Header list of 1p4q.pdb file
Complete list - b 1 2 Bytes
HEADER TRANSCRIPTION/TRANSFERASE 23-APR-03 1P4Q TITLE SOLUTION STRUCTURE OF THE CITED2 TRANSACTIVATION DOMAIN IN COMPLEX TITLE 2 WITH THE P300 CH1 DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: CBP/P300-INTERACTING TRANSACTIVATOR 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: TRANSACTIVATION DOMAIN; COMPND 5 SYNONYM: MSG-RELATED PROTEIN 1, MRG1 PROTEIN, P35SRJ; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: E1A-ASSOCIATED PROTEIN P300; COMPND 9 CHAIN: B; COMPND 10 FRAGMENT: CYSTEINE/HISTIDINE-RICH 1 (CH1) DOMAIN; COMPND 11 SYNONYM: P300; COMPND 12 EC: 2.3.1.48; COMPND 13 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: CITED2 OR MRG1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: EP300 OR P300; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PACYC KEYWDS HELIX, PROTEIN-PROTEIN COMPLEX, TRANSCRIPTION-TRANSFERASE COMPLEX EXPDTA SOLUTION NMR NUMMDL 17 AUTHOR S.J.FREEDMAN,Z.-Y.J.SUN,A.L.KUNG,D.S.FRANCE,G.WAGNER,M.J.ECK REVDAT 3 01-FEB-17 1P4Q 1 AUTHOR VERSN REVDAT 2 24-FEB-09 1P4Q 1 VERSN REVDAT 1 01-JUL-03 1P4Q 0 JRNL AUTH S.J.FREEDMAN,Z.Y.SUN,A.L.KUNG,D.S.FRANCE,G.WAGNER,M.J.ECK JRNL TITL STRUCTURAL BASIS FOR NEGATIVE REGULATION OF JRNL TITL 2 HYPOXIA-INDUCIBLE FACTOR-1ALPHA BY CITED2. JRNL REF NAT.STRUCT.BIOL. V. 10 504 2003 JRNL REFN ISSN 1072-8368 JRNL PMID 12778114 JRNL DOI 10.1038/NSB936 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 TITL STRUCTURAL BASIS FOR RECRUITMENT OF CBP/P300 BY REMARK 1 TITL 2 HYPOXIA-INDUCIBLE FACTOR-1ALPHA REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 99 5367 2002 REMARK 1 REFN ISSN 0027-8424 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1P4Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-03. REMARK 100 THE RCSB ID CODE IS RCSB019004. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6 REMARK 210 IONIC STRENGTH : 100MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM CITED/P300;10MM DEUT-MES, PH REMARK 210 6.0; 100MM NACL; 0.1MM ZNSO4; 1MM REMARK 210 CITED/P300 U-15N;10MM DEUT-MES, REMARK 210 PH 6.0; 100MM NACL; 0.1MM ZNSO4; REMARK 210 1MM CITED/P300 U-15N;10MM DEUT- REMARK 210 MES, PH 6.0; 100MM NACL; 0.1MM REMARK 210 ZNSO4; 1MM CITED/P300 U-15N,13C; REMARK 210 10MM DEUT-MES, PH 6.0; 100MM REMARK 210 NACL; 0.1MM ZNSO4; 1MM CITED/P300 REMARK 210 U-15N,13C;10MM DEUT-MES, PH 6.0; REMARK 210 100MM NACL; 0.1MM ZNSO4; 1MM REMARK 210 CITED/P300 10%13C;10MM DEUT-MES, REMARK 210 PH 6.0; 100MM NACL; 0.1MM ZNSO4 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N-SEPARATED_ REMARK 210 NOESY; 3D_13C-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : VNMR 5.3, PROSA 3.7, XEASY REMARK 210 1.3.13, CYANA 1.0.4 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 25 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST 