Header list of 1ktu.pdb file
Complete list - r 25 2 Bytes
HEADER PROTEIN BINDING 17-JAN-02 1KTU TITLE NUIA COMPND MOL_ID: 1; COMPND 2 MOLECULE: NUIA; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC SP.; SOURCE 3 ORGANISM_TAXID: 103690; SOURCE 4 STRAIN: PCC 7120; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS NUCLEASE A INHIBITOR, NUIA, NUCLEASE A, NUCA, PR-1-LIKE, NUCLEASE KEYWDS 2 INHIBITOR, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 7 AUTHOR T.W.KIRBY,G.A.MUELLER,E.F.DEROSE,M.S.LEBETKIN,G.MEISS,A.PINGOUD, AUTHOR 2 R.E.LONDON REVDAT 3 13-JUL-11 1KTU 1 VERSN REVDAT 2 24-FEB-09 1KTU 1 VERSN REVDAT 1 04-DEC-02 1KTU 0 JRNL AUTH T.W.KIRBY,G.A.MUELLER,E.F.DEROSE,M.S.LEBETKIN,G.MEISS, JRNL AUTH 2 A.PINGOUD,R.E.LONDON JRNL TITL THE NUCLEASE A INHIBITOR REPRESENTS A NEW VARIATION OF THE JRNL TITL 2 RARE PR-1 FOLD. JRNL REF J.MOL.BIOL. V. 320 771 2002 JRNL REFN ISSN 0022-2836 JRNL PMID 12095254 JRNL DOI 10.1016/S0022-2836(02)00460-6 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : ARIA 1.0 REMARK 3 AUTHORS : NILGES REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1KTU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-02. REMARK 100 THE RCSB ID CODE IS RCSB015338. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 7 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1ATM REMARK 210 SAMPLE CONTENTS : 3.3 MM NUIA 15N, 13C, 1H; 90 MM REMARK 210 DEUTERATED TRIS; REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; 4D_13C/15N- 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 : NMRPIPE 1.8, NMRVIEW 5.0.4, CNS REMARK 210 1.0 REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION REMARK 210 ANGLE DYNAMICS FOLLOWED BY REMARK 210 CARTESIAN DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 160 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 7 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY 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 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 HD3 LYS A 11 HG23 ILE A 16 1.36 REMARK 500 HA GLU A 89 HB VAL A 92 1.39 REMARK 500 HD13 LEU A 55 HD1 TYR A 113 1.42 REMARK 500 HG21 ILE A 53 HE21 GLN A 57 1.43 REMARK 500 HE22 GLN A 56 HE21 GLN A 62 1.43 REMARK 500 HA LYS A 21 HG SER A 24 1.46 REMARK 500 HB ILE A 71 HG2 PRO A 110 1.47 REMARK 500 H VAL A 118 HA THR A 143 1.49 REMARK 500 HA3 GLY A 59 HE2 PHE A 66 1.50 REMARK 500 HD2 LYS A 21 HB2 ASP A 25 1.51 REMARK 500 HE22 GLN A 111 HA2 GLY A 126 1.52 REMARK 500 HB3 SER A 45 HB2 LEU A 133 1.52 REMARK 500 HA GLN A 19 HB2 GLN A 22 1.53 REMARK 500 H THR A 79 H THR A 80 1.53 REMARK 500 HB3 MET A 30 HA GLU A 34 1.54 REMARK 500 HB2 GLU A 32 HB VAL A 141 1.54 REMARK 500 HG1 THR A 128 HD2 PRO A 129 1.55 REMARK 500 HG3 GLU A 88 H GLU A 89 1.55 REMARK 500 HA VAL A 39 HA ILE A 136 1.57 REMARK 500 HB2 GLU A 86 H GLU A 89 1.57 REMARK 500 HA ASP A 72 HB3 SER A 76 1.58 REMARK 500 O GLU A 89 H VAL A 93 1.58 REMARK 500 HD12 ILE A 71 HG LEU A 100 1.59 REMARK 500 HA2 GLY A 61 HD2 PHE A 66 1.60 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 5 TYR A 35 CE1 TYR A 35 CZ 0.120 REMARK 500 5 TYR A 35 CZ TYR A 35 CE2 -0.120 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 HIS A 3 -77.14 67.90 REMARK 500 1 HIS A 4 -174.58 64.15 REMARK 500 1 HIS A 7 -57.21 -151.45 REMARK 500 1 ASN A 13 -33.25 -39.10 REMARK 500 1 ASP A 25 -4.81 -58.34 REMARK 500 1 SER A 31 -99.91 -77.39 REMARK 500 1 SER A 33 -137.97 -125.59 REMARK 500 1 GLU A 34 103.54 -161.55 REMARK 500 1 