Header list of 1rgo.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN 12-NOV-03 1RGO
TITLE STRUCTURAL BASIS FOR RECOGNITION OF THE MRNA CLASS II AU-RICH ELEMENT
TITLE 2 BY THE TANDEM ZINC FINGER DOMAIN OF TIS11D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA (5'-R(*UP*UP*AP*UP*UP*UP*AP*UP*U)-3');
COMPND 3 CHAIN: D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: BUTYRATE RESPONSE FACTOR 2;
COMPND 7 CHAIN: A;
COMPND 8 SYNONYM: TIS11D PROTEIN, EGF-RESPONSE FACTOR 2, ERF-2;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHETIC;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 6 ORGANISM_COMMON: HUMAN;
SOURCE 7 ORGANISM_TAXID: 9606;
SOURCE 8 GENE: ZFP36L2, BRF2, TIS11D, ERF2;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS TIS11 TTP TRISTETRAPROLIN BUTYRATE RESPONSE FACTOR ERF NUP475 ZFP ZN
KEYWDS 2 ZINC FINGER RNA SS SINGLE-STRANDED ARE UTR TANDEM INTERCALATION
KEYWDS 3 INTERCALATE SPECIFIC, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.P.HUDSON,M.A.MARTINEZ-YAMOUT,H.J.DYSON,P.E.WRIGHT
REVDAT 3 02-MAR-22 1RGO 1 REMARK LINK
REVDAT 2 24-FEB-09 1RGO 1 VERSN
REVDAT 1 02-MAR-04 1RGO 0
JRNL AUTH B.P.HUDSON,M.A.MARTINEZ-YAMOUT,H.J.DYSON,P.E.WRIGHT
JRNL TITL RECOGNITION OF THE MRNA AU-RICH ELEMENT BY THE ZINC FINGER
JRNL TITL 2 DOMAIN OF TIS11D.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 257 2004
JRNL REFN ISSN 1545-9993
JRNL PMID 14981510
JRNL DOI 10.1038/NSMB738
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR VARIOUS, AMBER 8
REMARK 3 AUTHORS : BRUKER (XWINNMR), CASE, D. A., ET AL. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RGO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000020729.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : 20 MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM 15N-TIS11D TZF; 0.5 MM 5'
REMARK 210 -UUAUUUAUU-3'; 10 MM TRIS PH 6.2;
REMARK 210 20 MM KCL; 2.5 MM DTT; 25 UM
REMARK 210 ZNSO4; 0.5 MM 15N,13C-TIS11D TZF;
REMARK 210 0.5 MM 5'-UUAUUUAUU-3'; 10 MM
REMARK 210 TRIS PH 6.2; 20 MM KCL; 2.5 MM
REMARK 210 DTT; 25 UM ZNSO4; 0.5 MM 15N,13C-
REMARK 210 TIS11D TZF; 0.5 MM 5'-UUAUUUAUU-
REMARK 210 3'; 10 MM TRIS-D11 PD 6.2; 20 MM
REMARK 210 KCL; 2.5 MM DTT-D10; 25 UM ZNSO4;
REMARK 210 0.5 MM 15N,13C-TIS11D TZF; 0.5
REMARK 210 MM 5'-UUAUUUAUU-3'; 10 MM TRIS
REMARK 210 PH 6.2; 20 MM KCL; 2.5 MM DTT;
REMARK 210 25 UM ZNSO4; 12 MG/ML PF1
REMARK 210 BACTERIOPHAGE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D 13C F1-
REMARK 210 EDITED, F3-FILTERED NOESY; 2D
REMARK 210 13C DOUBLE-HALF-FILTERED NOESY;
REMARK 210 HNHA; HNHB; HACAHB COSY; 13C-{
REMARK 210 13CO} SPIN-ECHO DIFFERENCE CT-
REMARK 210 HSQC; 13C-{15N} SPIN-ECHO
REMARK 210 DIFFERENCE CT-HSQC; IPAP-[1H-15N]
REMARK 210 -HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 5.0, SANE,
REMARK 210 DYANA 1.5, AMBER 8
REMARK 210 METHOD USED : INDIVIDUAL ZINC FINGER DOMAINS
REMARK 210 WERE CREATED IN DYANA AND DOCKED
REMARK 210 TO UAUU (FINGER I) AND UUAUU
REMARK 210 (FINGER II) USING FIVE ROUNDS OF
REMARK 210 SIMULATED ANNEALING IN AMBER
REMARK 210 USING DISTANCE AND TORSIONAL
REMARK 210 RESTRAINTS. FINGER I/UAUU AND
REMARK 210 FINGER II/UUAUU COMPLEXES WERE
REMARK 210 CONNECTED TO FORM TZF/UUAUUUAUU
REMARK 210 COMPLEXES AND REFINED IN AMBER
REMARK 210 WITH RESIDUAL DIPOLAR COUPLING
REMARK 210 RESTRAINTS ADDED. CALCULATIONS
REMARK 210 WERE THEN SWITCHED FROM IN VACUO
REMARK 210 TO GENERALIZED BORN CONTINUUM
REMARK 210 SOLVENT MODEL AND ONE ADDITIONAL
