Header list of 1m5z.pdb file
Complete list - b 23 2 Bytes
HEADER PROTEIN BINDING 11-JUL-02 1M5Z TITLE THE PDZ7 OF GLUTAMATE RECEPTOR INTERACTING PROTEIN BINDS TO ITS TARGET TITLE 2 VIA A NOVEL HYDROPHOBIC SURFACE AREA COMPND MOL_ID: 1; COMPND 2 MOLECULE: AMPA RECEPTOR INTERACTING PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: THE SEVENTH PDZ DOMAIN OF GLUTAMATE RECEPTOR INTERACTING COMPND 5 PROTEIN; COMPND 6 SYNONYM: GRIP; 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; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET32A KEYWDS SIX BETA-STRANDS AND TWO ALPHA-HELICES, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR W.FENG,J.FAN,M.JIANG,Y.SHI,M.ZHANG REVDAT 3 23-FEB-22 1M5Z 1 REMARK REVDAT 2 24-FEB-09 1M5Z 1 VERSN REVDAT 1 06-NOV-02 1M5Z 0 JRNL AUTH W.FENG,J.-S.FAN,M.JIANG,Y.-W.SHI,M.ZHANG JRNL TITL THE PDZ7 OF GLUTAMATE RECEPTOR INTERACTING PROTEIN BINDS TO JRNL TITL 2 ITS TARGET VIA A NOVEL HYDROPHOBIC SURFACE AREA JRNL REF J.BIOL.CHEM. V. 277 41140 2002 JRNL REFN ISSN 0021-9258 JRNL PMID 12196542 JRNL DOI 10.1074/JBC.M207206200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1, CNS 1.1 REMARK 3 AUTHORS : BRUNGER (CNS), BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1826 RESTRAINTS, 1644 ARE REMARK 3 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 126 DIHEDRAL ANGLE RESTRAINTS, 56 DISTANCE REMARK 3 RESTRAINTS REMARK 3 FROM HYDROGEN BONDS REMARK 4 REMARK 4 1M5Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUL-02. REMARK 100 THE DEPOSITION ID IS D_1000016640. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 100MM POTASSIUM PHOSPHATE BUFFER REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1.0 MM UNLABELLED PDZ7 IN 99.9% REMARK 210 D2O; 1.0 MM 15N-LABELLED PROTEIN REMARK 210 IN 90% H2O/10% D2O; 1.0 MM 15N/ REMARK 210 13C-LABELLED SAMPLES IN 99.9% REMARK 210 D2O; 1.0 MM 15N/13C-LABELLED REMARK 210 SAMPLES IN 90% H2O/10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 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 : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 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 : 11 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: 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 THR A 18 -55.98 -163.00 REMARK 500 1 PRO A 19 95.70 -47.72 REMARK 500 1 VAL A 20 170.30 -50.00 REMARK 500 1 SER A 31 84.99 -60.11 REMARK 500 1 PHE A 38 134.45 -174.04 REMARK 500 1 GLU A 46 -83.78 -157.88 REMARK 500 1 LYS A 47 134.22 -175.68 REMARK 500 1 PRO A 56 109.17 -55.53 REMARK 500 1 ALA A 57 38.14 83.38 REMARK 500 1 PRO A 67 135.75 -39.47 REMARK 500 1 TYR A 68 -5.31 85.44 REMARK 500 1 ASP A 69 85.10 -56.22 REMARK 500 1 LEU A 71 107.28 -54.50 REMARK 500 1 HIS A 76 -19.37 86.59 REMARK 500 1 THR A 79 30.93 -96.51 REMARK 500 2 PRO A 17 -179.32 -61.79 REMARK 500 2 THR A 18 146.06 59.03 REMARK 500 2 PRO A 19 178.80 -50.72 REMARK 500 2 VAL A 20 170.11 -46.07 REMARK 500 2 PHE A 38 124.42 -172.05 REMARK 500 2 GLU A 46 25.44 -150.12 REMARK 500 2 LYS A 47 63.08 26.26 REMARK 500 2 ALA A 57 29.35 83.10 REMARK 500 2 TYR A 68 -17.21 90.32 REMARK 500 2 ASP A 69 83.75 -53.34 REMARK 500 2 ARG A 70 99.61 -67.92 REMARK 500 2 ASN A 75 -59.11 75.54 REMARK 500 2 HIS A 76 -14.71 -167.47 REMARK 500 2 ARG A 78 87.23 -69.73 REMARK 500 3 THR A 18 -52.98 -169.14 REMARK 500 3 VAL A 20 161.23 -44.27 REMARK 500 3 SER A 31 84.58 -60.59 REMARK 500 3 PHE A 38 130.62 -173.31 REMARK 500 3 GLU A 46 51.79 -155.92 REMARK 500 3 LYS A 47 96.44 21.62 REMARK 500 3 ALA A 57 75.34 35.77 REMARK 500 3 PRO A 67 66.67 -66.92 REMARK 500 3 TYR A 68 -24.18 -178.16 REMARK 500 3 ASP A 69 94.96 -44.00 REMARK 500 3 LEU A 71 107.05 -53.98 REMARK 500 3 ASN A 75 -61.58 72.11 REMARK 500 3 HIS A 76 -18.41 -168.07 REMARK 500 3 ARG A 78 93.61 -69.69 REMARK 500 3 THR A 79 34.41 -95.75 REMARK 500 4 THR A 18 -60.38 -167.49 REMARK 500 4 SER A 31 85.08 -56.86 REMARK 500 4 PHE A 38 128.01 -174.38 REMARK 500 4 GLU A 46 59.95 -156.20 REMARK 500 4 LYS A 47 -166.85 32.85 REMARK 500 4 ALA A 57 28.77 82.99 REMARK 500 REMARK 500 THIS ENTRY HAS 246 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1M5Z A 16 106 UNP P97879 GRIP1_RAT 980 1070 SEQRES 1 A 91 SER PRO THR PRO VAL GLU LEU HIS LYS VAL THR LEU TYR SEQRES 2 A 91 LYS ASP SER GLY MET GLU ASP PHE GLY PHE SER VAL ALA SEQRES 3 A 91 ASP GLY LEU LEU GLU LYS GLY VAL TYR VAL LYS ASN ILE SEQRES 4 A 91 ARG PRO ALA GLY PRO GLY ASP LEU GLY GLY LEU LYS PRO SEQRES 5 A 91 TYR ASP ARG LEU LEU GLN VAL ASN HIS VAL ARG THR ARG SEQRES 6 A 91 ASP PHE ASP CYS CYS LEU VAL VAL PRO LEU ILE ALA GLU SEQRES 7 A 91 SER GLY ASN LYS LEU ASP LEU VAL ILE SER ARG ASN PRO HELIX 1 1 GLY A 58 GLY A 64 1 7 HELIX 2 2 ASP A 83 GLU A 93 1 11 SHEET 1 A 4 GLU A 21 TYR A 28 0 SHEET 2 A 4 LYS A 97 ARG A 104 -1 O LEU A 100 N VAL A 25 SHEET 3 A 4 ARG A 70 VAL A 74 -1 N GLN A 73 O VAL A 101 SHEET 4 A 4 VAL A 77 ARG A 78 -1 O VAL A 77 N VAL A 74 SHEET 1 B 2 PHE A 38 ASP A 42 0 SHEET 2 B 2 VAL A 49 ILE A 54 -1 O TYR A 50 N ALA A 41 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