Header list of 2fej.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION 16-DEC-05 2FEJ
TITLE SOLUTION STRUCTURE OF HUMAN P53 DNA BINDING DOMAIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA BINDING DOMAIN;
COMPND 5 SYNONYM: TUMOR SUPPRESSOR P53, PHOSPHOPROTEIN P53, ANTIGEN NY-CO-13;
COMPND 6 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: TP53, P53;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: C41(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSET
KEYWDS BETA SANDWICH, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 36
AUTHOR J.M.PEREZ-CANADILLAS,H.TIDOW,S.M.FREUND,T.J.RUTHERFORD,H.C.ANG,
AUTHOR 2 A.R.FERSHT
REVDAT 4 09-MAR-22 2FEJ 1 REMARK
REVDAT 3 24-FEB-09 2FEJ 1 VERSN
REVDAT 2 07-MAR-06 2FEJ 1 JRNL
REVDAT 1 31-JAN-06 2FEJ 0
JRNL AUTH J.M.PEREZ-CANADILLAS,H.TIDOW,S.M.FREUND,T.J.RUTHERFORD,
JRNL AUTH 2 H.C.ANG,A.R.FERSHT
JRNL TITL SOLUTION STRUCTURE OF P53 CORE DOMAIN: STRUCTURAL BASIS FOR
JRNL TITL 2 ITS INSTABILITY
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 2109 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 16461916
JRNL DOI 10.1073/PNAS.0510941103
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER ET AL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FEJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000035782.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.1
REMARK 210 IONIC STRENGTH : 150 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.4 MM P53 CORE U-15N,13C, 2H;
REMARK 210 25 MM TRIS-HCL PH 7.1; 150 MM
REMARK 210 NACL; 90% H2O, 10% D2O; 0.3 MM
REMARK 210 P53 CORE U-15N,13C, 2H + REVERSE
REMARK 210 ILV 13CH3 ; 25 MM TRIS-HCL PH
REMARK 210 7.1; 150 MM NACL; 90% H2O, 10%
REMARK 210 D2O; 0.3 MM P53 CORE U-15N,13C,
REMARK 210 2H + REVERSE ILV 13CH3 + REVERSE
REMARK 210 TYR ; 25 MM TRIS-HCL PH 7.1; 150
REMARK 210 MM NACL; 100% D2O; 0.3 MM P53
REMARK 210 CORE U-15N,13C, 2H + MET AND PHE
REMARK 210 (1H); 25 MM TRIS-HCL PH 7.1; 150
REMARK 210 MM NACL; 90% H2O, 10% D2O; 0.3
REMARK 210 MM P53 CORE U-15N,13C, 2H + MET
REMARK 210 AND ARG (1H); 25 MM TRIS-HCL PH
REMARK 210 7.1; 150 MM NACL; 90% H2O, 10%
REMARK 210 D2O; 0.4 MM P53 CORE U-15N,13C,
REMARK 210 2H (50%); 25 MM TRIS-HCL PH 7.1;
REMARK 210 150 MM NACL; 90% H2O, 10% D2O;
REMARK 210 0.4 MM P53 CORE N/A; 25 MM TRIS-
REMARK 210 HCL PH 7.1; 150 MM NACL; 90% H2O,
REMARK 210 10% D2O; 0.4 MM P53 CORE N/A;
REMARK 210 25 MM TRIS-HCL PH 7.1; 150 MM
REMARK 210 NACL; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; AVANCE; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 36
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 A 152 HG1 THR A 155 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 96 -70.92 -67.11
REMARK 500 1 TYR A 103 -80.25 -80.68
REMARK 500 1 LYS A 120 -36.00 -175.73
REMARK 500 1 SER A 121 109.42 -163.54
REMARK 500 1 THR A 123 -72.49 -79.02
REMARK 500 1 PRO A 152 128.84 -36.66
REMARK 500 1 GLN A 165 97.36 -61.36
REMARK 500 1 HIS A 168 28.18 -147.76
REMARK 500 1 ASP A 184 -52.05 -121.07
REMARK 500 1 ASP A 186 -77.58 -136.73
REMARK 500 1 LEU A 188 -3.31 78.49
REMARK 500 1 LEU A 201 -55.12 -122.97
REMARK 500 1 ASP A 207 64.06 -177.88
REMARK 500 1 PRO A 222 140.84 -35.61
REMARK 500 1 VAL A 225 94.26 -53.77
REMARK 500 1 MET A 237 43.98 -99.78
REMARK 500 1 CYS A 238 115.04 -172.61
REMARK 500 1 CYS A 242 88.80 -56.96
REMARK 500 1 ASN A 247 52.18 71.44
REMARK 500 1 CYS A 275 30.67 -165.52
REMARK 500 1 ALA A 276 24.02 49.92
REMARK 500 1 CYS A 277 72.19 -152.55
REMARK 500 1 LYS A 292 72.64 56.17
