Header list of 1n91.pdb file
Complete list - g 9 2 Bytes
HEADER STRUCTURAL GENOMICS/UNKNOWN FUNCTION 21-NOV-02 1N91 TITLE SOLUTION NMR STRUCTURE OF PROTEIN YGGU FROM ESCHERICHIA COLI. TITLE 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET ER14. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ORF, HYPOTHETICAL PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 155864; SOURCE 4 STRAIN: O157:H7 EDL933; SOURCE 5 GENE: YGGU; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21PMGK; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET21; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: ER14-21 KEYWDS ALPHA+BETA; NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, PSI, PROTEIN KEYWDS 2 STRUCTURE INITIATIVE, NESG, STRUCTURAL GENOMICS-UNKNOWN FUNCTION KEYWDS 3 COMPLEX EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR J.M.ARAMINI,R.XIAO,Y.J.HUANG,T.B.ACTON,M.J.WU,J.L.MILLS,R.T.TEJERO, AUTHOR 2 T.SZYPERSKI,G.T.MONTELIONE,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM AUTHOR 3 (NESG) REVDAT 8 14-JUN-23 1N91 1 REMARK REVDAT 7 05-FEB-20 1N91 1 REMARK SEQADV REVDAT 6 13-JUL-11 1N91 1 VERSN REVDAT 5 28-APR-09 1N91 1 REMARK REVDAT 4 24-FEB-09 1N91 1 VERSN REVDAT 3 08-FEB-05 1N91 1 JRNL REVDAT 2 25-JAN-05 1N91 1 AUTHOR KEYWDS REMARK REVDAT 1 14-JAN-03 1N91 0 JRNL AUTH J.M.ARAMINI,J.L.MILLS,R.XIAO,T.B.ACTON,M.J.WU,T.SZYPERSKI, JRNL AUTH 2 G.T.MONTELIONE JRNL TITL RESONANCE ASSIGNMENTS FOR THE HYPOTHETICAL PROTEIN YGGU FROM JRNL TITL 2 ESCHERICHIA COLI. JRNL REF J.BIOMOL.NMR V. 27 285 2003 JRNL REFN ISSN 0925-2738 JRNL PMID 12975589 JRNL DOI 10.1023/A:1025494323225 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1B, DYANA 1.5, X-PLOR 2.0.4 (NIH), REMARK 3 AUTOSTRUCTURE 1.1.2 REMARK 3 AUTHORS : VARIAN INC. (VNMR), GUNTERT (DYANA), BRUNGER (X REMARK 3 -PLOR), HUANG (AUTOSTRUCTURE) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1419 REMARK 3 CONFORMATIONALLY-RESTRICTING NOE-DERIVED DISTANCE REMARK 3 RESTRAINTS, 210 DIHEDRAL ANGLE RESTRAINTS, AND 78 REMARK 3 HYDROGEN BOND RESTRAINTS. INITIAL STRUCTURE REMARK 3 DETERMINATION WAS PERFORMED BY TORSION ANGLE DYNAMICS REMARK 3 (DYANA). THE FINAL STRUCTURES SUBMITTED WERE REFINED REMARK 3 BY SIMULATED ANNEALING (XPLOR). REMARK 4 REMARK 4 1N91 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-02. REMARK 100 THE DEPOSITION ID IS D_1000017669. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 50 MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.0 MM ER14 U-15N,13C IN 20MM REMARK 210 MES, 50MM NACL, 5MM DTT, PH 6.5; REMARK 210 1.0 MM ER14 U-15N,13C IN 20MM REMARK 210 MES, 50MM NACL, 5MM DTT, PH 6.5 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N-NOESY; 3D 13C-NOESY; 3D REMARK 210 AROMATIC 13C-NOESY; 2D 15N,1H REMARK 210 HSQC-J; 2D 15N,1H MEXICO REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.1, SPARKY 3.106, REMARK 210 AUTOASSIGN 1.9, AUTOSTRUCTURE REMARK 210 1.1.2, HYPER 2.70, TALOS 2.1, REMARK 210 PDBSTAT 3.27 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 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: THE STRUCTURE WAS DETERMINED USING REMARK 210 TRIPLE-RESONANCE