REMARK 210 ROUND OF SIMULATED ANNEALING WAS
REMARK 210 PERFORMED.
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: 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 A D 3 C4 - C5 - C6 ANGL. DEV. = -3.0 DEGREES
REMARK 500 1 A D 3 C5 - C6 - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 A D 3 N1 - C6 - N6 ANGL. DEV. = -5.2 DEGREES
REMARK 500 1 A D 7 C4 - C5 - C6 ANGL. DEV. = -3.1 DEGREES
REMARK 500 1 A D 7 C5 - C6 - N1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 A D 7 N1 - C6 - N6 ANGL. DEV. = -4.2 DEGREES
REMARK 500 1 ARG A 184 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 2 A D 3 C5 - C6 - N1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 A D 3 N1 - C6 - N6 ANGL. DEV. = -4.8 DEGREES
REMARK 500 2 A D 7 C4 - C5 - C6 ANGL. DEV. = -3.1 DEGREES
REMARK 500 2 A D 7 C5 - C6 - N1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 A D 7 N1 - C6 - N6 ANGL. DEV. = -4.3 DEGREES
REMARK 500 3 A D 3 C4 - C5 - C6 ANGL. DEV. = -3.1 DEGREES
REMARK 500 3 A D 3 C5 - C6 - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 A D 3 N1 - C6 - N6 ANGL. DEV. = -5.3 DEGREES
REMARK 500 3 A D 7 C4 - C5 - C6 ANGL. DEV. = -3.1 DEGREES
REMARK 500 3 A D 7 C5 - C6 - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 A D 7 N1 - C6 - N6 ANGL. DEV. = -4.3 DEGREES
REMARK 500 3 U D 8 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 3 ARG A 188 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 3 ARG A 198 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 4 A D 3 C4 - C5 - C6 ANGL. DEV. = -3.3 DEGREES
REMARK 500 4 A D 3 C5 - C6 - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 4 A D 3 N1 - C6 - N6 ANGL. DEV. = -5.4 DEGREES
REMARK 500 4 U D 4 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 4 U D 6 C1' - O4' - C4' ANGL. DEV. = -4.3 DEGREES
REMARK 500 4 U D 6 O4' - C1' - N1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 4 A D 7 C5 - C6 - N1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 4 A D 7 N1 - C6 - N6 ANGL. DEV. = -4.4 DEGREES
REMARK 500 4 ARG A 153 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 5 A D 3 C4 - C5 - C6 ANGL. DEV. = -3.2 DEGREES
REMARK 500 5 A D 3 C5 - C6 - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 5 A D 3 N1 - C6 - N6 ANGL. DEV. = -5.5 DEGREES
REMARK 500 5 U D 6 O4' - C1' - N1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 5 A D 7 C4 - C5 - C6 ANGL. DEV. = -3.0 DEGREES
REMARK 500 5 A D 7 C5 - C6 - N1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 5 A D 7 N1 - C6 - N6 ANGL. DEV. = -4.3 DEGREES
REMARK 500 5 U D 8 O4' - C1' - N1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 6 U D 2 C1' - O4' - C4' ANGL. DEV. = -5.0 DEGREES
REMARK 500 6 U D 2 O4' - C1' - N1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 6 A D 3 C4 - C5 - C6 ANGL. DEV. = -3.1 DEGREES
REMARK 500 6 A D 3 C5 - C6 - N1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 6 A D 3 N1 - C6 - N6 ANGL. DEV. = -5.1 DEGREES
REMARK 500 6 A D 7 C5 - C6 - N1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 A D 7 N1 - C6 - N6 ANGL. DEV. = -4.4 DEGREES
REMARK 500 6 ARG A 184 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 6 ARG A 198 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 7 U D 2 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 7 A D 3 C5 - C6 - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 7 A D 3 N1 - C6 - N6 ANGL. DEV. = -5.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 142 ANGLE DEVIATIONS.
