Header list of 1z9e.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING/TRANSCRIPTION 01-APR-05 1Z9E TITLE SOLUTION STRUCTURE OF THE HIV-1 INTEGRASE-BINDING DOMAIN IN LEDGF/P75 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PC4 AND SFRS1 INTERACTING PROTEIN 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 347-471 CONTAINS: HIV-1 COMPND 5 INTEGRASE-BINDING DOMAIN (RESIDUES 347-429); COMPND 6 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: PSIP1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T1 KEYWDS HEAT REPEAT-LIKE, LEDGF, PROTEIN BINDING-TRANSCRIPTION COMPLEX EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR P.CHEREPANOV,Z.-Y.J.SUN,S.RAHMAN,G.MAERTENS,G.WAGNER,A.ENGELMAN REVDAT 5 02-MAR-22 1Z9E 1 REMARK SEQADV REVDAT 4 24-FEB-09 1Z9E 1 VERSN REVDAT 3 01-NOV-05 1Z9E 1 KEYWDS REVDAT 2 05-JUL-05 1Z9E 1 JRNL REVDAT 1 17-MAY-05 1Z9E 0 JRNL AUTH P.CHEREPANOV,Z.-Y.J.SUN,S.RAHMAN,G.MAERTENS,G.WAGNER, JRNL AUTH 2 A.ENGELMAN JRNL TITL SOLUTION STRUCTURE OF THE HIV-1 INTEGRASE-BINDING DOMAIN IN JRNL TITL 2 LEDGF/P75 JRNL REF NAT.STRUCT.MOL.BIOL. V. 12 526 2005 JRNL REFN ISSN 1545-9993 JRNL PMID 15895093 JRNL DOI 10.1038/NSMB937 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER, A. (X-PLOR), BRUNGER, A. (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1Z9E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-05. REMARK 100 THE DEPOSITION ID IS D_1000032463. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.25 REMARK 210 IONIC STRENGTH : 100 MM NACL, 50 MM POSPHATE REMARK 210 BUFFER REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.7 MM PROTEIN, 100 MM NACL, 50 REMARK 210 MM PHOSPHATE BUFFER, 90% H2O, 10% REMARK 210 D2O; 0.7 MM PROTEIN, 100 MM REMARK 210 NACL, 38 MM NA2HPO4, 12 MM REMARK 210 NAH2PO4, 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY; HNCA, HNCOCA, REMARK 210 HNCO, HNCACO, HNCACB, HNCOCACB, REMARK 210 HCCONH, CCONH; HCCH-TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : 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 : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY 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 1-15 REMARK 465 RES C SSSEQI REMARK 465 GLY A 345 REMARK 465 SER A 346 REMARK 465 GLY A 430 REMARK 465 GLU A 431 REMARK 465 GLY A 432 REMARK 465 ASP A 433 REMARK 465 SER A 434 REMARK 465 VAL A 435 REMARK 465 ILE A 436 REMARK 465 THR A 437 REMARK 465 GLN A 438 REMARK 465 VAL A 439 REMARK 465 LEU A 440 REMARK 465 ASN A 441 REMARK 465 LYS A 442 REMARK 465 SER A 443 REMARK 465 LEU A 444 REMARK 465 ALA A 445 REMARK 465 GLU A 446 REMARK 465 GLN A 447 REMARK 465 ARG A 448 REMARK 465 GLN A 449 REMARK 465 HIS A 450 REMARK 465 GLU A 451 REMARK 465 GLU A 452 REMARK 465 ALA A 453 REMARK 465 