Header list of 1k8v.pdb file
Complete list - b 23 2 Bytes
HEADER UNKNOWN FUNCTION 25-OCT-01 1K8V
TITLE THE NMR-DERIVED CONFORMATION OF NEUROPEPTIDE F FROM MONIEZIA EXPANSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROPEPTIDE F;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN MONIEZIA EXPANSA
SOURCE 4 (SHEEP TAPEWORM).
KEYWDS NEUROPEPTIDE F, MONIEZIA EXPANSA, NPF, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.MISKOLZIE,G.KOTOVYCH
REVDAT 4 23-FEB-22 1K8V 1 REMARK LINK
REVDAT 3 21-APR-09 1K8V 1 REMARK
REVDAT 2 24-FEB-09 1K8V 1 VERSN
REVDAT 1 12-JUN-02 1K8V 0
JRNL AUTH M.MISKOLZIE,G.KOTOVYCH
JRNL TITL THE NMR-DERIVED CONFORMATION OF NEUROPEPTIDE F FROM MONIEZIA
JRNL TITL 2 EXPANSA.
JRNL REF J.BIOMOL.STRUCT.DYN. V. 19 991 2002
JRNL REFN ISSN 0739-1102
JRNL PMID 12023801
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, CNS 1.0
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER, A.T. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K8V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014705.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.85
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.4MM NEUROPEPTIDE F
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.0.3, CNS 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 : 4
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 40
DBREF 1K8V A 1 39 UNP P41967 NPF_MONEX 1 39
SEQRES 1 A 40 PRO ASP LYS ASP PHE ILE VAL ASN PRO SER ASP LEU VAL
SEQRES 2 A 40 LEU ASP ASN LYS ALA ALA LEU ARG ASP TYR LEU ARG GLN
SEQRES 3 A 40 ILE ASN GLU TYR PHE ALA ILE ILE GLY ARG PRO ARG PHE
SEQRES 4 A 40 NH2
HET NH2 A 40 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 ALA A 18 ARG A 36 1 19
LINK C PHE A 39 N NH2 A 40 1555 1555 1.33
SITE 1 AC1 1 PHE A 39
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