Header list of 1iym.pdb file
Complete list - 9 20 Bytes
HEADER DNA BINDING PROTEIN 30-AUG-02 1IYM
TITLE RING-H2 FINGER DOMAIN OF EL5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EL5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RING-H2 FINGER DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYZA SATIVA;
SOURCE 3 ORGANISM_COMMON: RICE;
SOURCE 4 ORGANISM_TAXID: 4530;
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: PET32A
KEYWDS RING-H2 FINGER, UBIQUITIN LIGASE, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR E.KATOH,S.KATOH,E.MINAMI,T.YAMAZAKI
REVDAT 5 14-JUN-23 1IYM 1 REMARK LINK
REVDAT 4 26-FEB-20 1IYM 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1IYM 1 VERSN
REVDAT 2 05-AUG-03 1IYM 1 SOURCE
REVDAT 1 22-JUL-03 1IYM 0
JRNL AUTH S.KATOH,C.HONG,Y.TSUNODA,K.MURATA,R.TAKAI,E.MINAMI,
JRNL AUTH 2 T.YAMAZAKI,E.KATOH
JRNL TITL HIGH PRECISION NMR STRUCTURE AND FUNCTION OF THE RING-H2
JRNL TITL 2 FINGER DOMAIN OF EL5, A RICE PROTEIN WHOSE EXPRESSION IS
JRNL TITL 3 INCREASED UPON EXPOSURE TO PATHOGEN-DERIVED OLIGOSACCHARIDES
JRNL REF J.BIOL.CHEM. V. 278 15341 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12588869
JRNL DOI 10.1074/JBC.M210531200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IYM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-SEP-02.
REMARK 100 THE DEPOSITION ID IS D_1000005412.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM RING-H2 FINGER DOMAIN OF EL5
REMARK 210 U-15N, 13C; 20MM TRIS-HCL BUFFER,
REMARK 210 100MM NACL, 20UM ZNSO4, 1MM DTT;
REMARK 210 90%H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY;
REMARK 210 4D_13C/15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 15
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: 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 ASP A 129 45.64 -85.32
REMARK 500 1 VAL A 136 -66.38 -98.85
REMARK 500 1 LEU A 141 107.26 -58.68
REMARK 500 1 CYS A 153 -50.60 -120.97
REMARK 500 1 LEU A 166 -73.37 -70.84
REMARK 500 1 SER A 168 -62.61 140.96
REMARK 500 1 SER A 170 49.27 -94.95
REMARK 500 1 ARG A 176 35.46 102.28
REMARK 500 1 THR A 178 154.92 -41.98
REMARK 500 2 LEU A 138 42.07 73.50
REMARK 500 2 LEU A 141 106.59 -58.39
REMARK 500 2 CYS A 153 -51.78 -120.51
REMARK 500 2 SER A 168 -53.71 92.64
REMARK 500 2 SER A 170 52.70 -102.12
REMARK 500 2 ARG A 176 35.72 101.92
REMARK 500 2 THR A 178 154.73 -41.89
REMARK 500 3 VAL A 136 -66.37 -98.97
REMARK 500 3 GLU A 146 73.44 -114.56
REMARK 500 3 CYS A 153 -52.86 -120.40
REMARK 500 3 LEU A 166 -71.15 -64.60
REMARK 500 3 SER A 168 -63.41 127.08
REMARK 500 3 SER A 170 51.15 -95.82
REMARK 500 3 ARG A 176 37.07 101.31
REMARK 500 3 THR A 178 155.13 -41.99
REMARK 500 4 MET A 128 78.92 -178.65
REMARK 500 4 VAL A 136 -66.34 -98.68
REMARK 500 4 LEU A 141 98.20 -58.63
REMARK 500 4 GLU A 146 79.87 -118.19
REMARK 500 4 CYS A 153 -51.23 -120.51
REMARK 500 4 LEU A 166 -72.47 -68.76
REMARK 500 4 SER A 168 -64.81 136.23
REMARK 500 4 SER A 170 50.59 -95.23
REMARK 500 4 ARG A 176 35.29 102.68
REMARK 500 4 THR A 178 155.22 -41.82
REMARK 500 5 MET A 128 82.77 71.76
REMARK 500 5 VAL A 136 -66.28 -98.59
REMARK 500 5 LEU A 141 97.42 -60.30
REMARK 500 5 LEU A 166 -74.09 -77.11
REMARK 500 5 SER A 168 -61.45 144.67
REMARK 500 5 SER A 170 44.71 -94.58
REMARK 500 5 ARG A 176 31.90 99.25
REMARK 500 6 VAL A 136 -66.13 -98.57
REMARK 500 6 LEU A 141 95.82 -58.32
REMARK 500 6 CYS A 153 -50.63 -120.88
REMARK 500 6 PHE A 157 -169.55 -120.38
REMARK 500 6 SER A 168 -52.66 91.27
REMARK 500 6 SER A 170 43.74 -101.85
REMARK 500 6 ARG A 176 42.12 101.76
REMARK 500 6 THR A 178 153.79 -41.48
REMARK 500 7 MET A 128 -173.22 56.56
REMARK 500
