Header list of 1l3e.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION 26-FEB-02 1L3E
TITLE NMR STRUCTURES OF THE HIF-1ALPHA CTAD/P300 CH1 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOXIA INDUCIBLE FACTOR-1 ALPHA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL TRANSACTIVATION DOMAIN (CTAD);
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: P300 PROTEIN;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: CYSTEINE/HISTIDINE-RICH 1 DOMAIN (CH1);
COMPND 10 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: HYPOXIA INDUCIBLE FACTOR-1 ALPHA;
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: 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: P300;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PACYC
KEYWDS PROTEIN-PROTEIN COMPLEX, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 17
AUTHOR S.J.FREEDMAN,Z.J.SUN,F.POY,A.L.KUNG,D.M.LIVINGSTON,G.WAGNER,M.J.ECK
REVDAT 5 23-FEB-22 1L3E 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1L3E 1 VERSN
REVDAT 3 01-APR-03 1L3E 1 JRNL
REVDAT 2 11-FEB-03 1L3E 1 HEADER
REVDAT 1 24-APR-02 1L3E 0
JRNL AUTH S.J.FREEDMAN,Z.Y.SUN,F.POY,A.L.KUNG,D.M.LIVINGSTON,G.WAGNER,
JRNL AUTH 2 M.J.ECK
JRNL TITL STRUCTURAL BASIS FOR RECRUITMENT OF CBP/P300 BY
JRNL TITL 2 HYPOXIA-INDUCIBLE FACTOR-1 ALPHA.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 5367 2002
JRNL REFN ISSN 0027-8424
JRNL PMID 11959990
JRNL DOI 10.1073/PNAS.082117899
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1378 RESTRAINTS; 1126 ARE NOE-DERIVED DISTANCE RESTRAINTS
REMARK 3 (INCLUDING 1013 INTRAMOLECULAR, 113 INTERMOLECULAR), 158
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, AND 94 HYDROGEN BOND RESTRAINTS
REMARK 4
REMARK 4 1L3E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000015604.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM CTAD/CH1 COMPLEX U-15N,13C;
REMARK 210 0.1MM ZNSO4; 1MM DTT; 1MM CTAD/
REMARK 210 CH1 COMPLEX U-15N,13C; 0.1MM
REMARK 210 ZNSO4; 1MM DTT; 1MM CTAD/CH1
REMARK 210 COMPLEX U-15N; 0.1MM ZNSO4; 1MM
REMARK 210 DTT; 1MM CTAD/CH1 COMPLEX; 0.1MM
REMARK 210 ZNSO4; 1MM DTT; 1MM CTAD/CH1
REMARK 210 COMPLEX 10% U-13C; 0.1MM ZNSO4;
REMARK 210 1MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY;
REMARK 210 2D_NOESY; 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; UNITY; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 5.3, PROSA 3.7, XEASY
REMARK 210 1.3.13, DYANA 1.4
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17
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: 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 HIS B 125 H CYS B 129 1.50
REMARK 500 O MET B 150 H LEU B 154 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 2 89.49 -63.72
REMARK 500 1 MET A 3 57.47 -112.57
REMARK 500 1 PRO A 9 104.95 -50.74
REMARK 500 1 ALA A 20 91.43 -164.43
REMARK 500 1 GLN A 23 47.17 78.29
REMARK 500 1 SER A 25 99.47 64.24
REMARK 500 1 ARG A 26 149.91 -38.63
REMARK 500 1 GLN A 30 -72.73 -143.22
REMARK 500 1 ASP A 39 44.66 -92.82
REMARK 500 1 HIS B 106 64.94 62.30
REMARK 500 1 ALA B 108 107.16 179.78
REMARK 500 1 HIS B 125 -71.38 -61.28
REMARK 500 1 CYS B 142 141.45 -38.69
REMARK 500 1 LEU B 144 90.65 -162.81
REMARK 500 1 CYS B 160 64.79 -106.02
REMARK 500 1 LYS B 164 -43.93 83.94
REMARK 500 1 CYS B 166 -162.56 -77.15
REMARK 500 1 ARG B 186 60.79 61.49
REMARK 500 1 ASP B 188 46.88 -108.20
REMARK 500 1 CYS B 189 104.50 -46.44
REMARK 500 1 ASN B 197 96.85 -43.87
REMARK 500 2 ASP A 4 97.86 -50.00
REMARK 500 2 GLU A 5 19.57 -140.64
REMARK 500 2 SER A 6 127.44 175.13
REMARK 500 2 PRO A 9 104.85 -50.49
REMARK 500 2 GLN A 23 40.82 77.05
REMARK 500 2 SER A 25 -73.39 -57.30
REMARK 500 2 ARG A 26 -166.28 -128.88
