Header list of 2asq.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN BINDING 23-AUG-05 2ASQ
TITLE SOLUTION STRUCTURE OF SUMO-1 IN COMPLEX WITH A SUMO-BINDING MOTIF
TITLE 2 (SBM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SMALL UBIQUITIN-RELATED MODIFIER 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: STRUCTURED REGION OF SUMO-1 (RESIDUES 21-97);
COMPND 5 SYNONYM: SUMO-1, UBIQUITIN-LIKE PROTEIN SMT3C, SMT3 HOMOLOG 3,
COMPND 6 UBIQUITIN-HOMOLOGY DOMAIN PROTEIN PIC1, UBIQUITIN-LIKE PROTEIN UBL1,
COMPND 7 GAP MODIFYING PROTEIN 1, GMP1, SENTRIN;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PROTEIN INHIBITOR OF ACTIVATED STAT2;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: SUMO-BINDING MOTIF IN PIASX;
COMPND 13 SYNONYM: PROTEIN INHIBITOR OF ACTIVATED STAT X, MSX-INTERACTING ZINC
COMPND 14 FINGER PROTEIN, MIZ1, DAB2-INTERACTING PROTEIN, DIP, ANDROGEN
COMPND 15 RECEPTOR-INTERACTING PROTEIN 3, ARIP3, PIAS-NY PROTEIN;
COMPND 16 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: SUMO1, SMT3C, SMT3H3, UBL1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)(NOVAGEN);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A+ (NOVAGEN);
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: PIAS2, PIASX;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BLR(DE3)PLYSS (NOVAGEN);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET31A+
KEYWDS PROTEIN-PEPTIDE COMPLEX, SUMO-1, SMALL UBIQUITIN-LIKE MODIFIER 1,
KEYWDS 2 SUMO-BINDING MOTIF, SBM, PROTEIN INHIBITOR OF ACTIVATED STAT, PIASX,
KEYWDS 3 PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR J.SONG,Z.ZHANG,W.HU,Y.CHEN
REVDAT 5 09-MAR-22 2ASQ 1 REMARK SEQADV
REVDAT 4 24-FEB-09 2ASQ 1 VERSN
REVDAT 3 06-DEC-05 2ASQ 1 JRNL
REVDAT 2 22-NOV-05 2ASQ 1 JRNL
REVDAT 1 11-OCT-05 2ASQ 0
JRNL AUTH J.SONG,Z.ZHANG,W.HU,Y.CHEN
JRNL TITL SMALL UBIQUITIN-LIKE MODIFIER (SUMO) RECOGNITION OF A SUMO
JRNL TITL 2 BINDING MOTIF: A REVERSAL OF THE BOUND ORIENTATION
JRNL REF J.BIOL.CHEM. V. 280 40122 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 16204249
JRNL DOI 10.1074/JBC.M507059200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.1, HADDOCK 1.3
REMARK 3 AUTHORS : BRUKER (XWINNMR), BONVIN, ALEXANDRE (HADDOCK)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ASQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034269.
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 : 1 MM 15N,13C-ENRICHED PIASX-P
REMARK 210 PEPTIDE AND UNLABELED SUMO-1;
REMARK 210 20MM PHOSPHATE BUFFER PH6.8; 92%
REMARK 210 H2O, 8% D2O, 17OC; 1 MM 15N,13C-
REMARK 210 ENRICHED SUMO-1 AND UNLABELED
REMARK 210 PIASX-P PEPTIDE; 20MM PHOSPHATE
REMARK 210 BUFFER PH6.8; 92% H2O, 8% D2O,
REMARK 210 17OC
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; HNCA-J;
REMARK 210 HCCH-TOCSY; CC(CO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.1, FELIX 2000, NMRVIEW
REMARK 210 5
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 : 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 ASP A 3
REMARK 465 GLN A 4
REMARK 465 GLU A 5
REMARK 465 ALA A 6
REMARK 465 LYS A 7
REMARK 465 PRO A 8
REMARK 465 SER A 9
REMARK 465 THR A 10
REMARK 465 GLU A 11
REMARK 465 ASP A 12
REMARK 465 LEU A 13
REMARK 465 GLY A 14
REMARK 465 ASP A 15
REMARK 465 LYS A 16
REMARK 465 LYS A 17
REMARK 465 GLU A 18
REMARK 465 GLY A 19
