS 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 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 1-20 REMARK 465 RES C SSSEQI REMARK 465 LEU A 119 REMARK 465 GLU A 120 REMARK 465 HIS A 121 REMARK 465 HIS A 122 REMARK 465 HIS A 123 REMARK 465 HIS A 124 REMARK 465 HIS A 125 REMARK 465 HIS A 126 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 21 OD2 ASP A 23 1.57 REMARK 500 OE2 GLU A 110 HZ3 LYS A 111 1.59 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 ASP A 23 -69.11 -136.88 REMARK 500 1 VAL A 31 -146.35 -88.96 REMARK 500 1 ASP A 33 18.40 -154.23 REMARK 500 1 SER A 65 -163.87 62.77 REMARK 500 1 ASP A 66 -81.30 72.45 REMARK 500 1 ARG A 68 88.62 62.24 REMARK 500 1 ARG A 71 72.88 -101.05 REMARK 500 1 LEU A 73 -66.00 -121.33 REMARK 500 1 ASP A 84 -57.26 68.42 REMARK 500 2 ASP A 23 -69.05 -105.34 REMARK 500 2 LYS A 25 96.93 70.60 REMARK 500 2 VAL A 31 -135.04 -83.75 REMARK 500 2 ASN A 44 -0.69 69.35 REMARK 500 2 THR A 52 143.01 -173.90 REMARK 500 2 ARG A 71 31.60 -80.48 REMARK 500 2 LEU A 73 -63.95 -140.81 REMARK 500 2 LEU A 87 128.93 71.05 REMARK 500 3 ASP A 23 -103.67 -168.44 REMARK 500 3 LYS A 25 82.93 58.09 REMARK 500 3 GLU A 32 -52.52 -26.78 REMARK 500 3 THR A 52 97.31 -67.15 REMARK 500 3 SER A 70 -176.97 59.99 REMARK 500 3 ARG A 71 -74.03 -124.83 REMARK 500 3 LEU A 73 -73.73 -61.40 REMARK 500 3 HIS A 77 -48.91 75.17 REMARK 500 3 SER A 86 -66.57 72.03 REMARK 500 4 TRP A 24 16.53 -140.06 REMARK 500 4 LYS A 25 84.08 61.91 REMARK 500 4 VAL A 31 -141.56 -86.79 REMARK 500 4 ASP A 33 16.14 -142.01 REMARK 500 4 THR A 52 -160.15 -126.58 REMARK 500 4 SER A 53 113.40 75.66 REMARK 500 4 GLN A 63 54.42 -93.15 REMARK 500 4 HIS A 64 44.33 -77.21 REMARK 500 4 SER A 65 -39.27 -165.37 REMARK 500 4 ARG A 68 103.36 59.05 REMARK 500 4 ALA A 76 40.03 -104.96 REMARK 500 4 HIS A 77 -38.49 -152.12 REMARK 500 4 LEU A 83 30.78 -97.78 REMARK 500 5 ASP A 23 -71.25 175.12 REMARK 500 5 VAL A 31 -134.26 -94.57 REMARK 500 5 ASP A 66 -71.90 69.51 REMARK 500 5 PRO A 69 89.09 -69.27 REMARK 500 5 LEU A 73 -158.33 -89.59 REMARK 500 5 HIS A 77 -41.62 -176.30 REMARK 500 5 SER A 86 -81.87 -109.52 REMARK 500 6 ASN A 22 -169.36 -70.95 REMARK 500 6 ASP A 23 -66.28 73.07 REMARK 500 6 VAL A 31 -134.29 -90.28 REMARK 500 6 ASN A 44 -2.69 78.48 REMARK 500 REMARK 500 THIS ENTRY HAS 199 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: ER226 RELATED DB: TARGETDB DBREF 2FKI A 1 118 UNP P0AF50 YJBR_ECOLI 1 118 SEQADV 2FKI LEU A 119 UNP P0AF50 CLONING ARTIFACT SEQADV 2FKI GLU A 120 UNP P0AF50 CLONING ARTIFACT SEQADV 2FKI HIS A 121 UNP P0AF50 EXPRESSION TAG SEQADV 2FKI HIS A 122 UNP P0AF50 EXPRESSION TAG SEQADV 2FKI HIS A 123 UNP P0AF50 EXPRESSION TAG SEQADV 2FKI HIS A 124 UNP P0AF50 EXPRESSION TAG SEQADV 2FKI HIS A 125 UNP P0AF50 EXPRESSION TAG SEQADV 2FKI HIS A 126 UNP P0AF50 EXPRESSION TAG SEQRES 1 A 126 MET THR ILE SER GLU LEU LEU GLN TYR CYS MET ALA LYS SEQRES 2 A 126 PRO GLY ALA GLU GLN SER VAL HIS ASN ASP TRP LYS ALA SEQRES 3 A 126 THR GLN ILE LYS VAL GLU ASP VAL LEU PHE ALA MET VAL SEQRES 4 A 126 LYS GLU VAL GLU ASN ARG PRO ALA VAL SER LEU LYS THR SEQRES 5 A 126 SER PRO GLU LEU ALA GLU LEU LEU ARG GLN GLN HIS SER SEQRES 6 A 126 ASP VAL ARG PRO SER ARG HIS LEU ASN LYS ALA HIS TRP SEQRES 7 A 126 SER THR VAL TYR LEU ASP GLY SER LEU PRO ASP SER GLN SEQRES 8 A 126 ILE TYR TYR LEU VAL ASP ALA SER TYR GLN GLN ALA VAL SEQRES 9 A 126 ASN LEU LEU PRO GLU GLU LYS ARG LYS LEU LEU VAL GLN SEQRES 10 A 126 LEU LEU GLU HIS HIS HIS HIS HIS HIS HELIX 1 1 THR A 2 MET A 11 1 10 HELIX 2 2 SER A 53 GLN A 63 1 11 HELIX 3 3 PRO A 88 LEU A 106 1 19 HELIX 4 4 PRO A 108 LEU A 118 1 11 SHEET 1 A 5 GLU A 17 HIS A 21 0 SHEET 2 A 5 ALA A 26 LYS A 30 -1 O GLN A 28 N SER A 19 SHEET 3 A 5 LEU A 35 VAL A 39 -1 O VAL A 39 N THR A 27 SHEET 4 A 5 ALA A 47 LYS A 51 -1 O SER A 49 N MET A 38 SHEET 5 A 5 TRP A 78 TYR A 82 -1 O VAL A 81 N VAL A 48 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