Header list of 2fuh.pdb file
Complete list - r 9 2 Bytes
HEADER LIGASE 26-JAN-06 2FUH
TITLE SOLUTION STRUCTURE OF THE UBCH5C/UB NON-COVALENT COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 D3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UBCH5C;
COMPND 5 SYNONYM: UBIQUITIN-PROTEIN LIGASE D3, UBIQUITIN CARRIER PROTEIN D3,
COMPND 6 UBIQUITIN-CONJUGATING ENZYME E2-17 KDA 3, E217, KB 3;
COMPND 7 EC: 6.3.2.19;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: UBIQUITIN;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: UBIQUITIN;
COMPND 13 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: UBE2D3, UBCH5C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 13 ORGANISM_COMMON: NORWAY RAT;
SOURCE 14 ORGANISM_TAXID: 10116;
SOURCE 15 GENE: RPS27A, UBA80, UBCEP1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS PROTEIN-PROTEIN COMPLEX UBIQUITIN UBIQUITIN-CONJUGATING ENZYME,
KEYWDS 2 LIGASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR P.S.BRZOVIC,A.LISSOUNOV,D.W.HOYT,R.E.KLEVIT
REVDAT 3 09-MAR-22 2FUH 1 REMARK
REVDAT 2 24-FEB-09 2FUH 1 VERSN
REVDAT 1 28-MAR-06 2FUH 0
JRNL AUTH P.S.BRZOVIC,A.LISSOUNOV,D.E.CHRISTENSEN,D.W.HOYT,R.E.KLEVIT
JRNL TITL A UBCH5/UBIQUITIN NONCOVALENT COMPLEX IS REQUIRED FOR
JRNL TITL 2 PROCESSIVE BRCA1-DIRECTED UBIQUITINATION.
JRNL REF MOL.CELL V. 21 873 2006
JRNL REFN ISSN 1097-2765
JRNL PMID 16543155
JRNL DOI 10.1016/J.MOLCEL.2006.02.008
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR UNKNOWN, CNS CNS_SOLVE_1.1
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1649 CONSTRAINTS: 1230 NOE-DERIVED DISTANCE CONSTRAINTS
REMARK 3 INCLUDING 26 INTERMOLECULAR NOE CONSTRAINTS, 328 DIHEDRAL ANGLE
REMARK 3 RESTAINTS, AND 91 HYDROGEN-BOND RESTRAINTS
REMARK 4
REMARK 4 2FUH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036326.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 150MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM UBCH5C U-15N,13C 25MM SODIUM
REMARK 210 PHOSPHATE 150MM NACL; 1MM
REMARK 210 UBIQUITIN U-15N,13C 25MM SODIUM
REMARK 210 PHOSPHATE 150MM NACL; 1MM UBCH5C
REMARK 210 U-15N,13C 1MM UBIQUITIN 25MM
REMARK 210 SODIUM PHOSPHATE 150MM NACL; 1MM
REMARK 210 UBIQUITIN U-15N,13C 1MM UBCH5C
REMARK 210 25MM SODIUM PHOSPHATE 150MM NACL;
REMARK 210 1MM UBCH5C U-15N,13C 1MM
REMARK 210 UBIQUITIN 25MM SODIUM PHOSPHATE
REMARK 210 150MM NACL; 1MM UBIQUITIN U-15N,
REMARK 210 13C 1MM UBCH5C 25MM SODIUM
REMARK 210 PHOSPHATE 150MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 900 MHZ; 500
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; DMX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR UNKNOWN, NMRPIPE
REMARK 210 UNKNOWN, NMRVIEW 5.0.4, CNS CNS_
REMARK 210 SOLVE_1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 10
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE FOLLOWING EXPERIMENTS WERE CONDUCTED: (1) TRIPLE
REMARK 210 RESONANCE FOR ASSIGNMENT OF PROTEIN; (2) 3D HETERONUCLEAR
REMARK 210 SEPARATED AND FILTERED NOE EXPERIMENTS
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: A, B
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 90.80 -161.57
REMARK 500 1 PHE A 31 -39.37 -163.85
REMARK 500 1 PRO A 40 -6.90 -47.24
REMARK 500 1 ASN A 41 48.45 74.34
REMARK 500 1 ASP A 42 -47.21 -155.06
REMARK 500 1 PRO A 44 76.57 -67.54
REMARK 500 1 TYR A 45 15.32 -175.54
REMARK 500 1 TYR A 60 149.86 74.33
REMARK 500 1 PRO A 61 -23.05 -37.71
REMARK 500 1 PHE A 62 -17.67 -45.19
