Header list of 1r05.pdb file
Complete list - t 27 2 Bytes
HEADER TRANSCRIPTION 19-SEP-03 1R05 TITLE SOLUTION STRUCTURE OF MAX B-HLH-LZ COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAX PROTEIN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: MAX B-HLH-LZ; COMPND 5 ENGINEERED: YES; COMPND 6 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: MAX; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS BASIC-HELIX-LOOP-HELIX-LEUCINEZIPPER HOMODIMER, TRANSCRIPTION EXPDTA SOLUTION NMR NUMMDL 6 AUTHOR S.SAUV,L.TREMBLAY,P.LAVIGNE REVDAT 4 27-OCT-21 1R05 1 REMARK SEQADV REVDAT 3 24-FEB-09 1R05 1 VERSN REVDAT 2 11-JAN-05 1R05 1 JRNL REVDAT 1 21-OCT-03 1R05 0 JRNL AUTH S.SAUV,L.TREMBLAY,P.LAVIGNE JRNL TITL THE NMR SOLUTION STRUCTURE OF A MUTANT OF THE MAX B/HLH/LZ JRNL TITL 2 FREE OF DNA: INSIGHTS INTO THE SPECIFIC AND REVERSIBLE DNA JRNL TITL 3 BINDING MECHANISM OF DIMERIC TRANSCRIPTION FACTORS JRNL REF J.MOL.BIOL. V. 342 813 2004 JRNL REFN ISSN 0022-2836 JRNL PMID 15342239 JRNL DOI 10.1016/J.JMB.2004.07.058 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE, X-PLOR REMARK 3 AUTHORS : FRANK DELAGLIO, ET AL. (NMRPIPE), BRUNGER, ET AL. REMARK 3 (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1R05 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-SEP-03. REMARK 100 THE DEPOSITION ID IS D_1000020281. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 6.8 REMARK 210 IONIC STRENGTH : 250MM KCL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 25MM MAX 15N, 50MM PHOSPHATE REMARK 210 BUFFER, 250MM KCL; 25MM MAX 13C, REMARK 210 15N, 50MM PHOSPHATE BUFFER, REMARK 210 250MM KCL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-NOESYHSQC; 13C-NOESYHSQC; REMARK 210 13C-HCCH-TOCSY; 13C-HCCH-COSY; REMARK 210 TRIPLE RESONANCE, SUCH AS HNCA REMARK 210 AND HNCACB REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : 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 : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 6 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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: 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 ILE A 43 H ALA A 47 1.55 REMARK 500 O ILE B 43 H ALA B 47 1.55 REMARK 500 O LYS A 57 H LEU A 61 1.56 REMARK 500 O LYS B 57 H LEU B 61 1.56 REMARK 500 O GLN A 71 H LEU A 75 1.56 REMARK 500 O GLN B 71 H LEU B 75 1.56 REMARK 500 O PHE B 23 H ARG B 27 1.57 REMARK 500 O PHE A 23 H ARG A 27 1.57 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 ASP A 3 -78.60 -71.54 REMARK 500 1 ARG A 5 -92.65 -85.52 REMARK 500 1 ALA A 6 -88.55 53.01 REMARK 500 1 HIS A 7 -154.54 -119.67 REMARK 500 1 HIS A 8 63.54 -115.90 REMARK 500 1 ALA A 10 -169.72 -103.13 REMARK 500 1 GLU A 12 -157.67 -66.35 REMARK 500 1 ARG A 13 -152.18 37.95 REMARK 500 1 LYS A 14 -148.98 -164.95 REMARK 500 1 ARG A 15 32.21 -84.60 REMARK 500 1 ILE A 19 -79.49 -53.91 REMARK 500 1 LYS A 20 -42.68 -27.94 REMARK 500 1 LYS A 37 90.32 -47.47 REMARK 500 1 SER A 39 169.84 66.48 REMARK 500 1 TYR A 50 -71.51 -65.02 REMARK 500 1 GLN A 52 -74.91 -77.53 REMARK 500 1 LEU A 61 -77.95 -59.27 REMARK 500 1 GLN A 71 -86.04 -58.24 REMARK 500 1 SER A 85 109.78 64.05 REMARK 500 1 ASP B 3 -78.59 -71.58 REMARK 500 1 ARG B 5 -92.79 -85.52 REMARK 500 1 ALA B 6 -88.55 53.10 REMARK 500 1 HIS B 7 -154.45 -119.73 REMARK 500 1 HIS B 8 63.46 -115.91 REMARK 500 1 ALA B 10 -169.71 -103.09 REMARK 500 1 GLU B 12 -157.73 -66.32 REMARK 500 1 ARG B 13 -152.04 37.98 REMARK 500 1 LYS B 14 -149.07 -165.10 REMARK 500 1 ARG B 15 32.19 -84.53 REMARK 500 1 ILE B 19 -79.51 -53.87 REMARK 500 1 LYS B 20 -42.92 -27.96 REMARK 500 1 LYS B 37 90.33 -47.44 REMARK 500 1 SER B 39 169.91 66.50 REMARK 500 1 TYR B 50 -71.54 -65.05 REMARK 500 1 GLN B 52 -74.97 -77.48 REMARK 500 1 LEU B 61 -78.12 -59.13 REMARK 500 1 GLN B 71 -86.03 -58.23 REMARK 500 1 ASN B 72 -27.83 -39.93 REMARK 500 1 SER B 85 109.60 64.05 REMARK 500 2 ALA A 2 -164.87 -129.11 REMARK 500 2 LYS A 4 78.87 42.78 REMARK 500 2 ARG A 5 83.75 -63.99 REMARK 500 2 ALA A 6 -142.07 41.29 REMARK 500 2 HIS A 7 168.94 56.64 REMARK 500 2 LYS A 14 -151.18 64.84 REMARK 500 2 HIS A 18 -83.12 -63.38 REMARK 500 2 LEU A 33 -74.15 -87.63 REMARK 500 2 GLN A 34 -89.04 49.27 REMARK 500 2 GLU A 36 -139.48 -68.68 REMARK 500 2 ARG A 40 -110.68 58.21 REMARK 500 REMARK 500 THIS ENTRY HAS 222 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 5 0.27 SIDE CHAIN REMARK 500 1 ARG A 13 0.28 SIDE CHAIN REMARK 500 1 ARG A 15 0.23 SIDE CHAIN REMARK 500 1 ARG A 16 0.10 SIDE CHAIN REMARK 500 1 ARG A 27 0.29 SIDE CHAIN REMARK 500 1 ARG A 40 0.30 SIDE CHAIN REMARK 500 1 ARG A 55 0.22 SIDE CHAIN REMARK 500 1 ARG A 56 0.19 SIDE CHAIN REMARK 500 1 ARG A 70 0.24 SIDE CHAIN REMARK 500 1 ARG A 80 0.20 SIDE CHAIN REMARK 500 1 ARG B 5 0.27 SIDE CHAIN REMARK 500 1 ARG B 13 0.28 SIDE CHAIN REMARK 500 1 ARG B 15 0.23 SIDE CHAIN REMARK 500 1 ARG B 16 0.10 SIDE CHAIN REMARK 500 1 ARG B 27 0.29 SIDE CHAIN REMARK 500 1 ARG B 40 0.30 SIDE CHAIN REMARK 500 1 ARG B 55 0.21 SIDE CHAIN REMARK 500 1 ARG B 56 0.19 SIDE CHAIN REMARK 500 1 ARG B 70 0.24 SIDE CHAIN REMARK 500 1 ARG B 80 0.20 SIDE CHAIN REMARK 500 2 ARG A 5 0.23 SIDE CHAIN REMARK 500 2 ARG A 13 0.14 SIDE CHAIN REMARK 500 2 ARG A 15 0.23 SIDE CHAIN REMARK 500 2 ARG A 16 0.28 SIDE CHAIN REMARK 500 2 ARG A 27 0.22 SIDE CHAIN REMARK 500 2 ARG A 55 0.21 SIDE CHAIN REMARK 500 2 ARG A 56 0.32 SIDE CHAIN REMARK 500 2 ARG A 70 0.27 SIDE CHAIN REMARK 500 2 ARG A 80 0.32 SIDE CHAIN REMARK 500 2 ARG B 5 0.23 SIDE CHAIN REMARK 500 2 ARG B 13 0.14 SIDE CHAIN REMARK 500 2 ARG B 15 0.23 SIDE CHAIN REMARK 500 2 ARG B 16 0.28 SIDE CHAIN REMARK 500 2 ARG B 27 0.22 SIDE CHAIN REMARK 500 2 ARG B 55 0.21 