REMARK 465 GLU A 20
REMARK 465 GLU B 15
REMARK 465 GLU B 16
REMARK 465 GLU B 17
REMARK 465 ASP B 18
REMARK 465 PRO B 19
REMARK 465 PRO B 20
REMARK 465 ALA B 21
REMARK 465 LYS B 22
REMARK 465 ARG B 23
REMARK 465 GLN B 24
REMARK 465 MET B 25
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 HZ2 LYS A 48 OD1 ASP A 73 1.56
REMARK 500 HZ2 LYS A 23 OE2 GLU A 84 1.58
REMARK 500 HZ2 LYS A 25 OE1 GLU A 33 1.59
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 THR A 41 -20.53 154.31
REMARK 500 1 ASN A 60 -0.85 75.70
REMARK 500 1 ASN A 74 34.24 -86.99
REMARK 500 1 LEU A 80 -47.29 73.62
REMARK 500 1 ILE B 9 94.04 -67.55
REMARK 500 1 GLU B 10 -63.50 -156.24
REMARK 500 2 THR A 41 -46.32 -163.74
REMARK 500 2 LEU A 80 -36.24 72.72
REMARK 500 2 SER B 11 -57.30 -141.29
REMARK 500 2 SER B 12 -86.73 -166.75
REMARK 500 2 SER B 13 50.59 -94.48
REMARK 500 3 THR A 41 -60.31 -166.80
REMARK 500 3 ASN A 60 -0.19 78.96
REMARK 500 3 LEU A 80 -29.96 72.04
REMARK 500 3 GLU A 83 -169.06 -125.37
REMARK 500 4 THR A 41 -36.48 168.52
REMARK 500 4 LEU A 80 -9.37 70.13
REMARK 500 5 THR A 41 -51.59 -164.88
REMARK 500 5 ASN A 60 -12.09 78.53
REMARK 500 5 LEU A 80 -29.54 73.05
REMARK 500 6 THR A 41 -55.82 -166.30
REMARK 500 6 LEU A 80 -54.75 72.07
REMARK 500 6 GLU A 83 -168.74 -124.79
REMARK 500 6 GLU B 10 -67.43 -144.24
REMARK 500 6 SER B 12 108.22 -55.37
REMARK 500 6 SER B 13 -23.62 -165.53
REMARK 500 7 MET A 40 86.20 -69.39
REMARK 500 7 THR A 41 -52.32 -164.53
REMARK 500 7 ASN A 60 -18.36 -170.10
REMARK 500 7 LEU A 80 -1.13 68.68
REMARK 500 8 THR A 41 -46.90 -167.74
REMARK 500 8 LEU A 80 -49.94 73.92
REMARK 500 8 SER B 11 -54.71 -132.61
REMARK 500 9 THR A 41 -59.42 -165.04
REMARK 500 9 ASN A 60 -16.12 -156.87
REMARK 500 9 LEU A 80 -3.23 73.13
REMARK 500 10 THR A 41 -44.62 -170.45
REMARK 500 10 LEU A 80 -42.56 73.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Z5S RELATED DB: PDB
REMARK 900 ANOTHER EXAMPLE OF SUMO-1 IN COMPLEX WITH THE SUMO-BINDING MOTIF.
REMARK 900 RELATED ID: 1WYW RELATED DB: PDB
REMARK 900 ANOTHER EXAMPLE OF SUMO-1 IN COMPLEX WITH THE SUMO-BINDING MOTIF.
DBREF 2ASQ A 1 97 UNP P63165 SUMO1_HUMAN 1 97
DBREF 2ASQ B 1 23 UNP O75928 PIAS2_HUMAN 466 488
SEQADV 2ASQ GLN B 24 UNP O75928 CLONING ARTIFACT
SEQADV 2ASQ MET B 25 UNP O75928 CLONING ARTIFACT
SEQRES 1 A 97 MET SER ASP GLN GLU ALA LYS PRO SER THR GLU ASP LEU
SEQRES 2 A 97 GLY ASP LYS LYS GLU GLY GLU TYR ILE LYS LEU LYS VAL
SEQRES 3 A 97 ILE GLY GLN ASP SER SER GLU ILE HIS PHE LYS VAL LYS
SEQRES 4 A 97 MET THR THR HIS LEU LYS LYS LEU LYS GLU SER TYR CYS
SEQRES 5 A 97 GLN ARG GLN GLY VAL PRO MET ASN SER LEU ARG PHE LEU
SEQRES 6 A 97 PHE GLU GLY GLN ARG ILE ALA ASP ASN HIS THR PRO LYS
SEQRES 7 A 97 GLU LEU GLY MET GLU GLU GLU ASP VAL ILE GLU VAL TYR
SEQRES 8 A 97 GLN GLU GLN THR GLY GLY
SEQRES 1 B 25 LYS VAL ASP VAL ILE ASP LEU THR ILE GLU SER SER SER
SEQRES 2 B 25 ASP GLU GLU GLU ASP PRO PRO ALA LYS ARG GLN MET
HELIX 1 1 HIS A 43 GLY A 56 1 14
SHEET 1 A 6 GLN A 69 ARG A 70 0
SHEET 2 A 6 LEU A 62 PHE A 66 -1 N PHE A 66 O GLN A 69
SHEET 3 A 6 ASP A 86 GLN A 92 -1 O TYR A 91 N ARG A 63
SHEET 4 A 6 ILE A 22 GLY A 28 1 N LYS A 25 O ILE A 88
SHEET 5 A 6 SER A 32 VAL A 38 -1 O VAL A 38 N ILE A 22
SHEET 6 A 6 VAL B 4 ASP B 6 1 O ILE B 5 N HIS A 35
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