Header list of 1zok.pdb file
Complete list - 2 20 Bytes
HEADER MEMBRANE PROTEIN 13-MAY-05 1ZOK
TITLE PDZ1 DOMAIN OF SYNAPSE ASSOCIATED PROTEIN 97
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRESYNAPTIC PROTEIN SAP97;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ1 DOMAIN (RESIDUES 221-313);
COMPND 5 SYNONYM: SYNAPSE-ASSOCIATED PROTEIN 97, SAP-97, DISCS, LARGE HOMOLOG
COMPND 6 1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PDZ, PDZ1, SAP97, SYNAPSE ASSOCIATED PROTEIN 97, BETA STRAND, HELIX,
KEYWDS 2 MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
AUTHOR L.WANG,A.PISERCHIO,D.F.MIERKE
REVDAT 4 02-MAR-22 1ZOK 1 REMARK
REVDAT 3 24-FEB-09 1ZOK 1 VERSN
REVDAT 2 02-AUG-05 1ZOK 1 JRNL
REVDAT 1 07-JUN-05 1ZOK 0
JRNL AUTH L.WANG,A.PISERCHIO,D.F.MIERKE
JRNL TITL STRUCTURAL CHARACTERIZATION OF THE INTERMOLECULAR
JRNL TITL 2 INTERACTIONS OF SYNAPSE-ASSOCIATED PROTEIN-97 WITH THE NR2B
JRNL TITL 3 SUBUNIT OF N-METHYL-D-ASPARTATE RECEPTORS.
JRNL REF J.BIOL.CHEM. V. 280 26992 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15929985
JRNL DOI 10.1074/JBC.M503555200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, CNS 1.1
REMARK 3 AUTHORS : A.T.BRUNGER, P.D.ADAMS, G.M.CLORE, W.L.DELANO,
REMARK 3 P.GROS, R.W.GROSSE-KUNSTLEVE, J.-S.JIANG, J.KUSZEWSKI, M.NILGES,
REMARK 3 N.S.PANNU, R.J.READ, L.M.RICE, T.SIMONSON, G.L.WARREN (CNS),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZOK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000032960.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : NO SALT
REMARK 210 PRESSURE : NORMAL AIR PRESSURE
REMARK 210 SAMPLE CONTENTS : 1MM C13-N15 PDZ1 OF SAP97 IN
REMARK 210 20MM PHOSPHATE BUFFER, 10% D2O,
REMARK 210 90% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.3, XWINNMR 3.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
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 LEU A 227 H VAL A 303 1.53
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 ASN A 231 -38.28 179.75
REMARK 500 SER A 232 31.00 -161.86
REMARK 500 ASP A 243 13.52 -154.12
REMARK 500 ARG A 269 97.54 61.99
REMARK 500 ASN A 273 17.98 -151.76
REMARK 500 GLU A 281 -2.14 78.65
REMARK 500 VAL A 284 42.56 -97.38
REMARK 500 ASP A 286 61.54 -119.86
REMARK 500 THR A 288 -149.96 -103.82
REMARK 500 SER A 301 -87.10 -58.50
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ZOK A 221 313 UNP Q62696 DLG1_RAT 221 313
SEQRES 1 A 93 GLU TYR GLU GLU ILE THR LEU GLU ARG GLY ASN SER GLY
SEQRES 2 A 93 LEU GLY PHE SER ILE ALA GLY GLY THR ASP ASN PRO HIS
SEQRES 3 A 93 ILE GLY ASP ASP SER SER ILE PHE ILE THR LYS ILE ILE
SEQRES 4 A 93 THR GLY GLY ALA ALA ALA GLN ASP GLY ARG LEU ARG VAL
SEQRES 5 A 93 ASN ASP CYS ILE LEU ARG VAL ASN GLU ALA ASP VAL ARG
SEQRES 6 A 93 ASP VAL THR HIS SER LYS ALA VAL GLU ALA LEU LYS GLU
SEQRES 7 A 93 ALA GLY SER ILE VAL ARG LEU TYR VAL LYS ARG ARG LYS
SEQRES 8 A 93 ALA PHE
HELIX 1 1 GLY A 262 GLY A 268 1 7
HELIX 2 2 THR A 288 GLU A 298 1 11
SHEET 1 A 3 ILE A 225 LEU A 227 0
SHEET 2 A 3 VAL A 303 TYR A 306 -1 O VAL A 303 N LEU A 227
SHEET 3 A 3 ARG A 278 VAL A 279 -1 N ARG A 278 O TYR A 306
SHEET 1 B 2 PHE A 236 ALA A 239 0
SHEET 2 B 2 PHE A 254 ILE A 258 -1 O LYS A 257 N SER A 237
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 - 2 20 Bytes