Header list of 1xc5.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION COREPRESSOR 01-SEP-04 1XC5 TITLE SOLUTION STRUCTURE OF THE SMRT DEACETYLASE ACTIVATION DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: NUCLEAR RECEPTOR COREPRESSOR 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DEACETYLASE ACTIVATION DOMAIN (RESIDUES 410-480); COMPND 5 SYNONYM: SMRT, N-COR2, SILENCING MEDIATOR OF RETINOIC ACID AND COMPND 6 THYROID HORMONE RECEPTOR, SMRTE, THYROID-, RETINOIC-ACID-RECEPTOR- COMPND 7 ASSOCIATED COREPRESSOR, T3 RECEPTOR- ASSOCIATING FACTOR, TRAC, CTG COMPND 8 REPEAT PROTEIN 26, SMAP270; COMPND 9 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 BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1 KEYWDS FOUR-HELIX STRUCTURE, THREE-HELIX TRIANGLE, TRANSCRIPTION COREPRESSOR EXPDTA SOLUTION NMR NUMMDL 28 AUTHOR A.CODINA,J.D.LOVE,Y.LI,M.A.LAZAR,D.NEUHAUS,J.W.R.SCHWABE REVDAT 3 02-MAR-22 1XC5 1 REMARK SEQADV REVDAT 2 24-FEB-09 1XC5 1 VERSN REVDAT 1 03-MAY-05 1XC5 0 JRNL AUTH A.CODINA,J.D.LOVE,Y.LI,M.A.LAZAR,D.NEUHAUS,J.W.R.SCHWABE JRNL TITL STRUCTURAL INSIGHTS INTO THE INTERACTION AND ACTIVATION OF JRNL TITL 2 HISTONE DEACETYLASE 3 BY NUCLEAR RECEPTOR COREPRESSORS JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 6009 2005 JRNL REFN ISSN 0027-8424 JRNL PMID 15837933 JRNL DOI 10.1073/PNAS.0500299102 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR, CNS 1.1 REMARK 3 AUTHORS : BRUKER GMBH, KARLSRUHE, GERMANY (XWINNMR), REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI, REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SUPPLIED WITH THE PROGRAM CNS REMARK 4 REMARK 4 1XC5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-SEP-04. REMARK 100 THE DEPOSITION ID IS D_1000030191. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 290 REMARK 210 PH : 6.8 REMARK 210 IONIC STRENGTH : 0.35 M REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1-2MM DAD, 50MM NACL, 50MM REMARK 210 PHOSPHATE BUFFER NA; 1-2MM DAD, REMARK 210 50MM NACL, 50MM PHOSPHATE BUFFER REMARK 210 NA; 1-2MM DAD U-15N, 50MM NACL, REMARK 210 50MM PHOSPHATE BUFFER NA REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; DQ-CORRELATION; 2D REMARK 210 TOCSY; 2D NOESY; 3D_15N- REMARK 210 SEPARATED_TOCSY; 3D_15N- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; DMX; DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 02/2000, SPARKY 3.106, REMARK 210 CNS 1.1 REMARK 210 METHOD USED : SIMULATED ANNEALING PROTOCOL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 28 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: THIS STRUCTURE WAS DETERMINED USING A COMBINATION OF REMARK 210 STANDARD 2D HOMONUCLEAR TECHNIQUES AND 3D 15N TOCSY-HSQC AND 15N REMARK 210 NOESY-HSQC 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 1-28 REMARK 465 RES C SSSEQI REMARK 465 GLY A 410 REMARK 