ASN A 454 REMARK 465 LYS A 455 REMARK 465 THR A 456 REMARK 465 LYS A 457 REMARK 465 ASP A 458 REMARK 465 GLN A 459 REMARK 465 GLY A 460 REMARK 465 LYS A 461 REMARK 465 LYS A 462 REMARK 465 GLY A 463 REMARK 465 PRO A 464 REMARK 465 ASN A 465 REMARK 465 LYS A 466 REMARK 465 LYS A 467 REMARK 465 LEU A 468 REMARK 465 GLU A 469 REMARK 465 LYS A 470 REMARK 465 GLU A 471 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 LEU A 363 39.66 -94.85 REMARK 500 1 ASN A 367 41.00 -150.86 REMARK 500 1 LEU A 368 96.15 -40.83 REMARK 500 1 LEU A 383 107.30 -55.97 REMARK 500 2 LEU A 363 39.67 -94.31 REMARK 500 2 ASN A 367 39.31 -150.53 REMARK 500 2 LEU A 368 97.44 -40.33 REMARK 500 2 LEU A 383 108.12 -57.48 REMARK 500 2 GLN A 384 93.93 -69.49 REMARK 500 3 LEU A 363 39.47 -93.33 REMARK 500 3 ASN A 367 40.06 -149.06 REMARK 500 3 LEU A 368 95.51 -36.80 REMARK 500 4 LEU A 363 39.55 -95.04 REMARK 500 4 ASN A 367 44.22 -151.41 REMARK 500 4 LEU A 368 94.58 -41.08 REMARK 500 5 LEU A 363 39.71 -94.73 REMARK 500 5 ASN A 367 45.48 -157.91 REMARK 500 5 LEU A 368 93.36 -46.44 REMARK 500 5 LEU A 383 107.31 -53.35 REMARK 500 6 LEU A 363 39.75 -93.95 REMARK 500 6 ASN A 367 43.94 -151.67 REMARK 500 6 LEU A 368 95.28 -42.13 REMARK 500 6 LEU A 383 106.63 -55.57 REMARK 500 6 GLN A 384 92.55 -66.08 REMARK 500 7 LEU A 363 39.86 -96.35 REMARK 500 7 ASN A 367 47.74 -159.33 REMARK 500 7 LEU A 368 90.55 -50.27 REMARK 500 8 LEU A 363 39.56 -93.86 REMARK 500 8 ASN A 367 41.69 -150.74 REMARK 500 8 LEU A 368 95.47 -41.30 REMARK 500 8 GLN A 410 -33.20 -137.76 REMARK 500 9 LEU A 363 39.85 -95.42 REMARK 500 9 ASN A 367 47.28 -152.19 REMARK 500 9 LEU A 368 93.42 -44.42 REMARK 500 10 LEU A 363 40.21 -95.66 REMARK 500 10 ASN A 367 42.97 -158.78 REMARK 500 10 LEU A 368 92.76 -47.71 REMARK 500 10 GLN A 384 73.92 -110.09 REMARK 500 11 LEU A 363 40.08 -96.71 REMARK 500 11 ASN A 367 61.76 -157.99 REMARK 500 11 LEU A 383 106.54 -55.77 REMARK 500 11 GLN A 384 82.97 -67.16 REMARK 500 12 LEU A 363 39.71 -93.44 REMARK 500 12 ASN A 367 41.86 -147.97 REMARK 500 12 LEU A 368 95.45 -34.96 REMARK 500 12 GLN A 384 86.25 -67.81 REMARK 500 13 LEU A 363 39.56 -98.23 REMARK 500 13 ASN A 367 42.77 -151.00 REMARK 500 13 LEU A 368 88.04 -53.00 REMARK 500 14 LEU A 363 39.65 -92.33 REMARK 500 REMARK 500 THIS ENTRY HAS 59 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 351 0.24 SIDE CHAIN REMARK 500 1 ARG A 354 0.21 SIDE CHAIN REMARK 500 1 ARG A 372 0.28 SIDE CHAIN REMARK 500 1 ARG A 404 0.32 SIDE CHAIN REMARK 500 1 ARG A 405 0.31 SIDE CHAIN REMARK 500 2 ARG A 351 0.24 SIDE CHAIN REMARK 500 2 ARG A 354 0.32 SIDE CHAIN REMARK 500 2 ARG A 372 0.27 SIDE CHAIN REMARK 500 2 ARG A 404 0.32 SIDE CHAIN REMARK 500 2 ARG A 405 0.31 SIDE CHAIN REMARK 500 