Header list of 1ul5.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 09-SEP-03 1UL5
TITLE SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF SQUAMOSA PROMOTER
TITLE 2 BINDING PROTEIN-LIKE 7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SQUAMOSA PROMOTER BINDING PROTEIN-LIKE 7;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN (SBP DOMAIN);
COMPND 5 SYNONYM: SPL7;
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: SPL7;
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 1UL5 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1UL5 1 VERSN
REVDAT 1 09-MAR-04 1UL5 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 1UL5 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_1000005948.
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 133
REMARK 465 SER A 134
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 136 81.18 -63.90
REMARK 500 1 ARG A 137 117.34 -160.06
REMARK 500 1 GLN A 139 42.74 -89.98
REMARK 500 1 ASP A 146 62.57 -115.90
REMARK 500 1 ILE A 147 69.41 -67.89
REMARK 500 1 HIS A 157 23.60 -152.77
REMARK 500 1 SER A 167 -62.62 75.12
REMARK 500 1 LEU A 171 -172.01 -59.56
REMARK 500 1 ASP A 172 92.73 -50.78
REMARK 500 1 LYS A 184 -177.89 -68.46
REMARK 500 1 ASP A 190 42.78 -100.56
REMARK 500 1 LYS A 195 176.51 60.34
REMARK 500 1 ARG A 196 60.70 -107.45
REMARK 500 1 ARG A 204 -48.19 -165.64
REMARK 500 1 ASN A 206 -58.13 -142.68
REMARK 500 1 ASN A 207 31.11 -99.26
REMARK 500 1 VAL A 214 -75.36 -96.80
REMARK 500 1 LYS A 216 -38.50 178.64
REMARK 500 1 VAL A 219 -45.68 -153.44
REMARK 500 2 ALA A 136 99.85 -58.35
REMARK 500 2 CYS A 138 97.98 -62.64
REMARK 500 2 GLN A 139 42.18 -89.10
REMARK 500 2 GLU A 144 77.10 -100.58
REMARK 500 2 ASP A 146 68.59 -117.16
REMARK 500 2 HIS A 157 19.59 -145.45
REMARK 500 2 SER A 167 -64.47 72.98
REMARK 500 2 LEU A 171 -171.21 -59.86
REMARK 500 2 ASP A 172 90.63 -54.61
REMARK 500 2 TYR A 178 95.65 -64.06
REMARK 500 2 ARG A 196 31.62 -98.43
REMARK 500 2 ARG A 199 96.30 -59.61
REMARK 500 2 LYS A 201 100.85 -59.45
REMARK 500 2 ARG A 204 159.87 61.16
REMARK 500 2 ARG A 208 88.92 60.84
REMARK 500 2 ARG A 209 -47.56 -142.90
REMARK 500 2 LYS A 212 84.83 -169.54
REMARK 500 2 ASP A 215 -65.84 -156.16
REMARK 500 2 LYS A 216 99.53 60.75
REMARK 500 3 ARG A 137 114.83 -160.03
REMARK 500 3 CYS A 138 99.98 -57.56
REMARK 500 3 GLN A 139 42.07 -90.09
REMARK 500 3 ASP A 146 66.28 -111.67
REMARK 500 3 GLU A 149 29.97 -153.34
REMARK 500 3 LEU A 171 -172.21 -57.48
REMARK 500 3 ASP A 172 90.75 -54.14
REMARK 500 3 ASP A 190 31.86 -98.51
REMARK 500 3 ASP A 192 -168.48 -78.37
REMARK 500 3 HIS A 205 -61.53 -121.87
REMARK 500 3 ASN A 207 113.60 61.33
REMARK 500 3 ARG A 211 -46.47 -156.62
REMARK 500
REMARK 500 THIS ENTRY HAS 333 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 221 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 138 SG
REMARK 620 2 CYS A 143 SG 110.2
REMARK 620 3 CYS A 160 SG 114.7 110.0
REMARK 620 4 CYS A 163 SG 105.5 108.8 107.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 222 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 179 SG
REMARK 620 2 CYS A 182 SG 109.6
REMARK 620 3 HIS A 186 NE2 108.1 108.2
REMARK 620 4 CYS A 198 SG 111.3 109.9 109.7
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 221
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 222
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: ATR001006152.1 RELATED DB: TARGETDB
DBREF 1UL5 A 135 220 UNP Q8S9G8 SPL7_ARATH 135 220
SEQADV 1UL5 GLY A 133 UNP Q8S9G8 CLONING ARTIFACT
SEQADV 1UL5 SER A 134 UNP Q8S9G8 CLONING ARTIFACT
SEQRES 1 A 88 GLY SER VAL ALA ARG CYS GLN VAL PRO ASP CYS GLU ALA
SEQRES 2 A 88 ASP ILE SER GLU LEU LYS GLY TYR HIS LYS ARG HIS ARG
SEQRES 3 A 88 VAL CYS LEU ARG CYS ALA THR ALA SER PHE VAL VAL LEU
SEQRES 4 A 88 ASP GLY GLU ASN LYS ARG TYR CYS GLN GLN CYS GLY LYS
SEQRES 5 A 88 PHE HIS LEU LEU PRO ASP PHE ASP GLU GLY LYS ARG SER
SEQRES 6 A 88 CYS ARG ARG LYS LEU GLU ARG HIS ASN ASN ARG ARG LYS
SEQRES 7 A 88 ARG LYS PRO VAL ASP LYS GLY GLY VAL ALA
HET ZN A 221 1
HET ZN A 222 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 HIS A 154 ARG A 158 5 5
HELIX 2 2 CYS A 160 SER A 167 1 8
HELIX 3 3 PRO A 189 PHE A 191 5 3
SHEET 1 A 2 GLN A 139 VAL A 140 0
SHEET 2 A 2 CYS A 143 GLU A 144 -1 O CYS A 143 N VAL A 140
SHEET 1 B 3 PHE A 168 LEU A 171 0
SHEET 2 B 3 GLU A 174 TYR A 178 -1 N LYS A 176 O VAL A 169
SHEET 3 B 3 PHE A 185 LEU A 187 -1 O HIS A 186 N ARG A 177
LINK SG CYS A 138 ZN ZN A 221 1555 1555 2.46
LINK SG CYS A 143 ZN ZN A 221 1555 1555 2.47
LINK SG CYS A 160 ZN ZN A 221 1555 1555 2.47
LINK SG CYS A 163 ZN ZN A 221 1555 1555 2.46
LINK SG CYS A 179 ZN ZN A 222 1555 1555 2.47
LINK SG CYS A 182 ZN ZN A 222 1555 1555 2.46
LINK NE2 HIS A 186 ZN ZN A 222 1555 1555 2.14
LINK SG CYS A 198 ZN ZN A 222 1555 1555 2.46
SITE 1 AC1 4 CYS A 138 CYS A 143 CYS A 160 CYS A 163
SITE 1 AC2 4 CYS A 179 CYS A 182 HIS A 186 CYS A 198
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