Header list of 2hlw.pdb file
Complete list - r 9 2 Bytes
HEADER LIGASE, SIGNALING PROTEIN 10-JUL-06 2HLW
TITLE SOLUTION STRUCTURE OF THE HUMAN UBIQUITIN-CONJUGATING ENZYME VARIANT
TITLE 2 UEV1A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: UEV-1, CROC-1, UBIQUITIN-CONJUGATING ENZYME VARIANT KUA,
COMPND 5 TRAF6-REGULATED IKK ACTIVATOR 1 BETA UEV1A;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: UEV1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P
KEYWDS UBIQUITIN-CONJUGATING ENZYME VARIANT, UBIQUITIN, UBC13, HUBC13, E2,
KEYWDS 2 POLYUBIQUITINATION, LIGASE, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
MDLTYP MINIMIZED AVERAGE
AUTHOR D.D.HAU,M.J.LEWIS,L.F.SALTIBUS,L.PASTUSHOK,W.XIAO,L.SPYRACOPOULOS
REVDAT 3 09-MAR-22 2HLW 1 REMARK
REVDAT 2 24-FEB-09 2HLW 1 VERSN
REVDAT 1 05-SEP-06 2HLW 0
JRNL AUTH D.D.HAU,M.J.LEWIS,L.F.SALTIBUS,L.PASTUSHOK,W.XIAO,
JRNL AUTH 2 L.SPYRACOPOULOS
JRNL TITL STRUCTURE AND INTERACTIONS OF THE UBIQUITIN-CONJUGATING
JRNL TITL 2 ENZYME VARIANT HUMAN UEV1A: IMPLICATIONS FOR ENZYMATIC
JRNL TITL 3 SYNTHESIS OF POLYUBIQUITIN CHAINS(,).
JRNL REF BIOCHEMISTRY V. 45 9866 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16893187
JRNL DOI 10.1021/BI060631R
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, PROCHECK 3.5.4
REMARK 3 AUTHORS : BRUNGER (CNS), LASKOWSKI (PROCHECK)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 2080 NOE-DERIVED DISTANCE RESTRAINTS,
REMARK 3 56 JHNHA-DERIVED PHI RESTRAINTS, 69 TALOS-DERIVED PHI RESTRAINTS,
REMARK 3 68 TALOS-DERIVED PSI RESTRAINTS, 4 DNA/DAN-DERIVED PSI
REMARK 3 RESTRAINTS, 36 HYDROGEN BOND RESTRAINTS
REMARK 4
REMARK 4 2HLW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000038496.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50 MM NAH2PO4, 250 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM HUEV1A U-15N,13C; 50 MM
REMARK 210 NAH2PO4, 250 MM NACL, 0.9 MM DTT,
REMARK 210 1.7 MM DSS; 90% H2O, 10% D2O;
REMARK 210 0.75MM HUEV1A U-15N,U-10% 13C;
REMARK 210 50 MM NAH2PO4, 250 MM NACL, 0.9
REMARK 210 MM DTT, 1.7 MM DSS; 90% H2O, 10%
REMARK 210 D2O; 0.5MM HUEV1A U-15N; 50 MM
REMARK 210 NAH2PO4, 250 MM NACL, 0.9 MM DTT,
REMARK 210 1.7 MM DSS; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE UNKNOWN, NMRVIEW 5.2.2,
REMARK 210 VNMR 6.1, SPARKY 3.110
REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 GLU A 4 30.05 -152.77
REMARK 500 1 ALA A 7 -66.24 -159.30
REMARK 500 1 TYR A 9 -167.39 -171.13
REMARK 500 1 LYS A 11 104.28 60.09
REMARK 500 1 SER A 12 106.98 -165.23
REMARK 500 1 LEU A 16 -48.03 -141.70
REMARK 500 1 GLU A 19 -67.91 68.60
REMARK 500 1 LYS A 26 -65.97 -164.12
REMARK 500 1 HIS A 28 31.43 -143.59
REMARK 500 1 SER A 57 112.00 -160.86
REMARK 500 1 ASP A 63 46.38 -68.17
REMARK 500 1 GLU A 64 27.03 -157.38
REMARK 500 1 MET A 66 -60.49 -130.60
REMARK 500 1 LEU A 68 81.99 55.94
REMARK 500 1 THR A 69 -66.80 -97.72
REMARK 500 1 ARG A 70 93.70 -67.38
