Header list of 1p97.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION 09-MAY-03 1P97
TITLE NMR STRUCTURE OF THE C-TERMINAL PAS DOMAIN OF HIF2A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOTHELIAL PAS DOMAIN PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL PAS DOMAIN;
COMPND 5 SYNONYM: EPAS-1, MEMBER OF PAS PROTEIN 2, MOP2;
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: EPAS1;
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: PGB1-PARALLEL
KEYWDS MIXED ALPHA-BETA FOLD, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.J.ERBEL,P.B.CARD,O.KARAKUZU,R.K.BRUICK,K.H.GARDNER
REVDAT 3 23-FEB-22 1P97 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1P97 1 VERSN
REVDAT 1 13-JAN-04 1P97 0
JRNL AUTH P.J.ERBEL,P.B.CARD,O.KARAKUZU,R.K.BRUICK,K.H.GARDNER
JRNL TITL STRUCTURAL BASIS FOR PAS DOMAIN HETERODIMERIZATION IN THE
JRNL TITL 2 BASIC HELIX-LOOP-HELIX-PAS TRANSCRIPTION FACTOR
JRNL TITL 3 HYPOXIA-INDUCIBLE FACTOR.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 100 15504 2003
JRNL REFN ISSN 0027-8424
JRNL PMID 14668441
JRNL DOI 10.1073/PNAS.2533374100
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1P97 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019165.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.3
REMARK 210 IONIC STRENGTH : 15 MM - 75 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.9MM HIF2A (240-350) U-15N,13C;
REMARK 210 50 MM TRIS BUFFER, 15 MM NACL, 5
REMARK 210 MM DTT (PH 7.3); 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 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 : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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: 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 HB3 HIS A 12 HA MET A 16 1.30
REMARK 500 OE2 GLU A 51 HZ1 LYS A 55 1.58
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 ALA A 2 81.90 57.21
REMARK 500 1 SER A 5 155.47 64.42
REMARK 500 1 MET A 14 -85.22 44.59
REMARK 500 1 PHE A 18 114.67 156.26
REMARK 500 1 LEU A 37 92.77 -64.14
REMARK 500 1 TYR A 45 70.10 -68.85
REMARK 500 1 HIS A 46 133.52 74.33
REMARK 500 1 THR A 62 37.13 -147.84
REMARK 500 1 LEU A 96 9.40 57.77
REMARK 500 1 PRO A 98 98.62 -62.69
REMARK 500 1 LEU A 108 -67.67 -90.93
REMARK 500 2 SER A 5 -150.05 -156.02
REMARK 500 2 MET A 16 65.16 63.36
REMARK 500 2 PHE A 18 108.16 157.52
REMARK 500 2 LEU A 37 89.83 -59.16
REMARK 500 2 PHE A 44 -0.66 -151.90
REMARK 500 2 TYR A 45 66.33 -67.82
REMARK 500 2 HIS A 46 103.91 67.17
REMARK 500 2 THR A 62 29.81 -149.73
REMARK 500 2 HIS A 77 31.18 -98.69
REMARK 500 2 LEU A 96 -6.14 63.20
REMARK 500 2 PRO A 98 101.77 -59.20
REMARK 500 3 MET A 14 -78.58 31.83
REMARK 500 3 MET A 16 66.28 62.27
REMARK 500 3 PHE A 18 86.87 146.96
REMARK 500 3 LEU A 37 89.58 -56.87
REMARK 500 3 SER A 40 103.20 -41.66
REMARK 500 3 TYR A 42 -19.83 -49.46
REMARK 500 3 HIS A 46 141.47 77.88
REMARK 500 3 PRO A 98 87.98 -44.40
REMARK 500 3 LEU A 108 -73.25 -92.71
REMARK 500 4 MET A 14 -79.77 39.01
REMARK 500 4 MET A 16 38.72 73.95
REMARK 500 4 PHE A 18 106.46 149.16
REMARK 500 4 LEU A 37 88.95 -59.41
REMARK 500 4 SER A 40 101.75 -39.24
REMARK 500 4 PHE A 44 -2.26 -154.56
REMARK 500 4 TYR A 45 71.32 -68.13
REMARK 500 4 HIS A 46 106.41 69.97
REMARK 500 4 ALA A 75 -160.29 -79.70
REMARK 500 4 PRO A 98 99.01 -64.80
REMARK 500 4 LEU A 108 -67.61 -97.10
REMARK 500 5 ALA A 2 95.25 59.05
REMARK 500 5 ASP A 4 -72.53 -51.45
REMARK 500 5 MET A 14 -93.21 44.79
REMARK 500 5 MET A 16 35.08 71.35
REMARK 500 5 PHE A 18 110.50 155.06
REMARK 500 5 LEU A 37 95.38 -63.36
REMARK 500 5 PHE A 44 -8.84 -154.55
REMARK 500 5 HIS A 46 129.82 76.98
REMARK 500
REMARK 500 THIS ENTRY HAS 242 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 7 TYR A 91 0.06 SIDE CHAIN
REMARK 500 14 TYR A 31 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1P97 A 4 114 UNP Q99814 EPAS1_HUMAN 240 350
SEQADV 1P97 GLY A 1 UNP Q99814 CLONING ARTIFACT
SEQADV 1P97 ALA A 2 UNP Q99814 CLONING ARTIFACT
SEQADV 1P97 MET A 3 UNP Q99814 CLONING ARTIFACT
SEQRES 1 A 114 GLY ALA MET ASP SER LYS THR PHE LEU SER ARG HIS SER
SEQRES 2 A 114 MET ASP MET LYS PHE THR TYR CYS ASP ASP ARG ILE THR
SEQRES 3 A 114 GLU LEU ILE GLY TYR HIS PRO GLU GLU LEU LEU GLY ARG
SEQRES 4 A 114 SER ALA TYR GLU PHE TYR HIS ALA LEU ASP SER GLU ASN
SEQRES 5 A 114 MET THR LYS SER HIS GLN ASN LEU CYS THR LYS GLY GLN
SEQRES 6 A 114 VAL VAL SER GLY GLN TYR ARG MET LEU ALA LYS HIS GLY
SEQRES 7 A 114 GLY TYR VAL TRP LEU GLU THR GLN GLY THR VAL ILE TYR
SEQRES 8 A 114 ASN PRO ARG ASN LEU GLN PRO GLN CYS ILE MET CYS VAL
SEQRES 9 A 114 ASN TYR VAL LEU SER GLU ILE GLU LYS ASN
HELIX 1 1 ARG A 24 ILE A 29 1 6
HELIX 2 2 HIS A 32 LEU A 37 1 6
HELIX 3 3 SER A 40 PHE A 44 5 5
HELIX 4 4 ASP A 49 CYS A 61 1 13
SHEET 1 A 5 TYR A 20 CYS A 21 0
SHEET 2 A 5 LYS A 6 HIS A 12 -1 N ARG A 11 O TYR A 20
SHEET 3 A 5 PRO A 98 GLU A 112 -1 O VAL A 107 N LYS A 6
SHEET 4 A 5 TYR A 80 TYR A 91 -1 N TYR A 80 O GLU A 112
SHEET 5 A 5 GLN A 65 LEU A 74 -1 N MET A 73 O VAL A 81
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