SIDE CHAIN REMARK 500 2 ARG B 56 0.32 SIDE CHAIN REMARK 500 2 ARG B 70 0.27 SIDE CHAIN REMARK 500 2 ARG B 80 0.32 SIDE CHAIN REMARK 500 3 ARG A 5 0.23 SIDE CHAIN REMARK 500 3 ARG A 15 0.28 SIDE CHAIN REMARK 500 3 ARG A 16 0.14 SIDE CHAIN REMARK 500 3 ARG A 40 0.16 SIDE CHAIN REMARK 500 3 ARG A 55 0.31 SIDE CHAIN REMARK 500 3 ARG A 56 0.23 SIDE CHAIN REMARK 500 3 ARG A 70 0.20 SIDE CHAIN REMARK 500 3 ARG A 80 0.27 SIDE CHAIN REMARK 500 3 ARG B 5 0.23 SIDE CHAIN REMARK 500 3 ARG B 15 0.28 SIDE CHAIN REMARK 500 3 ARG B 16 0.14 SIDE CHAIN REMARK 500 3 ARG B 40 0.16 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 112 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8641 RELATED DB: BMRB REMARK 900 THE ASSIGNED CHEMICAL SHIFTS WERE SUBMITTED FOR BMRB ANALYSIS AND REMARK 900 VALIDATION DBREF 1R05 A 2 83 UNP P61244 MAX_HUMAN 22 103 DBREF 1R05 B 2 83 UNP P61244 MAX_HUMAN 22 103 SEQADV 1R05 MET A 1 UNP P61244 INITIATING METHIONINE SEQADV 1R05 VAL A 58 UNP P61244 ASN 78 ENGINEERED MUTATION SEQADV 1R05 LEU A 61 UNP P61244 HIS 81 ENGINEERED MUTATION SEQADV 1R05 GLY A 84 UNP P61244 CLONING ARTIFACT SEQADV 1R05 SER A 85 UNP P61244 CLONING ARTIFACT SEQADV 1R05 GLY A 86 UNP P61244 CLONING ARTIFACT SEQADV 1R05 CYS A 87 UNP P61244 CLONING ARTIFACT SEQADV 1R05 MET B 1 UNP P61244 INITIATING METHIONINE SEQADV 1R05 VAL B 58 UNP P61244 ASN 78 ENGINEERED MUTATION SEQADV 1R05 LEU B 61 UNP P61244 HIS 81 ENGINEERED MUTATION SEQADV 1R05 GLY B 84 UNP P61244 CLONING ARTIFACT SEQADV 1R05 SER B 85 UNP P61244 CLONING ARTIFACT SEQADV 1R05 GLY B 86 UNP P61244 CLONING ARTIFACT SEQADV 1R05 CYS B 87 UNP P61244 CLONING ARTIFACT SEQRES 1 A 87 MET ALA ASP LYS ARG ALA HIS HIS ASN ALA LEU GLU ARG SEQRES 2 A 87 LYS ARG ARG ASP HIS ILE LYS ASP SER PHE HIS SER LEU SEQRES 3 A 87 ARG ASP SER VAL PRO SER LEU GLN GLY GLU LYS ALA SER SEQRES 4 A 87 ARG ALA GLN ILE LEU ASP LYS ALA THR GLU TYR ILE GLN SEQRES 5 A 87 TYR MET ARG ARG LYS VAL HIS THR LEU GLN GLN ASP ILE SEQRES 6 A 87 ASP ASP LEU LYS ARG GLN ASN ALA LEU LEU GLU GLN GLN SEQRES 7 A 87 VAL ARG ALA LEU GLU GLY SER GLY CYS SEQRES 1 B 87 MET ALA ASP LYS ARG ALA HIS HIS ASN ALA LEU GLU ARG SEQRES 2 B 87 LYS ARG ARG ASP HIS ILE LYS ASP SER PHE HIS SER LEU SEQRES 3 B 87 ARG ASP SER VAL PRO SER LEU GLN GLY GLU LYS ALA SER SEQRES 4 B 87 ARG ALA GLN ILE LEU ASP LYS ALA THR GLU TYR ILE GLN SEQRES 5 B 87 TYR MET ARG ARG LYS VAL HIS THR LEU GLN GLN ASP ILE SEQRES 6 B 87 ASP ASP LEU LYS ARG GLN ASN ALA LEU LEU GLU GLN GLN SEQRES 7 B 87 VAL ARG ALA LEU GLU GLY SER GLY CYS HELIX 1 1 ASP A 17 VAL A 30 1 14 HELIX 2 2 SER A 32 LYS A 37 5 6 HELIX 3 3 ALA A 41 GLU A 83 1 43 HELIX 4 4 ASP B 17 VAL B 30 1 14 HELIX 5 5 SER B 32 LYS B 37 5 6 HELIX 6 6 ALA B 41 GLU B 83 1 43 SSBOND 1 CYS A 87 CYS B 87 1555 1555 2.02 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 27 2 Bytes