Header list of 2a7o.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION 05-JUL-05 2A7O
TITLE SOLUTION STRUCTURE OF THE HSET2/HYPB SRI DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUNTINGTIN INTERACTING PROTEIN B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SET2 RPB1-INTERACTING (SRI) DOMAIN, HSET2/HYBP SRI DOMAIN,
COMPND 5 RESIDUES 1954-2061;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: ISOFORM 1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HSET2/HYPB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-15B
KEYWDS SRI DOMAIN, SRI, HSRI, SET2, HSET2, PHOSPHOCTD ASSOCIATING PROTEIN,
KEYWDS 2 SET2 RPB1-INTERACTING DOMAIN, PCID, PCAP, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.LI,H.P.PHATNANI,Z.GUAN,H.SAGE,A.GREENLEAF,P.ZHOU
REVDAT 4 09-MAR-22 2A7O 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2A7O 1 VERSN
REVDAT 2 27-DEC-05 2A7O 1 JRNL
REVDAT 1 01-NOV-05 2A7O 0
JRNL AUTH M.LI,H.P.PHATNANI,Z.GUAN,H.SAGE,A.GREENLEAF,P.ZHOU
JRNL TITL SOLUTION STRUCTURE OF THE SET2 RPB1 INTERACTING DOMAIN OF
JRNL TITL 2 HUMAN SET2 AND ITS INTERACTION WITH THE HYPERPHOSPHORYLATED
JRNL TITL 3 C-TERMINAL DOMAIN OF RPB1
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 17636 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 16314571
JRNL DOI 10.1073/PNAS.0506350102
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, XPLOR-NIH 2.9.7
REMARK 3 AUTHORS : C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJANDRA,G.M.CLORE
REMARK 3 (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 STRUCTURES WERE INITIALLY CALCULATED USING DYANA.
REMARK 3
REMARK 3 CYANA 2.0 WAS USED FOR AUTOMATED DATA ANALYSIS TO OBTAIN
REMARK 3 ADDITIONAL NOE CONSTRAINTS. THE STRUCTURES WERE THEN REFINED
REMARK 3 AGAINST RESIDUAL DIPOLAR COUPLINGS USING XPLOR-NIH AND A WATER-
REMARK 3 REFINEMENT PROTOCOL.
REMARK 4
REMARK 4 2A7O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033590.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100 MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : U-15N (RANDOM LABELING) HYPB,
REMARK 210 90% H2O, 10% D2O; U-95% 13C, U-
REMARK 210 98% 15N LABELED HYPB, 90% H2O,
REMARK 210 10% D2O; RESIDUE SELECTIVE
REMARK 210 LABELING WITH 15N-LYSINE HYPB,
REMARK 210 90% H2O, 10% D2O; U-95% 13C, U-
REMARK 210 98% 15N HYPB, 100% D2O;
REMARK 210 UNLABELED HYPB,100% D2O; 10% 13C
REMARK 210 (FRACTIONAL LABELING) HYPB,100%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY; 2D
REMARK 210 TOCSY; HNCA; HN(CO)CA; HN(CA)CB;
REMARK 210 HN(COCA)CB; HNCO; HNCA-J; 4D
REMARK 210 HC(CCO)NH-TOCSY; 15N-HSQC; HIGH-
REMARK 210 RESOLUTION 13C-HSQC; RDC
REMARK 210 EXPERIMENT IN PHAGE
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.2, DYANA 1.5, CYANA 2.0
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND 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 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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 MET A 4
REMARK 465 THR A 5
REMARK 465 ALA A 6
REMARK 465 GLU A 7
REMARK 465 ALA A 8
REMARK 465 ASP A 9
REMARK 465 GLU A 110
REMARK 465 LEU A 111
REMARK 465 GLU A 112
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 59 OD2 ASP A 108 1.59
REMARK 500 OE1 GLU A 68 HZ2 LYS A 87 1.60
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 73 -30.77 71.67
REMARK 500 2 LYS A 73 -43.23 70.29
REMARK 500 2 ASP A 108 -168.90 -79.64
REMARK 500 3 CYS A 72 -50.49 -133.78
REMARK 500 3 LYS A 73 -35.57 73.49
REMARK 500 4 LYS A 73 -50.93 68.70
REMARK 500 5 LYS A 73 -34.97 74.05
REMARK 500 6 LYS A 73 -34.93 71.56
REMARK 500 7 LYS A 73 -34.68 72.64
REMARK 500 8 LYS A 73 -49.99 73.46
REMARK 500 9 ASN A 81 -169.90 -100.82
REMARK 500 10 PRO A 75 11.19 -68.86
REMARK 500 12 LYS A 73 -43.63 73.40
REMARK 500 14 LYS A 73 -0.41 69.05
REMARK 500 14 ASP A 108 -174.84 -66.65
REMARK 500 15 LYS A 73 -47.45 70.16
REMARK 500 16 LYS A 73 -50.86 71.82
REMARK 500 17 LYS A 73 -37.40 68.14
REMARK 500 18 LYS A 73 -51.41 71.40
REMARK 500 19 LYS A 73 -44.43 72.60
REMARK 500 20 LYS A 73 -41.55 73.13
REMARK 500 20 ASP A 108 -169.56 -76.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6834 RELATED DB: BMRB
DBREF 2A7O A 5 112 UNP Q9BYW2 Q9BYW2_HUMAN 1954 2061
SEQADV 2A7O GLY A 1 UNP Q9BYW2 CLONING ARTIFACT
SEQADV 2A7O SER A 2 UNP Q9BYW2 CLONING ARTIFACT
SEQADV 2A7O HIS A 3 UNP Q9BYW2 CLONING ARTIFACT
SEQADV 2A7O MET A 4 UNP Q9BYW2 CLONING ARTIFACT
SEQRES 1 A 112 GLY SER HIS MET THR ALA GLU ALA ASP THR SER SER GLU
SEQRES 2 A 112 LEU ALA LYS LYS SER LYS GLU VAL PHE ARG LYS GLU MET
SEQRES 3 A 112 SER GLN PHE ILE VAL GLN CYS LEU ASN PRO TYR ARG LYS
SEQRES 4 A 112 PRO ASP CYS LYS VAL GLY ARG ILE THR THR THR GLU ASP
SEQRES 5 A 112 PHE LYS HIS LEU ALA ARG LYS LEU THR HIS GLY VAL MET
SEQRES 6 A 112 ASN LYS GLU LEU LYS TYR CYS LYS ASN PRO GLU ASP LEU
SEQRES 7 A 112 GLU CYS ASN GLU ASN VAL LYS HIS LYS THR LYS GLU TYR
SEQRES 8 A 112 ILE LYS LYS TYR MET GLN LYS PHE GLY ALA VAL TYR LYS
SEQRES 9 A 112 PRO LYS GLU ASP THR GLU LEU GLU
HELIX 1 1 THR A 10 ASN A 35 1 26
HELIX 2 2 THR A 49 LYS A 73 1 25
HELIX 3 3 ASN A 74 LEU A 78 5 5
HELIX 4 4 ASN A 81 GLN A 97 1 17
HELIX 5 5 LYS A 104 ASP A 108 5 5
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