Header list of 1svq.pdb file
Complete list - v 29 2 Bytes
HEADER ACTIN-BINDING 12-OCT-94 1SVQ
TITLE STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEVERIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DICTYOSTELIUM DISCOIDEUM;
SOURCE 3 ORGANISM_TAXID: 44689
KEYWDS ACTIN-BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.SCHNUCHEL,T.A.HOLAK
REVDAT 3 29-NOV-17 1SVQ 1 REMARK HELIX
REVDAT 2 24-FEB-09 1SVQ 1 VERSN
REVDAT 1 07-FEB-95 1SVQ 0
JRNL AUTH A.SCHNUCHEL,R.WILTSCHECK,L.EICHINGER,M.SCHLEICHER,T.A.HOLAK
JRNL TITL STRUCTURE OF SEVERIN DOMAIN 2 IN SOLUTION.
JRNL REF J.MOL.BIOL. V. 247 21 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7897658
JRNL DOI 10.1006/JMBI.1994.0118
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.EICHINGER,M.SCHLEICHER
REMARK 1 TITL CHARACTERIZATION OF ACTIN-AND LIPID-BINDING DOMAINS IN
REMARK 1 TITL 2 SEVERIN, A CA(2+)-DEPENDENT F-ACTIN FRAGMENTING PROTEIN
REMARK 1 REF BIOCHEMISTRY V. 31 4779 1992
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.ANDRE,F.LOTTSPEICH,M.SCHLEICHER,A.NOEGEL
REMARK 1 TITL SEVERIN, GELSOLIN, AND VILLIN SHARE A HOMOLOGOUS SEQUENCE IN
REMARK 1 TITL 2 REGIONS PRESUMED TO CONTAIN F-ACTIN SEVERING DOMAINS
REMARK 1 REF J.BIOL.CHEM. V. 263 722 1988
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SVQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176534.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: 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 SER A 149
REMARK 465 GLY A 150
REMARK 465 PHE A 151
REMARK 465 ASN A 152
REMARK 465 HIS A 153
REMARK 465 VAL A 154
REMARK 465 LYS A 155
REMARK 465 PRO A 156
REMARK 465 THR A 157
REMARK 465 LYS A 252
REMARK 465 GLY A 253
REMARK 465 ALA A 254
REMARK 465 ILE A 255
REMARK 465 ALA A 256
REMARK 465 ALA A 257
REMARK 465 LYS A 258
REMARK 465 HIS A 259
REMARK 465 GLU A 260
REMARK 465 THR A 261
REMARK 465 ALA A 262
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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 5 CYS A 189 CB CYS A 189 SG 0.106
REMARK 500 6 CYS A 189 CB CYS A 189 SG 0.107
REMARK 500 9 CYS A 189 CB CYS A 189 SG 0.120
REMARK 500 9 CYS A 235 CB CYS A 235 SG 0.105
REMARK 500 11 CYS A 189 CB CYS A 189 SG 0.107
REMARK 500 12 CYS A 189 CB CYS A 189 SG 0.104
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 TYR A 159 170.91 -49.56
REMARK 500 1 ASP A 169 -127.60 37.44
REMARK 500 1 ASN A 171 72.80 -101.63
REMARK 500 1 ALA A 175 166.17 177.97
REMARK 500 1 ALA A 180 85.58 -175.45