ALA A 46 168.46 148.61 REMARK 500 1 PRO A 47 102.35 -50.65 REMARK 500 1 GLU A 52 -14.00 158.75 REMARK 500 1 THR A 58 -69.19 -98.77 REMARK 500 1 HIS A 60 -28.33 161.09 REMARK 500 1 ASP A 63 -28.01 179.38 REMARK 500 1 PRO A 65 27.77 -74.34 REMARK 500 1 THR A 79 19.46 170.88 REMARK 500 1 ASP A 83 -35.68 87.45 REMARK 500 1 TYR A 85 -82.96 -22.14 REMARK 500 1 ASN A 106 -17.98 64.20 REMARK 500 1 ASN A 109 118.01 -28.79 REMARK 500 1 VAL A 118 -28.98 74.23 REMARK 500 1 GLU A 119 107.02 -178.65 REMARK 500 2 HIS A 2 -136.80 56.36 REMARK 500 2 HIS A 3 102.93 -54.68 REMARK 500 2 HIS A 4 64.59 -106.25 REMARK 500 2 LYS A 11 30.00 94.66 REMARK 500 2 THR A 12 -160.45 -76.29 REMARK 500 2 LEU A 27 66.23 -114.36 REMARK 500 2 SER A 31 -88.91 -110.67 REMARK 500 2 SER A 33 168.30 179.53 REMARK 500 2 SER A 45 -177.22 -66.11 REMARK 500 2 ALA A 46 165.19 80.93 REMARK 500 2 PRO A 48 -121.81 -98.97 REMARK 500 2 GLU A 52 4.19 161.40 REMARK 500 2 THR A 58 -82.75 -105.01 REMARK 500 2 HIS A 60 114.67 73.29 REMARK 500 2 GLN A 62 32.01 34.46 REMARK 500 2 ASP A 63 -57.89 -162.77 REMARK 500 2 PRO A 65 39.69 -72.33 REMARK 500 2 LYS A 67 117.47 179.92 REMARK 500 2 THR A 79 -10.55 105.27 REMARK 500 2 ASP A 83 -23.20 162.55 REMARK 500 2 TYR A 85 -106.44 0.38 REMARK 500 2 ASN A 106 -44.16 70.39 REMARK 500 2 ASN A 109 98.37 -45.57 REMARK 500 2 VAL A 118 -47.52 105.10 REMARK 500 2 THR A 128 26.34 -158.59 REMARK 500 2 ASN A 132 -121.68 176.50 REMARK 500 2 LEU A 133 97.61 -57.80 REMARK 500 2 ALA A 134 105.61 -177.03 REMARK 500 REMARK 500 THIS ENTRY HAS 189 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 7 MET A 30 24.3 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1J57 RELATED DB: PDB REMARK 900 1J57 REPRESENTS THE MINIMIZED AVERAGE STRUCTURE. DBREF 1KTU A 10 143 UNP Q44296 Q44296_9NOST 2 135 SEQADV 1KTU MET A 1 UNP Q44296 CLONING ARTIFACT SEQADV 1KTU HIS A 2 UNP Q44296 EXPRESSION TAG SEQADV 1KTU HIS A 3 UNP Q44296 EXPRESSION TAG SEQADV 1KTU HIS A 4 UNP Q44296 EXPRESSION TAG SEQADV 1KTU HIS A 5 UNP Q44296 EXPRESSION TAG SEQADV 1KTU HIS A 6 UNP Q44296 EXPRESSION TAG SEQADV 1KTU HIS A 7 UNP Q44296 EXPRESSION TAG SEQADV 1KTU GLY A 8 UNP Q44296 CLONING ARTIFACT SEQADV 1KTU SER A 9 UNP Q44296 CLONING ARTIFACT SEQRES 1 A 143 MET HIS HIS HIS HIS HIS HIS GLY SER THR LYS THR ASN SEQRES 2 A 143 SER GLU ILE LEU GLU GLN LEU LYS GLN ALA SER ASP GLY SEQRES 3 A 143 LEU LEU PHE MET SER GLU SER GLU TYR PRO PHE GLU VAL SEQRES 4 A 143 PHE LEU TRP GLU GLY SER ALA PRO PRO VAL THR HIS GLU SEQRES 5 A 143 ILE VAL LEU GLN GLN THR GLY HIS GLY GLN ASP ALA PRO SEQRES 6 A 143 PHE LYS VAL VAL ASP ILE ASP SER PHE PHE SER ARG ALA SEQRES 7 A 143 THR THR PRO GLN ASP TRP TYR GLU ASP GLU GLU ASN ALA SEQRES 8 A 143 VAL VAL ALA LYS PHE GLN LYS LEU LEU GLU VAL ILE LYS SEQRES 9 A 143 SER ASN LEU LYS ASN PRO GLN VAL TYR ARG LEU GLY GLU SEQRES 10 A 143 VAL GLU LEU ASP VAL TYR VAL ILE GLY GLU THR PRO ALA SEQRES 11 A 143 GLY ASN LEU ALA GLY ILE SER THR LYS VAL VAL GLU THR HELIX 1 1 THR A 12 ASP A 25 1 14 HELIX 2 2 GLU A 52 GLY A 59 1 8 HELIX 3 3 ASP A 70 PHE A 75 1 6 HELIX 4 4 GLU A 86 VAL A 102 1 17 SHEET 1 A 5 GLU A 38 TRP A 42 0 SHEET 2 A 5 LEU A 133 VAL A 140 -1 O GLY A 135 N PHE A 40 SHEET 3 A 5 LEU A 120 ILE A 125 -1 N VAL A 122 O THR A 138 SHEET 4 A 5 GLN A 111 LEU A 115 -1 N LEU A 115 O ASP A 121 SHEET 5 A 5 LYS A 67 VAL A 68 -1 N LYS A 67 O ARG A 114 CISPEP 1 PRO A 48 VAL A 49 1 0.35 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 25 2 Bytes