Header list of 1tte.pdb file
Complete list - t 27 2 Bytes
HEADER LIGASE 22-JUN-04 1TTE
TITLE THE STRUCTURE OF A CLASS II UBIQUITIN-CONJUGATING ENZYME, UBC1.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2-24 KDA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UBC1;
COMPND 5 SYNONYM: UBIQUITIN-PROTEIN LIGASE, UBIQUITIN CARRIER PROTEIN;
COMPND 6 EC: 6.3.2.19;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: UBC1, YDR177W, YD9395.10;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS UBC1, E2, UBIQUITIN-DEPENDENT DEGRADATION, LIGASE
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR N.MERKLEY,G.S.SHAW
REVDAT 4 27-OCT-21 1TTE 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1TTE 1 VERSN
REVDAT 2 16-NOV-04 1TTE 1 JRNL
REVDAT 1 31-AUG-04 1TTE 0
JRNL AUTH N.MERKLEY,G.S.SHAW
JRNL TITL SOLUTION STRUCTURE OF THE FLEXIBLE CLASS II
JRNL TITL 2 UBIQUITIN-CONJUGATING ENZYME UBC1 PROVIDES INSIGHTS FOR
JRNL TITL 3 POLYUBIQUITIN CHAIN ASSEMBLY.
JRNL REF J.BIOL.CHEM. V. 279 47139 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15328341
JRNL DOI 10.1074/JBC.M409576200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : A.T.BRUNGER, P.D.ADAMS, G.M.CLORE, W.L.DELANO,
REMARK 3 P.GROS, R.W.GROSSE-KUNSTLEVE, J.-S.JIANG,
REMARK 3 J.KUSZEWSKI, M.NILGES, N.S.PANNU, R.J.READ,
REMARK 3 L.M.RICE, T.SIMONSON, G.L.WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TTE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022887.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 150 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.48MM U-15N,13C UBC1; 25 MM
REMARK 210 TRIS; 1 MM EDTA, 1MM
REMARK 210 DITHIOTHREITOL, 150 MM NACL;
REMARK 210 0.48 MM U-15N UBC1; 25 MM TRIS;
REMARK 210 1 MM, 1 MM EDTA, 1MM DTT, 150 MM
REMARK 210 NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, PIPP/STAPP 4.3.3,
REMARK 210 VNMR 6.1C
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
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: 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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
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 ASP A 16 78.48 -65.28
REMARK 500 1 ASP A 17 145.41 62.64
REMARK 500 1 PRO A 18 86.99 -54.99
REMARK 500 1 ALA A 20 -4.88 78.85
REMARK 500 1 GLU A 29 -164.93 -58.72
REMARK 500 1 ILE A 32 105.44 -56.83
REMARK 500 1 PRO A 43 -158.77 -72.96
REMARK 500 1 THR A 45 144.99 -177.81
REMARK 500 1 PRO A 59 -166.99 -76.38
REMARK 500 1 MET A 60 50.31 -114.22
REMARK 500 1 PHE A 64 79.58 57.45
REMARK 500 1 PHE A 71 -91.12 63.34
REMARK 500 1 ASP A 72 93.34 41.36
REMARK 500 1 THR A 73 23.38 46.22
REMARK 500 1 LYS A 74 36.19 35.47
REMARK 500 1 SER A 81 82.29 70.89
REMARK 500 1 VAL A 83 -46.25 -144.98
REMARK 500 1 THR A 84 30.80 -142.13
REMARK 500 1 ASP A 90 -83.24 56.00
REMARK 500 1 LEU A 92 -53.55 -144.61
REMARK 500 1 ASN A 94 83.97 -167.66
REMARK 500 1 SER A 97 120.23 -179.19
REMARK 500 1 ILE A 100 91.36 -55.20