REMARK 500 1 SER A 183 2.94 -68.47
REMARK 500 1 LEU A 184 -169.13 -50.96
REMARK 500 1 THR A 237 -62.32 -124.54
REMARK 500 1 SER A 239 10.66 57.51
REMARK 500 1 ASP A 240 -8.70 -58.07
REMARK 500 1 ILE A 241 76.71 -118.00
REMARK 500 1 ALA A 243 -25.71 -36.67
REMARK 500 2 ASP A 169 -129.52 37.86
REMARK 500 2 ASN A 171 73.06 -102.79
REMARK 500 2 ALA A 175 164.55 177.74
REMARK 500 2 LEU A 179 150.30 -49.10
REMARK 500 2 ALA A 180 -158.09 -148.81
REMARK 500 2 THR A 181 -38.95 85.61
REMARK 500 2 LEU A 184 -169.55 -50.43
REMARK 500 2 LYS A 205 22.31 -76.36
REMARK 500 2 GLN A 209 -71.78 -69.34
REMARK 500 2 PHE A 234 126.36 -171.28
REMARK 500 2 THR A 237 -64.76 -132.69
REMARK 500 2 SER A 239 18.95 50.94
REMARK 500 2 ASP A 240 38.84 -79.34
REMARK 500 2 ALA A 243 -24.98 -39.10
REMARK 500 3 ASP A 169 -125.26 38.09
REMARK 500 3 ASN A 171 74.13 -103.93
REMARK 500 3 ALA A 175 155.58 178.83
REMARK 500 3 ALA A 180 88.64 -179.48
REMARK 500 3 LEU A 184 -171.09 -51.30
REMARK 500 3 PHE A 234 121.77 -174.68
REMARK 500 3 THR A 237 -65.00 -137.11
REMARK 500 3 ASP A 240 40.47 -78.91
REMARK 500 3 ALA A 243 -25.46 -36.40
REMARK 500 4 TYR A 159 164.19 -41.09
REMARK 500 4 ASP A 169 -127.28 38.61
REMARK 500 4 ALA A 175 167.01 178.13
REMARK 500 4 ALA A 180 85.21 -171.55
REMARK 500 4 LEU A 184 -169.50 -53.11
REMARK 500 4 PHE A 234 121.47 -176.77
REMARK 500 4 THR A 237 -66.65 -123.88
REMARK 500 4 SER A 239 17.44 51.15
REMARK 500 5 ASP A 169 -130.02 38.17
REMARK 500 5 ASN A 171 74.56 -102.27
REMARK 500 5 ALA A 175 164.60 179.70
REMARK 500 5 PRO A 178 -168.20 -75.32
REMARK 500 5 ALA A 180 -158.23 -152.46
REMARK 500 5 THR A 181 -37.03 88.17
REMARK 500 5 LEU A 184 -166.95 -52.46
REMARK 500
REMARK 500 THIS ENTRY HAS 222 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 162 0.10 SIDE CHAIN
REMARK 500 1 ARG A 219 0.24 SIDE CHAIN
REMARK 500 1 ARG A 225 0.27 SIDE CHAIN
REMARK 500 2 ARG A 162 0.30 SIDE CHAIN
REMARK 500 2 ARG A 219 0.31 SIDE CHAIN
REMARK 500 2 ARG A 225 0.32 SIDE CHAIN
REMARK 500 3 ARG A 162 0.28 SIDE CHAIN
REMARK 500 3 ARG A 219 0.32 SIDE CHAIN
REMARK 500 3 ARG A 225 0.22 SIDE CHAIN
REMARK 500 4 ARG A 162 0.29 SIDE CHAIN
REMARK 500 4 ARG A 219 0.27 SIDE CHAIN
REMARK 500 4 ARG A 225 0.30 SIDE CHAIN
REMARK 500 5 ARG A 162 0.22 SIDE CHAIN
REMARK 500 5 ARG A 219 0.31 SIDE CHAIN
REMARK 500 6 ARG A 162 0.32 SIDE CHAIN
REMARK 500 6 ARG A 219 0.08 SIDE CHAIN
REMARK 500 6 ARG A 225 0.31 SIDE CHAIN
REMARK 500 7 ARG A 162 0.31 SIDE CHAIN
REMARK 500 7 ARG A 219 0.18 SIDE CHAIN
