Header list of 1f2r.pdb file
Complete list - 16 20 Bytes
HEADER DNA BINDING PROTEIN 29-MAY-00 1F2R TITLE NMR STRUCTURE OF THE HETERODIMERIC COMPLEX BETWEEN CAD DOMAINS OF CAD TITLE 2 AND ICAD COMPND MOL_ID: 1; COMPND 2 MOLECULE: CASPASE-ACTIVATED DNASE; COMPND 3 CHAIN: C; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN (CAD DOMAIN), RESIDUES 1-87; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: INHIBITOR OF CASPASE-ACTIVATED DNASE; COMPND 8 CHAIN: I; COMPND 9 FRAGMENT: N-TERMINAL DOMAIN (CAD DOMAIN), RESIDUES 1-100; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET32; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 12 ORGANISM_TAXID: 10090; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET32 KEYWDS ALPHA-BETA ROLL, PROTEIN-PROTEIN COMPLEX, DNA BINDING PROTEIN EXPDTA SOLUTION NMR AUTHOR T.OTOMO,H.SAKAHIRA,K.UEGAKI,S.NAGATA,T.YAMAZAKI REVDAT 4 16-FEB-22 1F2R 1 REMARK REVDAT 3 24-FEB-09 1F2R 1 VERSN REVDAT 2 30-AUG-00 1F2R 1 JRNL REVDAT 1 08-JUN-00 1F2R 0 JRNL AUTH T.OTOMO,H.SAKAHIRA,K.UEGAKI,S.NAGATA,T.YAMAZAKI JRNL TITL STRUCTURE OF THE HETERODIMERIC COMPLEX BETWEEN CAD DOMAINS JRNL TITL 2 OF CAD AND ICAD. JRNL REF NAT.STRUCT.BIOL. V. 7 658 2000 JRNL REFN ISSN 1072-8368 JRNL PMID 10932250 JRNL DOI 10.1038/77957 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.UEGAKI,T.OTOMO,H.SAKAHIRA,M.SHIMIZU,N.YUMOTO,Y.KYOGOKU, REMARK 1 AUTH 2 S.NAGATA,T.YAMAZAKI REMARK 1 TITL STRUCTURE OF THE CAD DOMAIN OF CASPASE-ACTIVATED DNASE AND REMARK 1 TITL 2 INTERACTION WITH THE CAD DOMAIN OF ITS INHIBITOR. REMARK 1 REF J.MOL.BIOL. V. 297 1121 2000 REMARK 1 REFN ISSN 0022-2836 REMARK 1 DOI 10.1006/JMBI.2000.3643 REMARK 1 REFERENCE 2 REMARK 1 AUTH M.ENARI,H.SAKAHIRA,H.YOKOYAMA,K.OKAWA,A.IWAMATSU,S.NAGATA REMARK 1 TITL A CASPASE-ACTIVATED DNASE THAT DEGRADES DNA DURING REMARK 1 TITL 2 APOPTOSIS, AND ITS INHIBITOR ICAD. REMARK 1 REF NATURE V. 391 43 1998 REMARK 1 REFN ISSN 0028-0836 REMARK 1 DOI 10.1038/34112 REMARK 1 REFERENCE 3 REMARK 1 AUTH H.SAKAHIRA,M.ENARI,S.NAGATA REMARK 1 TITL CLEAVAGE OF CAD INHIBITOR IN CAD ACTIVATION AND DNA REMARK 1 TITL 2 DEGRADATION DURING APOPTOSIS. REMARK 1 REF NATURE V. 391 96 1998 REMARK 1 REFN ISSN 0028-0836 REMARK 1 DOI 10.1038/34214 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.841, X-PLOR 3.841 REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2646 RESTRAINTS, 2503 ARE REMARK 3 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 93 DIHEDRAL ANGLE RESTRAINTS,50 DISTANCE REMARK 3 RESTRAINTS REMARK 3 FROM HYDROGEN BONDS. REMARK 4 REMARK 4 1F2R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-00. REMARK 100 THE DEPOSITION ID IS D_1000011172. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 6.4 REMARK 210 IONIC STRENGTH : 0 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.6MM CAD U-15N,13C/0.6MM ICAD REMARK 210 UNLABELED; 20MM PHOPHATE BUFFER REMARK 210 PH6.4; 0.6MM CAD U-15N,13C/0.6MM REMARK 210 ICAD UNLABELED; 20MM PHOPHATE REMARK 210 BUFFER PH6.4; 0.6MM ICAD U-15N, REMARK 210 13C/0.6MM CAD UNLABELED; 20MM REMARK 210 PHOPHATE BUFFER PH6.4; 0.6MM REMARK 210 ICAD U-15N,13C/0.6MM CAD REMARK 210 UNLABELED; 20MM PHOPHATE BUFFER REMARK 210 PH6.4 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 4D_13C- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DMX; DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, I 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 ARG I 16 H LEU I 18 1.56 REMARK 500 O PRO I 80 H ASN I 82 1.56 