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 LEU B 115 H GLN B 119 1.49 REMARK 500 O SER B 173 H ILE B 177 1.50 REMARK 500 O HIS B 170 H SER B 174 1.55 REMARK 500 O HIS B 180 H CYS B 184 1.58 REMARK 500 O ILE B 116 H LEU B 120 1.58 REMARK 500 O LEU B 120 H LEU B 124 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 SER A 4 132.69 -176.91 REMARK 500 1 SER A 8 89.81 -159.76 REMARK 500 1 ILE A 11 156.87 52.35 REMARK 500 1 ASP A 12 44.35 -98.46 REMARK 500 1 LEU A 41 89.05 -35.44 REMARK 500 1 GLN A 43 170.86 -56.00 REMARK 500 1 ALA B 105 62.13 -176.49 REMARK 500 1 ALA B 108 -173.75 57.71 REMARK 500 1 ASN B 143 -71.06 -59.19 REMARK 500 1 ALA B 169 -102.90 33.16 REMARK 500 1 THR B 185 131.97 -170.09 REMARK 500 1 ARG B 186 -165.31 63.23 REMARK 500 1 HIS B 187 -164.61 65.57 REMARK 500 1 VAL B 191 -73.78 -98.05 REMARK 500 2 SER A 2 -173.21 58.79 REMARK 500 2 SER A 4 -69.81 -165.73 REMARK 500 2 SER A 8 48.13 -163.92 REMARK 500 2 ASN A 9 84.02 62.73 REMARK 500 2 VAL A 10 -91.53 -77.79 REMARK 500 2 ILE A 11 -159.04 -83.52 REMARK 500 2 ARG A 32 41.08 -178.99 REMARK 500 2 SER B 103 93.07 -62.15 REMARK 500 2 ALA B 108 135.15 175.70 REMARK 500 2 ALA B 169 -102.14 33.24 REMARK 500 2 ARG B 186 44.79 -97.72 REMARK 500 2 HIS B 187 -66.76 -98.06 REMARK 500 2 ASP B 188 81.83 -165.31 REMARK 500 2 VAL B 191 -75.31 -97.83 REMARK 500 2 ASP B 200 122.85 62.67 REMARK 500 3 SER A 4 84.39 60.85 REMARK 500 3 SER A 8 62.84 62.28 REMARK 500 3 ASN A 9 58.49 164.63 REMARK 500 3 VAL A 10 -91.51 -78.99 REMARK 500 3 THR A 13 34.51 -89.25 REMARK 500 3 ASP A 31 35.06 -97.07 REMARK 500 3 ARG A 32 48.94 -174.99 REMARK 500 3 THR A 50 -83.41 -77.04 REMARK 500 3 SER B 103 95.75 -166.06 REMARK 500 3 ALA B 105 -124.86 -115.75 REMARK 500 3 HIS B 106 -63.22 74.52 REMARK 500 3 ALA B 108 117.37 176.25 REMARK 500 3 HIS B 127 -70.48 -63.64 REMARK 500 3 ALA B 169 -104.81 35.42 REMARK 500 3 THR B 185 59.05 -159.70 REMARK 500 3 HIS B 187 89.47 -59.56 REMARK 500 3 ASP B 188 -44.30 -162.70 REMARK 500 3 VAL B 191 -73.46 -96.98 REMARK 500 3 ALA B 198 92.82 53.62 REMARK 500 4 SER A 2 -66.46 -128.62 REMARK 500 4 SER A 6 102.36 -162.82 REMARK 500 REMARK 500 THIS ENTRY HAS 274 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 1 ZN B 301 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS B 125 NE2 REMARK 620 2 CYS B 129 SG 95.4 REMARK 620 3 CYS B 142 SG 123.6 73.6 REMARK 620 4 CYS B 147 SG 123.9 111.5 111.