Header list of 1y7q.pdb file
Complete list - t 20 2 Bytes
HEADER TRANSCRIPTION 09-DEC-04 1Y7Q TITLE MAMMALIAN SCAN DOMAIN DIMER IS A DOMAIN-SWAPPED HOMOLOGUE OF THE HIV TITLE 2 CAPSID C-TERMINAL DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: ZINC FINGER PROTEIN 174; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: SCAN DOMAIN, RESIDUES 37-132; COMPND 5 SYNONYM: AW-1; ZINC FINGER AND SCAN DOMAIN CONTAINING PROTEIN 8; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ZNF174, ZSCAN8; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS SCAN DOMAIN; RETROVIRAL CAPSID C-TERMINAL DOMAIN; DIMER; C2H2 ZINC KEYWDS 2 FINGER ASSOCIATED, TRANSCRIPTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR D.IVANOV,J.R.STONE,J.L.MAKI,T.COLLINS,G.WAGNER REVDAT 3 20-OCT-21 1Y7Q 1 REMARK SEQADV REVDAT 2 24-FEB-09 1Y7Q 1 VERSN REVDAT 1 18-JAN-05 1Y7Q 0 JRNL AUTH D.IVANOV,J.R.STONE,J.L.MAKI,T.COLLINS,G.WAGNER JRNL TITL MAMMALIAN SCAN DOMAIN DIMER IS A DOMAIN-SWAPPED HOMOLOG OF JRNL TITL 2 THE HIV CAPSID C-TERMINAL DOMAIN JRNL REF MOL.CELL V. 17 137 2005 JRNL REFN ISSN 1097-2765 JRNL PMID 15629724 JRNL DOI 10.1016/J.MOLCEL.2004.12.015 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 1.0.6, CYANA 1.0.6 REMARK 3 AUTHORS : HERMANN, T.,GUNTERT, P., WUTHRICH, K. (CYANA), REMARK 3 HERMANN, T.,GUNTERT, P., WUTHRICH, K. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1Y7Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-05. REMARK 100 THE DEPOSITION ID IS D_1000031221. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 200MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2 MM SCAN DOMAIN, U-15N,13C; 2 REMARK 210 MM SCAN DOMAIN, U-15N,2D; 2 MM REMARK 210 SCAN DOMAIN, UNLABELED REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX; UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE .04 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON REMARK 210 -BOND 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 O PRO B 99 H ILE B 102 1.49 REMARK 500 O PRO B 60 H ALA B 63 1.51 REMARK 500 O LEU B 64 H ARG B 68 1.59 REMARK 500 O LEU B 89 HE21 GLN B 93 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 SER A 36 131.81 179.84 REMARK 500 1 ASN A 38 166.16 57.82 REMARK 500 1 CYS A 39 91.12 178.65 REMARK 500 1 GLU A 43 -40.08 -175.26 REMARK 500 1 CYS A 53 124.75 60.85 REMARK 500 1 TYR A 54 117.49 -33.98 REMARK 500 1 GLN A 55 -82.02 -179.36 REMARK 500 1 GLU A 56 -62.28 -29.15 REMARK 500 1 PRO A 60 -75.66 -75.04 REMARK 500 1 GLN A 76 61.24 38.33 REMARK 500 1 LEU A 79 -34.80 177.32 REMARK 500 1 THR A 81 -159.40 -61.61 REMARK 500 1 PRO A 99 -162.03 -74.94 REMARK 500 1 ARG A 109 122.41 65.20 REMARK 500 1 CYS A 110 -40.41 179.94 REMARK 500 1 MET A 112 -39.88 -173.39 REMARK 500 1 ALA A 127 -165.79 -111.09 REMARK 500 1 SER A 128 74.06 -162.34 REMARK 500 1 CYS B 39 79.15 46.60 REMARK 500 1 ASP B 41 86.67 -165.69 REMARK 500 1 GLU B 43 50.37 -156.78 REMARK 500 1 ARG B 50 96.56 -38.89 REMARK 500 1 ARG B 51 52.48 81.38 REMARK 500 1 CYS B 53 