Header list of 1ul4.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 09-SEP-03 1UL4 TITLE SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF SQUAMOSA PROMOTER TITLE 2 BINDING PROTEIN-LIKE 4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SQUAMOSA PROMOTER BINDING PROTEIN-LIKE 4; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DNA-BINDING DOMAIN (SBP DOMAIN); COMPND 5 SYNONYM: SPL4; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA; SOURCE 3 ORGANISM_COMMON: THALE CRESS; SOURCE 4 ORGANISM_TAXID: 3702; SOURCE 5 GENE: SPL4; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PCR2.1; SOURCE 8 OTHER_DETAILS: CELL-FREE SYNTHESIS KEYWDS TRANSCRIPTION FACTOR, SBP, FLOWER DEVELOPMENT, DNA BINDING PROTEIN, KEYWDS 2 STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS KEYWDS 3 INITIATIVE, RSGI EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.YAMASAKI,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 02-MAR-22 1UL4 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1UL4 1 VERSN REVDAT 1 09-MAR-04 1UL4 0 JRNL AUTH K.YAMASAKI,T.KIGAWA,M.INOUE,M.TATENO,T.YAMASAKI,T.YABUKI, JRNL AUTH 2 M.AOKI,E.SEKI,T.MATSUDA,E.NUNOKAWA,Y.ISHIZUKA,T.TERADA, JRNL AUTH 3 M.SHIROUZU,T.OSANAI,A.TANAKA,M.SEKI,K.SHINOZAKI,S.YOKOYAMA JRNL TITL A NOVEL ZINC-BINDING MOTIF REVEALED BY SOLUTION STRUCTURES JRNL TITL 2 OF DNA-BINDING DOMAINS OF ARABIDOPSIS SBP-FAMILY JRNL TITL 3 TRANSCRIPTION FACTORS. JRNL REF J.MOL.BIOL. V. 337 49 2004 JRNL REFN ISSN 0022-2836 JRNL PMID 15001351 JRNL DOI 10.1016/J.JMB.2004.01.015 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1, CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,SIMONSON, REMARK 3 WARREN (CNS), BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE, REMARK 3 JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1UL4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-SEP-03. REMARK 100 THE DEPOSITION ID IS D_1000005947. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 20MM KPI, 300MM KCL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 0.02MM ZNCL2 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; HMQC-J; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY 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 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 GLY A 44 REMARK 465 SER A 45 REMARK 465 SER A 46 REMARK 465 GLY A 47 REMARK 465 SER A 48 REMARK 465 SER A 49 REMARK 465 GLY A 50 REMARK 465 SER A 132 REMARK 465 GLY A 133 REMARK 465 PRO A 134 REMARK 465 SER A 135 REMARK 465 SER A 136 REMARK 465 GLY A 137 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 SER A 84 109.59 62.98 REMARK 500 1 SER A 99 -1.00 69.61 REMARK 500 1 GLU A 109 176.19 60.52 REMARK 500 1 ARG A 112 52.98 -93.57 REMARK 500 1 ARG A 117 -59.45 77.18 REMARK 500 1 ASN A 122 156.68 63.90 REMARK 500 1 GLU A 123 -71.64 -63.49 REMARK 500 1 ARG A 124 179.94 60.24 REMARK 500 1 ARG A 126 -56.14 -130.61 REMARK 500 2 HIS A 70 32.50 -98.16 REMARK 500 2 ARG A 71 -51.86 -125.99 REMARK 500 2 LYS A 81 41.06 -100.51 REMARK 500 2 SER A 84 102.80 -172.23 REMARK 500 2 SER A 99 25.12 44.27 REMARK 500 2 ASP A 108 -178.47 -172.93 REMARK 500 2 GLU A 109 -178.68 -60.34 REMARK 500 2 ALA A 110 -78.95 64.32 REMARK 500 2 ARG A 112 44.18 -141.54 REMARK 500 2 SER A 113 56.23 -146.23 REMARK 500 2 CYS A 114 164.43 61.43 REMARK 500 2 ARG A 116 -70.08 -90.14 REMARK 500 2 ARG A 124 -49.45 -142.58 REMARK 500 2 ARG A 126 -68.45 -149.36 REMARK 500 2 SER A 128 100.79 63.39 REMARK 500 2 SER A 129 -71.19 -87.70 REMARK 500 3 MET A 63 30.96 -98.94 REMARK 500 3 GLU A 