Header list of 1uel.pdb file
Complete list - r 2 2 Bytes
HEADER GENE REGULATION/PROTEIN BINDING 19-MAY-03 1UEL
TITLE SOLUTION STRUCTURE OF UBIQUITIN-LIKE DOMAIN OF HHR23B COMPLEXED WITH
TITLE 2 UBIQUITIN-INTERACTING MOTIF OF PROTEASOME SUBUNIT S5A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UV EXCISION REPAIR PROTEIN RAD23 HOMOLOG B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UBIQUITIN-LIKE DOMAIN (RESIDUES 1-95);
COMPND 5 SYNONYM: HHR23B;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 4;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UBIQUITIN-INTERACTING MOTIF (RESIDUES 201-248);
COMPND 11 SYNONYM: S5A, 26S PROTEASOME REGULATORY SUBUNIT S5A;
COMPND 12 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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET24D;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET11D
KEYWDS UBL, UIM, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 2 STRUCTURAL GENOMICS, GENE REGULATION-PROTEIN BINDING COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.FUJIWARA,T.TENNO,J.G.JEE,K.SUGASAWA,I.OHKI,C.KOJIMA,H.TOCHIO,
AUTHOR 2 H.HIROAKI,H.HANAOKA,M.SHIRAKAWA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 3 INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1UEL 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1UEL 1 VERSN
REVDAT 1 10-FEB-04 1UEL 0
JRNL AUTH K.FUJIWARA,T.TENNO,K.SUGASAWA,J.G.JEE,I.OHKI,C.KOJIMA,
JRNL AUTH 2 H.TOCHIO,H.HIROAKI,F.HANAOKA,M.SHIRAKAWA
JRNL TITL STRUCTURE OF THE UBIQUITIN-INTERACTING MOTIF OF S5A BOUND TO
JRNL TITL 2 THE UBIQUITIN-LIKE DOMAIN OF HR23B
JRNL REF J.BIOL.CHEM. V. 279 4760 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14585839
JRNL DOI 10.1074/JBC.M309448200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER 7
REMARK 3 AUTHORS :
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 RESIDUES INCLUDING MET1 THROUGH THR75 OF HHR23B AND
REMARK 3 LEU278 THROUGH GLN 296 OF S5A ARE ORDERED IN SOLUTION,
REMARK 3 WHILE THE REST IS HIGHLY FLEXIBLE
REMARK 3 (BASED ON 1H-15N HETERONUCLEAR NOE ANALYSIS).
REMARK 4
REMARK 4 1UEL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000005736.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : U-15N, U-13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING PROCEDURE IN
REMARK 210 CNS AND FURTHER REFINED BY AMBER
REMARK 210 7
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 20 STRUCTURES WITH THE
REMARK 210 LOWEST
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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: 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 15 ARG B 272 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
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 LYS A 76 -96.08 52.73
REMARK 500 1 PRO A 85 93.60 -55.74
REMARK 500 1 HIS A 90 -43.05 -135.13
REMARK 500 1 HIS A 91 22.75 45.41
REMARK 500 1 THR B 264 -11.59 54.41
REMARK 500 1 LEU B 278 -8.66 68.79
REMARK 500 1 ALA B 298 1.82 -68.89
REMARK 500 1 GLU B 299 17.74 86.09
REMARK 500 1 SER B 305 94.01 -68.32
REMARK 500 2 LYS A 76 80.01 23.84
REMARK 500 2 VAL A 80 56.58 39.16
REMARK 500 2 ALA A 84 -66.62 -147.65
REMARK 500 2 ALA B 298 -131.50 -100.20
REMARK 500 2 SER B 305 0.79 58.60
