Header list of 1hra.pdb file
Complete list - 23 20 Bytes
HEADER DNA-BINDING RECEPTOR 25-JUL-93 1HRA TITLE THE SOLUTION STRUCTURE OF THE HUMAN RETINOIC ACID RECEPTOR-BETA DNA- TITLE 2 BINDING DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: RETINOIC ACID RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606 KEYWDS DNA-BINDING RECEPTOR EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR R.M.A.KNEGTEL,M.KATAHIRA,J.G.SCHILTHUIS,A.M.J.J.BONVIN,R.BOELENS, AUTHOR 2 D.EIB,P.T.VAN DER SAAG,R.KAPTEIN REVDAT 4 23-FEB-22 1HRA 1 REMARK LINK REVDAT 3 24-FEB-09 1HRA 1 VERSN REVDAT 2 01-APR-03 1HRA 1 JRNL REVDAT 1 31-JAN-94 1HRA 0 JRNL AUTH R.M.KNEGTEL,M.KATAHIRA,J.G.SCHILTHUIS,A.M.BONVIN,R.BOELENS, JRNL AUTH 2 D.EIB,P.T.VAN DER SAAG,R.KAPTEIN JRNL TITL THE SOLUTION STRUCTURE OF THE HUMAN RETINOIC ACID JRNL TITL 2 RECEPTOR-BETA DNA-BINDING DOMAIN. JRNL REF J.BIOMOL.NMR V. 3 1 1993 JRNL REFN ISSN 0925-2738 JRNL PMID 8383553 JRNL DOI 10.1007/BF00242472 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.M.A.KNEGTEL,R.BOELENS,M.L.GANADU,A.V.E.GEORGE, REMARK 1 AUTH 2 P.T.VAN DER SAAG,R.KAPTEIN REMARK 1 TITL HETERONUCLEAR 113CD-1H NMR STUDY OF METAL COORDINATION IN REMARK 1 TITL 2 THE HUMAN RETINOIC ACID RECEPTOR-BETA DNA BINDING DOMAIN REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 192 492 1993 REMARK 1 REFN ISSN 0006-291X REMARK 1 REFERENCE 2 REMARK 1 AUTH M.KATAHIRA,R.M.A.KNEGTEL,R.BOELENS,D.EIB,J.G.SCHILTHUIS, REMARK 1 AUTH 2 P.T.VAN DER SAAG,R.KAPTEIN REMARK 1 TITL HOMO-AND HETERONUCLEAR NMR STUDIES OF THE HUMAN RETINOIC REMARK 1 TITL 2 ACID RECEPTOR BETA DNA-BINDING DOMAIN: SEQUENTIAL REMARK 1 TITL 3 ASSIGNMENTS AND IDENTIFICATION OF SECONDARY STRUCTURE REMARK 1 TITL 4 ELEMENTS REMARK 1 REF BIOCHEMISTRY V. 31 6474 1992 REMARK 1 REFN ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NULL REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1HRA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000173969. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 81 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 8 SG REMARK 620 2 CYS A 11 SG 108.7 REMARK 620 3 CYS A 25 SG 95.2 128.7 REMARK 620 4 CYS A 28 SG 129.8 92.9 105.7 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 82 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 44 SG REMARK 620 2 