3 ARG A 351 0.25 SIDE CHAIN REMARK 500 3 ARG A 354 0.22 SIDE CHAIN REMARK 500 3 ARG A 372 0.21 SIDE CHAIN REMARK 500 3 ARG A 404 0.32 SIDE CHAIN REMARK 500 3 ARG A 405 0.23 SIDE CHAIN REMARK 500 4 ARG A 351 0.24 SIDE CHAIN REMARK 500 4 ARG A 354 0.28 SIDE CHAIN REMARK 500 4 ARG A 372 0.28 SIDE CHAIN REMARK 500 4 ARG A 404 0.22 SIDE CHAIN REMARK 500 4 ARG A 405 0.22 SIDE CHAIN REMARK 500 5 ARG A 351 0.30 SIDE CHAIN REMARK 500 5 ARG A 354 0.30 SIDE CHAIN REMARK 500 5 ARG A 372 0.22 SIDE CHAIN REMARK 500 5 ARG A 404 0.30 SIDE CHAIN REMARK 500 5 ARG A 405 0.32 SIDE CHAIN REMARK 500 6 ARG A 351 0.25 SIDE CHAIN REMARK 500 6 ARG A 354 0.29 SIDE CHAIN REMARK 500 6 ARG A 372 0.30 SIDE CHAIN REMARK 500 6 ARG A 404 0.27 SIDE CHAIN REMARK 500 6 ARG A 405 0.31 SIDE CHAIN REMARK 500 7 ARG A 351 0.23 SIDE CHAIN REMARK 500 7 ARG A 354 0.24 SIDE CHAIN REMARK 500 7 ARG A 372 0.25 SIDE CHAIN REMARK 500 7 ARG A 404 0.22 SIDE CHAIN REMARK 500 7 ARG A 405 0.25 SIDE CHAIN REMARK 500 8 ARG A 351 0.29 SIDE CHAIN REMARK 500 8 ARG A 354 0.26 SIDE CHAIN REMARK 500 8 ARG A 372 0.31 SIDE CHAIN REMARK 500 8 ARG A 404 0.23 SIDE CHAIN REMARK 500 8 ARG A 405 0.30 SIDE CHAIN REMARK 500 9 ARG A 351 0.24 SIDE CHAIN REMARK 500 9 ARG A 354 0.26 SIDE CHAIN REMARK 500 9 ARG A 372 0.24 SIDE CHAIN REMARK 500 9 ARG A 404 0.30 SIDE CHAIN REMARK 500 9 ARG A 405 0.25 SIDE CHAIN REMARK 500 10 ARG A 351 0.22 SIDE CHAIN REMARK 500 10 ARG A 354 0.24 SIDE CHAIN REMARK 500 10 ARG A 372 0.32 SIDE CHAIN REMARK 500 10 ARG A 404 0.28 SIDE CHAIN REMARK 500 10 ARG A 405 0.23 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 75 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1Z9E A 347 471 UNP O75475 O75475_HUMAN 347 471 SEQADV 1Z9E GLY A 345 UNP O75475 CLONING ARTIFACT SEQADV 1Z9E SER A 346 UNP O75475 CLONING ARTIFACT SEQRES 1 A 127 GLY SER SER MET ASP SER ARG LEU GLN ARG ILE HIS ALA SEQRES 2 A 127 GLU ILE LYS ASN SER LEU LYS ILE ASP ASN LEU ASP VAL SEQRES 3 A 127 ASN ARG CYS ILE GLU ALA LEU ASP GLU LEU ALA SER LEU SEQRES 4 A 127 GLN VAL THR MET GLN GLN ALA GLN LYS HIS THR GLU MET SEQRES 5 A 127 ILE THR THR LEU LYS LYS ILE ARG ARG PHE LYS VAL SER SEQRES 6 A 127 GLN VAL ILE MET GLU LYS SER THR MET LEU TYR ASN LYS SEQRES 7 A 127 PHE LYS ASN MET PHE LEU VAL GLY GLU GLY ASP SER VAL SEQRES 8 A 127 ILE THR GLN VAL LEU ASN LYS SER LEU ALA GLU GLN ARG SEQRES 9 A 127 GLN HIS GLU GLU ALA ASN LYS THR LYS ASP GLN GLY LYS SEQRES 10 A 127 LYS GLY PRO ASN LYS LYS LEU GLU LYS GLU HELIX 1 1 SER A 347 LEU A 363 1 17 HELIX 2 2 LYS A 364 LEU A 368 5 5 HELIX 3 3 ASP A 369 LEU A 383 1 15 HELIX 4 4 THR A 386 GLN A 391 1 6 HELIX 5 5 HIS A 393 ARG A 404 1 12 HELIX 6 6 VAL A 411 VAL A 429 1 19 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