Header list of 1ckx.pdb file
Complete list - 16 20 Bytes
HEADER METAL TRANSPORT 26-APR-99 1CKX
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: CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR (CFTR);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: P26 IN TRIFLUOROETHANOL;
COMPND 5 SYNONYM: P26_TFE;
COMPND 6 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.
KEYWDS P26_TFE, 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 1CKX 1 REMARK
REVDAT 3 24-FEB-09 1CKX 1 VERSN
REVDAT 2 29-DEC-99 1CKX 1 JRNL REMARK HEADER
REVDAT 1 04-MAY-99 1CKX 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 1CKX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000943.
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 : 43% TRIFLUROETHANOL-D2 / H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY SPECTRA
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:
REMARK 210 THE SOLUTION STRUCTURES OF THE PEPTIDE (P26) BASED ON THE PHE508
REMARK 210 REGION OF
REMARK 210 CFTR WERE DETERMINED BY HOMONUCLEAR 1H NMR SPECTROSCOPY PERFORMED
REMARK 210 AT 600 MHZ.
REMARK 210 THE PEPTIDE WAS SYNTHETICALLY MADE AND WAS UNLABELED. NOESY AT 100,
REMARK 210 200 AND 300
REMARK 210 MS MIXING TIMES, A TOCSY AT 65 MS AND COSY SPECTRA WERE COLLECTED
REMARK 210 AT 25OC IN
REMARK 210 43% TFE-D2 AND H2O.
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 GLU A 7 H PHE A 11 1.44
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 2 LYS A 25 -170.14 -64.21
REMARK 500 4 PRO A 2 -168.02 -72.64
REMARK 500 4 LYS A 25 -94.36 40.81
REMARK 500 7 ILE A 10 -52.23 -124.85
REMARK 500 7 ILE A 24 38.61 -142.80
REMARK 500 7 LYS A 25 -71.93 -54.00
REMARK 500 9 THR A 4 -36.41 -137.94
REMARK 500 9 TYR A 20 -72.72 -95.42
REMARK 500 10 ILE A 10 -52.32 -121.96
REMARK 500 11 THR A 4 -42.79 -137.88
REMARK 500 11 ILE A 10 -52.11 -120.55
REMARK 500 13 LYS A 25 84.22 42.38
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 19 0.32 SIDE CHAIN
REMARK 500 1 ARG A 21 0.17 SIDE CHAIN
REMARK 500 2 ARG A 19 0.16 SIDE CHAIN
REMARK 500 2 ARG A 21 0.30 SIDE CHAIN
REMARK 500 3 ARG A 19 0.13 SIDE CHAIN
REMARK 500 3 ARG A 21 0.25 SIDE CHAIN
REMARK 500 4 ARG A 19 0.31 SIDE CHAIN
REMARK 500 4 ARG A 21 0.32 SIDE CHAIN
REMARK 500 5 ARG A 19 0.09 SIDE CHAIN
REMARK 500 5 ARG A 21 0.32 SIDE CHAIN
REMARK 500 6 ARG A 19 0.23 SIDE CHAIN
REMARK 500 6 ARG A 21 0.31 SIDE CHAIN
REMARK 500 7 ARG A 19 0.27 SIDE CHAIN
REMARK 500 7 ARG A 21 0.20 SIDE CHAIN
REMARK 500 8 ARG A 21 0.28 SIDE CHAIN
REMARK 500 9 ARG A 19 0.28 SIDE CHAIN
REMARK 500 9 ARG A 21 0.30 SIDE CHAIN
REMARK 500 10 ARG A 19 0.31 SIDE CHAIN
REMARK 500 10 ARG A 21 0.32 SIDE CHAIN
REMARK 500 11 ARG A 19 0.13 SIDE CHAIN
REMARK 500 11 ARG A 21 0.32 SIDE CHAIN
REMARK 500 12 ARG A 19 0.26 SIDE CHAIN
REMARK 500 12 ARG A 21 0.17 SIDE CHAIN
REMARK 500 13 ARG A 19 0.15 SIDE CHAIN
REMARK 500 13 ARG A 21 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CKX A 1 26 UNP Q00555 CFTR_SHEEP 497 522
SEQADV 1CKX GLU A 7 UNP Q00555 ASP 503 SEE REMARK 999
SEQRES 1 A 26 MET PRO GLY THR ILE LYS GLU ASN ILE ILE PHE GLY VAL
SEQRES 2 A 26 SER TYR ASP GLU TYR ARG TYR ARG SER VAL ILE LYS ALA
HELIX 1 H1 THR A 4 LYS A 25 1 22
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