CYS A 50 SG 150.6 REMARK 620 3 CYS A 60 SG 84.8 122.1 REMARK 620 4 CYS A 63 SG 100.5 92.1 89.3 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 81 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 82 DBREF 1HRA A 2 80 UNP P10826 RARB_HUMAN 75 153 SEQRES 1 A 80 MET PRO ARG VAL TYR LYS PRO CYS PHE VAL CYS GLN ASP SEQRES 2 A 80 LYS SER SER GLY TYR HIS TYR GLY VAL SER ALA CYS GLU SEQRES 3 A 80 GLY CYS LYS GLY PHE PHE ARG ARG SER ILE GLN LYS ASN SEQRES 4 A 80 MET ILE TYR THR CYS HIS ARG ASP LYS ASN CYS VAL ILE SEQRES 5 A 80 ASN LYS VAL THR ARG ASN ARG CYS GLN TYR CYS ARG LEU SEQRES 6 A 80 GLN LYS CYS PHE GLU VAL GLY MET SER LYS GLU SER VAL SEQRES 7 A 80 ARG ASN HET ZN A 81 1 HET ZN A 82 1 HETNAM ZN ZINC ION FORMUL 2 ZN 2(ZN 2+) HELIX 1 1 GLU A 26 ASN A 39 1 14 HELIX 2 2 CYS A 60 PHE A 69 1 10 HELIX 3 3 GLU A 70 GLY A 72 5 3 LINK SG CYS A 8 ZN ZN A 81 1555 1555 2.49 LINK SG CYS A 11 ZN ZN A 81 1555 1555 2.41 LINK SG CYS A 25 ZN ZN A 81 1555 1555 2.51 LINK SG CYS A 28 ZN ZN A 81 1555 1555 2.52 LINK SG CYS A 44 ZN ZN A 82 1555 1555 2.36 LINK SG CYS A 50 ZN ZN A 82 1555 1555 2.46 LINK SG CYS A 60 ZN ZN A 82 1555 1555 2.78 LINK SG CYS A 63 ZN ZN A 82 1555 1555 2.64 CISPEP 1 CYS A 8 PHE A 9 1 2.55 CISPEP 2 CYS A 11 GLN A 12 1 -4.67 CISPEP 3 ARG A 57 ASN A 58 1 6.63 CISPEP 4 VAL A 78 ARG A 79 1 -8.37 CISPEP 5 CYS A 8 PHE A 9 2 1.33 CISPEP 6 CYS A 11 GLN A 12 2 1.36 CISPEP 7 GLY A 17 TYR A 18 2 11.75 CISPEP 8 LYS A 38 ASN A 39 2 -13.67 CISPEP 9 ARG A 57 ASN A 58 2 8.18 CISPEP 10 VAL A 78 ARG A 79 2 2.48 CISPEP 11 ARG A 3 VAL A 4 3 3.89 CISPEP 12 CYS A 8 PHE A 9 3 8.48 CISPEP 13 CYS A 11 GLN A 12 3 -26.44 CISPEP 14 ASP A 13 LYS A 14 3 -0.76 CISPEP 15 CYS A 44 HIS A 45 3 10.49 CISPEP 16 VAL A 78 ARG A 79 3 -6.45 CISPEP 17 MET A 1 PRO A 2 4 -17.83 CISPEP 18 CYS A 8 PHE A 9 4 7.52 CISPEP 19 SER A 15 SER A 16 4 8.61 CISPEP 20 THR A 43 CYS A 44 4 2.79 CISPEP 21 CYS A 44 HIS A 45 4 -8.24 CISPEP 22 ARG A 57 ASN A 58 4 -3.58 CISPEP 23 VAL A 78 ARG A 79 4 -0.08 CISPEP 24 PRO A 2 ARG A 3 5 -3.43 CISPEP 25 CYS A 8 PHE A 9 5 6.06 CISPEP 26 CYS A 11 GLN A 12 5 -29.02 CISPEP 27 ILE A 41 TYR A 42 5 0.65 CISPEP 28 THR A 43 CYS A 44 5 -2.31 CISPEP 29 CYS A 44 HIS A 45 5 -13.50 CISPEP 30 ARG A 57 ASN A 58 5 -5.46 CISPEP 31 VAL A 78 ARG A 79 5 -3.61 CISPEP 32 CYS A 8 PHE A 9 6 6.98 CISPEP 33 