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 1 ZN B 302 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS B 171 SG REMARK 620 2 CYS B 160 SG 62.9 REMARK 620 3 HIS B 156 NE2 69.8 125.9 REMARK 620 4 CYS B 166 SG 88.8 95.0 109.0 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 1 ZN B 303 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS B 184 SG REMARK 620 2 CYS B 189 SG 56.6 REMARK 620 3 HIS B 180 NE2 119.2 120.1 REMARK 620 4 CYS B 192 SG 101.7 110.3 126.7 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 303 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1L3E RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE HIF-1ALPHA C-TERMINAL REMARK 900 TRANSACTIVATION DOMAIN IN COMPLEX WITH THE P300 CH1 DOMAIN DBREF 1P4Q A 9 52 UNP Q99967 CITE2_HUMAN 216 259 DBREF 1P4Q B 101 201 UNP Q09472 EP300_HUMAN 323 423 SEQADV 1P4Q GLY A 1 UNP Q99967 CLONING ARTIFACT SEQADV 1P4Q SER A 2 UNP Q99967 CLONING ARTIFACT SEQADV 1P4Q GLY A 3 UNP Q99967 CLONING ARTIFACT SEQADV 1P4Q SER A 4 UNP Q99967 CLONING ARTIFACT SEQADV 1P4Q GLY A 5 UNP Q99967 CLONING ARTIFACT SEQADV 1P4Q SER A 6 UNP Q99967 CLONING ARTIFACT SEQADV 1P4Q GLY A 7 UNP Q99967 CLONING ARTIFACT SEQADV 1P4Q SER A 8 UNP Q99967 CLONING ARTIFACT SEQRES 1 A 52 GLY SER GLY SER GLY SER GLY SER ASN VAL ILE ASP THR SEQRES 2 A 52 ASP PHE ILE ASP GLU GLU VAL LEU MET SER LEU VAL ILE SEQRES 3 A 52 GLU MET GLY LEU ASP ARG ILE LYS GLU LEU PRO GLU LEU SEQRES 4 A 52 TRP LEU GLY GLN ASN GLU PHE ASP PHE MET THR ASP PHE SEQRES 1 B 101 MET GLY SER GLY ALA HIS THR ALA ASP PRO GLU LYS ARG SEQRES 2 B 101 LYS LEU ILE GLN GLN GLN LEU VAL LEU LEU LEU HIS ALA SEQRES 3 B 101 HIS LYS CYS GLN ARG ARG GLU GLN ALA ASN GLY GLU VAL SEQRES 4 B 101 ARG GLN CYS ASN LEU PRO HIS CYS ARG THR MET LYS ASN SEQRES 5 B 101 VAL LEU ASN HIS MET THR HIS CYS GLN SER GLY LYS SER SEQRES 6 B 101 CYS GLN VAL ALA HIS CYS ALA SER SER ARG GLN ILE ILE SEQRES 7 B 101 SER HIS TRP LYS ASN CYS THR ARG HIS ASP CYS PRO VAL SEQRES 8 B 101 CYS LEU PRO LEU LYS ASN ALA GLY ASP LYS HET ZN B 301 1 HET ZN B 302 1 HET ZN B 303 1 HETNAM ZN ZINC ION FORMUL 3 ZN 3(ZN 2+) HELIX 1 1 GLU A 19 GLY A 29 1 11 HELIX 2 2 PHE A 46 THR A 50 5 5 HELIX 3 3 PRO B 110 ALA B 135 1 26 HELIX 4 4 HIS B 146 CYS B 160 1 15 HELIX 5 5 HIS B 170 CYS B 184 1 15 HELIX 6 6 VAL B 191 ALA B 198 1 8 SSBOND 1 CYS B 129 CYS B 142 1555 1555 2.82 SSBOND 2 CYS B 160 CYS B 171 1555 1555 2.45 SSBOND 3 CYS B 184 CYS B 189 1555 1555 2.23 LINK ZN ZN B 301 NE2 HIS B 125 1555 1555 2.05 LINK ZN ZN B 301 SG CYS B 129 1555 1555 2.35 LINK ZN ZN B 301 SG CYS B 142 1555 1555 2.35 LINK ZN ZN B 301 SG CYS B 147 1555 1555 2.35 LINK ZN ZN B 302 SG CYS B 171 1555 1555 2.36 LINK ZN ZN B 302 SG CYS B 160 1555 1555 2.34 LINK ZN ZN B 302 NE2 HIS B 156 1555 1555 2.04 LINK ZN ZN B 302 SG CYS B 166 1555 1555 2.35 LINK ZN ZN B 303 SG CYS B 184 1555 1555 2.35 LINK ZN ZN B 303 SG CYS B 189 1555 1555 2.35 LINK ZN ZN B 303 NE2 HIS B 180 1555 1555 2.05 LINK ZN ZN B 303 SG CYS B 192 1555 1555 2.35 SITE 1 AC1 4 HIS B 125 CYS B 129 CYS B 142 CYS B 147 SITE 1 AC2 4 HIS B 156 CYS B 160 CYS B 166 CYS B 171 SITE 1 AC3 5 HIS B 180 CYS B 184 CYS B 189 VAL B 191 SITE 2 AC3 5 CYS B 192 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 - b 1 2 Bytes