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 HIS A 216 -94.09 -88.59
REMARK 500 2 HIS A 216 -95.01 -86.65
REMARK 500 3 HIS A 216 -95.75 -89.64
REMARK 500 4 HIS A 216 -95.62 -91.70
REMARK 500 5 HIS A 216 -90.23 -85.98
REMARK 500 6 HIS A 216 -93.96 -93.46
REMARK 500 7 HIS A 216 -97.28 -96.00
REMARK 500 8 HIS A 216 -95.26 -89.38
REMARK 500 9 HIS A 216 -97.29 -83.77
REMARK 500 10 HIS A 216 -98.46 -87.19
REMARK 500 11 HIS A 216 -95.26 -90.71
REMARK 500 12 HIS A 216 -92.57 -82.79
REMARK 500 12 ALA A 218 97.24 -69.33
REMARK 500 13 HIS A 216 -94.61 -89.72
REMARK 500 14 HIS A 216 -97.53 -87.24
REMARK 500 15 HIS A 216 -94.50 -90.72
REMARK 500 16 HIS A 216 -94.50 -89.80
REMARK 500 17 ARG A 153 42.08 -82.20
REMARK 500 17 HIS A 216 -89.17 -88.52
REMARK 500 18 HIS A 216 -87.30 -89.54
REMARK 500 18 ALA A 218 -94.51 -92.35
REMARK 500 19 HIS A 216 -89.78 -82.79
REMARK 500 20 ARG A 153 41.66 -81.10
REMARK 500 20 HIS A 216 -87.72 -91.74
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 A D 7 0.10 SIDE CHAIN
REMARK 500 2 U D 5 0.07 SIDE CHAIN
REMARK 500 2 A D 7 0.07 SIDE CHAIN
REMARK 500 4 U D 4 0.08 SIDE CHAIN
REMARK 500 4 U D 5 0.06 SIDE CHAIN
REMARK 500 4 A D 7 0.08 SIDE CHAIN
REMARK 500 6 A D 3 0.06 SIDE CHAIN
REMARK 500 6 A D 7 0.06 SIDE CHAIN
REMARK 500 7 U D 5 0.08 SIDE CHAIN
REMARK 500 7 A D 7 0.11 SIDE CHAIN
REMARK 500 8 A D 3 0.08 SIDE CHAIN
REMARK 500 8 U D 6 0.07 SIDE CHAIN
REMARK 500 8 A D 7 0.08 SIDE CHAIN
REMARK 500 9 A D 7 0.08 SIDE CHAIN
REMARK 500 10 U D 2 0.07 SIDE CHAIN
REMARK 500 10 U D 6 0.06 SIDE CHAIN
REMARK 500 10 A D 7 0.07 SIDE CHAIN
REMARK 500 11 U D 2 0.07 SIDE CHAIN
REMARK 500 11 A D 3 0.06 SIDE CHAIN
REMARK 500 11 U D 6 0.10 SIDE CHAIN
REMARK 500 11 A D 7 0.07 SIDE CHAIN
REMARK 500 12 A D 3 0.09 SIDE CHAIN
REMARK 500 12 U D 6 0.07 SIDE CHAIN
REMARK 500 12 A D 7 0.06 SIDE CHAIN
REMARK 500 13 U D 6 0.07 SIDE CHAIN
REMARK 500 13 TYR A 170 0.08 SIDE CHAIN
REMARK 500 14 U D 2 0.07 SIDE CHAIN
REMARK 500 14 U D 6 0.08 SIDE CHAIN
REMARK 500 14 A D 7 0.10 SIDE CHAIN
REMARK 500 15 U D 2 0.15 SIDE CHAIN
REMARK 500 15 A D 7 0.07 SIDE CHAIN
