Header list of 1xwh.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION 01-NOV-04 1XWH TITLE NMR STRUCTURE OF THE FIRST PHD FINGER OF AUTOIMMUNE REGULATOR PROTEIN TITLE 2 (AIRE1): INSIGHTS INTO APECED COMPND MOL_ID: 1; COMPND 2 MOLECULE: AUTOIMMUNE REGULATOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FIRST PHDDOMAIN; COMPND 5 SYNONYM: AUTOIMMUNE POLYENDOCRINOPATHY CANDIDIASIS ECTODERMAL COMPND 6 DYSTROPHY PROTEIN, APECED PROTEIN; COMPND 7 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: AIRE1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24D KEYWDS PHD DOMAIN, ZN BINDING DOMAIN, APECED, NUCLEOSOME, E3 LIGASE, KEYWDS 2 TRANSCRIPTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.J.BOTTOMLEY,G.STIER,J.KRASOTKINA,G.LEGUBE,B.SIMON,A.AKHTAR, AUTHOR 2 M.SATTLER,G.MUSCO REVDAT 4 02-MAR-22 1XWH 1 REMARK SEQADV LINK REVDAT 3 24-FEB-09 1XWH 1 VERSN REVDAT 2 26-APR-05 1XWH 1 JRNL REVDAT 1 25-JAN-05 1XWH 0 JRNL AUTH M.J.BOTTOMLEY,G.STIER,D.PENNACCHINI,G.LEGUBE,B.SIMON, JRNL AUTH 2 A.AKHTAR,M.SATTLER,G.MUSCO JRNL TITL NMR STRUCTURE OF THE FIRST PHD FINGER OF AUTOIMMUNE JRNL TITL 2 REGULATOR PROTEIN (AIRE1). INSIGHTS INTO AUTOIMMUNE JRNL TITL 3 POLYENDOCRINOPATHY-CANDIDIASIS-ECTODERMAL DYSTROPHY (APECED) JRNL TITL 4 DISEASE JRNL REF J.BIOL.CHEM. V. 280 11505 2005 JRNL REFN ISSN 0021-9258 JRNL PMID 15649886 JRNL DOI 10.1074/JBC.M413959200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 3.0, CNS 1.0 REMARK 3 AUTHORS : DELAGLIO ET AL. (NMRPIPE), 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: THE AIRE1-PHD1 SOLUTION STRUCTURE WAS REMARK 3 DETERMINED FROM A TOTAL OF 970 NMR-DERIVED DISTANCE AND 66 REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 44 RESIDUAL DIPOLAR REMARK 4 REMARK 4 1XWH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-NOV-04. REMARK 100 THE DEPOSITION ID IS D_1000030846. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 295 REMARK 210 PH : 6.3 REMARK 210 IONIC STRENGTH : 150MM NACL, 20MM PHOSPHATE REMARK 210 BUFFER REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM AIRE1-PHD1, U-15N,13C; 20MM REMARK 210 PHOSPHATE BUFFER, PH 6.3, 150MM REMARK 210 NACL, 5MM DTT REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : ARIA ARIA1.2, XEASY 1.2 REMARK 210 METHOD USED : STRUCTURES WERE CALCULATED USING REMARK 210 ARIA (1.2) IN COMBINATION WITH REMARK 210 CNS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 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: THE FIRST 4 AMINO ACIDS (GAMA) DO NOT BELONG TO AIRE1 REMARK 210 SEQUENCE. 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 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 ALA A 290 -179.41 59.86 REMARK 500 1 ALA A 292 63.73 -150.94 REMARK 500 1 ASP A 312 -75.18 -52.62 REMARK 500 2 ALA A 290 -65.95 -166.69 REMARK 500 2 ASP A 297 33.34 -86.68 REMARK 500 2 PRO A 315 2.68 -69.19 REMARK 500 2 PRO A 350 89.61 -67.81 REMARK 500 3 GLN A 293 -73.71 67.59 REMARK 500 3 ASP A 297 33.14 -86.71 REMARK 500 3 ALA A 300 43.96 -69.11 REMARK 500 3 VAL A 301 -67.52 -133.26 REMARK 500 4 ALA A 290 121.04 68.92 REMARK 500 4 ALA A 292 -75.06 -90.23 REMARK 500 4 GLN A 293 -68.54 -137.05 REMARK 500 4 ALA A 352 -75.62 -133.40 REMARK 500 5 ALA A 290 -42.88 70.86 REMARK 500 5 ALA A 292 -40.69 -140.05 REMARK 500 5 ASP A 297 31.77 -87.15 REMARK 500 5 ALA A 300 7.01 -61.82 REMARK 500 5 VAL A 301 -60.26 -96.81 REMARK 500 6 ALA A 290 69.18 -159.28 REMARK 500 6 ALA A 292 -44.27 -133.10 REMARK 500 6 GLN A 293 -68.49 70.90 REMARK 500 6 ALA A 300 42.34 -65.94 REMARK 500 6 VAL A 301 -57.30 -140.95 REMARK 500 6 PRO A 350 32.21 -77.26 REMARK 500 7 ASP A 297 33.83 -84.71 REMARK 500 7 GLN A 346 73.63 -100.20 REMARK 500 7 PRO A 350 96.11 -66.97 REMARK 500 7 ALA A 352 88.05 62.97 REMARK 500 8 ALA A 300 43.42 -63.83 REMARK 500 8 VAL A 301 -53.33 -141.13 REMARK 500 8 ARG A 303 -5.40 71.99 REMARK 500 9 ALA A 300 1.93 -58.92 REMARK 500 9 PRO A 350 106.22 -59.34 REMARK 500 11 ASP A 297 32.31 -98.74 REMARK 500 11 PRO A 350 8.92 -65.42 REMARK 500 11 GLU A 353 -48.52 74.63 REMARK 500 12 GLN A 293 -16.08 74.15 REMARK 500 12 PRO A 315 2.10 -68.69 REMARK 500 12 PRO A 350 3.85 -67.89 REMARK 500 13 GLN A 293 -52.20 70.13 REMARK 500 13 ASP A 297 32.53 -86.30 REMARK 500 13 ALA A 300 38.41 -64.81 REMARK 500 13 VAL A 301 -49.53 -135.72 REMARK 500 13 PRO A 350 49.69 -76.16 REMARK 500 13 ALA A 352 54.32 -115.80 REMARK 500 14 ALA A 292 55.60 -140.60 REMARK 500 14 GLN A 293 -87.20 -91.21 REMARK 500 14 ASP A 297 31.57 -88.10 REMARK 500 REMARK 500 THIS ENTRY HAS 78 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 355 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 299 SG REMARK 620 2 CYS A 302 SG 108.4 REMARK 620 3 HIS A 319 ND1 81.1 79.6 REMARK 620 4 CYS A 322 SG 146.7 104.9 103.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 356 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 311 SG REMARK 620 2 CYS A 314 SG 136.8 REMARK 620 3 CYS A 337 SG 107.3 110.4 REMARK 620 4 CYS A 340 SG 87.0 98.5 110.8 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 355 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 356 DBREF 1XWH A 293 354 UNP O43918 AIRE_HUMAN 293 354 SEQADV 1XWH GLY A 289 UNP O43918 EXPRESSION TAG SEQADV 1XWH ALA A 290 UNP O43918 EXPRESSION TAG SEQADV 1XWH MET A 291 UNP O43918 EXPRESSION TAG SEQADV 1XWH ALA A 292 UNP O43918 EXPRESSION TAG SEQRES 1 A 66 GLY ALA MET ALA GLN LYS ASN GLU ASP GLU CYS ALA VAL SEQRES 2 A 66 CYS ARG ASP GLY GLY GLU LEU ILE CYS CYS ASP GLY CYS SEQRES 3 A 66 PRO ARG ALA PHE HIS LEU ALA CYS LEU SER PRO PRO LEU SEQRES 4 A 66 ARG GLU ILE PRO SER GLY THR TRP ARG CYS SER SER CYS SEQRES 5 A 66 LEU GLN ALA THR VAL GLN GLU VAL GLN PRO ARG ALA GLU SEQRES 6 A 66 GLU HET ZN A 355 1 HET ZN A 356 1 HETNAM ZN ZINC ION FORMUL 2 ZN 2(ZN 2+) HELIX 1 1 CYS A 337 ALA A 343 1 7 SHEET 1 A 2 ILE A 309 CYS A 310 0 SHEET 2 A 2 ALA A 317 PHE A 318 -1 O PHE A 318 N ILE A 309 LINK SG CYS A 299 ZN ZN A 355 1555 1555 2.51 LINK SG CYS A 302 ZN ZN A 355 1555 1555 2.50 LINK SG CYS A 311 ZN ZN A 356 1555 1555 2.43 LINK SG CYS A 314 ZN ZN A 356 1555 1555 2.42 LINK ND1 HIS A 319 ZN ZN A 355 1555 1555 2.45 LINK SG CYS A 322 ZN ZN A 355 1555 1555 2.51 LINK SG CYS A 337 ZN ZN A 356 1555 1555 2.45 LINK SG CYS A 340 ZN ZN A 356 1555 1555 2.44 CISPEP 1 SER A 324 PRO A 325 1 0.19 CISPEP 2 SER A 324 PRO A 325 2 2.20 CISPEP 3 SER A 324 PRO A 325 3 1.08 CISPEP 4 SER A 324 PRO A 325 4 0.86 CISPEP 5 SER A 324 PRO A 325 5 0.10 CISPEP 6 SER A 324 PRO A 325 6 1.29 CISPEP 7 SER A 324 PRO A 325 7 0.85 CISPEP 8 SER A 324 PRO A 325 8 3.47 CISPEP 9 SER A 324 PRO A 325 9 2.57 CISPEP 10 SER A 324 PRO A 325 10 0.30 CISPEP 11 SER A 324 PRO A 325 11 2.16 CISPEP 12 SER A 324 PRO A 325 12 -0.75 CISPEP 13 SER A 324 PRO A 325 13 0.51 CISPEP 14 SER A 324 PRO A 325 14 0.67 CISPEP 15 SER A 324 PRO A 325 15 -0.09 CISPEP 16 SER A 324 PRO A 325 16 1.90 CISPEP 17 SER A 324 PRO A 325 17 2.84 CISPEP 18 SER A 324 PRO A 325 18 1.23 CISPEP 19 SER A 324 PRO A 325 19 2.03 CISPEP 20 SER A 324 PRO A 325 20 -0.88 SITE 1 AC1 5 CYS A 299 VAL A 301 CYS A 302 HIS A 319 SITE 2 AC1 5 CYS A 322 SITE 1 AC2 4 CYS A 311 CYS A 314 CYS A 337 CYS A 340 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