Header list of 1m3v.pdb file
Complete list - g 9 2 Bytes
HEADER METAL BINDING PROTEIN 30-JUN-02 1M3V TITLE FLIN4: FUSION OF THE LIM BINDING DOMAIN OF LDB1 AND THE N-TERMINAL LIM TITLE 2 DOMAIN OF LMO4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FUSION OF THE LIM INTERACTING DOMAIN OF LDB1 AND THE N- COMPND 3 TERMINAL LIM DOMAIN OF LMO4; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: FLIN4; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: FUSION PROTEIN COMPRISES LIM DOMAIN TRANSCRIPTION COMPND 9 FACTOR LMO4 (RESIDUES 16-86) VIA GLYCINE-RICH LINKER (GGSGGHMGSGG), COMPND 10 LIM DOMAIN-BINDING PROTEIN 1 (RESIDUES 300-339). SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T KEYWDS LIM DOMAIN, FUSION PROTEIN, LMO PROTEINS, LDB1, METAL BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.E.DEANE,J.P.MACKAY,A.H.Y.KWAN,E.Y.SUM,J.E.VISVADER,J.M.MATTHEWS REVDAT 5 14-JUN-23 1M3V 1 REMARK REVDAT 4 10-NOV-21 1M3V 1 REMARK SEQADV LINK REVDAT 3 26-FEB-20 1M3V 1 REMARK REVDAT 2 24-FEB-09 1M3V 1 VERSN REVDAT 1 13-MAY-03 1M3V 0 JRNL AUTH J.E.DEANE,J.P.MACKAY,A.H.KWAN,E.Y.SUM,J.E.VISVADER, JRNL AUTH 2 J.M.MATTHEWS JRNL TITL STRUCTURAL BASIS FOR THE RECOGNITION OF LDB1 BY THE JRNL TITL 2 N-TERMINAL LIM DOMAINS OF LMO2 AND LMO4 JRNL REF EMBO J. V. 22 2224 2003 JRNL REFN ISSN 0261-4189 JRNL PMID 12727888 JRNL DOI 10.1093/EMBOJ/CDG196 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.E.DEANE,J.E.VISVADER,J.P.MACKAY,J.M.MATTHEWS REMARK 1 TITL 1H, 15N AND 13C ASSIGNMENTS OF FLIN4, AN INTRAMOLECULAR REMARK 1 TITL 2 LMO4:LDB1 COMPLEX. REMARK 1 REF J.BIOMOL.NMR V. 23 165 2002 REMARK 1 REFN ISSN 0925-2738 REMARK 1 DOI 10.1023/A:1016363414644 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.E.DEANE,E.SUM,J.P.MACKAY,G.J.LINDEMAN,J.E.VISVADER, REMARK 1 AUTH 2 J.M.MATTHEWS REMARK 1 TITL DESIGN, PRODUCTION AND CHARACTERIZATION OF FLIN2 AND FLIN4: REMARK 1 TITL 2 THE ENGINEERING OF INTRAMOLECULAR LDB1:LMO COMPLEXES REMARK 1 REF PROTEIN ENG. V. 14 493 2001 REMARK 1 REFN ISSN 0269-2139 REMARK 1 DOI 10.1093/PROTEIN/14.7.493 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.5, DYANA 1.5 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT ET AL (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE CALCULATIONS WERE PERFORMED REMARK 3 USING ARIA 1.1. FINAL STRUCTURES ARE BASED ON 1804 UNAMBIGUOUS REMARK 3 AND 81 AMBIGUOUS NOE-DERIVED DISTANCE RESTRAINTS AND 112 ANGLE REMARK 3 CONSTRAINTS FROM COUPLING CONSTANT DATA AND PREDICTIONS FROM REMARK 3 CHEMICAL SHIFT ANALYSIS USING TALOS. REMARK 4 REMARK 4 1M3V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUL-02. REMARK 100 THE DEPOSITION ID IS D_1000016564. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.2MM FLIN4, 20MM NAH2PO4, REMARK 210 PH7.0, 50MM NACL, 1MM DTT, 20UM REMARK 210 D4-TSP; 0.5MM [15N]-FLIN4, 20MM REMARK 210 NAH2PO4, PH7.0, 50MM NACL, 1MM REMARK 210 DTT, 20UM D4-TSP; 1.0MM [13C,15N] REMARK 210 -FLIN4, 20MM NAH2PO4, PH7.0, REMARK 210 50MM NACL, 1MM DTT, 20UM D4-TSP REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY; REMARK 210 3D_15N-SEPARATED_NOESY; HNHA; REMARK 210 HNCA; HN(CO)CA; HNCACB; CBCA(CO) REMARK 210 NH; HCCH-TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.3.13, ARIA 1.1.2, TALOS REMARK 210 98.040.21.02 REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR REMARK 210 DYNAMICS TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 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: THIS STRUCTURE WAS SOLVED USING TRIPLE RESONANCE NMR REMARK 210 TECHNIQUES. IN ADDITION TO THE EXPERIMENTS LISTED ABOVE HNCO, REMARK 210 HN(CA)CO, CC(CO)NH-TOCSY AND HCC(CO)NH-TOCSY WERE ALSO USED FOR REMARK 210 BACKBONE AND SIDE CHAIN ASSIGNMENTS. 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 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 ARG A 7 154.29 62.64 REMARK 500 1 CYS A 11 -121.39 -116.61 REMARK 500 1 LEU A 33 -72.98 -60.50 REMARK 500 1 LYS A 34 166.66 56.31 REMARK 500 1 ALA A 40 -161.31 -100.07 REMARK 500 1 SER A 69 97.72 -63.68 REMARK 500 1 PRO A 90 102.75 -56.59 REMARK 500 1 MET A 93 46.03 -88.71 REMARK 500 1 GLU A 102 -139.58 -85.89 REMARK 500 1 ASN A 110 -169.48 177.29 REMARK 500 1 PHE A 113 -161.19 -101.25 REMARK 500 1 ASP A 114 44.69 -78.36 REMARK 500 2 SER A 2 84.93 60.35 REMARK 500 2 SER A 49 147.51 -175.34 REMARK 500 2 ASN A 68 -57.39 72.90 REMARK 500 2 ALA A 71 81.62 62.20 REMARK 500 2 GLU A 89 77.06 58.01 REMARK 500 2 PRO A 90 31.49 -81.37 REMARK 500 2 ASN A 117 -3.79 75.60 REMARK 500 2 ASP A 121 -68.82 -128.43 REMARK 500 3 ARG A 7 156.76 66.78 REMARK 500 3 CYS A 11 -88.26 -112.35 REMARK 500 3 ASP A 25 -40.64 74.38 REMARK 500 3 ALA A 40 -155.24 -100.17 REMARK 500 3 ILE A 45 52.78 -94.90 REMARK 500 3 SER A 48 111.42 -162.02 REMARK 500 3 LEU A 65 -70.28 -113.54 REMARK 500 3 MET A 85 67.09 -165.17 REMARK 500 3 GLU A 89 73.85 -153.11 REMARK 500 3 LEU A 92 -135.72 -163.48 REMARK 500 3 GLN A 112 -100.79 -103.02 REMARK 500 3 ASN A 117 36.54 -99.18 REMARK 500 4 ARG A 7 107.60 70.13 REMARK 500 4 CYS A 11 -120.32 -122.39 REMARK 500 4 PHE A 19 67.86 -160.04 REMARK 500 4 ALA A 40 -149.87 -91.11 REMARK 500 4 SER A 80 99.66 -68.42 REMARK 500 4 MET A 85 -158.85 -135.00 REMARK 500 4 VAL A 87 -19.44 -144.00 REMARK 500 4 GLU A 100 43.51 -79.06 REMARK 500 4 ASP A 101 33.06 -99.65 REMARK 500 4 ASN A 110 -48.12 172.50 REMARK 500 4 THR A 111 31.27 -143.40 REMARK 500 4 GLN A 112 -81.52 -92.50 REMARK 500 4 ALA A 115 54.39 -98.72 REMARK 500 5 CYS A 11 -73.78 -106.42 REMARK 500 5 SER A 48 111.24 -161.04 REMARK 500 5 PRO A 90 29.19 -75.34 REMARK 500 5 PHE A 97 71.92 -162.42 REMARK 