REMARK 500 1 GLU A 294 -63.33 -174.35
REMARK 500 1 PRO A 295 -87.37 -67.10
REMARK 500 1 HIS A 296 166.48 56.91
REMARK 500 2 SER A 99 172.83 -58.03
REMARK 500 2 SER A 116 -161.08 -178.87
REMARK 500 2 SER A 121 93.24 175.40
REMARK 500 2 SER A 149 -148.23 -118.81
REMARK 500 2 PRO A 152 119.09 -34.62
REMARK 500 2 PRO A 153 90.36 -60.25
REMARK 500 2 CYS A 182 152.58 -40.73
REMARK 500 2 ASP A 184 -174.90 49.39
REMARK 500 2 SER A 185 -177.04 -67.77
REMARK 500 2 LEU A 188 -47.43 -162.33
REMARK 500 2 LEU A 201 26.50 -154.60
REMARK 500 2 ARG A 202 35.94 -177.69
REMARK 500 2 PRO A 222 156.46 -35.19
REMARK 500 2 VAL A 225 93.70 -56.66
REMARK 500 2 MET A 237 50.83 -112.65
REMARK 500 2 CYS A 238 111.15 -164.18
REMARK 500 2 CYS A 242 93.43 -51.93
REMARK 500 2 CYS A 275 34.54 -161.26
REMARK 500 2 CYS A 277 72.59 -174.80
REMARK 500 2 PRO A 295 -170.11 -54.86
REMARK 500 3 SER A 95 -74.48 -163.17
REMARK 500 3 SER A 96 -175.24 60.95
REMARK 500 3 PRO A 98 -170.80 -54.32
REMARK 500 3 GLN A 104 -63.98 70.32
REMARK 500
REMARK 500 THIS ENTRY HAS 880 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 A 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 176 SG
REMARK 620 2 HIS A 179 ND1 115.8
REMARK 620 3 CYS A 238 SG 131.0 96.8
REMARK 620 4 CYS A 242 SG 96.1 106.9 108.9
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 A 1
DBREF 2FEJ A 94 297 UNP Q9NP68 P53_HUMAN 94 297
SEQRES 1 A 204 SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER
SEQRES 2 A 204 TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA
SEQRES 3 A 204 LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS
SEQRES 4 A 204 MET PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU
SEQRES 5 A 204 TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG
SEQRES 6 A 204 ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU
SEQRES 7 A 204 VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP
SEQRES 8 A 204 SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL
SEQRES 9 A 204 GLU GLY ASN LEU ARG VAL GLU TYR LEU ASP ASP ARG ASN
SEQRES 10 A 204 THR PHE ARG HIS SER VAL VAL VAL PRO TYR GLU PRO PRO
SEQRES 11 A 204 GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR
SEQRES 12 A 204 MET CYS ASN SER SER CYS MET GLY GLY MET ASN ARG ARG
SEQRES 13 A 204 PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY
SEQRES 14 A 204 ASN LEU LEU GLY ARG ASN SER PHE GLU VAL ARG VAL CYS
SEQRES 15 A 204 ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN
SEQRES 16 A 204 LEU ARG LYS LYS GLY GLU PRO HIS HIS
HET ZN A 1 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 GLN A 165 MET A 169 5 5
HELIX 2 2 CYS A 176 SER A 183 1 8
HELIX 3 3 CYS A 277 LYS A 292 1 16
SHEET 1 A 4 ARG A 110 GLY A 112 0
SHEET 2 A 4 THR A 140 TRP A 146 -1 O TRP A 146 N ARG A 110
SHEET 3 A 4 THR A 230 TYR A 236 -1 O THR A 230 N LEU A 145
SHEET 4 A 4 ILE A 195 GLU A 198 -1 N ARG A 196 O ASN A 235
SHEET 1 B 7 THR A 125 SER A 127 0
SHEET 2 B 7 LYS A 132 CYS A 135 -1 O LYS A 132 N SER A 127
SHEET 3 B 7 LEU A 264 VAL A 274 1 O ARG A 273 N CYS A 135
SHEET 4 B 7 ILE A 251 GLU A 258 -1 N LEU A 257 O LEU A 265
SHEET 5 B 7 ARG A 156 ILE A 162 -1 N ARG A 156 O GLU A 258
SHEET 6 B 7 SER A 215 PRO A 219 -1 O VAL A 216 N ALA A 159
SHEET 7 B 7 GLU A 204 TYR A 205 -1 N GLU A 204 O VAL A 217
LINK ZN ZN A 1 SG CYS A 176 1555 1555 2.35
LINK ZN ZN A 1 ND1 HIS A 179 1555 1555 2.33
LINK ZN ZN A 1 SG CYS A 238 1555 1555 2.41
LINK ZN ZN A 1 SG CYS A 242 1555 1555 2.41
SITE 1 AC1 4 CYS A 176 HIS A 179 CYS A 238 CYS A 242
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 - r 9 2 Bytes