Header list of 1ckz.pdb file
Complete list - 16 20 Bytes
HEADER METAL TRANSPORT 26-APR-99 1CKZ TITLE CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR: SOLUTION TITLE 2 STRUCTURES OF PEPTIDES BASED ON THE PHE508 REGION, THE MOST COMMON TITLE 3 SITE OF DISEASE-CAUSING DELTA-F508 MUTATION COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE COMPND 3 REGULATOR (CFTR)); COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: P25, F508 MUTATION REGION; COMPND 6 SYNONYM: P25_H2O; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE SOURCE 4 IS BASED ON THE PHE508 REGION OF CF TRANSMEMBRANE REGULATOR SOURCE 5 NUCLEOTIDE BINDING DOMAIN 1. KEYWDS CYSTIC FIBROSIS, PEPTIDES, METAL TRANSPORT EXPDTA SOLUTION NMR NUMMDL 13 AUTHOR M.A.MASSIAH,Y.H.KO,P.L.PEDERSEN,A.S.MILDVAN REVDAT 4 16-FEB-22 1CKZ 1 REMARK SEQADV REVDAT 3 24-FEB-09 1CKZ 1 VERSN REVDAT 2 29-DEC-99 1CKZ 1 JRNL HEADER REMARK REVDAT 1 04-MAY-99 1CKZ 0 JRNL AUTH M.A.MASSIAH,Y.H.KO,P.L.PEDERSEN,A.S.MILDVAN JRNL TITL CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR: JRNL TITL 2 SOLUTION STRUCTURES OF PEPTIDES BASED ON THE PHE508 REGION, JRNL TITL 3 THE MOST COMMON SITE OF DISEASE-CAUSING DELTAF508 MUTATION. JRNL EDIT H.GORDON JRNL REF BIOCHEMISTRY V. 38 7453 1999 JRNL REFN ISSN 0006-2960 JRNL PMID 10360942 JRNL DOI 10.1021/BI9903603 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.8 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1CKZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-99. REMARK 100 THE DEPOSITION ID IS D_1000000945. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 4.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 90% WATER / 10% DMSO-D6 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW2.1 REMARK 210 METHOD USED : DISTANCE GEOMETRY REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 13 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINTS VIOLATIONS AND REMARK 210 LOW ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE SOLUTION STRUCTURES OF THE PEPTIDE (P25) BASED ON THE REMARK 210 PHE508 REGION OF CFTR WAS DETERMINED BY HOMONUCLEAR 1H NMR REMARK 210 SPECTROSCOPY PERFORMED AT 600 MHZ. THE PEPTIDE WAS SYNTHETICALLY REMARK 210 MADE AND WAS UNLABELED. 2D 1H NOESY SPECTRUM USING 100,200 AND REMARK 210 300 MIXING TIMES, 2D TOCSY AT 65 MS AND 2D COSY SPECTRA WERE REMARK 210 COLLECTED WITH THE PEPTIDE IN 90%H2O/10%DMSO-D6. 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 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 THR A 4 58.26 -119.69 REMARK 500 1 ILE A 5 48.43 -80.03 REMARK 500 1 LYS A 6 35.00 -152.82 REMARK 500 1 GLU A 7 70.64 -169.16 REMARK 500 1 ASN A 8 45.62 -80.99 REMARK 500 1 ILE A 10 44.60 -71.83 REMARK 500 1 VAL A 12 -67.29 -91.77 REMARK 500 1 GLU A 16 17.93 -155.23 REMARK 500 1 TYR A 17 41.94 171.76 REMARK 500 1 ARG A 18 51.27 -92.78 REMARK 500 1 LYS A 24 161.03 -48.40 REMARK 500 2 PRO A 2 -163.67 -72.18 REMARK 500 2 THR A 4 43.65 -86.10 REMARK 500 2 LYS A 6 51.26 179.29 REMARK 500 2 GLU A 7 58.41 -96.30 REMARK 500 2 ASN A 8 47.71 -76.45 REMARK 500 2 ILE A 10 45.24 -66.11 REMARK 500 2 ASP A 15 55.31 -154.76 REMARK 500 2 GLU A 16 -39.89 -161.74 REMARK 500 2 TYR A 17 42.33 -93.26 REMARK 500 2 ARG A 20 40.41 35.33 REMARK 500 2 ILE A 23 32.85 -94.80 REMARK 500 2 LYS A 24 56.40 158.37 REMARK 500 3 THR A 4 40.21 -89.89 REMARK 500 3 LYS A 6 49.11 -148.07 REMARK 500 3 VAL A 12 -53.94 67.34 REMARK 500 3 TYR A 14 48.07 -146.89 REMARK 500 3 GLU A 16 40.58 -145.83 REMARK 500 3 TYR A 19 62.21 78.94 REMARK 500 3 ARG A 20 39.99 -70.00 REMARK 500 3 ILE A 23 54.99 -118.10 REMARK 500 4 ILE A 5 58.08 23.66 REMARK 500 4 ILE A 9 -51.97 -122.89 REMARK 500 4 ILE A 10 48.64 28.29 REMARK 500 4 VAL A 12 -83.07 -105.93 REMARK 500 4 SER A 13 92.42 -68.25 REMARK 500 4 TYR A 17 26.44 -159.55 REMARK 500 4 ARG A 18 43.91 27.42 REMARK 500 4 ARG A 20 40.24 -90.82 REMARK 500 4 SER A 21 34.55 -89.30 REMARK 500 4 ILE A 23 73.52 37.38 REMARK 500 4 LYS A 24 99.54 43.39 REMARK 500 5 THR A 4 38.87 -88.42 REMARK 500 5 ILE A 5 44.25 35.27 REMARK 500 5 LYS A 6 19.07 -151.04 REMARK 500 5 GLU A 7 68.60 169.36 REMARK 500 5 ILE A 9 -51.97 -147.49 REMARK 500 5 ILE A 10 42.68 35.43 REMARK 500 5 VAL A 12 -92.39 -68.63 REMARK 500 5 SER A 13 63.59 35.61 REMARK 500 REMARK 500 THIS ENTRY HAS 138 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 18 0.26 SIDE CHAIN REMARK 500 1 ARG A 20 0.32 SIDE CHAIN REMARK 500 2 ARG A 18 0.29 SIDE CHAIN REMARK 500 2 ARG A 20 0.17 SIDE CHAIN REMARK 500 3 ARG A 18 0.30 SIDE CHAIN REMARK 500 3 ARG A 20 0.22 SIDE CHAIN REMARK 500 4 ARG A 18 0.29 SIDE CHAIN REMARK 500 4 ARG A 20 0.21 SIDE CHAIN REMARK 500 5 ARG A 18 0.22 SIDE CHAIN REMARK 500 5 ARG A 20 0.22 SIDE CHAIN REMARK 500 6 ARG A 18 0.23 SIDE CHAIN REMARK 500 6 ARG A 20 0.17 SIDE CHAIN REMARK 500 7 ARG A 18 0.30 SIDE CHAIN REMARK 500 7 ARG A 20 0.29 SIDE CHAIN REMARK 500 8 ARG A 18 0.32 SIDE CHAIN REMARK 500 8 ARG A 20 0.28 SIDE CHAIN REMARK 500 9 ARG A 18 0.26 SIDE CHAIN REMARK 500 9 ARG A 20 0.31 SIDE CHAIN REMARK 500 10 ARG A 18 0.29 SIDE CHAIN REMARK 500 10 ARG A 20 0.32 SIDE CHAIN REMARK 500 11 ARG A 18 0.31 SIDE CHAIN REMARK 500 11 ARG A 20 0.27 SIDE CHAIN REMARK 500 12 ARG A 18 0.27 SIDE CHAIN REMARK 500 12 ARG A 20 0.25 SIDE CHAIN REMARK 500 13 ARG A 18 0.28 SIDE CHAIN REMARK 500 13 ARG A 20 0.32 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1CKW RELATED DB: PDB REMARK 900 RELATED ID: 1CKX RELATED DB: PDB REMARK 900 RELATED ID: 1CKY RELATED DB: PDB DBREF 1CKZ A 1 25 UNP Q00555 CFTR_SHEEP 497 522 SEQADV 1CKZ GLU A 7 UNP Q00555 ASP 503 SEE REMARK 999 SEQADV 1CKZ A UNP Q00555 PHE 507 DELETION SEQRES 1 A 25 MET PRO GLY THR ILE LYS GLU ASN ILE ILE GLY VAL SER SEQRES 2 A 25 TYR ASP GLU TYR ARG TYR ARG SER VAL ILE LYS ALA 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 - 16 20 Bytes