CYS A 11 GLN A 12 6 -28.73 CISPEP 34 ASP A 13 LYS A 14 6 2.80 CISPEP 35 THR A 43 CYS A 44 6 25.28 CISPEP 36 VAL A 51 ILE A 52 6 12.17 CISPEP 37 ARG A 57 ASN A 58 6 11.94 CISPEP 38 VAL A 78 ARG A 79 6 -8.37 CISPEP 39 CYS A 8 PHE A 9 7 6.37 CISPEP 40 CYS A 11 GLN A 12 7 -23.09 CISPEP 41 GLY A 17 TYR A 18 7 10.26 CISPEP 42 THR A 43 CYS A 44 7 -5.75 CISPEP 43 CYS A 44 HIS A 45 7 -7.22 CISPEP 44 ARG A 57 ASN A 58 7 -2.97 CISPEP 45 VAL A 78 ARG A 79 7 4.24 CISPEP 46 MET A 1 PRO A 2 8 -0.37 CISPEP 47 CYS A 8 PHE A 9 8 8.66 CISPEP 48 CYS A 11 GLN A 12 8 -29.72 CISPEP 49 CYS A 44 HIS A 45 8 3.76 CISPEP 50 ASN A 58 ARG A 59 8 -19.56 CISPEP 51 VAL A 78 ARG A 79 8 -9.35 CISPEP 52 CYS A 8 PHE A 9 9 5.88 CISPEP 53 CYS A 11 GLN A 12 9 -28.25 CISPEP 54 GLY A 17 TYR A 18 9 6.90 CISPEP 55 ARG A 57 ASN A 58 9 -0.95 CISPEP 56 VAL A 78 ARG A 79 9 -7.70 CISPEP 57 MET A 1 PRO A 2 10 -7.96 CISPEP 58 CYS A 8 PHE A 9 10 6.07 CISPEP 59 GLY A 17 TYR A 18 10 -13.19 CISPEP 60 THR A 43 CYS A 44 10 3.03 CISPEP 61 CYS A 44 HIS A 45 10 -13.64 CISPEP 62 ARG A 57 ASN A 58 10 7.42 CISPEP 63 VAL A 78 ARG A 79 10 -2.05 CISPEP 64 CYS A 8 PHE A 9 11 -0.61 CISPEP 65 GLY A 17 TYR A 18 11 8.57 CISPEP 66 VAL A 78 ARG A 79 11 -7.00 CISPEP 67 CYS A 8 PHE A 9 12 -1.20 CISPEP 68 CYS A 11 GLN A 12 12 -4.59 CISPEP 69 GLY A 17 TYR A 18 12 6.82 CISPEP 70 THR A 43 CYS A 44 12 4.52 CISPEP 71 CYS A 44 HIS A 45 12 -11.48 CISPEP 72 ARG A 57 ASN A 58 12 9.89 CISPEP 73 VAL A 78 ARG A 79 12 0.44 CISPEP 74 CYS A 8 PHE A 9 13 5.65 CISPEP 75 GLY A 17 TYR A 18 13 10.23 CISPEP 76 ILE A 41 TYR A 42 13 10.10 CISPEP 77 CYS A 44 HIS A 45 13 -13.23 CISPEP 78 ARG A 57 ASN A 58 13 7.67 CISPEP 79 VAL A 78 ARG A 79 13 -7.95 CISPEP 80 MET A 1 PRO A 2 14 -12.90 CISPEP 81 CYS A 8 PHE A 9 14 7.31 CISPEP 82 GLY A 17 TYR A 18 14 11.52 CISPEP 83 ARG A 57 ASN A 58 14 -2.37 CISPEP 84 VAL A 78 ARG A 79 14 -2.03 CISPEP 85 CYS A 8 PHE A 9 15 0.32 CISPEP 86 CYS A 11 GLN A 12 15 5.83 CISPEP 87 GLY A 17 TYR A 18 15 -13.87 CISPEP 88 THR A 43 CYS A 44 15 2.62 CISPEP 89 CYS A 44 HIS A 45 15 -8.00 CISPEP 90 ARG A 57 ASN A 58 15 0.05 CISPEP 91 VAL A 78 ARG A 79 15 -3.30 SITE 1 AC1 4 CYS A 8 CYS A 11 CYS A 25 CYS A 28 SITE 1 AC2 6 CYS A 44 ARG A 46 ASP A 47 CYS A 50 SITE 2 AC2 6 CYS A 60 CYS A 63 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 - 23 20 Bytes