REMARK 500 1 PRO A 76 66.58 -69.08
REMARK 500 1 ASN A 77 -6.34 -173.86
REMARK 500 1 ASN A 79 -159.04 -73.50
REMARK 500 1 ARG A 90 -167.76 -65.64
REMARK 500 1 SER A 91 -26.38 -37.36
REMARK 500 1 GLN A 92 28.93 -77.32
REMARK 500 1 PRO A 95 -9.52 -45.76
REMARK 500 1 ILE A 99 -23.57 -38.63
REMARK 500 1 ASP A 112 68.23 -170.82
REMARK 500 1 ASP A 116 -93.50 -140.92
REMARK 500 1 VAL A 120 66.21 -150.78
REMARK 500 1 TYR A 145 -33.37 -133.23
REMARK 500 1 GLN B 62 -170.69 55.71
REMARK 500 2 LEU A 3 -19.95 -50.00
REMARK 500 2 ASP A 16 100.51 -176.39
REMARK 500 2 CYS A 21 62.58 -151.03
REMARK 500 2 PRO A 40 179.24 -46.15
REMARK 500 2 PRO A 44 -9.78 -45.59
REMARK 500 2 TYR A 45 10.70 -68.50
REMARK 500 2 TYR A 60 149.76 72.05
REMARK 500 2 PRO A 61 -24.26 -37.25
REMARK 500 2 PHE A 62 -15.01 -45.78
REMARK 500 2 TYR A 74 31.82 -94.79
REMARK 500 2 PRO A 76 178.23 -43.79
REMARK 500 2 ASN A 77 -3.06 62.11
REMARK 500 2 ASN A 79 -158.24 -98.11
REMARK 500 2 ARG A 90 -165.19 -74.75
REMARK 500 2 SER A 91 -30.39 -37.31
REMARK 500 2 GLN A 92 29.01 -71.93
REMARK 500 2 ILE A 99 -3.27 -55.39
REMARK 500 2 PRO A 113 -156.73 -53.67
REMARK 500 2 ASN A 114 72.16 -166.38
REMARK 500 2 LEU A 119 -9.36 67.86
REMARK 500 2 ALA A 146 -2.79 -164.05
REMARK 500 2 ASP B 39 -7.92 -54.81
REMARK 500 2 ALA B 46 29.14 47.31
REMARK 500 2 ASN B 60 -79.42 61.28
REMARK 500 2 ILE B 61 98.80 50.57
REMARK 500 2 ARG B 74 102.41 -44.06
REMARK 500 3 ASP A 28 71.25 54.81
REMARK 500
REMARK 500 THIS ENTRY HAS 203 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2FUH A 2 147 UNP P61077 UB2D3_HUMAN 2 147
DBREF 2FUH B 1 76 UNP P62988 UBIQ_HUMAN 1 76
SEQRES 1 A 146 ALA LEU LYS ARG ILE ASN LYS GLU LEU SER ASP LEU ALA
SEQRES 2 A 146 ARG ASP PRO PRO ALA GLN CYS SER ALA GLY PRO VAL GLY
SEQRES 3 A 146 ASP ASP MET PHE HIS TRP GLN ALA THR ILE MET GLY PRO
SEQRES 4 A 146 ASN ASP SER PRO TYR GLN GLY GLY VAL PHE PHE LEU THR
SEQRES 5 A 146 ILE HIS PHE PRO THR ASP TYR PRO PHE LYS PRO PRO LYS
SEQRES 6 A 146 VAL ALA PHE THR THR ARG ILE TYR HIS PRO ASN ILE ASN
SEQRES 7 A 146 SER ASN GLY SER ILE CYS LEU ASP ILE LEU ARG SER GLN
SEQRES 8 A 146 TRP SER PRO ALA LEU THR ILE SER LYS VAL LEU LEU SER
SEQRES 9 A 146 ILE CYS SER LEU LEU CYS ASP PRO ASN PRO ASP ASP PRO
SEQRES 10 A 146 LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS THR ASP ARG
SEQRES 11 A 146 ASP LYS TYR ASN ARG ILE SER ARG GLU TRP THR GLN LYS
SEQRES 12 A 146 TYR ALA MET
SEQRES 1 B 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 B 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 B 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 B 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 B 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 B 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
HELIX 1 1 ALA A 2 ASP A 16 1 15
HELIX 2 2 LEU A 86 ARG A 90 5 5
HELIX 3 3 THR A 98 CYS A 111 1 14
HELIX 4 4 VAL A 120 THR A 129 1 10
HELIX 5 5 ASP A 130 ALA A 146 1 17
HELIX 6 6 THR B 22 GLY B 35 1 14
HELIX 7 7 THR B 55 ASN B 60 1 6
SHEET 1 A 4 ALA A 23 PRO A 25 0
SHEET 2 A 4 TRP A 33 MET A 38 -1 O GLN A 34 N GLY A 24
SHEET 3 A 4 VAL A 49 HIS A 55 -1 O PHE A 50 N ILE A 37
SHEET 4 A 4 LYS A 66 VAL A 67 -1 O LYS A 66 N HIS A 55
SHEET 1 B 4 THR B 12 GLU B 16 0
SHEET 2 B 4 GLN B 2 LYS B 6 -1 N ILE B 3 O LEU B 15
SHEET 3 B 4 THR B 66 LEU B 69 1 O LEU B 69 N LYS B 6
SHEET 4 B 4 LEU B 43 ILE B 44 -1 N ILE B 44 O HIS B 68
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