Header list of 1ni7.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 21-DEC-02 1NI7 TITLE NORTHEAST STRUCTURAL GENOMIC CONSORTIUM TARGET ER75 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN YGDK; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ER75; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 GENE: YGDK; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET21-ER75-21 KEYWDS ER75, RD-NMR, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, KEYWDS 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR G.LIU,Y.CHIANG,T.ACTON,G.T.MONTELIONE,T.SZYPERSKI,NORTHEAST AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (NESG) REVDAT 5 23-FEB-22 1NI7 1 REMARK SEQADV REVDAT 4 24-FEB-09 1NI7 1 VERSN REVDAT 3 26-JUL-05 1NI7 1 JRNL REVDAT 2 25-JAN-05 1NI7 1 AUTHOR KEYWDS REMARK REVDAT 1 03-JUN-03 1NI7 0 JRNL AUTH G.LIU,Z.LI,Y.CHIANG,T.ACTON,G.T.MONTELIONE,D.MURRAY, JRNL AUTH 2 T.SZYPERSKI JRNL TITL HIGH-QUALITY HOMOLOGY MODELS DERIVED FROM NMR AND X-RAY JRNL TITL 2 STRUCTURES OF E. COLI PROTEINS YGDK AND SUF E SUGGEST THAT JRNL TITL 3 ALL MEMBERS OF THE YGDK/SUF E PROTEIN FAMILY ARE ENHANCERS JRNL TITL 4 OF CYSTEINE DESULFURASES. JRNL REF PROTEIN SCI. V. 14 1597 2005 JRNL REFN ISSN 0961-8368 JRNL PMID 15930006 JRNL DOI 10.1110/PS.041322705 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 1.0, DYANA 1.5 REMARK 3 AUTHORS : A.BAX (NMRPIPE), P. GUNTERT (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THIS STRUCTURE WAS DETERMINED WITH THE HELP OF REDUCED-DIMENSIONAL REMARK 3 NMR TECHNIQUES (RD-NMR).THE RESIDUE RANGES OF WELL DEFINED REGIONS REMARK 3 OF REMARK 3 THE STRUCTURE ARE :16-27,31-45,51-58,63-72,74-120,134-148; THE REMARK 3 BACKBONE REMARK 3 MEAN RMSD FOR WELL-DEFINED REGIONS IS 0.48+-0.07A, AND ALL HEAVY REMARK 3 ATOM REMARK 3 MEAN RMSD FOR WELL-DEFINED REGIONS IS 0.87+-0.07A. REMARK 4 REMARK 4 1NI7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-DEC-02. REMARK 100 THE DEPOSITION ID IS D_1000017894. 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 : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM ER75 (U-15N,13C), 20MM MES, REMARK 210 100MM NACL, 5MM GACL2,10MM DTT, REMARK 210 0.02% AZIDE, 95% H2O, 5% D2O; REMARK 210 1MM ER75 (U-15N), 20MM MES, REMARK 210 100MM NACL, 5MM GACL2,10MM DTT, REMARK 210 0.02% AZIDE, 95% H2O, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNCA-J; 3D REMARK 210 HNCACB; 3D HCCH-TOCSY; 3D_RD_ REMARK 210 HNNCAHA; 3D_RD_HACACONHN; 3D_RD_ REMARK 210 HABCABCONH; 3D_RD_HCCH-COSY; 2D_ REMARK 210 RD_HBCB(CGHG)HD; 2D_RD_H-TOC-HCH- REMARK 210 COSY 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 : DYANA 1.5, XEASY 1.3 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED WITH THE HELP OF REDUCED REMARK 210 -DIMENSIONAL NMR TECHNIQUES (RD-NMR) 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 HIS A 150 REMARK 465 HIS A 151 REMARK 465 HIS A 152 REMARK 465 HIS A 153 REMARK 465 HIS A 154 REMARK 465 HIS A 155 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 H LYS A 56 O LEU A 67 1.45 REMARK 500 O ALA A 114 H GLU A 118 1.52 REMARK 500 O LEU A 92 H LEU A 96 1.53 REMARK 500 O ILE A 140 H THR A 144 1.56 REMARK 500 O ASP A 32 H GLN A 36 1.56 REMARK 500 O LEU A 115 H LEU A 119 1.60 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 ALA A 7 75.35 57.80 REMARK 500 1 PRO A 10 -85.97 -75.02 REMARK 500 1 PHE A 11 92.73 33.53 REMARK 500 1 VAL A 15 70.41 -116.44 REMARK 500 1 ARG A 64 147.52 -39.68 