Header list of 1c9f.pdb file
Complete list - b 16 2 Bytes
HEADER HYDROLASE 02-AUG-99 1C9F
TITLE NMR STRUCTURE OF THE CAD DOMAIN OF CASPASE-ACTIVATED DNASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-ACTIVATED DNASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 1-87;
COMPND 5 SYNONYM: DNASE INHIBITED BY DNA FRAGMENTATION FACTOR;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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
KEYWDS ALPHA-BETA ROLL, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.YAMAZAKI,K.UEGAKI
REVDAT 5 16-FEB-22 1C9F 1 REMARK
REVDAT 4 24-FEB-09 1C9F 1 VERSN
REVDAT 3 26-JUN-00 1C9F 3 SOURCE ATOM
REVDAT 2 24-APR-00 1C9F 1 JRNL
REVDAT 1 16-FEB-00 1C9F 0
JRNL AUTH K.UEGAKI,T.OTOMO,H.SAKAHIRA,M.SHIMIZU,N.YUMOTO,Y.KYOGOKU,
JRNL AUTH 2 S.NAGATA,T.YAMAZAKI
JRNL TITL STRUCTURE OF THE CAD DOMAIN OF CASPASE-ACTIVATED DNASE AND
JRNL TITL 2 INTERACTION WITH THE CAD DOMAIN OF ITS INHIBITOR.
JRNL REF J.MOL.BIOL. V. 297 1121 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10764577
JRNL DOI 10.1006/JMBI.2000.3643
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: NULL
REMARK 4
REMARK 4 1C9F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000009456.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.6
REMARK 210 IONIC STRENGTH : 50MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : U-15N; U-13C;U-15N; U-13C;U-15N;
REMARK 210 U-15N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HMQC-J; 3D_13C-SEPARATED_NOESY;
REMARK 210 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
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 : 100
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 : 6
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 VAL A -2
REMARK 465 PRO A -1
REMARK 465 HIS A 0
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 SER A 28 H GLU A 31 1.50
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 CYS A 2 -172.52 66.02
REMARK 500 1 ALA A 3 63.61 179.87
REMARK 500 1 ARG A 6 48.29 -87.47
REMARK 500 1 GLN A 7 113.57 172.73
REMARK 500 1 CYS A 20 -163.01 174.69
REMARK 500 1 VAL A 38 -71.83 -85.33
REMARK 500 1 GLN A 41 85.79 54.01
REMARK 500 1 ARG A 48 148.81 172.75
REMARK 500 1 ASP A 54 15.52 -151.00
REMARK 500 1 PRO A 64 -91.05 -72.13
REMARK 500 1 LEU A 66 152.76 -42.84
REMARK 500 1 HIS A 82 -71.30 -66.82
REMARK 500 1 TYR A 84 53.21 -114.20
REMARK 500 1 SER A 86 59.65 -114.17
REMARK 500 2 CYS A 2 -175.04 171.25
REMARK 500 2 ALA A 3 78.81 -157.90
REMARK 500 2 ARG A 6 46.51 -100.43
REMARK 500 2 GLN A 7 114.68 178.40
REMARK 500 2 SER A 18 -163.04 -123.97
REMARK 500 2 CYS A 20 -159.70 172.95
REMARK 500 2 GLN A 41 84.22 56.86
REMARK 500 2 ARG A 48 117.38 -179.25
REMARK 500 2 ASP A 54 22.39 -141.54
REMARK 500 2 PHE A 63 100.53 -41.17
REMARK 500 2 LEU A 66 161.39 -48.33
REMARK 500 2 PRO A 67 -167.31 -72.13
REMARK 500 2 ALA A 70 101.98 -45.46
REMARK 500 2 TYR A 84 62.94 -118.70
REMARK 500 2 SER A 86 56.65 -112.85
REMARK 500 3 CYS A 2 149.61 169.98
REMARK 500 3 ALA A 3 56.21 -146.37
REMARK 500 3 ARG A 6 40.37 -94.04
REMARK 500 3 GLN A 7 132.74 171.58
REMARK 500 3 LEU A 13 85.50 -65.29
REMARK 500 3 SER A 18 -162.36 -129.98
REMARK 500 3 CYS A 20 -160.63 -175.93
REMARK 500 3 ARG A 34 -70.26 -46.33
REMARK 500 3 GLN A 41 80.30 57.41
REMARK 500 3 ARG A 48 141.95 175.99
REMARK 500 3 ASP A 54 10.87 -145.90
