Header list of 1owx.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION 31-MAR-03 1OWX
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL RRM OF HUMAN LA (LA225-334)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LUPUS LA PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL RRM;
COMPND 5 SYNONYM: SJOGREN SYNDROME TYPE B ANTIGEN; SS-B; LA AUTOANTIGEN; LA
COMPND 6 RIBONUCLEOPROTEIN; RIBONUCLEOPROTEIN SS-B/LA;
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: SSB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE9
KEYWDS RRM, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.JACKS,J.BABON,G.KELLY,I.MANOLARIDIS,P.D.CARY,S.CURRY,M.R.CONTE
REVDAT 3 23-FEB-22 1OWX 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1OWX 1 VERSN
REVDAT 1 29-JUL-03 1OWX 0
JRNL AUTH A.JACKS,J.BABON,G.KELLY,I.MANOLARIDIS,P.D.CARY,S.CURRY,
JRNL AUTH 2 M.R.CONTE
JRNL TITL STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN LA PROTEIN
JRNL TITL 2 REVEALS A NOVEL RNA RECOGNITION MOTIF COUPLED TO A HELICAL
JRNL TITL 3 NUCLEAR RETENTION ELEMENT
JRNL REF STRUCTURE V. 11 833 2003
JRNL REFN ISSN 0969-2126
JRNL PMID 12842046
JRNL DOI 10.1016/S0969-2126(03)00121-7
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.0, X-PLOR 3.851
REMARK 3 AUTHORS : DELAGLIO ET AL. (NMRPIPE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OWX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018754.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 100 MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7 MM LA U-15N,13C; 20MM TRIS;
REMARK 210 100 MM KCL, 1MM DTT, 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, VNMR 6C
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURE WITH THE LOWEST 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 MET A 214
REMARK 465 ARG A 215
REMARK 465 GLY A 216
REMARK 465 SER A 217
REMARK 465 HIS A 218
REMARK 465 HIS A 219
REMARK 465 HIS A 220
REMARK 465 HIS A 221
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 HA LYS A 287 HD13 LEU A 294 1.34
REMARK 500 O GLU A 307 H GLU A 311 1.51
REMARK 500 O LEU A 294 HA THR A 302 1.55
REMARK 500 O ALA A 279 H LEU A 283 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 HIS A 223 70.16 54.65
REMARK 500 1 GLU A 228 91.50 65.22
REMARK 500 1 THR A 244 156.18 -40.58
REMARK 500 1 HIS A 256 33.50 169.79
REMARK 500 1 GLU A 270 -165.08 -161.68
REMARK 500 1 LYS A 278 115.97 148.71
REMARK 500 1 ALA A 289 -22.53 -39.42
REMARK 500 1 ASN A 290 -86.20 -131.63
REMARK 500 1 LYS A 299 58.39 132.60
REMARK 500 1 GLU A 300 -73.67 -162.26
REMARK 500 1 LEU A 306 -161.34 -74.30
REMARK 500 1 ASN A 327 157.71 56.67
REMARK 500 1 LYS A 330 -69.85 -167.59
REMARK 500 2 HIS A 223 -87.99 -119.36
REMARK 500 2 LEU A 226 -123.18 -130.80
REMARK 500 2 GLU A 228 81.39 50.41
REMARK 500 2 THR A 244 157.88 -41.17
REMARK 500 2 HIS A 256 30.40 -151.45
REMARK 500 2 GLU A 258 155.29 162.88