500 5 GLU A 100 49.02 -87.11 REMARK 500 REMARK 500 THIS ENTRY HAS 252 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL 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 123 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 8 SG REMARK 620 2 CYS A 11 SG 109.7 REMARK 620 3 HIS A 29 ND1 109.8 108.3 REMARK 620 4 CYS A 32 SG 109.4 110.8 108.9 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 124 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 35 SG REMARK 620 2 CYS A 38 SG 117.2 REMARK 620 3 CYS A 58 SG 117.7 118.2 REMARK 620 4 ASP A 61 OD1 122.1 71.0 101.1 REMARK 620 5 ASP A 61 OD2 97.7 98.2 100.4 30.5 REMARK 620 N 1 2 3 4 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 123 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 124 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5309 RELATED DB: BMRB REMARK 900 5309 CONTAINS DEPOSITION OF 1H, 15N AND 13C ASSIGNMENTS OF FLIN4 DBREF 1M3V A 1 71 UNP P70662 LDB1_MOUSE 16 86 DBREF 1M3V A 83 122 UNP P70662 LDB1_MOUSE 300 339 SEQADV 1M3V SER A 37 UNP P70662 CYS 52 ENGINEERED MUTATION SEQADV 1M3V SER A 49 UNP P70662 CYS 64 ENGINEERED MUTATION SEQRES 1 A 122 GLY SER LEU SER TRP LYS ARG CYS ALA GLY CYS GLY GLY SEQRES 2 A 122 LYS ILE ALA ASP ARG PHE LEU LEU TYR ALA MET ASP SER SEQRES 3 A 122 TYR TRP HIS SER ARG CYS LEU LYS CYS SER SER CYS GLN SEQRES 4 A 122 ALA GLN LEU GLY ASP ILE GLY THR SER SER TYR THR LYS SEQRES 5 A 122 SER GLY MET ILE LEU CYS ARG ASN ASP TYR ILE ARG LEU SEQRES 6 A 122 PHE GLY ASN SER GLY ALA GLY GLY SER GLY GLY HIS MET SEQRES 7 A 122 GLY SER GLY GLY ASP VAL MET VAL VAL GLY GLU PRO THR SEQRES 8 A 122 LEU MET GLY GLY GLU PHE GLY ASP GLU ASP GLU ARG LEU SEQRES 9 A 122 ILE THR ARG LEU GLU ASN THR GLN PHE ASP ALA ALA ASN SEQRES 10 A 122 GLY ILE ASP ASP GLU HET ZN A 123 1 HET ZN A 124 1 HETNAM ZN ZINC ION FORMUL 2 ZN 2(ZN 2+) HELIX 1 1 HIS A 29 LYS A 34 1 6 HELIX 2 2 CYS A 58 GLY A 67 1 10 SHEET 1 A 3 SER A 26 TRP A 28 0 SHEET 2 A 3 LEU A 21 ALA A 23 -1 N LEU A 21 O TRP A 28 SHEET 3 A 3 THR A 106 ARG A 107 -1 O THR A 106 N TYR A 22 SHEET 1 B 2 GLY A 46 THR A 47 0 SHEET 2 B 2 GLY A 82 ASP A 83 -1 O GLY A 82 N THR A 47 SHEET 1 C 2 TYR A 50 LYS A 52 0 SHEET 2 C 2 MET A 55 LEU A 57 -1 O LEU A 57 N TYR A 50 LINK SG CYS A 8 ZN ZN A 123 1555 1555 2.28 LINK SG CYS A 11 ZN ZN A 123 1555 1555 2.30 LINK ND1 HIS A 29 ZN ZN A 123 1555 1555 1.99 LINK SG CYS A 32 ZN ZN A 123 1555 1555 2.31 LINK SG CYS A 35 ZN ZN A 124 1555 1555 2.26 LINK SG CYS A 38 ZN ZN A 124 1555 1555 2.30 LINK SG CYS A 58 ZN ZN A 124 1555 1555 2.28 LINK OD1 ASP A 61 ZN ZN A 124 1555 1555 3.70 LINK OD2 ASP A 61 ZN ZN A 124 1555 1555 2.05 SITE 1 AC1 4 CYS A 8 CYS A 11 HIS A 29 CYS A 32 SITE 1 AC2 4 CYS A 35 CYS A 38 CYS A 58 ASP A 61 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 - g 9 2 Bytes