Header list of 1jsp.pdb file
Complete list - b 23 2 Bytes
HEADER DNA BINDING PROTEIN 17-AUG-01 1JSP TITLE NMR STRUCTURE OF CBP BROMODOMAIN IN COMPLEX WITH P53 PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: TUMOR PROTEIN P53; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL FRAGMENT; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: CREB-BINDING PROTEIN; COMPND 8 CHAIN: B; COMPND 9 FRAGMENT: BROMODOMAIN; COMPND 10 SYNONYM: CBP; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 6 ORGANISM_COMMON: HUMAN; SOURCE 7 ORGANISM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET15B KEYWDS BROMODOMAIN, CBP, NMR STRUCTURE., DNA BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR Y.HE,S.MUJTABA,L.ZENG,S.YAN,M.-M.ZHOU REVDAT 3 23-FEB-22 1JSP 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1JSP 1 VERSN REVDAT 1 17-AUG-02 1JSP 0 JRNL AUTH S.MUJTABA,Y.HE,L.ZENG,S.YAN,O.PLOTNIKOVA,SACHCHIDANAND, JRNL AUTH 2 R.SANCHEZ,N.J.ZELEZNIK-LE,Z.RONAI,M.M.ZHOU JRNL TITL STRUCTURAL MECHANISM OF THE BROMODOMAIN OF THE COACTIVATOR JRNL TITL 2 CBP IN P53 TRANSCRIPTIONAL ACTIVATION. JRNL REF MOL.CELL V. 13 251 2004 JRNL REFN ISSN 1097-2765 JRNL PMID 14759370 JRNL DOI 10.1016/S1097-2765(03)00528-8 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 1, X-PLOR 3.1 REMARK 3 AUTHORS : FRANK DELAGLIO (NMRPIPE), AXEL BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 71 INTER-MOLECULAR NOES ARE OBSERVED REMARK 3 BETWEEN PROTEIN AND PEPTIDE. REMARK 4 REMARK 4 1JSP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-AUG-01. REMARK 100 THE DEPOSITION ID IS D_1000014140. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298; 298 REMARK 210 PH : 6.5; 6.5; 6.5; 6.5 REMARK 210 IONIC STRENGTH : NULL; NULL; NULL; NULL REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT; REMARK 210 AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5MM CBP BROMODOMAIN U-15N; REMARK 210 0.5MM P53 PEPTIDE; 100MM REMARK 210 PHOSPHATE BUFFER; PH 6.5; 0.5MM REMARK 210 CBP BROMODOMAIN U-15N,13C; 0.5MM REMARK 210 P53 PEPTIDE;100MM PHOSPHATE REMARK 210 BUFFER; PH 6.5; 0.5MM CBP REMARK 210 BROMODOMAIN U-15N,13C; 0.5MM P53 REMARK 210 PEPTIDE;100MM PHOSPHATE BUFFER; REMARK 210 PH 6.5; 0.5MM CBP BROMODOMAIN U- REMARK 210 15N,13C,75% 2H; 0.5MM P53 REMARK 210 PEPTIDE;100MM PHOSPHATE BUFFER; REMARK 210 PH 6.5 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D_15N-HSQC; 3D CBCA(CO)NH; 3D REMARK 210 HCCH-TOCSY; 3D_13C-EDITED_13C/15N-FILTERED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; 3D_13C-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW 5.0.3, X-PLOR 3.1, ARIA REMARK 210 0.1 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 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 : NULL 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: 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 OD1 ASP B 1116 H GLN B 1118 1.56 REMARK 500 O ASP B 1156 H MET B 1160 1.58 REMARK 500 O ASP B 1190 H MET B 1193 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 LYS A 373 -61.93 -106.68 REMARK 500 1 ARG A 379 88.27 52.77 REMARK 500 1 ALY A 382 -146.76 25.79 REMARK 500 1 MET A 384 40.13 -92.28 REMARK 500 1 PHE A 385 -48.46 -172.14 REMARK 500 1 ARG B1081 63.16 -153.80 REMARK 500 1 ILE B1084 -74.23 61.36 REMARK 500 1 PHE B1085 -70.98 -175.93 REMARK 500 1 ALA B1100 -70.71 -75.00 REMARK 500 1 TYR B1102 73.60 -110.55 REMARK 500 1 PRO B1114 -163.24 -73.47 REMARK 500 1 ASP B1124 89.09 48.33 REMARK 500 1 VAL B1129 -50.63 -150.03 REMARK 500 1 LYS B1130 -66.90 