Header list of 1gea.pdb file
Complete list - 23 20 Bytes
HEADER NEUROPEPTIDE 20-OCT-00 1GEA TITLE RECEPTOR-BOUND CONFORMATION OF PACAP21 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PITUITARY ADENYLATE CYCLASE ACTIVATING POLYPEPTIDE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN(RESIDUE 132-152); COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS. KEYWDS BETA COIL, CONSECUTIVE BETA TURNS, TYPE-II BETA TURN, TYPE-I BETA KEYWDS 2 TURN, HELIX, NEUROPEPTIDE EXPDTA SOLUTION NMR NUMMDL 25 AUTHOR H.INOOKA,T.OHTAKI,O.KITAHARA,T.IKEGAMI,S.ENDO,C.KITADA,K.OGI,H.ONDA, AUTHOR 2 M.FUJINO,M.SHIRAKAWA REVDAT 4 23-FEB-22 1GEA 1 REMARK SEQADV LINK REVDAT 3 24-FEB-09 1GEA 1 VERSN REVDAT 2 21-JAN-03 1GEA 1 REMARK REVDAT 1 20-APR-01 1GEA 0 JRNL AUTH H.INOOKA,T.OHTAKI,O.KITAHARA,T.IKEGAMI,S.ENDO,C.KITADA, JRNL AUTH 2 K.OGI,H.ONDA,M.FUJINO,M.SHIRAKAWA JRNL TITL CONFORMATION OF A PEPTIDE LIGAND BOUND TO ITS G-PROTEIN JRNL TITL 2 COUPLED RECEPTOR. JRNL REF NAT.STRUCT.BIOL. V. 8 161 2001 JRNL REFN ISSN 1072-8368 JRNL PMID 11175907 JRNL DOI 10.1038/84159 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER, A.T. (X-PLOR), BRUNGER, A.T. (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE CALCULATED BY SA REMARK 3 PROTOCOL OF X-PLOR BASED ON A TOTAL OF 387 TRNOE-DERIVED REMARK 3 DISTANCE RESTRAINTS OBTAINED FROM THE IRMA REFINEMENT. REMARK 4 REMARK 4 1GEA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-NOV-00. REMARK 100 THE DEPOSITION ID IS D_1000005070. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.3 REMARK 210 IONIC STRENGTH : 0.41 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.7MM PACAP21; 40MM PACAP REMARK 210 RECEPTOR; 80MM PHOSPHATE BUFFER REMARK 210 (PH 6.3); 1.7MM PACAP21; 40MM REMARK 210 PACAP RECEPTOR; 80MM PHOSPHATE REMARK 210 BUFFER (PH 6.3) REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : TRNOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : IRMA 30-JUL-90 REMARK 210 METHOD USED : ITERATIVE RELAXATION MATRIX REMARK 210 ANALYSIS (IRMA) AND SIMULATED REMARK 210 ANNEALING (SA) REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 12 REMARK 210 REMARK 210 REMARK: BOTH TRNOE AND NOE CROSS PEAKS WERE OBSERVED IN THE REMARK 210 SPECTRUM: THE FORMER REFLECTS THE CONFORMATION OF PACAP21 IN THE REMARK 210 RECEPTOR-BOUND FORM, WHILE THE LATTER REFLECTS THAT OF UNBOUND REMARK 210 PACAP21. UPON ADDITION OF A HIGHER AFFINITY LIGAND, PACAP27, THE REMARK 210 TRNOE CROSS PEAKS WERE SELECTIVELY ELIMINATED DUE TO A REMARK 210 COMPETITIVE INHIBITION OF THE SPECIFIC BINDING OF PACAP21 TO THE REMARK 210 RECEPTOR. ACCORDINGLY, THE SUBTRACTION OF THESE TWO SPECTRA REMARK 210 YIELDS TRNOE-RELATED CROSS PEAKS EXCLUSIVELY. 