REMARK 500 1 GLN A 114 31.64 -97.95
REMARK 500 1 PRO A 121 -158.72 -79.86
REMARK 500 1 SER A 153 -178.59 60.96
REMARK 500 1 LYS A 157 -57.63 -131.47
REMARK 500 1 GLU A 161 -176.10 61.10
REMARK 500 1 SER A 163 -47.77 -144.72
REMARK 500 1 ASP A 169 -85.14 -155.44
REMARK 500 1 LEU A 193 -80.19 -76.06
REMARK 500 1 ASN A 201 45.65 -140.54
REMARK 500 1 ASP A 202 58.14 -165.47
REMARK 500 1 LEU A 214 35.07 -85.82
REMARK 500 2 PRO A 18 69.99 -65.40
REMARK 500 2 ALA A 19 -66.17 -153.51
REMARK 500 2 HIS A 21 89.84 62.20
REMARK 500 2 SER A 28 -78.74 174.96
REMARK 500 2 TYR A 47 52.26 -93.42
REMARK 500 2 LYS A 51 88.11 -151.63
REMARK 500 2 PRO A 59 -156.84 -69.14
REMARK 500 2 PHE A 64 36.27 -178.01
REMARK 500 2 PRO A 66 167.49 -49.75
REMARK 500 2 LYS A 74 144.59 63.11
REMARK 500 2 SER A 81 114.28 64.75
REMARK 500 2 SER A 82 -51.39 -160.26
REMARK 500 2 VAL A 83 -45.98 -135.73
REMARK 500 2 ILE A 91 18.19 -149.85
REMARK 500 2 ASN A 94 40.25 179.41
REMARK 500 2 VAL A 99 -81.54 -121.08
REMARK 500
REMARK 500 THIS ENTRY HAS 763 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TTE A 1 215 UNP P21734 UBC1_YEAST 1 215
SEQADV 1TTE SER A 1 UNP P21734 MET 1 ENGINEERED MUTATION
SEQADV 1TTE ARG A 93 UNP P21734 LYS 93 ENGINEERED MUTATION
SEQRES 1 A 215 SER SER ARG ALA LYS ARG ILE MET LYS GLU ILE GLN ALA
SEQRES 2 A 215 VAL LYS ASP ASP PRO ALA ALA HIS ILE THR LEU GLU PHE
SEQRES 3 A 215 VAL SER GLU SER ASP ILE HIS HIS LEU LYS GLY THR PHE
SEQRES 4 A 215 LEU GLY PRO PRO GLY THR PRO TYR GLU GLY GLY LYS PHE
SEQRES 5 A 215 VAL VAL ASP ILE GLU VAL PRO MET GLU TYR PRO PHE LYS
SEQRES 6 A 215 PRO PRO LYS MET GLN PHE ASP THR LYS VAL TYR HIS PRO
SEQRES 7 A 215 ASN ILE SER SER VAL THR GLY ALA ILE CYS LEU ASP ILE
SEQRES 8 A 215 LEU ARG ASN ALA TRP SER PRO VAL ILE THR LEU LYS SER
SEQRES 9 A 215 ALA LEU ILE SER LEU GLN ALA LEU LEU GLN SER PRO GLU
SEQRES 10 A 215 PRO ASN ASP PRO GLN ASP ALA GLU VAL ALA GLN HIS TYR
SEQRES 11 A 215 LEU ARG ASP ARG GLU SER PHE ASN LYS THR ALA ALA LEU
SEQRES 12 A 215 TRP THR ARG LEU TYR ALA SER GLU THR SER ASN GLY GLN
SEQRES 13 A 215 LYS GLY ASN VAL GLU GLU SER ASP LEU TYR GLY ILE ASP
SEQRES 14 A 215 HIS ASP LEU ILE ASP GLU PHE GLU SER GLN GLY PHE GLU
SEQRES 15 A 215 LYS ASP LYS ILE VAL GLU VAL LEU ARG ARG LEU GLY VAL
SEQRES 16 A 215 LYS SER LEU ASP PRO ASN ASP ASN ASN THR ALA ASN ARG
SEQRES 17 A 215 ILE ILE GLU GLU LEU LEU LYS
HELIX 1 1 ARG A 3 ASP A 16 1 14
HELIX 2 2 THR A 101 GLN A 114 1 14
HELIX 3 3 ASP A 123 ASP A 133 1 11
HELIX 4 4 ASP A 133 TYR A 148 1 16
HELIX 5 5 ASP A 169 GLY A 180 1 12
HELIX 6 6 GLU A 182 LEU A 193 1 12
HELIX 7 7 ASN A 203 LEU A 214 1 12
SHEET 1 A 4 THR A 23 LEU A 24 0
SHEET 2 A 4 HIS A 34 THR A 38 -1 O THR A 38 N THR A 23
SHEET 3 A 4 VAL A 53 GLU A 57 -1 O ILE A 56 N LEU A 35
SHEET 4 A 4 LYS A 68 GLN A 70 -1 O GLN A 70 N ASP A 55
SHEET 1 B 2 GLY A 41 THR A 45 0
SHEET 2 B 2 GLU A 48 GLY A 50 -1 O GLY A 50 N GLY A 41
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 - t 27 2 Bytes