NMR SPECTROSCOPY. AUTOMATIC BACKBONE REMARK 210 RESONANCE ASSIGNMENTS WERE MADE USING AUTOASSIGN. REMARK 210 AUTOMATIC NOESY ASSIGNMENTS AS WELL AS DISTANCE AND REMARK 210 HYDROGEN BOND RESTRAINTS WERE DETERMINED USING THE REMARK 210 AUTOSTRUCTURE PROGRAM. DIHEDRAL ANGLE RESTRAINTS WERE REMARK 210 DETERMINED USING HYPER AND TALOS. REMARK 210 BACKBONE CONFORMATIONS FOR RESIDUES 1-5, 25-26, 66, REMARK 210 101-108 ARE NOT WELL-DEFINED [S(PHI) + S(PSI) < 1.8] REMARK 210 IN THIS SOLUTION NMR STRUCTURE. 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 MODELS 1-10 REMARK 470 RES CSSEQI ATOMS REMARK 470 HIS A 108 O 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 O ALA A 96 H ASN A 100 1.48 REMARK 500 O LEU A 59 H PHE A 63 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 2 -106.78 -125.61 REMARK 500 1 VAL A 4 -46.62 -149.05 REMARK 500 1 MET A 5 91.57 56.09 REMARK 500 1 SER A 6 -169.68 -126.19 REMARK 500 1 ALA A 7 -25.85 151.19 REMARK 500 1 ASN A 11 -151.97 -80.28 REMARK 500 1 ALA A 25 -70.95 -92.22 REMARK 500 1 SER A 26 -22.09 160.01 REMARK 500 1 ARG A 27 140.73 -171.36 REMARK 500 1 ASP A 28 86.89 -63.90 REMARK 500 1 THR A 43 38.79 -95.28 REMARK 500 1 PRO A 45 175.36 -51.98 REMARK 500 1 VAL A 65 -125.25 -65.42 REMARK 500 1 LYS A 74 142.31 165.90 REMARK 500 1 GLU A 76 -39.08 -35.03 REMARK 500 1 LEU A 101 82.76 47.77 REMARK 500 1 HIS A 105 56.97 -150.08 REMARK 500 2 MET A 5 30.52 -68.09 REMARK 500 2 SER A 6 -168.53 -104.00 REMARK 500 2 ALA A 7 -19.61 153.99 REMARK 500 2 ASN A 11 -155.32 -76.84 REMARK 500 2 LYS A 24 30.05 88.33 REMARK 500 2 ALA A 66 157.64 -49.34 REMARK 500 2 GLU A 73 0.44 -66.66 REMARK 500 2 LYS A 74 127.67 160.44 REMARK 500 2 GLU A 76 -47.65 -29.95 REMARK 500 2 ASN A 87 79.25 55.36 REMARK 500 2 LEU A 101 73.29 53.66 REMARK 500 2 HIS A 104 -64.22 -167.61 REMARK 500 2 HIS A 106 -143.65 51.51 REMARK 500 3 VAL A 4 75.23 53.17 REMARK 500 3 SER A 6 -168.59 -113.75 REMARK 500 3 ALA A 7 -18.96 150.89 REMARK 500 3 ASN A 11 -154.94 -92.22 REMARK 500 3 LYS A 24 42.64 76.63 REMARK 500 3 ARG A 64 5.03 59.22 REMARK 500 3 VAL A 65 -118.49 -65.32 REMARK 500 3 GLU A 73 5.22 -67.54 REMARK 500 3 LYS A 74 142.10 162.43 REMARK 500 3 LEU A 101 -61.21 71.90 REMARK 500 3 GLU A 102 -94.97 50.57 REMARK 500 3 HIS A 103 17.71 52.70 REMARK 500 3 HIS A 106 -136.33 -95.59 REMARK 500 3 HIS A 107 70.83 -156.42 REMARK 500 4 ALA A 7 -17.59 159.68 REMARK 500 4 ASN A 11 -158.04 -79.58 REMARK 500 4 LYS A 24 48.61 73.59 REMARK 500 4 ALA A 25 -62.88 -99.55 REMARK 500 4 SER A 26 -28.52 153.08 REMARK 500 4 ASP A 28 94.22 -63.47 REMARK 500 REMARK 500 THIS ENTRY HAS 154 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 1 ARG A 18 0.31 SIDE CHAIN REMARK 500 1 ARG A 27 0.30 SIDE CHAIN REMARK 500 1 ARG A 64 0.10 SIDE CHAIN REMARK 500 1 ARG A 79 0.22 SIDE CHAIN REMARK 500 2 ARG A 18 0.28 SIDE CHAIN REMARK 500 2 ARG A 27 0.19 SIDE CHAIN REMARK 500 2 ARG A 64 0.15 SIDE CHAIN REMARK 500 2 ARG A 79 0.13 SIDE CHAIN REMARK 500 3 ARG A 18 0.29 SIDE CHAIN REMARK 500 3 ARG A 27 0.23 SIDE CHAIN REMARK 500 3 ARG A 64 0.16 SIDE CHAIN REMARK 500 3 ARG A 79 0.27 SIDE CHAIN REMARK 500 4 ARG A 18 0.14 