465 SER A 411 REMARK 465 MET A 412 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 O LEU A 458 H LYS A 461 1.55 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 LEU A 415 -65.92 -131.81 REMARK 500 1 ALA A 417 85.75 -174.99 REMARK 500 1 MET A 420 -84.88 -134.25 REMARK 500 1 LYS A 421 94.63 -48.02 REMARK 500 1 VAL A 422 -42.70 178.36 REMARK 500 1 MET A 431 87.84 171.06 REMARK 500 1 HIS A 447 78.80 -105.72 REMARK 500 1 LYS A 449 79.91 43.78 REMARK 500 1 ASN A 450 -50.32 -126.43 REMARK 500 1 LEU A 458 41.87 -106.53 REMARK 500 1 GLU A 459 -65.00 0.21 REMARK 500 1 LYS A 475 34.37 -98.23 REMARK 500 1 ASN A 476 -29.95 -177.66 REMARK 500 1 TYR A 479 36.93 -97.57 REMARK 500 2 LEU A 415 -66.70 -109.11 REMARK 500 2 MET A 416 -177.38 60.10 REMARK 500 2 MET A 420 -83.14 -130.72 REMARK 500 2 LYS A 421 103.92 -47.27 REMARK 500 2 VAL A 422 -44.35 175.93 REMARK 500 2 ASP A 425 36.93 -152.68 REMARK 500 2 MET A 431 78.40 167.37 REMARK 500 2 HIS A 447 79.53 -105.27 REMARK 500 2 PRO A 448 108.86 -38.43 REMARK 500 2 LYS A 449 84.03 43.90 REMARK 500 2 ASN A 450 -50.92 -128.39 REMARK 500 2 GLU A 459 -59.25 -5.35 REMARK 500 2 ASN A 478 128.73 63.79 REMARK 500 2 TYR A 479 134.33 -176.92 REMARK 500 3 LEU A 415 87.52 -152.68 REMARK 500 3 ASP A 418 87.43 -175.01 REMARK 500 3 MET A 420 -84.21 -127.54 REMARK 500 3 LYS A 421 99.41 -48.63 REMARK 500 3 VAL A 422 -46.26 178.41 REMARK 500 3 TYR A 423 -32.86 -37.44 REMARK 500 3 GLN A 427 31.86 -96.99 REMARK 500 3 MET A 431 86.96 170.04 REMARK 500 3 LYS A 449 -7.40 79.48 REMARK 500 3 ASN A 450 -84.10 -73.50 REMARK 500 3 PHE A 451 -7.36 77.55 REMARK 500 3 GLU A 459 -41.25 -28.94 REMARK 500 3 ASN A 478 78.78 60.22 REMARK 500 4 MET A 416 171.75 60.61 REMARK 500 4 ALA A 417 -171.28 -60.22 REMARK 500 4 ASP A 418 -54.11 177.51 REMARK 500 4 MET A 420 -86.55 -127.15 REMARK 500 4 LYS A 421 91.63 -52.28 REMARK 500 4 VAL A 422 -42.80 -178.14 REMARK 500 4 GLN A 427 32.93 -97.92 REMARK 500 4 MET A 431 87.59 171.88 REMARK 500 4 PRO A 448 100.11 -42.94 REMARK 500 REMARK 500 THIS ENTRY HAS 378 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6286 RELATED DB: BMRB REMARK 900 1H AND 15N CHEMICAL SHIFT ASSIGNMENT DBREF 1XC5 A 412 480 UNP Q9Y618 NCOR2_HUMAN 412 480 SEQADV 1XC5 GLY A 410 UNP Q9Y618 CLONING ARTIFACT SEQADV 1XC5 SER A 411 UNP Q9Y618 CLONING ARTIFACT SEQRES 1 A 71 GLY SER MET ASN GLY LEU MET ALA ASP PRO MET LYS VAL SEQRES 2 A 71 TYR LYS ASP ARG GLN VAL MET ASN MET TRP SER GLU GLN SEQRES 3 A 71 GLU LYS GLU THR PHE ARG GLU LYS PHE MET GLN HIS PRO SEQRES 4 A 71 LYS ASN PHE GLY LEU ILE ALA SER PHE LEU GLU ARG LYS SEQRES 5 A 71 THR VAL ALA GLU CYS VAL LEU TYR TYR TYR LEU THR LYS SEQRES 6 A 71 LYS ASN GLU ASN TYR LYS HELIX 1 1 GLU A 436 HIS A 447 1 12 HELIX 2 2 LEU A 453 LEU A 458 1 6 HELIX 3 3 THR A 462 LYS A 474 1 13 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