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 TYR A 10 H ARG A 14 1.37 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 ASP A 3 70.76 -168.79 REMARK 500 1 ILE A 5 -28.25 -39.51 REMARK 500 1 PHE A 6 76.70 -107.77 REMARK 500 1 THR A 7 -144.08 -177.37 REMARK 500 1 MET A 17 -77.50 -49.02 REMARK 500 2 ASP A 3 67.62 -158.84 REMARK 500 2 ILE A 5 -27.81 -39.55 REMARK 500 2 PHE A 6 75.81 -107.10 REMARK 500 2 THR A 7 -144.49 -178.79 REMARK 500 2 ARG A 14 -71.62 -101.59 REMARK 500 2 MET A 17 -74.62 -44.29 REMARK 500 3 ASP A 3 70.21 -166.70 REMARK 500 3 ILE A 5 -28.37 -38.70 REMARK 500 3 PHE A 6 76.20 -107.74 REMARK 500 3 THR A 7 -143.29 -178.54 REMARK 500 3 ARG A 14 -72.86 -102.13 REMARK 500 3 MET A 17 -76.82 -45.56 REMARK 500 3 LYS A 20 -155.41 -77.00 REMARK 500 4 SER A 2 154.12 58.69 REMARK 500 4 ASP A 3 75.90 178.52 REMARK 500 4 ILE A 5 -28.02 -38.52 REMARK 500 4 PHE A 6 76.14 -108.56 REMARK 500 4 THR A 7 -141.16 -177.61 REMARK 500 4 ASP A 8 -60.84 -99.42 REMARK 500 4 ARG A 14 -72.19 -108.58 REMARK 500 4 MET A 17 -73.36 -43.26 REMARK 500 4 LYS A 20 47.74 -83.41 REMARK 500 5 ASP A 3 70.96 -167.03 REMARK 500 5 ILE A 5 -29.91 -37.31 REMARK 500 5 PHE A 6 76.23 -107.59 REMARK 500 5 THR A 7 -142.26 -178.51 REMARK 500 5 MET A 17 -76.77 -45.79 REMARK 500 5 LYS A 20 -160.34 -68.91 REMARK 500 6 ILE A 5 -30.91 -36.92 REMARK 500 6 PHE A 6 75.01 -109.06 REMARK 500 6 THR A 7 -141.66 -173.98 REMARK 500 6 ARG A 14 -70.01 -94.47 REMARK 500 6 MET A 17 -73.52 -43.82 REMARK 500 6 LYS A 20 45.50 -86.50 REMARK 500 7 ASP A 3 72.82 -171.25 REMARK 500 7 ILE A 5 -27.92 -39.05 REMARK 500 7 PHE A 6 77.31 -109.12 REMARK 500 7 THR A 7 -143.43 -177.50 REMARK 500 7 ARG A 14 -75.47 -110.24 REMARK 500 7 MET A 17 -71.99 -41.94 REMARK 500 8 SER A 2 158.96 57.32 REMARK 500 8 ASP A 3 74.22 -177.35 REMARK 500 8 ILE A 5 -28.06 -38.92 REMARK 500 8 PHE A 6 76.38 -107.12 REMARK 500 8 THR A 7 -145.20 -179.01 REMARK 500 REMARK 500 THIS ENTRY HAS 161 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 12 0.28 SIDE CHAIN REMARK 500 1 ARG A 14 0.26 SIDE CHAIN REMARK 500 2 