Header list of 1i42.pdb file
Complete list - b 23 2 Bytes
HEADER PROTEIN BINDING 19-FEB-01 1I42 TITLE NMR STRUCTURE OF THE UBX DOMAIN FROM P47 COMPND MOL_ID: 1; COMPND 2 MOLECULE: P47; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN(RESIDUES 282-370); COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; 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: PPRO-EX HTB KEYWDS UBIQUITIN SUPERFOLD, UBX, UNUSUAL N-TERMINAL FEATURE, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR X.YUAN,A.SHAW,X.ZHANG,H.KONDO,J.LALLY,P.S.FREEMONT,S.MATTHEWS REVDAT 5 23-FEB-22 1I42 1 REMARK REVDAT 4 24-FEB-09 1I42 1 VERSN REVDAT 3 01-APR-03 1I42 1 JRNL REVDAT 2 31-DEC-02 1I42 1 REMARK REVDAT 1 29-AUG-01 1I42 0 JRNL AUTH X.YUAN,A.SHAW,X.ZHANG,H.KONDO,J.LALLY,P.S.FREEMONT, JRNL AUTH 2 S.MATTHEWS JRNL TITL SOLUTION STRUCTURE AND INTERACTION SURFACE OF THE C-TERMINAL JRNL TITL 2 DOMAIN FROM P47: A MAJOR P97-COFACTOR INVOLVED IN SNARE JRNL TITL 3 DISASSEMBLY. JRNL REF J.MOL.BIOL. V. 311 255 2001 JRNL REFN ISSN 0022-2836 JRNL PMID 11478859 JRNL DOI 10.1006/JMBI.2001.4864 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AURELIA 2.1.5, X-PLOR 3.853 REMARK 3 AUTHORS : A. BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1I42 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-FEB-01. REMARK 100 THE DEPOSITION ID IS D_1000012877. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 302; 302; 302 REMARK 210 PH : 5.2; 5.2; 5.2 REMARK 210 IONIC STRENGTH : NULL; NULL; NULL REMARK 210 PRESSURE : 1 ATM; 1 ATM; 1 ATM REMARK 210 SAMPLE CONTENTS : 1MM 13C, 15N-LABELLED P47 C REMARK 210 DOMAIN SAMPLE; 1MM 15N P47 C REMARK 210 DOMAIN SAMPLE; 1MM P47 C DOMAIN REMARK 210 SAMPLE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA, HN(CO)CA, CBCA(CO)NH, REMARK 210 HBHA(CO)NH, 15N-NOESY; IPAP-HSQC; REMARK 210 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE, X-PLOR 3.853, NMRVIEW REMARK 210 3.1.1, XWINNMR REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH REMARK 210 EXPERIMENTAL NOESY SPECTRUM, REMARK 210 STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY,STRUCTURES REMARK 210 WITH FAVORABLE NON-BOND ENERGY, REMARK 210 STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST ENERGY 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: 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 HB2 LEU A 302 HA3 GLY A 306 1.31 REMARK 500 O HIS A 314 H LYS A 356 1.47 REMARK 500 O ASN A 290 H GLU A 293 1.54 REMARK 500 H ASN A 297 O ALA A 363 1.56 REMARK 500 O THR A 296 H PHE A 312 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 ALA A 283 106.76 177.64 REMARK 500 1 SER A 285 -9.39 74.36 REMARK 500 1 SER A 286 32.40 -145.38 REMARK 500 1 GLU A 291 -17.18 -43.63 REMARK 500 1 ASP A 304 42.70 -89.54 REMARK 500 1 HIS A 316 -117.34 -91.16 REMARK 500 1 ARG A 317 122.66 163.02 REMARK 500 1 ALA A 328 44.72 -148.26 REMARK 500 1 ALA A 334 69.05 83.03 REMARK 500 1 ASN A 345 53.81 37.45 REMARK 500 1 LEU A 348 175.24 -55.98 REMARK 500 1 ALA A 349 -66.92 -166.39 REMARK 500 1 ASP A 350 172.73 54.46 REMARK 500 1 GLU A 351 -78.78 -139.87 REMARK 500 1 ASN A 352 -33.00 -155.85 REMARK 500 1 GLN A 353 -142.56 -58.71 REMARK 500 1 THR A 354 -158.16 -56.18 REMARK 500 1 ASN A 359 -2.08 74.13 REMARK 500 1 LEU A 361 83.90 -51.76 REMARK 500 1 ALA A 363 -40.11 80.82 REMARK 500 2 ALA A 283 107.05 177.89 REMARK 500 2 SER A 286 -5.99 70.12 REMARK 500 2 ILE A 287 98.24 -64.48 REMARK 500 2 ALA A 328 45.21 -143.09 REMARK 500 2 ARG A 329 50.88 -117.22 REMARK 500 2 ALA A 334 69.54 81.35 REMARK 500 2 PHE A 343 -72.95 -65.87 REMARK 500 2 ASN A 345 61.28 39.94 REMARK 500 2 LEU A 348 160.68 -46.21 REMARK 500 2 ASP A 350 136.85 -14.28 REMARK 500 2 GLU A 351 -102.97 -128.80 