REMARK 500 3 PHE A 63 101.64 -42.26
REMARK 500 3 LEU A 66 164.46 -44.86
REMARK 500 3 PRO A 67 -168.45 -69.53
REMARK 500 3 ALA A 70 106.09 -48.76
REMARK 500 4 LEU A 5 119.72 -162.40
REMARK 500 4 ARG A 6 41.44 -94.45
REMARK 500 4 GLN A 7 120.99 173.52
REMARK 500 4 CYS A 20 -161.55 -170.76
REMARK 500 4 ALA A 26 134.85 178.38
REMARK 500 4 GLN A 41 88.49 56.46
REMARK 500
REMARK 500 THIS ENTRY HAS 282 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 1 ARG A 6 0.30 SIDE CHAIN
REMARK 500 1 ARG A 14 0.11 SIDE CHAIN
REMARK 500 1 ARG A 27 0.31 SIDE CHAIN
REMARK 500 1 ARG A 34 0.30 SIDE CHAIN
REMARK 500 1 ARG A 39 0.31 SIDE CHAIN
REMARK 500 1 ARG A 48 0.32 SIDE CHAIN
REMARK 500 2 ARG A 6 0.29 SIDE CHAIN
REMARK 500 2 ARG A 14 0.20 SIDE CHAIN
REMARK 500 2 ARG A 27 0.20 SIDE CHAIN
REMARK 500 2 ARG A 34 0.29 SIDE CHAIN
REMARK 500 2 ARG A 39 0.27 SIDE CHAIN
REMARK 500 2 ARG A 48 0.27 SIDE CHAIN
REMARK 500 3 ARG A 6 0.24 SIDE CHAIN
REMARK 500 3 ARG A 14 0.30 SIDE CHAIN
REMARK 500 3 ARG A 27 0.13 SIDE CHAIN
REMARK 500 3 ARG A 34 0.30 SIDE CHAIN
REMARK 500 3 ARG A 39 0.27 SIDE CHAIN
REMARK 500 3 ARG A 48 0.32 SIDE CHAIN
REMARK 500 4 ARG A 6 0.31 SIDE CHAIN
REMARK 500 4 ARG A 14 0.32 SIDE CHAIN
REMARK 500 4 ARG A 27 0.24 SIDE CHAIN
REMARK 500 4 ARG A 34 0.17 SIDE CHAIN
REMARK 500 4 ARG A 39 0.11 SIDE CHAIN
REMARK 500 4 ARG A 48 0.14 SIDE CHAIN
REMARK 500 5 ARG A 6 0.25 SIDE CHAIN
REMARK 500 5 ARG A 14 0.24 SIDE CHAIN
REMARK 500 5 ARG A 27 0.24 SIDE CHAIN
REMARK 500 5 ARG A 34 0.27 SIDE CHAIN
REMARK 500 5 ARG A 39 0.25 SIDE CHAIN
REMARK 500 5 ARG A 48 0.32 SIDE CHAIN
REMARK 500 6 ARG A 6 0.32 SIDE CHAIN
REMARK 500 6 ARG A 14 0.29 SIDE CHAIN
REMARK 500 6 ARG A 27 0.30 SIDE CHAIN
REMARK 500 6 ARG A 34 0.32 SIDE CHAIN
REMARK 500 6 ARG A 39 0.27 SIDE CHAIN
REMARK 500 7 ARG A 6 0.11 SIDE CHAIN
REMARK 500 7 ARG A 14 0.13 SIDE CHAIN
REMARK 500 7 ARG A 27 0.32 SIDE CHAIN
REMARK 500 7 ARG A 34 0.28 SIDE CHAIN
REMARK 500 7 ARG A 39 0.18 SIDE CHAIN
REMARK 500 7 ARG A 48 0.32 SIDE CHAIN
REMARK 500 8 ARG A 6 0.23 SIDE CHAIN
REMARK 500 8 ARG A 14 0.27 SIDE CHAIN
REMARK 500 8 ARG A 27 0.24 SIDE CHAIN
REMARK 500 8 ARG A 34 0.32 SIDE CHAIN
REMARK 500 8 ARG A 39 0.30 SIDE CHAIN
REMARK 500 8 ARG A 48 0.28 SIDE CHAIN
REMARK 500 9 ARG A 6 0.26 SIDE CHAIN
REMARK 500 9 ARG A 14 0.10 SIDE CHAIN
REMARK 500 9 ARG A 27 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 112 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1C9F A 1 87 UNP O54788 DFFB_MOUSE 1 87
SEQADV 1C9F VAL A -2 UNP O54788 INSERTION
SEQADV 1C9F PRO A -1 UNP O54788 INSERTION
SEQADV 1C9F HIS A 0 UNP O54788 INSERTION
SEQRES 1 A 90 VAL PRO HIS MET CYS ALA VAL LEU ARG GLN PRO LYS CYS
SEQRES 2 A 90 VAL LYS LEU ARG ALA LEU HIS SER ALA CYS LYS PHE GLY
SEQRES 3 A 90 VAL ALA ALA ARG SER CYS GLN GLU LEU LEU ARG LYS GLY
SEQRES 4 A 90 CYS VAL ARG PHE GLN LEU PRO MET PRO GLY SER ARG LEU
SEQRES 5 A 90 CYS LEU TYR GLU ASP GLY THR GLU VAL THR ASP ASP CYS
SEQRES 6 A 90 PHE PRO GLY LEU PRO ASN ASP ALA GLU LEU LEU LEU LEU
SEQRES 7 A 90 THR ALA GLY GLU THR TRP HIS GLY TYR VAL SER ASP
HELIX 1 1 SER A 28 PHE A 40 1 13
SHEET 1 A 4 GLY A 23 ALA A 26 0
SHEET 2 A 4 LYS A 9 ALA A 15 -1 O LYS A 9 N ALA A 26
SHEET 3 A 4 ALA A 70 LEU A 75 1 N ALA A 70 O CYS A 10
SHEET 4 A 4 ARG A 48 LEU A 51 -1 N ARG A 48 O LEU A 75
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 16 2 Bytes