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 CYS C 2 66.76 -114.37 REMARK 500 SER C 47 131.24 170.38 REMARK 500 THR C 59 -148.71 -146.99 REMARK 500 PRO C 67 -159.72 -61.21 REMARK 500 ASN C 68 -136.96 -61.12 REMARK 500 ASP C 69 82.53 -28.68 REMARK 500 GLU C 71 86.32 -59.11 REMARK 500 ALA C 77 73.82 -68.26 REMARK 500 TYR C 84 89.86 -50.31 REMARK 500 SER I 4 102.98 -51.03 REMARK 500 ALA I 7 -31.11 171.79 REMARK 500 ALA I 9 151.24 59.47 REMARK 500 PRO I 10 -157.63 -61.67 REMARK 500 ARG I 16 63.12 63.10 REMARK 500 PRO I 17 58.25 -63.63 REMARK 500 LEU I 18 119.35 57.74 REMARK 500 PRO I 20 83.86 -62.81 REMARK 500 ASN I 26 165.19 -45.90 REMARK 500 ARG I 29 70.63 -64.14 REMARK 500 SER I 37 -71.51 -85.30 REMARK 500 ASP I 53 156.82 -46.10 REMARK 500 VAL I 70 69.91 -106.78 REMARK 500 ASP I 73 30.51 -141.27 REMARK 500 LEU I 79 153.83 -40.89 REMARK 500 PRO I 80 173.36 -59.34 REMARK 500 SER I 81 59.11 -66.81 REMARK 500 ASN I 82 116.78 173.12 REMARK 500 ALA I 89 63.23 -66.65 REMARK 500 ASN I 91 -57.82 -158.46 REMARK 500 THR I 95 31.75 -89.60 REMARK 500 TYR I 96 -60.37 -127.01 REMARK 500 SER I 99 51.73 -94.19 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 ARG C 6 0.19 SIDE CHAIN REMARK 500 ARG C 14 0.19 SIDE CHAIN REMARK 500 ARG C 27 0.21 SIDE CHAIN REMARK 500 ARG C 34 0.21 SIDE CHAIN REMARK 500 ARG C 39 0.30 SIDE CHAIN REMARK 500 ARG C 48 0.29 SIDE CHAIN REMARK 500 ARG I 5 0.27 SIDE CHAIN REMARK 500 ARG I 16 0.30 SIDE CHAIN REMARK 500 ARG I 24 0.29 SIDE CHAIN REMARK 500 ARG I 25 0.31 SIDE CHAIN REMARK 500 ARG I 29 0.29 SIDE CHAIN REMARK 500 ARG I 43 0.32 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1C9F RELATED DB: PDB REMARK 900 1C9F IS THE NMR STRUCTURE OF THE CAD DOMAIN OF CAD IN THE FREE REMARK 900 STATE. DBREF 1F2R C 1 87 UNP O54788 DFFB_MOUSE 1 87 DBREF 1F2R I 1 100 UNP O54786 DFFA_MOUSE 1 100 SEQRES 1 C 87 MET CYS ALA VAL LEU ARG GLN PRO LYS CYS VAL LYS LEU SEQRES 2 C 87 ARG ALA LEU HIS SER ALA CYS LYS PHE GLY VAL ALA ALA SEQRES 3 C 87 ARG SER CYS GLN GLU LEU LEU ARG LYS GLY CYS VAL ARG SEQRES 4 C 87 PHE GLN LEU PRO MET PRO GLY SER ARG LEU CYS LEU TYR SEQRES 5 C 87 GLU ASP GLY THR GLU VAL THR ASP ASP CYS PHE PRO GLY SEQRES 6 C 87 LEU PRO ASN ASP ALA GLU LEU LEU LEU LEU THR ALA GLY SEQRES 7 C 87 GLU THR TRP HIS GLY TYR VAL SER ASP SEQRES 1 I 100 MET GLU LEU SER ARG GLY ALA SER ALA PRO ASP PRO ASP SEQRES 2 I 100 ASP VAL ARG PRO LEU LYS PRO CYS LEU LEU ARG ARG ASN SEQRES 3 I 100 HIS SER ARG ASP GLN HIS GLY VAL ALA ALA SER SER LEU SEQRES 4 I 100 GLU GLU LEU ARG SER LYS ALA CYS GLU LEU LEU ALA ILE SEQRES 5 I 100 ASP LYS SER LEU THR PRO ILE THR LEU VAL LEU ALA GLU SEQRES 6 I 100 ASP GLY THR ILE VAL ASP ASP ASP ASP TYR PHE LEU CYS SEQRES 7 I 100 LEU PRO SER ASN THR LYS PHE VAL ALA LEU ALA CYS ASN SEQRES 8 I 100 GLU LYS TRP THR TYR ASN ASP SER ASP HELIX 1 1 SER C 28 GLN C 41 1 14 HELIX 2 2 SER I 38 ALA I 51 1 14 HELIX 3 3 ASP I 53 THR I 57 5 5 SHEET 1 A 5 LYS C 21 ALA C 26 0 SHEET 2 A 5 LYS C 9 ARG C 14 -1 N LYS C 9 O ALA C 26 SHEET 3 A 5 ALA C 70 LEU C 75 1 O ALA C 70 N LYS C 12 SHEET 4 A 5 ARG C 48 LEU C 51 -1 N ARG C 48 O LEU C 75 SHEET 5 A 5 GLU C 57 VAL C 58 -1 N VAL C 58 O LEU C 49 SHEET 1 B 4 SER I 28 ALA I 36 0 SHEET 2 B 4 LYS I 19 ARG I 25 -1 N LYS I 19 O ALA I 36 SHEET 3 B 4 LYS I 84 LEU I 88 1 N PHE I 85 O LEU I 22 SHEET 4 B 4 THR I 60 LEU I 63 -1 O THR I 60 N LEU I 88 CISPEP 1 THR I 57 PRO I 58 0 -0.69 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
Complete list - 16 20 Bytes