REMARK 500 2 ASN A 352 -47.63 -146.93 REMARK 500 2 GLN A 353 -138.68 -77.11 REMARK 500 2 THR A 354 -173.21 -47.97 REMARK 500 2 ASN A 359 -2.71 78.28 REMARK 500 2 LEU A 361 93.47 -49.32 REMARK 500 2 ALA A 363 -74.24 75.75 REMARK 500 3 SER A 285 -15.47 78.26 REMARK 500 3 ILE A 287 98.72 -64.84 REMARK 500 3 ASP A 304 36.35 -90.06 REMARK 500 3 ARG A 329 44.59 -109.67 REMARK 500 3 MET A 332 -17.63 -46.49 REMARK 500 3 THR A 342 -93.37 -57.68 REMARK 500 3 PHE A 343 -68.26 -17.24 REMARK 500 3 ASN A 345 45.16 37.74 REMARK 500 3 ALA A 349 -28.87 170.05 REMARK 500 3 ASP A 350 -174.31 45.55 REMARK 500 3 GLU A 351 -76.58 -128.05 REMARK 500 3 ASN A 352 18.17 -160.14 REMARK 500 3 GLN A 353 -149.75 -123.69 REMARK 500 REMARK 500 THIS ENTRY HAS 170 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 301 0.23 SIDE CHAIN REMARK 500 1 ARG A 307 0.29 SIDE CHAIN REMARK 500 1 ARG A 317 0.26 SIDE CHAIN REMARK 500 1 ARG A 322 0.28 SIDE CHAIN REMARK 500 1 ARG A 329 0.22 SIDE CHAIN REMARK 500 2 ARG A 301 0.32 SIDE CHAIN REMARK 500 2 ARG A 307 0.22 SIDE CHAIN REMARK 500 2 ARG A 317 0.31 SIDE CHAIN REMARK 500 2 ARG A 322 0.25 SIDE CHAIN REMARK 500 2 ARG A 329 0.31 SIDE CHAIN REMARK 500 2 ARG A 368 0.22 SIDE CHAIN REMARK 500 3 ARG A 301 0.32 SIDE CHAIN REMARK 500 3 ARG A 307 0.23 SIDE CHAIN REMARK 500 3 ARG A 317 0.26 SIDE CHAIN REMARK 500 3 ARG A 329 0.32 SIDE CHAIN REMARK 500 3 ARG A 368 0.20 SIDE CHAIN REMARK 500 4 ARG A 301 0.23 SIDE CHAIN REMARK 500 4 ARG A 307 0.21 SIDE CHAIN REMARK 500 4 ARG A 317 0.08 SIDE CHAIN REMARK 500 4 ARG A 322 0.13 SIDE CHAIN REMARK 500 4 ARG A 368 0.13 SIDE CHAIN REMARK 500 5 ARG A 301 0.21 SIDE CHAIN REMARK 500 5 ARG A 307 0.25 SIDE CHAIN REMARK 500 5 ARG A 317 0.28 SIDE CHAIN REMARK 500 5 ARG A 322 0.30 SIDE CHAIN REMARK 500 5 ARG A 329 0.20 SIDE CHAIN REMARK 500 5 ARG A 368 0.25 SIDE CHAIN REMARK 500 6 ARG A 301 0.31 SIDE CHAIN REMARK 500 6 ARG A 317 0.25 SIDE CHAIN REMARK 500 6 ARG A 322 0.32 SIDE CHAIN REMARK 500 6 ARG A 329 0.21 SIDE CHAIN REMARK 500 6 ARG A 368 0.27 SIDE CHAIN REMARK 500 7 ARG A 301 0.22 SIDE CHAIN REMARK 500 7 ARG A 307 0.30 SIDE CHAIN REMARK 500 7 ARG A 317 0.29 SIDE CHAIN REMARK 500 7 ARG A 322 0.26 SIDE CHAIN REMARK 500 7 ARG A 329 0.14 SIDE CHAIN REMARK 500 7 ARG A 368 0.25 SIDE CHAIN REMARK 500 8 ARG A 301 0.19 SIDE CHAIN REMARK 500 8 ARG A 307 0.30 SIDE CHAIN REMARK 500 8 ARG A 317 0.17 SIDE CHAIN REMARK 500 8 ARG A 322 0.19 SIDE CHAIN REMARK 500 8 ARG A 329 0.21 SIDE CHAIN REMARK 500 8 ARG A 368 0.32 SIDE CHAIN REMARK 500 9 ARG A 301 0.19 SIDE CHAIN REMARK 500 9 ARG A 307 0.21 SIDE CHAIN REMARK 500 9 ARG A 317 0.32 SIDE CHAIN REMARK 500 9 ARG A 322 0.32 SIDE CHAIN REMARK 500 9 ARG A 329 0.18 SIDE CHAIN REMARK 500 9 ARG A 368 0.11 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 56 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1I42 A 282 370 UNP O35987 NSF1C_RAT 282 370 SEQRES 1 A 89 LYS ALA SER SER SER ILE LEU ILE ASN GLU ALA GLU PRO SEQRES 2 A 89 THR THR ASN ILE GLN ILE ARG LEU ALA ASP GLY GLY ARG SEQRES 3 A 89 LEU VAL GLN LYS PHE ASN HIS SER HIS ARG ILE SER ASP SEQRES 4 A 89 ILE ARG LEU PHE ILE VAL ASP ALA ARG PRO ALA MET ALA SEQRES 5 A 89 ALA THR SER PHE VAL LEU MET THR THR PHE PRO ASN LYS SEQRES 6 A 89 GLU LEU ALA ASP GLU ASN GLN THR LEU LYS GLU ALA ASN SEQRES 7 A 89 LEU LEU ASN ALA VAL ILE VAL GLN ARG LEU THR HELIX 1 1 ARG A 317 SER A 319 5 3 HELIX 2 2 ASP A 320 ARG A 329 1 10 HELIX 3 3 ALA A 331 THR A 335 5 5 SHEET 1 A 4 GLY A 306 PHE A 312 0 SHEET 2 A 4 THR A 296 LEU A 302 -1 O THR A 296 N PHE A 312 SHEET 3 A 4 VAL A 364 THR A 370 1 O ILE A 365 N GLN A 299 SHEET 4 A 4 SER A 336 MET A 340 -1 O SER A 336 N THR A 370 CRYST1 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