REMARK 500 2 LEU A 28 -74.44 -65.12
REMARK 500 2 GLN A 30 -87.90 -133.96
REMARK 500 2 ASP A 39 46.23 -96.88
REMARK 500 2 GLN A 40 51.07 -104.78
REMARK 500 2 HIS B 106 92.15 -176.71
REMARK 500 2 THR B 107 106.29 -173.26
REMARK 500 2 ALA B 108 77.98 -64.48
REMARK 500 2 ALA B 126 -35.48 -36.17
REMARK 500 2 CYS B 142 99.07 -38.85
REMARK 500 2 LYS B 164 29.81 43.40
REMARK 500 2 SER B 165 38.87 174.88
REMARK 500 2 ASP B 188 76.63 67.82
REMARK 500 2 CYS B 189 64.20 -158.06
REMARK 500 2 VAL B 191 -63.94 -90.32
REMARK 500 2 LYS B 196 58.22 -154.49
REMARK 500 2 ALA B 198 172.66 64.75
REMARK 500 3 SER A 6 135.78 176.08
REMARK 500 3 ALA A 20 82.18 -150.93
REMARK 500 3 GLN A 23 60.29 75.45
REMARK 500 3 SER A 25 100.47 69.88
REMARK 500 3 ARG A 26 170.20 -46.49
REMARK 500 3 GLN A 30 -74.30 -145.15
REMARK 500
REMARK 500 THIS ENTRY HAS 339 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 ZN B 202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 125 NE2
REMARK 620 2 CYS B 129 SG 77.0
REMARK 620 3 CYS B 142 SG 154.8 93.6
REMARK 620 4 CYS B 147 SG 86.8 86.4 116.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 203 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 156 NE2
REMARK 620 2 CYS B 160 SG 146.2
REMARK 620 3 CYS B 166 SG 122.8 60.6
REMARK 620 4 CYS B 171 SG 88.0 84.4 144.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 204 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 180 NE2
REMARK 620 2 CYS B 184 SG 141.9
REMARK 620 3 CYS B 189 SG 144.8 35.5
REMARK 620 4 CYS B 192 SG 96.2 120.5 107.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZN1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: Zinc coordinate site 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZN2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: Zinc coordinate site 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZN3
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: Zinc coordinate site 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 204
DBREF 1L3E A 1 42 UNP Q16665 HIF1A_HUMAN 785 826
DBREF 1L3E B 101 201 UNP Q09472 EP300_HUMAN 323 423
SEQADV 1L3E GLY A 1 UNP Q16665 GLN 785 CLONING ARTIFACT
SEQRES 1 A 42 GLY SER MET ASP GLU SER GLY LEU PRO GLN LEU THR SER
SEQRES 2 A 42 TYR ASP CYS GLU VAL ASN ALA PRO ILE GLN GLY SER ARG
SEQRES 3 A 42 ASN LEU LEU GLN GLY GLU GLU LEU LEU ARG ALA LEU ASP
SEQRES 4 A 42 GLN VAL ASN
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 202 1
HET ZN B 203 1
HET ZN B 204 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 3(ZN 2+)
HELIX 1 1 THR A 12 ALA A 20 1 9
HELIX 2 2 GLY A 31 ASP A 39 1 9
HELIX 3 3 ASP B 109 GLU B 111 5 3
HELIX 4 4 LYS B 112 GLN B 134 1 23
HELIX 5 5 LEU B 144 THR B 158 1 15
HELIX 6 6 VAL B 168 CYS B 184 1 17
HELIX 7 7 VAL B 191 ASN B 197 1 7
SSBOND 1 CYS B 160 CYS B 166 1555 1555 2.37
SSBOND 2 CYS B 184 CYS B 189 1555 1555 1.44
LINK NE2 HIS B 125 ZN ZN B 202 1555 1555 2.05
LINK SG CYS B 129 ZN ZN B 202 1555 1555 2.35
LINK SG CYS B 142 ZN ZN B 202 1555 1555 2.35
LINK SG CYS B 147 ZN ZN B 202 1555 1555 2.35
LINK NE2 HIS B 156 ZN ZN B 203 1555 1555 2.05
LINK SG CYS B 160 ZN ZN B 203 1555 1555 2.35
LINK SG CYS B 166 ZN ZN B 203 1555 1555 2.35
LINK SG CYS B 171 ZN ZN B 203 1555 1555 2.35
LINK NE2 HIS B 180 ZN ZN B 204 1555 1555 2.05
LINK SG CYS B 184 ZN ZN B 204 1555 1555 2.35
LINK SG CYS B 189 ZN ZN B 204 1555 1555 2.35
LINK SG CYS B 192 ZN ZN B 204 1555 1555 2.35
SITE 1 ZN1 4 HIS B 125 CYS B 129 CYS B 142 CYS B 147
SITE 1 ZN2 4 HIS B 156 CYS B 160 CYS B 166 CYS B 171
SITE 1 ZN3 4 HIS B 180 CYS B 184 CYS B 189 CYS B 192
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 4 HIS B 180 CYS B 184 CYS B 189 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 23 2 Bytes