66.24 REMARK 500 1 TYR B1147 52.00 -110.10 REMARK 500 1 TRP B1165 -44.64 -144.11 REMARK 500 1 ARG B1169 -160.62 60.79 REMARK 500 1 THR B1171 35.59 -165.98 REMARK 500 1 SER B1172 -151.51 -101.65 REMARK 500 1 ARG B1173 37.61 -99.59 REMARK 500 1 VAL B1174 -41.30 -143.30 REMARK 500 1 LYS B1176 -64.76 -154.50 REMARK 500 2 HIS A 368 -59.54 -164.42 REMARK 500 2 LYS A 372 -161.50 -121.73 REMARK 500 2 LYS A 373 -66.02 -128.66 REMARK 500 2 SER A 376 63.87 -163.62 REMARK 500 2 SER A 378 30.40 -94.84 REMARK 500 2 LYS A 381 -89.57 53.07 REMARK 500 2 ALY A 382 -156.58 30.08 REMARK 500 2 PHE A 385 -47.30 -136.25 REMARK 500 2 SER B1078 -58.99 -133.01 REMARK 500 2 ILE B1084 -62.90 -90.92 REMARK 500 2 PHE B1085 -67.30 -175.66 REMARK 500 2 LEU B1101 -77.70 -70.98 REMARK 500 2 ARG B1103 -93.68 -121.61 REMARK 500 2 GLN B1104 35.02 -177.26 REMARK 500 2 PRO B1110 47.36 -84.81 REMARK 500 2 GLN B1113 53.58 -162.49 REMARK 500 2 PRO B1114 -81.99 -77.84 REMARK 500 2 GLN B1118 -73.14 -59.30 REMARK 500 2 LEU B1119 -145.66 -73.79 REMARK 500 2 TYR B1125 -169.94 -114.38 REMARK 500 2 PHE B1126 -56.64 67.71 REMARK 500 2 LYS B1130 -75.22 -64.00 REMARK 500 2 ASP B1134 153.56 72.31 REMARK 500 2 ARG B1169 -86.55 -127.68 REMARK 500 2 LYS B1170 -68.45 -173.58 REMARK 500 2 SER B1172 -158.44 -175.68 REMARK 500 2 ARG B1173 39.60 -96.37 REMARK 500 2 VAL B1174 -46.83 -142.66 REMARK 500 REMARK 500 THIS ENTRY HAS 566 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1JSP A 367 386 UNP P04637 P53_HUMAN 367 386 DBREF 1JSP B 1081 1197 UNP Q92793 CBP_HUMAN 1081 1197 SEQADV 1JSP ALY A 382 UNP P04637 LYS 382 MODIFIED RESIDUE SEQADV 1JSP GLY B 1077 UNP Q92793 CLONING ARTIFACT SEQADV 1JSP SER B 1078 UNP Q92793 CLONING ARTIFACT SEQADV 1JSP HIS B 1079 UNP Q92793 CLONING ARTIFACT SEQADV 1JSP MET B 1080 UNP Q92793 CLONING ARTIFACT SEQRES 1 A 20 SER HIS LEU LYS SER LYS LYS GLY GLN SER THR SER ARG SEQRES 2 A 20 HIS LYS ALY LEU MET PHE LYS SEQRES 1 B 121 GLY SER HIS MET ARG LYS LYS ILE PHE LYS PRO GLU GLU SEQRES 2 B 121 LEU ARG GLN ALA LEU MET PRO THR LEU GLU ALA LEU TYR SEQRES 3 B 121 ARG GLN ASP PRO GLU SER LEU PRO PHE ARG GLN PRO VAL SEQRES 4 B 121 ASP PRO GLN LEU LEU GLY ILE PRO ASP TYR PHE ASP ILE SEQRES 5 B 121 VAL LYS ASN PRO MET ASP LEU SER THR ILE LYS ARG LYS SEQRES 6 B 121 LEU ASP THR GLY GLN TYR GLN GLU PRO TRP GLN TYR VAL SEQRES 7 B 121 ASP ASP VAL TRP LEU MET PHE ASN ASN ALA TRP LEU TYR SEQRES 8 B 121 ASN ARG LYS THR SER ARG VAL TYR LYS PHE CYS SER LYS SEQRES 9 B 121 LEU ALA GLU VAL PHE GLU GLN GLU ILE ASP PRO VAL MET SEQRES 10 B 121 GLN SER LEU GLY MODRES 1JSP ALY A 382 LYS N(6)-ACETYLLYSINE HET ALY A 382 26 HETNAM ALY N(6)-ACETYLLYSINE FORMUL 1 ALY C8 H16 N2 O3 HELIX 1 1 LYS B 1086 TYR B 1102 1 17 HELIX 2 2 ASP B 1105 LEU B 1109 5 5 HELIX 3 3 ASP B 1134 LYS B 1141 1 8 HELIX 4 4 GLU B 1149 ASN B 1163 1 15 HELIX 5 5 CYS B 1178 MET B 1193 1 16 LINK C LYS A 381 N ALY A 382 1555 1555 1.32 LINK C ALY A 382 N LEU A 383 1555 1555 1.31 CISPEP 1 LEU B 1109 PRO B 1110 4 1.80 CISPEP 2 ILE B 1122 PRO B 1123 7 16.21 CISPEP 3 ASP B 1116 PRO B 1117 8 4.54 CISPEP 4 ASP B 1116 PRO B 1117 9 -0.93 CISPEP 5 ASP B 1116 PRO B 1117 11 -1.39 CISPEP 6 LEU B 1109 PRO B 1110 14 2.61 CISPEP 7 LEU B 1109 PRO B 1110 15 1.34 CISPEP 8 GLN B 1113 PRO B 1114 16 1.69 CISPEP 9 LEU B 1109 PRO B 1110 17 2.02 CISPEP 10 ILE B 1122 PRO B 1123 17 13.82 CISPEP 11 GLN B 1113 PRO B 1114 19 0.03 CISPEP 12 ASP B 1105 PRO B 1106 20 -3.87 CISPEP 13 LEU B 1109 PRO B 1110 20 2.11 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