SIDE CHAIN REMARK 500 4 ARG A 64 0.30 SIDE CHAIN REMARK 500 4 ARG A 79 0.28 SIDE CHAIN REMARK 500 5 ARG A 18 0.31 SIDE CHAIN REMARK 500 5 ARG A 27 0.13 SIDE CHAIN REMARK 500 5 ARG A 79 0.23 SIDE CHAIN REMARK 500 6 ARG A 27 0.29 SIDE CHAIN REMARK 500 6 ARG A 64 0.19 SIDE CHAIN REMARK 500 6 ARG A 79 0.30 SIDE CHAIN REMARK 500 7 ARG A 18 0.17 SIDE CHAIN REMARK 500 7 ARG A 27 0.17 SIDE CHAIN REMARK 500 7 ARG A 64 0.30 SIDE CHAIN REMARK 500 7 ARG A 79 0.31 SIDE CHAIN REMARK 500 8 ARG A 18 0.29 SIDE CHAIN REMARK 500 8 ARG A 27 0.18 SIDE CHAIN REMARK 500 8 ARG A 64 0.10 SIDE CHAIN REMARK 500 8 ARG A 79 0.26 SIDE CHAIN REMARK 500 9 ARG A 18 0.31 SIDE CHAIN REMARK 500 9 ARG A 27 0.21 SIDE CHAIN REMARK 500 9 ARG A 64 0.24 SIDE CHAIN REMARK 500 9 ARG A 79 0.30 SIDE CHAIN REMARK 500 10 ARG A 18 0.29 SIDE CHAIN REMARK 500 10 ARG A 27 0.29 SIDE CHAIN REMARK 500 10 ARG A 64 0.28 SIDE CHAIN REMARK 500 10 ARG A 79 0.25 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 AUTHOR DEFINED SECONDARY STRUCTURE. REMARK 700 REMARK 700 SHEET REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. REMARK 700 IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET REPORT REMARK 700 BELOW, TWO SHEETS ARE DEFINED. STRANDS 1,2 AND 3 IN REMARK 700 SHEET A AND B ARE IDENTICAL. REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5596 RELATED DB: BMRB REMARK 900 CHEMICAL SHIFT ASSIGNMENTS AND J-COUPLING CONSTANT DATA USED IN REMARK 900 THIS STRUCTURE DETERMINATION REMARK 900 RELATED ID: ER14 RELATED DB: TARGETDB DBREF 1N91 A 1 100 UNP Q8XCU6 YGGU_ECO57 1 100 SEQADV 1N91 LEU A 101 UNP Q8XCU6 EXPRESSION TAG SEQADV 1N91 GLU A 102 UNP Q8XCU6 EXPRESSION TAG SEQADV 1N91 HIS A 103 UNP Q8XCU6 EXPRESSION TAG SEQADV 1N91 HIS A 104 UNP Q8XCU6 EXPRESSION TAG SEQADV 1N91 HIS A 105 UNP Q8XCU6 EXPRESSION TAG SEQADV 1N91 HIS A 106 UNP Q8XCU6 EXPRESSION TAG SEQADV 1N91 HIS A 107 UNP Q8XCU6 EXPRESSION TAG SEQADV 1N91 HIS A 108 UNP Q8XCU6 EXPRESSION TAG SEQRES 1 A 108 MET ASP GLY VAL MET SER ALA VAL THR VAL ASN ASP ASP SEQRES 2 A 108 GLY LEU VAL LEU ARG LEU TYR ILE GLN PRO LYS ALA SER SEQRES 3 A 108 ARG ASP SER ILE VAL GLY LEU HIS GLY ASP GLU VAL LYS SEQRES 4 A 108 VAL ALA ILE THR ALA PRO PRO VAL ASP GLY GLN ALA ASN SEQRES 5 A 108 SER HIS LEU VAL LYS PHE LEU GLY LYS GLN PHE ARG VAL SEQRES 6 A 108 ALA LYS SER GLN VAL VAL ILE GLU LYS GLY GLU LEU GLY SEQRES 7 A 108 ARG HIS LYS GLN ILE LYS ILE ILE ASN PRO GLN GLN ILE SEQRES 8 A 108 PRO PRO GLU VAL ALA ALA LEU ILE ASN LEU GLU HIS HIS SEQRES 9 A 108 HIS HIS HIS HIS HELIX 1 1 VAL A 47 PHE A 63 1 17 HELIX 2 2 GLU A 94 ALA A 97 1 4 SHEET 1 A 4 VAL A 70 ILE A 72 0 SHEET 2 A 4 HIS A 80 ILE A 86 -1 O LYS A 84 N VAL A 71 SHEET 3 A 4 GLY A 14 GLN A 22 -1 N LEU A 17 O ILE A 83 SHEET 4 A 4 VAL A 8 VAL A 10 -1 N THR A 9 O VAL A 16 SHEET 1 B 5 VAL A 70 ILE A 72 0 SHEET 2 B 5 HIS A 80 ILE A 86 -1 O LYS A 84 N VAL A 71 SHEET 3 B 5 GLY A 14 GLN A 22 -1 N LEU A 17 O ILE A 83 SHEET 4 B 5 VAL A 38 ALA A 41 1 O VAL A 38 N TYR A 20 SHEET 5 B 5 SER A 29 LEU A 33 -1 N SER A 29 O ALA A 41 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
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