REMARK 500 1 LYS A 76 95.23 -48.90 REMARK 500 1 GLU A 100 97.56 -54.60 REMARK 500 1 GLN A 110 115.48 -162.53 REMARK 500 1 ARG A 122 -44.12 -153.93 REMARK 500 2 HIS A 9 91.96 51.01 REMARK 500 2 PHE A 11 88.00 -53.79 REMARK 500 2 THR A 13 -70.65 -88.40 REMARK 500 2 VAL A 15 76.99 -116.01 REMARK 500 2 LEU A 27 87.71 -65.49 REMARK 500 2 ASN A 63 -174.52 -170.23 REMARK 500 2 LYS A 76 96.32 -44.60 REMARK 500 2 ASP A 82 -168.88 -168.80 REMARK 500 2 VAL A 99 31.17 -99.55 REMARK 500 2 GLU A 100 95.40 -55.59 REMARK 500 2 SER A 126 -177.45 -65.20 REMARK 500 3 HIS A 9 134.50 -177.98 REMARK 500 3 PHE A 11 76.50 -67.19 REMARK 500 3 THR A 13 -76.16 -90.30 REMARK 500 3 VAL A 15 79.32 -109.17 REMARK 500 3 LEU A 27 87.22 -68.69 REMARK 500 3 CYS A 61 -53.73 -134.53 REMARK 500 3 GLU A 62 -31.06 167.72 REMARK 500 3 ARG A 64 150.64 -41.90 REMARK 500 3 LYS A 76 106.31 -45.09 REMARK 500 3 VAL A 99 31.20 -94.70 REMARK 500 3 GLU A 100 88.44 -55.30 REMARK 500 3 ARG A 122 33.51 -86.73 REMARK 500 3 SER A 126 149.45 -39.70 REMARK 500 4 THR A 13 -70.49 -101.34 REMARK 500 4 GLU A 31 -39.26 -38.48 REMARK 500 4 LEU A 47 108.67 -54.78 REMARK 500 4 LYS A 76 101.80 -45.24 REMARK 500 4 PHE A 80 118.61 -165.59 REMARK 500 4 VAL A 99 32.30 -96.49 REMARK 500 4 GLU A 100 96.42 -55.48 REMARK 500 4 LEU A 125 175.19 -47.98 REMARK 500 5 HIS A 9 119.17 66.33 REMARK 500 5 THR A 13 -76.53 -89.85 REMARK 500 5 LEU A 27 86.39 -64.33 REMARK 500 5 GLU A 62 -39.49 -38.93 REMARK 500 5 ARG A 64 147.94 -38.14 REMARK 500 5 LYS A 76 104.56 -44.94 REMARK 500 5 PHE A 80 112.23 -165.68 REMARK 500 5 VAL A 99 33.01 -94.41 REMARK 500 5 GLU A 100 88.50 -55.19 REMARK 500 REMARK 500 THIS ENTRY HAS 218 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: ER75 RELATED DB: TARGETDB DBREF 1NI7 A 1 147 UNP Q46926 YGDK_ECOLI 1 147 SEQADV 1NI7 LEU A 148 UNP Q46926 EXPRESSION TAG SEQADV 1NI7 GLU A 149 UNP Q46926 EXPRESSION TAG SEQADV 1NI7 HIS A 150 UNP Q46926 EXPRESSION TAG SEQADV 1NI7 HIS A 151 UNP Q46926 EXPRESSION TAG SEQADV 1NI7 HIS A 152 UNP Q46926 EXPRESSION TAG SEQADV 1NI7 HIS A 153 UNP Q46926 EXPRESSION TAG SEQADV 1NI7 HIS A 154 UNP Q46926 EXPRESSION TAG SEQADV 1NI7 HIS A 155 UNP Q46926 EXPRESSION TAG SEQRES 1 A 155 MET THR ASN PRO GLN PHE ALA GLY HIS PRO PHE GLY THR SEQRES 2 A 155 THR VAL THR ALA GLU THR LEU ARG ASN THR PHE ALA PRO SEQRES 3 A 155 LEU THR GLN TRP GLU ASP LYS TYR ARG GLN LEU ILE MET SEQRES 4 A 155 LEU GLY LYS GLN LEU PRO ALA LEU PRO ASP GLU LEU LYS SEQRES 5 A 155 ALA GLN ALA LYS GLU ILE ALA GLY CYS GLU ASN ARG VAL SEQRES 6 A 155 TRP LEU GLY TYR THR VAL ALA GLU ASN GLY LYS MET HIS SEQRES 7 A 155 PHE PHE GLY ASP SER GLU GLY ARG ILE VAL ARG GLY LEU SEQRES 8 A 155 LEU ALA VAL LEU LEU THR ALA VAL GLU GLY LYS THR ALA SEQRES 9 A 155 ALA GLU LEU GLN ALA GLN SER PRO LEU ALA LEU PHE ASP SEQRES 10 A 155 GLU LEU GLY LEU ARG ALA GLN LEU SER ALA SER ARG SER SEQRES 11 A 155 GLN GLY LEU ASN ALA LEU SER GLU ALA ILE ILE ALA ALA SEQRES 12 A 155 THR LYS GLN VAL LEU GLU HIS HIS HIS HIS HIS HIS HELIX 1 1 THR A 16 ALA A 25 1 10 HELIX 2 2 GLN A 29 LEU A 44 1 16 HELIX 3 3 PRO A 48 ALA A 55 1 8 HELIX 4 4 GLY A 85 VAL A 99 1 15 HELIX 5 5 THR A 103 GLN A 110 1 8 HELIX 6 6 PRO A 112 GLY A 120 1 9 HELIX 7 7 SER A 126 GLU A 149 1 24 SHEET 1 A 3 LYS A 56 ILE A 58 0 SHEET 2 A 3 VAL A 65 GLY A 68 -1 O LEU A 67 N LYS A 56 SHEET 3 A 3 PHE A 80 SER A 83 -1 O ASP A 82 N TRP A 66 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 - b 23 2 Bytes