119.35 92.63 REMARK 500 1 GLN B 55 27.87 39.96 REMARK 500 1 GLU B 56 94.62 35.44 REMARK 500 1 SER B 58 -29.78 90.02 REMARK 500 1 ARG B 68 -34.32 -34.71 REMARK 500 1 GLN B 76 127.18 56.61 REMARK 500 1 GLU B 78 52.34 -178.87 REMARK 500 1 THR B 81 -155.54 -61.77 REMARK 500 1 GLU B 92 -36.91 -35.75 REMARK 500 1 GLU B 100 -33.63 -34.89 REMARK 500 1 VAL B 106 -60.78 -105.55 REMARK 500 1 HIS B 108 12.05 88.15 REMARK 500 1 ARG B 109 40.69 160.99 REMARK 500 1 CYS B 110 -170.40 162.13 REMARK 500 1 MET B 112 -77.73 -143.43 REMARK 500 1 ARG B 126 71.23 175.53 REMARK 500 1 ALA B 127 -167.07 -57.23 REMARK 500 1 SER B 128 -39.82 -170.68 REMARK 500 1 LYS B 130 150.55 -47.58 REMARK 500 2 ASP A 41 84.13 -159.97 REMARK 500 2 PHE A 52 -71.46 -48.69 REMARK 500 2 CYS A 53 63.50 70.36 REMARK 500 2 TYR A 54 -152.62 33.85 REMARK 500 2 GLN A 55 -61.02 71.55 REMARK 500 2 SER A 58 26.15 41.62 REMARK 500 2 PRO A 60 -89.16 -74.96 REMARK 500 2 GLN A 76 62.24 37.25 REMARK 500 REMARK 500 THIS ENTRY HAS 847 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1Y7Q A 37 132 UNP Q15697 ZN174_HUMAN 37 132 DBREF 1Y7Q B 37 132 UNP Q15697 ZN174_HUMAN 37 132 SEQADV 1Y7Q GLY A 35 UNP Q15697 CLONING ARTIFACT SEQADV 1Y7Q SER A 36 UNP Q15697 CLONING ARTIFACT SEQADV 1Y7Q GLU A 100 UNP Q15697 PRO 100 ENGINEERED MUTATION SEQADV 1Y7Q LEU A 111 UNP Q15697 PRO 111 ENGINEERED MUTATION SEQADV 1Y7Q GLY B 35 UNP Q15697 CLONING ARTIFACT SEQADV 1Y7Q SER B 36 UNP Q15697 CLONING ARTIFACT SEQADV 1Y7Q GLU B 100 UNP Q15697 PRO 100 ENGINEERED MUTATION SEQADV 1Y7Q LEU B 111 UNP Q15697 PRO 111 ENGINEERED MUTATION SEQRES 1 A 98 GLY SER LYS ASN CYS PRO ASP PRO GLU LEU CYS ARG GLN SEQRES 2 A 98 SER PHE ARG ARG PHE CYS TYR GLN GLU VAL SER GLY PRO SEQRES 3 A 98 GLN GLU ALA LEU SER GLN LEU ARG GLN LEU CYS ARG GLN SEQRES 4 A 98 TRP LEU GLN PRO GLU LEU HIS THR LYS GLU GLN ILE LEU SEQRES 5 A 98 GLU LEU LEU VAL MET GLU GLN PHE LEU THR ILE LEU PRO SEQRES 6 A 98 GLU GLU ILE GLN ALA ARG VAL ARG HIS ARG CYS LEU MET SEQRES 7 A 98 SER SER LYS GLU ILE VAL THR LEU VAL GLU ASP PHE HIS SEQRES 8 A 98 ARG ALA SER LYS LYS PRO LYS SEQRES 1 B 98 GLY SER LYS ASN CYS PRO ASP PRO GLU LEU CYS ARG GLN SEQRES 2 B 98 SER PHE ARG ARG PHE CYS TYR GLN GLU VAL SER GLY PRO SEQRES 3 B 98 GLN GLU ALA LEU SER GLN LEU ARG GLN LEU CYS ARG GLN SEQRES 4 B 98 TRP LEU GLN PRO GLU LEU HIS THR LYS GLU GLN ILE LEU SEQRES 5 B 98 GLU LEU LEU VAL MET GLU GLN PHE LEU THR ILE LEU PRO SEQRES 6 B 98 GLU GLU ILE GLN ALA ARG VAL ARG HIS ARG CYS LEU MET SEQRES 7 B 98 SER SER LYS GLU ILE VAL THR LEU VAL GLU ASP PHE HIS SEQRES 8 B 98 ARG ALA SER LYS LYS PRO LYS HELIX 1 1 GLU A 43 ARG A 51 1 9 HELIX 2 2 PRO A 60 GLN A 76 1 17 HELIX 3 3 THR A 81 LEU A 98 1 18 HELIX 4 4 GLU A 100 HIS A 108 1 9 HELIX 5 5 SER A 113 ARG A 126 1 14 HELIX 6 6 GLU B 43 ARG B 50 1 8 HELIX 7 7 GLN B 61 GLN B 76 1 16 HELIX 8 8 THR B 81 LEU B 98 1 18 HELIX 9 9 GLU B 100 ARG B 107 1 8 HELIX 10 10 SER B 113 ALA B 127 1 15 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 - t 20 2 Bytes