REMARK 500 3 ALA A 84 73.80 -119.58
REMARK 500 3 HIS B 262 -35.38 49.55
REMARK 500 3 ASP B 277 49.78 -82.93
REMARK 500 3 LEU B 278 -5.18 61.75
REMARK 500 3 ALA B 298 -73.56 -85.56
REMARK 500 4 THR A 22 174.03 82.17
REMARK 500 4 ALA A 79 -158.50 47.93
REMARK 500 4 ALA A 86 99.36 -68.94
REMARK 500 4 LEU A 88 14.63 55.84
REMARK 500 4 HIS A 92 0.55 -69.01
REMARK 500 4 THR B 273 -63.51 -127.95
REMARK 500 4 ASP B 277 45.77 -79.23
REMARK 500 4 ALA B 298 20.07 -74.89
REMARK 500 5 ALA A 49 25.74 49.87
REMARK 500 5 LYS A 76 -37.20 -131.91
REMARK 500 5 PRO A 77 170.52 -57.70
REMARK 500 5 LYS A 78 7.53 47.46
REMARK 500 5 PRO A 83 40.35 -77.00
REMARK 500 5 ALA A 86 -62.07 -143.28
REMARK 500 5 HIS A 93 -56.98 50.33
REMARK 500 5 HIS A 94 90.91 -68.17
REMARK 500 5 SER B 266 -159.74 -134.79
REMARK 500 5 GLN B 268 -49.14 62.56
REMARK 500 5 PRO B 276 171.75 -56.58
REMARK 500 5 ALA B 298 30.76 -74.24
REMARK 500 5 PHE B 300 6.01 59.83
REMARK 500 6 THR A 22 174.14 87.02
REMARK 500 6 VAL A 80 -12.64 49.35
REMARK 500 6 PRO A 85 97.94 -68.86
REMARK 500 6 ALA A 86 -173.19 54.89
REMARK 500 6 THR B 273 -66.10 -130.40
REMARK 500 6 LEU B 278 -10.86 62.89
REMARK 500 6 PHE B 300 19.47 51.59
REMARK 500 7 ALA A 49 25.45 49.97
REMARK 500 7 VAL A 80 87.94 65.10
REMARK 500 7 HIS A 90 168.09 61.74
REMARK 500
REMARK 500 THIS ENTRY HAS 149 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TRT001000364.1 RELATED DB: TARGETDB
DBREF 1UEL A 1 87 UNP P54727 RD23B_HUMAN 1 87
DBREF 1UEL B 263 307 UNP P55036 PSD4_HUMAN 263 307
SEQADV 1UEL LEU A 88 UNP P54727 EXPRESSION TAG
SEQADV 1UEL GLU A 89 UNP P54727 EXPRESSION TAG
SEQADV 1UEL HIS A 90 UNP P54727 EXPRESSION TAG
SEQADV 1UEL HIS A 91 UNP P54727 EXPRESSION TAG
SEQADV 1UEL HIS A 92 UNP P54727 EXPRESSION TAG
SEQADV 1UEL HIS A 93 UNP P54727 EXPRESSION TAG
SEQADV 1UEL HIS A 94 UNP P54727 EXPRESSION TAG
SEQADV 1UEL HIS A 95 UNP P54727 EXPRESSION TAG
SEQADV 1UEL GLY B 260 UNP P55036 CLONING ARTIFACT
SEQADV 1UEL SER B 261 UNP P55036 CLONING ARTIFACT
SEQADV 1UEL HIS B 262 UNP P55036 CLONING ARTIFACT
SEQRES 1 A 95 MET GLN VAL THR LEU LYS THR LEU GLN GLN GLN THR PHE
SEQRES 2 A 95 LYS ILE ASP ILE ASP PRO GLU GLU THR VAL LYS ALA LEU
SEQRES 3 A 95 LYS GLU LYS ILE GLU SER GLU LYS GLY LYS ASP ALA PHE
SEQRES 4 A 95 PRO VAL ALA GLY GLN LYS LEU ILE TYR ALA GLY LYS ILE
SEQRES 5 A 95 LEU ASN ASP ASP THR ALA LEU LYS GLU TYR LYS ILE ASP
SEQRES 6 A 95 GLU LYS ASN PHE VAL VAL VAL MET VAL THR LYS PRO LYS
SEQRES 7 A 95 ALA VAL SER THR PRO ALA PRO ALA THR LEU GLU HIS HIS
SEQRES 8 A 95 HIS HIS HIS HIS
SEQRES 1 B 48 GLY SER HIS MET THR ILE SER GLN GLN GLU PHE GLY ARG
SEQRES 2 B 48 THR GLY LEU PRO ASP LEU SER SER MET THR GLU GLU GLU
SEQRES 3 B 48 GLN ILE ALA TYR ALA MET GLN MET SER LEU GLN GLY ALA
SEQRES 4 B 48 GLU PHE GLY GLN ALA GLU SER ALA ASP
HELIX 1 1 THR A 22 GLY A 35 1 14
HELIX 2 2 ALA A 58 LYS A 63 5 6
HELIX 3 3 PRO A 85 HIS A 90 5 6
HELIX 4 4 THR B 282 ALA B 298 1 17
SHEET 1 A 5 THR A 12 ASP A 16 0
SHEET 2 A 5 GLN A 2 THR A 7 -1 N VAL A 3 O ILE A 15
SHEET 3 A 5 PHE A 69 VAL A 74 1 O VAL A 70 N THR A 4
SHEET 4 A 5 GLN A 44 TYR A 48 -1 N ILE A 47 O VAL A 71
SHEET 5 A 5 LYS A 51 ILE A 52 -1 O LYS A 51 N TYR A 48
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