REMARK 500 16 U D 2 0.08 SIDE CHAIN
REMARK 500 16 A D 7 0.06 SIDE CHAIN
REMARK 500 17 U D 6 0.08 SIDE CHAIN
REMARK 500 17 A D 7 0.08 SIDE CHAIN
REMARK 500 18 U D 6 0.06 SIDE CHAIN
REMARK 500 18 A D 7 0.07 SIDE CHAIN
REMARK 500 19 U D 6 0.08 SIDE CHAIN
REMARK 500 19 A D 7 0.07 SIDE CHAIN
REMARK 500 20 A D 3 0.08 SIDE CHAIN
REMARK 500 20 U D 6 0.08 SIDE CHAIN
REMARK 500 20 A D 7 0.07 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 221 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 159 SG
REMARK 620 2 CYS A 168 SG 112.1
REMARK 620 3 CYS A 174 SG 108.5 108.1
REMARK 620 4 HIS A 178 NE2 112.2 107.3 108.5
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 197 SG
REMARK 620 2 CYS A 206 SG 111.1
REMARK 620 3 CYS A 212 SG 109.6 110.4
REMARK 620 4 HIS A 216 NE2 111.8 107.2 106.6
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
DBREF 1RGO A 151 220 UNP P47974 TISD_HUMAN 151 220
DBREF 1RGO D 1 9 PDB 1RGO 1RGO 1 9
SEQRES 1 D 9 U U A U U U A U U
SEQRES 1 A 70 SER THR ARG TYR LYS THR GLU LEU CYS ARG PRO PHE GLU
SEQRES 2 A 70 GLU SER GLY THR CYS LYS TYR GLY GLU LYS CYS GLN PHE
SEQRES 3 A 70 ALA HIS GLY PHE HIS GLU LEU ARG SER LEU THR ARG HIS
SEQRES 4 A 70 PRO LYS TYR LYS THR GLU LEU CYS ARG THR PHE HIS THR
SEQRES 5 A 70 ILE GLY PHE CYS PRO TYR GLY PRO ARG CYS HIS PHE ILE
SEQRES 6 A 70 HIS ASN ALA ASP GLU
HET ZN A 221 1
HET ZN A 222 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 2(ZN 2+)
HELIX 1 1 CYS A 159 GLY A 166 1 8
HELIX 2 2 TYR A 170 CYS A 174 5 5
HELIX 3 3 GLY A 179 LEU A 183 5 5
HELIX 4 4 CYS A 197 GLY A 204 1 8
HELIX 5 5 TYR A 208 CYS A 212 5 5
LINK SG CYS A 159 ZN ZN A 221 1555 1555 2.30
LINK SG CYS A 168 ZN ZN A 221 1555 1555 2.29
LINK SG CYS A 174 ZN ZN A 221 1555 1555 2.28
LINK NE2 HIS A 178 ZN ZN A 221 1555 1555 2.09
LINK SG CYS A 197 ZN ZN A 222 1555 1555 2.30
LINK SG CYS A 206 ZN ZN A 222 1555 1555 2.29
LINK SG CYS A 212 ZN ZN A 222 1555 1555 2.29
LINK NE2 HIS A 216 ZN ZN A 222 1555 1555 2.08
SITE 1 AC1 4 CYS A 159 CYS A 168 CYS A 174 HIS A 178
SITE 1 AC2 4 CYS A 197 CYS A 206 CYS A 212 HIS A 216
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