REMARK 500 7 ARG A 225 0.31 SIDE CHAIN
REMARK 500 8 ARG A 162 0.31 SIDE CHAIN
REMARK 500 8 ARG A 219 0.14 SIDE CHAIN
REMARK 500 8 ARG A 225 0.29 SIDE CHAIN
REMARK 500 9 ARG A 162 0.32 SIDE CHAIN
REMARK 500 9 ARG A 219 0.27 SIDE CHAIN
REMARK 500 9 ARG A 225 0.16 SIDE CHAIN
REMARK 500 10 ARG A 162 0.23 SIDE CHAIN
REMARK 500 10 ARG A 219 0.21 SIDE CHAIN
REMARK 500 10 ARG A 225 0.24 SIDE CHAIN
REMARK 500 11 ARG A 162 0.29 SIDE CHAIN
REMARK 500 11 ARG A 219 0.23 SIDE CHAIN
REMARK 500 11 ARG A 225 0.32 SIDE CHAIN
REMARK 500 12 ARG A 162 0.32 SIDE CHAIN
REMARK 500 12 ARG A 219 0.25 SIDE CHAIN
REMARK 500 12 ARG A 225 0.12 SIDE CHAIN
REMARK 500 13 ARG A 162 0.21 SIDE CHAIN
REMARK 500 13 ARG A 219 0.26 SIDE CHAIN
REMARK 500 13 ARG A 225 0.31 SIDE CHAIN
REMARK 500 14 ARG A 162 0.31 SIDE CHAIN
REMARK 500 14 ARG A 219 0.31 SIDE CHAIN
REMARK 500 14 ARG A 225 0.32 SIDE CHAIN
REMARK 500 15 ARG A 162 0.25 SIDE CHAIN
REMARK 500 15 ARG A 219 0.28 SIDE CHAIN
REMARK 500 15 ARG A 225 0.31 SIDE CHAIN
REMARK 500 16 ARG A 162 0.29 SIDE CHAIN
REMARK 500 16 ARG A 219 0.26 SIDE CHAIN
REMARK 500 16 ARG A 225 0.12 SIDE CHAIN
REMARK 500 17 ARG A 162 0.30 SIDE CHAIN
REMARK 500 17 ARG A 219 0.20 SIDE CHAIN
REMARK 500 17 ARG A 225 0.30 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 58 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SVR RELATED DB: PDB
DBREF 1SVQ A 149 262 UNP P10733 SEVE_DICDI 149 262
SEQRES 1 A 114 SER GLY PHE ASN HIS VAL LYS PRO THR GLU TYR LYS PRO
SEQRES 2 A 114 ARG LEU LEU HIS ILE SER GLY ASP LYS ASN ALA LYS VAL
SEQRES 3 A 114 ALA GLU VAL PRO LEU ALA THR SER SER LEU ASN SER GLY
SEQRES 4 A 114 ASP CYS PHE LEU LEU ASP ALA GLY LEU THR ILE TYR GLN
SEQRES 5 A 114 PHE ASN GLY SER LYS SER SER PRO GLN GLU LYS ASN LYS
SEQRES 6 A 114 ALA ALA GLU VAL ALA ARG ALA ILE ASP ALA GLU ARG LYS
SEQRES 7 A 114 GLY LEU PRO LYS VAL GLU VAL PHE CYS GLU THR ASP SER
SEQRES 8 A 114 ASP ILE PRO ALA GLU PHE TRP LYS LEU LEU GLY GLY LYS
SEQRES 9 A 114 GLY ALA ILE ALA ALA LYS HIS GLU THR ALA
HELIX 1 H1 GLU A 210 ASP A 222 1 13
HELIX 2 H2 ALA A 243 GLY A 251 1 9
SHEET 1 B1 5 ALA A 172 VAL A 177 0
SHEET 2 B1 5 ARG A 162 GLY A 168 -1 N LEU A 163 O VAL A 177
SHEET 3 B1 5 ASP A 188 ALA A 194 -1 N CYS A 189 O ILE A 166
SHEET 4 B1 5 LEU A 196 ASN A 202 -1 N TYR A 199 O LEU A 192
SHEET 5 B1 5 LYS A 230 GLU A 236 1 O LYS A 230 N ILE A 198
SSBOND 1 CYS A 189 CYS A 235 1555 1555 2.07
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 - v 29 2 Bytes