REMARK 500 2 LYS A 278 116.71 150.00
REMARK 500 2 ALA A 289 -22.45 -39.82
REMARK 500 2 ASN A 290 -86.38 -126.39
REMARK 500 2 LYS A 299 47.19 137.38
REMARK 500 2 GLU A 300 -70.41 -151.03
REMARK 500 2 LEU A 306 -165.64 -72.96
REMARK 500 2 LYS A 328 45.69 -146.04
REMARK 500 2 TRP A 329 75.77 -160.97
REMARK 500 2 LYS A 330 -58.34 -155.04
REMARK 500 2 SER A 331 169.71 61.47
REMARK 500 2 LYS A 332 -38.54 -130.22
REMARK 500 3 LEU A 226 114.77 165.15
REMARK 500 3 LYS A 229 69.36 -166.91
REMARK 500 3 ASP A 239 96.56 -69.74
REMARK 500 3 THR A 244 148.70 -37.65
REMARK 500 3 SER A 254 59.26 -66.90
REMARK 500 3 HIS A 256 26.21 -143.15
REMARK 500 3 GLU A 258 168.23 80.55
REMARK 500 3 LYS A 278 115.17 151.61
REMARK 500 3 ASN A 290 -84.57 -131.78
REMARK 500 3 LYS A 299 40.47 138.45
REMARK 500 3 GLU A 300 -71.82 -145.04
REMARK 500 3 ASN A 327 -161.88 168.15
REMARK 500 3 TRP A 329 133.80 63.22
REMARK 500 3 SER A 331 61.35 60.04
REMARK 500 4 HIS A 223 -150.91 50.94
REMARK 500 4 LEU A 226 17.82 41.90
REMARK 500 4 LYS A 229 79.25 -177.03
REMARK 500 4 THR A 244 154.32 -40.43
REMARK 500 4 SER A 254 67.66 -68.66
REMARK 500 4 ASN A 255 28.67 170.35
REMARK 500
REMARK 500 THIS ENTRY HAS 329 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1OWX A 225 334 UNP P05455 LA_HUMAN 225 334
SEQADV 1OWX MET A 214 UNP P05455 CLONING ARTIFACT
SEQADV 1OWX ARG A 215 UNP P05455 CLONING ARTIFACT
SEQADV 1OWX GLY A 216 UNP P05455 CLONING ARTIFACT
SEQADV 1OWX SER A 217 UNP P05455 CLONING ARTIFACT
SEQADV 1OWX HIS A 218 UNP P05455 CLONING ARTIFACT
SEQADV 1OWX HIS A 219 UNP P05455 CLONING ARTIFACT
SEQADV 1OWX HIS A 220 UNP P05455 CLONING ARTIFACT
SEQADV 1OWX HIS A 221 UNP P05455 CLONING ARTIFACT
SEQADV 1OWX HIS A 222 UNP P05455 CLONING ARTIFACT
SEQADV 1OWX HIS A 223 UNP P05455 CLONING ARTIFACT
SEQADV 1OWX GLY A 224 UNP P05455 CLONING ARTIFACT
SEQADV 1OWX GLU A 258 UNP P05455 CLONING ARTIFACT
SEQRES 1 A 121 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER LEU
SEQRES 2 A 121 GLU GLU LYS ILE GLY CYS LEU LEU LYS PHE SER GLY ASP
SEQRES 3 A 121 LEU ASP ASP GLN THR CYS ARG GLU ASP LEU HIS ILE LEU
SEQRES 4 A 121 PHE SER ASN HIS GLY GLU ILE LYS TRP ILE ASP PHE VAL
SEQRES 5 A 121 ARG GLY ALA LYS GLU GLY ILE ILE LEU PHE LYS GLU LYS
SEQRES 6 A 121 ALA LYS GLU ALA LEU GLY LYS ALA LYS ASP ALA ASN ASN
SEQRES 7 A 121 GLY ASN LEU GLN LEU ARG ASN LYS GLU VAL THR TRP GLU
SEQRES 8 A 121 VAL LEU GLU GLY GLU VAL GLU LYS GLU ALA LEU LYS LYS
SEQRES 9 A 121 ILE ILE GLU ASP GLN GLN GLU SER LEU ASN LYS TRP LYS
SEQRES 10 A 121 SER LYS GLY ARG
HELIX 1 1 CYS A 245 PHE A 253 1 9
HELIX 2 2 LYS A 278 ALA A 289 1 12
HELIX 3 3 GLU A 307 ASN A 327 1 21
SHEET 1 A 4 ILE A 259 ASP A 263 0
SHEET 2 A 4 GLU A 270 PHE A 275 -1 O ILE A 272 N ASP A 263
SHEET 3 A 4 LEU A 233 GLY A 238 -1 N LEU A 234 O ILE A 273
SHEET 4 A 4 VAL A 301 GLU A 304 -1 O GLU A 304 N LYS A 235
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 - b 23 2 Bytes