65 46.21 -101.84 REMARK 500 3 SER A 99 23.59 45.69 REMARK 500 3 GLU A 109 -81.56 63.16 REMARK 500 3 ALA A 110 41.19 -146.56 REMARK 500 3 LYS A 111 97.80 62.40 REMARK 500 3 SER A 113 175.48 60.74 REMARK 500 3 CYS A 114 178.81 -59.41 REMARK 500 3 ALA A 119 97.92 -63.33 REMARK 500 3 GLU A 123 77.82 -117.01 REMARK 500 3 ARG A 124 -47.25 -137.50 REMARK 500 3 ARG A 126 78.13 -172.94 REMARK 500 3 LYS A 127 54.17 -161.46 REMARK 500 3 SER A 128 82.95 -162.91 REMARK 500 3 SER A 129 -60.43 -104.88 REMARK 500 4 LEU A 53 23.60 -142.18 REMARK 500 4 THR A 60 29.43 -140.44 REMARK 500 4 GLU A 65 56.37 -98.16 REMARK 500 4 HIS A 70 33.67 -98.63 REMARK 500 4 ARG A 71 -78.62 -120.59 REMARK 500 4 ARG A 112 33.86 -98.35 REMARK 500 4 CYS A 114 176.10 -56.22 REMARK 500 4 SER A 129 177.58 60.59 REMARK 500 5 SER A 84 118.49 -165.49 REMARK 500 5 SER A 99 17.30 52.11 REMARK 500 REMARK 500 THIS ENTRY HAS 204 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 138 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 54 SG REMARK 620 2 CYS A 59 SG 109.1 REMARK 620 3 CYS A 76 SG 105.8 104.6 REMARK 620 4 HIS A 79 ND1 111.1 112.0 113.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 139 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 95 SG REMARK 620 2 CYS A 98 SG 110.0 REMARK 620 3 HIS A 102 NE2 107.8 111.1 REMARK 620 4 CYS A 114 SG 106.1 112.4 109.1 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 138 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 139 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: ATR002002959.1 RELATED DB: TARGETDB DBREF 1UL4 A 51 131 UNP Q9S7A9 SPL4_ARATH 51 131 SEQADV 1UL4 GLY A 44 UNP Q9S7A9 CLONING ARTIFACT SEQADV 1UL4 SER A 45 UNP Q9S7A9 CLONING ARTIFACT SEQADV 1UL4 SER A 46 UNP Q9S7A9 CLONING ARTIFACT SEQADV 1UL4 GLY A 47 UNP Q9S7A9 CLONING ARTIFACT SEQADV 1UL4 SER A 48 UNP Q9S7A9 CLONING ARTIFACT SEQADV 1UL4 SER A 49 UNP Q9S7A9 CLONING ARTIFACT SEQADV 1UL4 GLY A 50 UNP Q9S7A9 CLONING ARTIFACT SEQADV 1UL4 SER A 132 UNP Q9S7A9 CLONING ARTIFACT SEQADV 1UL4 GLY A 133 UNP Q9S7A9 CLONING ARTIFACT SEQADV 1UL4 PRO A 134 UNP Q9S7A9 CLONING ARTIFACT SEQADV 1UL4 SER A 135 UNP Q9S7A9 CLONING ARTIFACT SEQADV 1UL4 SER A 136 UNP Q9S7A9 CLONING ARTIFACT SEQADV 1UL4 GLY A 137 UNP Q9S7A9 CLONING ARTIFACT SEQRES 1 A 94 GLY SER SER GLY SER SER GLY LEU ARG LEU CYS GLN VAL SEQRES 2 A 94 ASP ARG CYS THR ALA ASP MET LYS GLU ALA LYS LEU TYR SEQRES 3 A 94 HIS ARG ARG HIS LYS VAL CYS GLU VAL HIS ALA LYS ALA SEQRES 4 A 94 SER SER VAL PHE LEU SER GLY LEU ASN GLN ARG PHE CYS SEQRES 5 A 94 GLN GLN CYS SER ARG PHE HIS ASP LEU GLN GLU PHE ASP SEQRES 6 A 94 GLU ALA LYS ARG SER CYS ARG ARG ARG LEU ALA GLY HIS SEQRES 7 A 94 ASN GLU ARG ARG ARG LYS SER SER GLY GLU SER GLY PRO SEQRES 8 A 94 SER SER GLY HET ZN A 138 1 HET ZN A 139 1 HETNAM ZN ZINC ION FORMUL 2 ZN 2(ZN 2+) HELIX 1 1 LYS A 67 HIS A 73 1 7 HELIX 2 2 CYS A 76 LYS A 81 1 6 SHEET 1 A 3 VAL A 85 LEU A 87 0 SHEET 2 A 3 LEU A 90 PHE A 94 -1 O GLN A 92 N VAL A 85 SHEET 3 A 3 PHE A 101 ASP A 103 -1 O HIS A 102 N ARG A 93 LINK SG CYS A 54 ZN ZN A 138 1555 1555 2.46 LINK SG CYS A 59 ZN ZN A 138 1555 1555 2.47 LINK SG CYS A 76 ZN ZN A 138 1555 1555 2.47 LINK ND1 HIS A 79 ZN ZN A 138 1555 1555 2.16 LINK SG CYS A 95 ZN ZN A 139 1555 1555 2.47 LINK SG CYS A 98 ZN ZN A 139 1555 1555 2.46 LINK NE2 HIS A 102 ZN ZN A 139 1555 1555 2.13 LINK SG CYS A 114 ZN ZN A 139 1555 1555 2.45 SITE 1 AC1 4 CYS A 54 CYS A 59 CYS A 76 HIS A 79 SITE 1 AC2 4 CYS A 95 CYS A 98 HIS A 102 CYS A 114 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 2 2 Bytes