ARG A 12 0.19 SIDE CHAIN REMARK 500 2 ARG A 14 0.19 SIDE CHAIN REMARK 500 3 ARG A 12 0.26 SIDE CHAIN REMARK 500 3 ARG A 14 0.20 SIDE CHAIN REMARK 500 4 ARG A 12 0.24 SIDE CHAIN REMARK 500 4 ARG A 14 0.23 SIDE CHAIN REMARK 500 5 ARG A 12 0.21 SIDE CHAIN REMARK 500 5 ARG A 14 0.27 SIDE CHAIN REMARK 500 6 ARG A 12 0.25 SIDE CHAIN REMARK 500 6 ARG A 14 0.28 SIDE CHAIN REMARK 500 7 ARG A 12 0.31 SIDE CHAIN REMARK 500 7 ARG A 14 0.26 SIDE CHAIN REMARK 500 8 ARG A 12 0.26 SIDE CHAIN REMARK 500 8 ARG A 14 0.17 SIDE CHAIN REMARK 500 9 ARG A 12 0.28 SIDE CHAIN REMARK 500 9 ARG A 14 0.23 SIDE CHAIN REMARK 500 10 ARG A 12 0.28 SIDE CHAIN REMARK 500 10 ARG A 14 0.21 SIDE CHAIN REMARK 500 11 ARG A 12 0.20 SIDE CHAIN REMARK 500 11 ARG A 14 0.15 SIDE CHAIN REMARK 500 12 ARG A 12 0.28 SIDE CHAIN REMARK 500 12 ARG A 14 0.22 SIDE CHAIN REMARK 500 13 ARG A 12 0.19 SIDE CHAIN REMARK 500 13 ARG A 14 0.22 SIDE CHAIN REMARK 500 14 ARG A 12 0.25 SIDE CHAIN REMARK 500 14 ARG A 14 0.24 SIDE CHAIN REMARK 500 15 ARG A 12 0.27 SIDE CHAIN REMARK 500 15 ARG A 14 0.22 SIDE CHAIN REMARK 500 16 ARG A 12 0.30 SIDE CHAIN REMARK 500 16 ARG A 14 0.14 SIDE CHAIN REMARK 500 17 ARG A 12 0.19 SIDE CHAIN REMARK 500 17 ARG A 14 0.27 SIDE CHAIN REMARK 500 18 ARG A 12 0.31 SIDE CHAIN REMARK 500 18 ARG A 14 0.24 SIDE CHAIN REMARK 500 19 ARG A 12 0.27 SIDE CHAIN REMARK 500 19 ARG A 14 0.26 SIDE CHAIN REMARK 500 20 ARG A 12 0.20 SIDE CHAIN REMARK 500 20 ARG A 14 0.22 SIDE CHAIN REMARK 500 21 ARG A 12 0.30 SIDE CHAIN REMARK 500 21 ARG A 14 0.27 SIDE CHAIN REMARK 500 22 ARG A 12 0.31 SIDE CHAIN REMARK 500 22 ARG A 14 0.29 SIDE CHAIN REMARK 500 23 ARG A 12 0.24 SIDE CHAIN REMARK 500 23 ARG A 14 0.13 SIDE CHAIN REMARK 500 24 ARG A 12 0.20 SIDE CHAIN REMARK 500 24 ARG A 14 0.26 SIDE CHAIN REMARK 500 25 ARG A 12 0.21 SIDE CHAIN REMARK 500 25 ARG A 14 0.24 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1GEA A 1 21 UNP P18509 PACA_HUMAN 132 152 SEQADV 1GEA LYN A 21 UNP P18509 LYS 152 MODIFIED RESIDUE SEQRES 1 A 21 HIS SER ASP GLY ILE PHE THR ASP SER TYR SER ARG TYR SEQRES 2 A 21 ARG LYS GLN MET ALA VAL LYS LYN MODRES 1GEA LYN A 21 LYS 2,6-DIAMINO-HEXANOIC ACID AMIDE HET LYN A 21 25 HETNAM LYN 2,6-DIAMINO-HEXANOIC ACID AMIDE FORMUL 1 LYN C6 H16 N3 O 1+ HELIX 1 1 ASP A 8 LYS A 20 1 13 LINK C LYS A 20 N LYN A 21 1555 1555 1.31 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 - 23 20 Bytes