REMARK 500 THIS ENTRY HAS 122 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 148 0.27 SIDE CHAIN
REMARK 500 1 ARG A 152 0.12 SIDE CHAIN
REMARK 500 1 ARG A 176 0.27 SIDE CHAIN
REMARK 500 2 ARG A 148 0.08 SIDE CHAIN
REMARK 500 2 ARG A 152 0.25 SIDE CHAIN
REMARK 500 2 ARG A 176 0.18 SIDE CHAIN
REMARK 500 3 ARG A 152 0.22 SIDE CHAIN
REMARK 500 3 ARG A 176 0.32 SIDE CHAIN
REMARK 500 4 ARG A 148 0.21 SIDE CHAIN
REMARK 500 4 ARG A 152 0.26 SIDE CHAIN
REMARK 500 4 ARG A 176 0.30 SIDE CHAIN
REMARK 500 5 ARG A 148 0.23 SIDE CHAIN
REMARK 500 5 ARG A 152 0.21 SIDE CHAIN
REMARK 500 5 ARG A 176 0.25 SIDE CHAIN
REMARK 500 6 ARG A 148 0.18 SIDE CHAIN
REMARK 500 6 ARG A 152 0.25 SIDE CHAIN
REMARK 500 6 ARG A 176 0.31 SIDE CHAIN
REMARK 500 7 ARG A 148 0.26 SIDE CHAIN
REMARK 500 7 ARG A 152 0.32 SIDE CHAIN
REMARK 500 7 ARG A 176 0.32 SIDE CHAIN
REMARK 500 8 ARG A 148 0.22 SIDE CHAIN
REMARK 500 8 ARG A 152 0.17 SIDE CHAIN
REMARK 500 8 ARG A 176 0.20 SIDE CHAIN
REMARK 500 9 ARG A 148 0.29 SIDE CHAIN
REMARK 500 9 ARG A 176 0.31 SIDE CHAIN
REMARK 500 10 ARG A 148 0.30 SIDE CHAIN
REMARK 500 10 ARG A 152 0.31 SIDE CHAIN
REMARK 500 10 ARG A 176 0.26 SIDE CHAIN
REMARK 500 11 ARG A 148 0.30 SIDE CHAIN
REMARK 500 11 ARG A 152 0.24 SIDE CHAIN
REMARK 500 11 ARG A 176 0.25 SIDE CHAIN
REMARK 500 12 ARG A 148 0.30 SIDE CHAIN
REMARK 500 12 ARG A 152 0.32 SIDE CHAIN
REMARK 500 12 ARG A 176 0.31 SIDE CHAIN
REMARK 500 13 ARG A 148 0.27 SIDE CHAIN
REMARK 500 13 ARG A 152 0.29 SIDE CHAIN
REMARK 500 13 ARG A 176 0.28 SIDE CHAIN
REMARK 500 14 ARG A 148 0.31 SIDE CHAIN
REMARK 500 14 ARG A 152 0.26 SIDE CHAIN
REMARK 500 14 ARG A 176 0.28 SIDE CHAIN
REMARK 500 15 ARG A 148 0.17 SIDE CHAIN
REMARK 500 15 ARG A 152 0.32 SIDE CHAIN
REMARK 500 15 ARG A 176 0.32 SIDE CHAIN
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 182 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 134 SG
REMARK 620 2 CYS A 137 SG 108.1
REMARK 620 3 HIS A 158 ND1 108.5 111.0
REMARK 620 4 CYS A 161 SG 112.1 108.2 108.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 183 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 153 SG
REMARK 620 2 HIS A 155 ND1 107.5
REMARK 620 3 CYS A 172 SG 109.9 109.9
REMARK 620 4 CYS A 175 SG 107.5 113.6 108.5
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 182
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 183
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5459 RELATED DB: BMRB
REMARK 900 5459 CONTAINS THE CHEMICAL SHIFTS
DBREF 1IYM A 129 181 UNP Q9LRB7 EL5_ORYSA 129 181
SEQADV 1IYM ALA A 127 UNP Q9LRB7 CLONING ARTIFACT
SEQADV 1IYM MET A 128 UNP Q9LRB7 CLONING ARTIFACT
SEQRES 1 A 55 ALA MET ASP ASP GLY VAL GLU CYS ALA VAL CYS LEU ALA
SEQRES 2 A 55 GLU LEU GLU ASP GLY GLU GLU ALA ARG PHE LEU PRO ARG
SEQRES 3 A 55 CYS GLY HIS GLY PHE HIS ALA GLU CYS VAL ASP MET TRP
SEQRES 4 A 55 LEU GLY SER HIS SER THR CYS PRO LEU CYS ARG LEU THR
SEQRES 5 A 55 VAL VAL VAL
HET ZN A 182 1
HET ZN A 183 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 GLU A 160 TRP A 165 1 6
SHEET 1 A 2 ARG A 148 PHE A 149 0
SHEET 2 A 2 GLY A 156 PHE A 157 -1 O PHE A 157 N ARG A 148
LINK SG CYS A 134 ZN ZN A 182 1555 1555 2.29
LINK SG CYS A 137 ZN ZN A 182 1555 1555 2.28
LINK SG CYS A 153 ZN ZN A 183 1555 1555 2.28
LINK ND1 HIS A 155 ZN ZN A 183 1555 1555 2.10
LINK ND1 HIS A 158 ZN ZN A 182 1555 1555 2.08
LINK SG CYS A 161 ZN ZN A 182 1555 1555 2.30
LINK SG CYS A 172 ZN ZN A 183 1555 1555 2.30
LINK SG CYS A 175 ZN ZN A 183 1555 1555 2.31
SITE 1 AC1 4 CYS A 134 CYS A 137 HIS A 158 CYS A 161
SITE 1 AC2 4 CYS A 153 HIS A 155 CYS A 172 CYS A 175
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 - 9 20 Bytes