Header list of 1wd2.pdb file
Complete list - r 2 2 Bytes
HEADER LIGASE 11-MAY-04 1WD2
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL RING FROM A RING-IBR-RING (TRIAD)
TITLE 2 MOTIF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARIADNE-1 PROTEIN HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL RING;
COMPND 5 SYNONYM: ARI-1, UBIQUITIN-CONJUGATING ENZYME E2- BINDING PROTEIN 1,
COMPND 6 UBCH7-BINDING PROTEIN, UBCM4-INTERACTING PROTEIN, HHARI, H7-AP2,
COMPND 7 HUSSY-27, MOP-6;
COMPND 8 EC: 6.3.2.19;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX4T
KEYWDS RING, IBR, TRIAD, ZINC FINGER, LIGASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.D.CAPILI,E.L.EDGHILL,K.WU,K.L.B.BORDEN
REVDAT 3 02-MAR-22 1WD2 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1WD2 1 VERSN
REVDAT 1 20-JUL-04 1WD2 0
JRNL AUTH A.D.CAPILI,E.L.EDGHILL,K.WU,K.L.B.BORDEN
JRNL TITL STRUCTURE OF THE C-TERMINAL RING FINGER FROM A
JRNL TITL 2 RING-IBR-RING/TRIAD MOTIF REVEALS A NOVEL ZINC-BINDING
JRNL TITL 3 DOMAIN DISTINCT FROM A RING
JRNL REF J.MOL.BIOL. V. 340 1117 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15236971
JRNL DOI 10.1016/J.JMB.2004.05.035
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WD2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000023446.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 8.0
REMARK 210 IONIC STRENGTH : 120MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM RING2, U-15N,13C; 20MM TRIS
REMARK 210 -D11(PH 8.0), 120MM NACL; 1MM
REMARK 210 RING2, U-15N; 20MM TRIS-D11(PH
REMARK 210 8.0), 120MM NACL; 1MM RING2, U-
REMARK 210 13C; 20MM TRIS-D11(PH 8.0),
REMARK 210 120MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA & HN(CO)CA; HNCACB &
REMARK 210 HN(CO)CACB; (H)C(CO)NH-TOCSY;
REMARK 210 H(CCO)NH-TOCSY; 3D_15N-SEPARATED_
REMARK 210 TOCSY; 3D_15N-SEPARATED_NOESY;
REMARK 210 HNHA; 3D_13C-SEPARATED_NOESY; 3D_
REMARK 210 13C-SEPARATED_HCCH-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 3.1.2, CNS 1.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, FOLLOWED
REMARK 210 BY SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 : 6
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 29 95.45 -64.56
REMARK 500 1 MET A 35 -157.37 -171.07
REMARK 500 1 VAL A 36 94.13 -67.39
REMARK 500 1 ASN A 39 -89.52 -78.21
REMARK 500 1 GLN A 40 -82.42 -107.40
REMARK 500 1 TRP A 48 -176.50 49.62
REMARK 500 1 PRO A 53 170.17 -57.67
REMARK 500 1 TYR A 62 -65.15 -94.85
REMARK 500 1 ASN A 63 -61.82 -105.53
REMARK 500 1 CYS A 64 -63.79 175.80
REMARK 500 1 ARG A 66 38.99 -96.38
REMARK 500 1 TYR A 67 116.40 -173.90
REMARK 500 2 ALA A 13 -165.46 -175.89
REMARK 500 2 ALA A 14 142.94 66.44
REMARK 500 2 ASP A 29 95.63 -64.52
REMARK 500 2 MET A 35 -156.15 -169.63
REMARK 500 2 VAL A 36 92.66 -65.99
REMARK 500 2 ARG A 38 38.78 -140.34
REMARK 500 2 ASN A 39 -90.17 -78.28
REMARK 500 2 GLN A 40 -81.38 -105.84
REMARK 500 2 TRP A 48 -176.48 50.30
REMARK 500 2 TYR A 62 -65.71 -94.69
REMARK 500 2 ASN A 63 -63.23 -106.14
REMARK 500 2 CYS A 64 -72.41 174.51
REMARK 500 3 ALA A 14 -68.90 -132.55
REMARK 500 3 ASN A 15 164.89 58.61
REMARK 500 3 ASP A 29 95.12 -64.43
REMARK 500 3 MET A 35 -155.99 -172.25
REMARK 500 3 VAL A 36 91.07 -66.64
REMARK 500 3 ASN A 39 -86.56 -69.30
REMARK 500 3 GLN A 40 -81.14 -111.93
REMARK 500 3 TRP A 48 -175.07 47.40
REMARK 500 3 LEU A 51 37.72 70.20
REMARK 500 3 PRO A 53 171.60 -57.93
REMARK 500 3 TYR A 62 -65.60 -94.95
REMARK 500 3 ASN A 63 -61.69 -105.86
REMARK 500 3 CYS A 64 -177.62 179.00
REMARK 500 3 ASN A 65 -175.75 -65.83
REMARK 500 4 MET A 35 -157.01 -172.97
REMARK 500 4 VAL A 36 95.29 -66.54
REMARK 500 4 ASN A 39 -84.18 -66.90
REMARK 500 4 GLN A 40 -81.22 -115.28
REMARK 500 4 TRP A 48 -173.62 43.98
REMARK 500 4 LEU A 51 35.21 71.12
REMARK 500 4 TYR A 62 -63.86 -96.79
REMARK 500 4 CYS A 64 32.39 70.27
REMARK 500 5 ALA A 14 -81.31 62.95
REMARK 500 5 ASN A 15 -173.79 45.77
REMARK 500 5 GLU A 27 -60.43 -90.17
REMARK 500 5 ASP A 29 95.68 -64.75
REMARK 500
REMARK 500 THIS ENTRY HAS 230 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 71 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 19 SG
REMARK 620 2 CYS A 22 SG 101.0
REMARK 620 3 CYS A 37 SG 108.5 149.5
REMARK 620 4 CYS A 42 SG 104.2 83.1 82.4
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 71
DBREF 1WD2 A 11 69 UNP Q9Y4X5 ARI1_HUMAN 336 394
SEQADV 1WD2 PHE A 70 UNP Q9Y4X5 CLONING ARTIFACT
SEQRES 1 A 60 TRP ILE ALA ALA ASN THR LYS GLU CYS PRO LYS CYS HIS
SEQRES 2 A 60 VAL THR ILE GLU LYS ASP GLY GLY CYS ASN HIS MET VAL
SEQRES 3 A 60 CYS ARG ASN GLN ASN CYS LYS ALA GLU PHE CYS TRP VAL
SEQRES 4 A 60 CYS LEU GLY PRO TRP GLU PRO HIS GLY SER ALA TRP TYR
SEQRES 5 A 60 ASN CYS ASN ARG TYR ASN GLU PHE
HET ZN A 71 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 GLN A 40 ALA A 44 5 5
HELIX 2 2 TRP A 54 SER A 59 5 6
LINK SG CYS A 19 ZN ZN A 71 1555 1555 2.54
LINK SG CYS A 22 ZN ZN A 71 1555 1555 2.48
LINK SG CYS A 37 ZN ZN A 71 1555 1555 2.48
LINK SG CYS A 42 ZN ZN A 71 1555 1555 2.61
SITE 1 AC1 5 CYS A 19 CYS A 22 CYS A 37 CYS A 42
SITE 2 AC1 5 PHE A 46
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