Header list of 1b8q.pdb file
Complete list - b 16 2 Bytes
HEADER OXIDOREDUCTASE 01-FEB-99 1B8Q TITLE SOLUTION STRUCTURE OF THE EXTENDED NEURONAL NITRIC OXIDE SYNTHASE PDZ TITLE 2 DOMAIN COMPLEXED WITH AN ASSOCIATED PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (NEURONAL NITRIC OXIDE SYNTHASE); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PDZ DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: PROTEIN (HEPTAPEPTIDE); COMPND 8 CHAIN: B; COMPND 9 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 MOL_ID: 2; SOURCE 8 SYNTHETIC: YES KEYWDS PDZ DOMAIN, NNOS, NITRIC OXIDE SYNTHASE, OXIDOREDUCTASE EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR H.TOCHIO,Q.ZHANG,P.MANDAL,M.LI,M.ZHANG REVDAT 4 16-FEB-22 1B8Q 1 REMARK SEQADV REVDAT 3 24-FEB-09 1B8Q 1 VERSN REVDAT 2 06-MAR-00 1B8Q 1 HEADER DBREF SEQADV EXPDTA REVDAT 1 29-APR-99 1B8Q 0 JRNL AUTH H.TOCHIO,Q.ZHANG,P.MANDAL,M.LI,M.ZHANG JRNL TITL SOLUTION STRUCTURE OF THE EXTENDED NEURONAL NITRIC OXIDE JRNL TITL 2 SYNTHASE PDZ DOMAIN COMPLEXED WITH AN ASSOCIATED PEPTIDE. JRNL REF NAT.STRUCT.BIOL. V. 6 417 1999 JRNL REFN ISSN 1072-8368 JRNL PMID 10331866 JRNL DOI 10.1038/8216 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1B8Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-99. REMARK 100 THE DEPOSITION ID IS D_1000000429. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 6.0 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 : 15 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: A, B 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 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 HIS A 3 63.34 60.51 REMARK 500 1 GLU A 6 -67.86 -144.84 REMARK 500 1 PRO A 7 176.66 -48.08 REMARK 500 1 ASN A 8 -74.22 -150.09 REMARK 500 1 VAL A 9 113.37 -161.84 REMARK 500 1 ILE A 10 -164.61 -161.19 REMARK 500 1 LYS A 18 23.47 44.47 REMARK 500 1 VAL A 19 34.54 -169.14 REMARK 500 1 LEU A 22 -26.96 -38.44 REMARK 500 1 PRO A 34 94.60 -41.89 REMARK 500 1 ARG A 42 -67.70 -95.47 REMARK 500 1 ALA A 45 -83.01 -94.12 REMARK 500 1 ASP A 56 -85.37 -92.69 REMARK 500 1 ILE A 58 113.81 -160.47 REMARK 500 1 PRO A 65 86.30 -57.81 REMARK 500 1 VAL A 67 -63.57 -139.64 REMARK 500 1 SER A 70 98.75 -68.09 REMARK 500 1 ALA A 82 -167.65 -61.24 REMARK 500 1 PRO A 94 -155.99 -58.69 REMARK 500 1 HIS A 100 -159.03 -74.60 REMARK 500 1 GLU A 102 169.52 178.24 REMARK 500 1 THR A 103 -167.95 47.72 REMARK 500 1 THR A 106 -40.70 -174.69 REMARK 500 1 ASP A 108 36.67 -162.82 REMARK 500 1 LYS A 112 160.53 70.21 REMARK 500 1 ARG A 115 91.04 -160.12 REMARK 500 1 VAL A 116 55.60 -162.64 REMARK 500 1 LEU A 120 -70.28 -87.39 REMARK 500 1 PRO A 123 97.25 -50.87 REMARK 500 1 THR A 124 59.66 -175.70 REMARK 500 1 LYS B 3 -48.10 -137.53 REMARK 500 2 SER A 2 -68.77 -94.14 REMARK 500 2 HIS A 3 -71.10 67.78 REMARK 500 2 ILE A 5 97.38 -58.08 REMARK 500 2 GLU A 6 142.21 -176.80 REMARK 500 2 PRO A 7 -165.32 -76.30 REMARK 500 2 ASN A 8 -66.67 -127.16 REMARK 500 2 VAL A 9 99.07 -161.02 REMARK 500 2 ARG A 17 29.43 45.51 REMARK 500 2 LYS A 18 24.77 43.50 REMARK 500 2 VAL A 19 32.67 -165.81 REMARK 500 2 PRO A 33 -171.55 -53.19 REMARK 500 2 PRO A 34 174.44 -45.28 REMARK 500 2 ASP A 39 135.74 -173.46 REMARK 500 2 ARG A 42 -68.38 -93.20 REMARK 500 2 ALA A 45 -83.11 -93.72 REMARK 500 2 ASP A 56 -88.94 -83.25 REMARK 500 2 PRO A 65 84.84 -59.22 REMARK 500 2 VAL A 67 -55.19 -128.61 REMARK 500 2 ASP A 68 26.03 -140.10 REMARK 500 REMARK 500 THIS ENTRY HAS 422 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1B8Q A 1 127 UNP P29476 NOS1_RAT 7 133 DBREF 1B8Q B 1 7 PDB 1B8Q 1B8Q 1 7 SEQADV 1B8Q SER A 2 UNP P29476 VAL 8 CONFLICT SEQADV 1B8Q HIS A 3 UNP P29476 GLN 9 CONFLICT SEQADV 1B8Q MET A 4 UNP P29476 GLN 10 CONFLICT SEQADV 1B8Q GLU A 6 UNP P29476 GLN 12 CONFLICT SEQRES 1 A 127 GLY SER HIS MET ILE GLU PRO ASN VAL ILE SER VAL ARG SEQRES 2 A 127 LEU PHE LYS ARG LYS VAL GLY GLY LEU GLY PHE LEU VAL SEQRES 3 A 127 LYS GLU ARG VAL SER LYS PRO PRO VAL ILE ILE SER ASP SEQRES 4 A 127 LEU ILE ARG GLY GLY ALA ALA GLU GLN SER GLY LEU ILE SEQRES 5 A 127 GLN ALA GLY ASP ILE ILE LEU ALA VAL ASN ASP ARG PRO SEQRES 6 A 127 LEU VAL ASP LEU SER TYR ASP SER ALA LEU GLU VAL LEU SEQRES 7 A 127 ARG GLY ILE ALA SER GLU THR HIS VAL VAL LEU ILE LEU SEQRES 8 A 127 ARG GLY PRO GLU GLY PHE THR THR HIS LEU GLU THR THR SEQRES 9 A 127 PHE THR GLY ASP GLY THR PRO LYS THR ILE ARG VAL THR SEQRES 10 A 127 GLN PRO LEU GLY PRO PRO THR LYS ALA VAL SEQRES 1 B 7 VAL VAL LYS VAL ASP SER VAL HELIX 1 1 ALA A 46 SER A 49 1 4 HELIX 2 2 TYR A 71 ARG A 79 1 9 SHEET 1 A 2 ILE A 10 PHE A 15 0 SHEET 2 A 2 HIS A 86 LEU A 91 -1 N LEU A 91 O ILE A 10 SHEET 1 B 2 VAL A 26 GLU A 28 0 SHEET 2 B 2 VAL A 35 ILE A 37 -1 N ILE A 36 O LYS A 27 SHEET 1 C 2 PHE A 97 THR A 99 0 SHEET 2 C 2 THR A 117 PRO A 119 -1 N GLN A 118 O THR A 98 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