REMARK 500 1 ARG A 80 40.47 79.70
REMARK 500 1 GLU A 84 138.01 -38.36
REMARK 500 1 LYS A 97 87.94 61.81
REMARK 500 1 TYR A 98 -66.82 -105.27
REMARK 500 1 PRO A 99 2.91 -69.63
REMARK 500 1 THR A 109 -179.38 -69.00
REMARK 500 1 SER A 119 -58.16 -123.66
REMARK 500 1 LYS A 133 45.62 -105.92
REMARK 500 1 PRO A 163 34.93 -87.32
REMARK 500 1 GLU A 164 163.56 169.20
REMARK 500 1 CYS A 167 -168.83 -76.90
REMARK 500 2 GLN A 6 82.20 60.56
REMARK 500 2 LYS A 15 159.48 60.24
REMARK 500 2 SER A 17 95.53 -164.31
REMARK 500 2 ARG A 21 33.42 -167.65
REMARK 500 2 LYS A 30 -75.63 -66.55
REMARK 500 2 LYS A 33 122.18 62.87
REMARK 500 2 LYS A 49 -78.27 -58.79
REMARK 500 2 SER A 57 111.46 -162.35
REMARK 500 2 ASP A 63 -6.54 97.49
REMARK 500 2 GLU A 64 28.49 -155.68
REMARK 500 2 ARG A 80 43.77 80.53
REMARK 500 2 CYS A 94 -169.16 -108.74
REMARK 500 2 LYS A 97 68.99 60.05
REMARK 500 2 THR A 109 -173.51 -68.59
REMARK 500 2 LYS A 133 45.19 -105.88
REMARK 500 2 MET A 157 42.77 -88.10
REMARK 500 2 LYS A 158 -35.15 -141.19
REMARK 500 2 GLU A 164 -59.00 165.97
REMARK 500 2 SER A 169 156.28 61.18
REMARK 500 3 SER A 14 167.23 61.71
REMARK 500 3 GLU A 19 76.79 -155.18
REMARK 500 3 SER A 57 110.78 -161.05
REMARK 500 3 ASP A 63 -3.54 96.04
REMARK 500
REMARK 500 THIS ENTRY HAS 358 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A4D RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HUMAN UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 1
REMARK 900 (UEV-1)
REMARK 900 RELATED ID: 2C2V RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CHIP-UBC13-UEV1A COMPLEX
DBREF 2HLW A 31 170 UNP Q13404 UB2V1_HUMAN 74 221
SEQRES 1 A 170 MET PRO GLY GLU VAL GLN ALA SER TYR LEU LYS SER GLN
SEQRES 2 A 170 SER LYS LEU SER ASP GLU GLY ARG LEU GLU PRO ARG LYS
SEQRES 3 A 170 PHE HIS CYS LYS GLY VAL LYS VAL PRO ARG ASN PHE ARG
SEQRES 4 A 170 LEU LEU GLU GLU LEU GLU GLU GLY GLN LYS GLY VAL GLY
SEQRES 5 A 170 ASP GLY THR VAL SER TRP GLY LEU GLU ASP ASP GLU ASP
SEQRES 6 A 170 MET THR LEU THR ARG TRP THR GLY MET ILE ILE GLY PRO
SEQRES 7 A 170 PRO ARG THR ILE TYR GLU ASN ARG ILE TYR SER LEU LYS
SEQRES 8 A 170 ILE GLU CYS GLY PRO LYS TYR PRO GLU ALA PRO PRO PHE
SEQRES 9 A 170 VAL ARG PHE VAL THR LYS ILE ASN MET ASN GLY VAL ASN
SEQRES 10 A 170 SER SER ASN GLY VAL VAL ASP PRO ARG ALA ILE SER VAL
SEQRES 11 A 170 LEU ALA LYS TRP GLN ASN SER TYR SER ILE LYS VAL VAL
SEQRES 12 A 170 LEU GLN GLU LEU ARG ARG LEU MET MET SER LYS GLU ASN
SEQRES 13 A 170 MET LYS LEU PRO GLN PRO PRO GLU GLY GLN CYS TYR SER
SEQRES 14 A 170 ASN
HELIX 1 1 PRO A 35 GLY A 50 1 16
HELIX 2 2 VAL A 51 GLY A 54 5 4
HELIX 3 3 ILE A 128 LYS A 133 1 6
HELIX 4 4 SER A 139 SER A 153 1 15
SHEET 1 A 2 VAL A 56 LEU A 60 0
SHEET 2 A 2 TRP A 71 ILE A 75 -1 O MET A 74 N SER A 57
SHEET 1 B 2 LEU A 90 GLU A 93 0
SHEET 2 B 2 PHE A 104 PHE A 107 -1 O PHE A 104 N GLU A 93
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 9 2 Bytes