Header list of 1ay3.pdb file
Complete list - 27 20 Bytes
HEADER TOXIN 14-NOV-97 1AY3
TITLE NODULARIN FROM NODULARIA SPUMIGENA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDIC TOXIN NODULARIN;
COMPND 3 CHAIN: A;
COMPND 4 OTHER_DETAILS: TOXIN IS CYCLIC PEPTIDE WITH SEQUENCE 2AS-ARG-MFD-GLU-
COMPND 5 MDH. ALL PEPTIDIC BONDS ARE NON-STANDARD
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NODULARIA SPUMIGENA;
SOURCE 3 ORGANISM_TAXID: 258823;
SOURCE 4 STRAIN: BY1
KEYWDS HEPATOTOXIN, INHIBITOR OF SER/THR-SPECIFIC PROTEIN PHOSPHATASES,
KEYWDS 2 TOXIN
EXPDTA SOLUTION NMR
NUMMDL 27
AUTHOR A.J.ANNILA
REVDAT 6 27-FEB-19 1AY3 1 LINK
REVDAT 5 27-JUL-11 1AY3 1 HETNAM HETSYN REMARK
REVDAT 4 13-JUL-11 1AY3 1 VERSN
REVDAT 3 24-FEB-09 1AY3 1 VERSN
REVDAT 2 26-SEP-01 1AY3 3 ATOM
REVDAT 1 16-AUG-99 1AY3 0
JRNL AUTH A.ANNILA,J.LEHTIMAKI,K.MATTILA,J.E.ERIKSSON,K.SIVONEN,
JRNL AUTH 2 T.T.RANTALA,T.DRAKENBERG
JRNL TITL SOLUTION STRUCTURE OF NODULARIN. AN INHIBITOR OF
JRNL TITL 2 SERINE/THREONINE-SPECIFIC PROTEIN PHOSPHATASES.
JRNL REF J.BIOL.CHEM. V. 271 16695 1996
JRNL REFN ISSN 0021-9258
JRNL PMID 8663277
JRNL DOI 10.1074/JBC.271.28.16695
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : IRMA
REMARK 3 AUTHORS : BOELENS
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ITERATIVE RELAXATION MATRIX ANALYSIS
REMARK 3 T_C = 1.0 NS
REMARK 4
REMARK 4 1AY3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000001216.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 274
REMARK 210 PH : 4.7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY; ROESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIXREMARK 210 METHOD METHOD
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 27
REMARK 210 CONFORMERS, SELECTION CRITERIA : RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 22
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TWO-DIMENSIONAL NMR
REMARK 210 SPECTROSCOPY ON NON-LABELED NODULARIN
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 400
REMARK 400 COMPOUND
REMARK 400 THE SEQUENCE OF NODULARIN MATCHES TO THE SEQUENCE OF NOR00279 IN
REMARK 400 NORINE DATABASE, EXCEPT THAT THE STEREO CHEMISTRY OF RESIDUE MFD IS
REMARK 400 DIFFERENT FROM THAT OF THE CORRESPONDING RESIDUE 1ZN AS INDICATED
REMARK 400 AS ADDA IN NOR00279 SEQUENCE.
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 CG ACB A 1 N ARG A 2 1.38
REMARK 500 N ACB A 1 C MDH A 5 1.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 ARG A 2 CZ ARG A 2 NH1 0.099
REMARK 500 1 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500 2 ARG A 2 CZ ARG A 2 NH1 0.099
REMARK 500 2 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500 3 ARG A 2 CZ ARG A 2 NH1 0.099
REMARK 500 3 ARG A 2 CZ ARG A 2 NH2 0.095
REMARK 500 4 ARG A 2 CZ ARG A 2 NH1 0.099
REMARK 500 4 ARG A 2 CZ ARG A 2 NH2 0.096
REMARK 500 5 ARG A 2 CZ ARG A 2 NH1 0.098
REMARK 500 5 ARG A 2 CZ ARG A 2 NH2 0.095
REMARK 500 6 ARG A 2 CZ ARG A 2 NH1 0.099
REMARK 500 6 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500 7 ARG A 2 CZ ARG A 2 NH1 0.099
REMARK 500 7 ARG A 2 CZ ARG A 2 NH2 0.095
REMARK 500 8 ARG A 2 CZ ARG A 2 NH1 0.098
REMARK 500 8 ARG A 2 CZ ARG A 2 NH2 0.095
REMARK 500 9 ARG A 2 CZ ARG A 2 NH1 0.098
REMARK 500 9 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500 10 ARG A 2 CZ ARG A 2 NH1 0.100
REMARK 500 10 ARG A 2 CZ ARG A 2 NH2 0.095
REMARK 500 11 ARG A 2 CZ ARG A 2 NH1 0.099
REMARK 500 11 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500 12 ARG A 2 CZ ARG A 2 NH1 0.098
REMARK 500 12 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500 13 ARG A 2 CZ ARG A 2 NH1 0.099
REMARK 500 13 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500 14 ARG A 2 CZ ARG A 2 NH1 0.098
REMARK 500 14 ARG A 2 CZ ARG A 2 NH2 0.095
REMARK 500 15 ARG A 2 CZ ARG A 2 NH1 0.098
REMARK 500 15 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500 16 ARG A 2 CZ ARG A 2 NH1 0.099
REMARK 500 16 ARG A 2 CZ ARG A 2 NH2 0.095
REMARK 500 17 ARG A 2 CZ ARG A 2 NH1 0.097
REMARK 500 17 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500 18 ARG A 2 CZ ARG A 2 NH1 0.099
REMARK 500 18 ARG A 2 CZ ARG A 2 NH2 0.095
REMARK 500 19 ARG A 2 CZ ARG A 2 NH1 0.099
REMARK 500 19 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500 20 ARG A 2 CZ ARG A 2 NH1 0.098
REMARK 500 20 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500 21 ARG A 2 CZ ARG A 2 NH1 0.099
REMARK 500 21 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500 22 ARG A 2 CZ ARG A 2 NH1 0.099
REMARK 500 22 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500 23 ARG A 2 CZ ARG A 2 NH1 0.098
REMARK 500 23 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500 24 ARG A 2 CZ ARG A 2 NH1 0.099
REMARK 500 24 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500 25 ARG A 2 CZ ARG A 2 NH1 0.099
REMARK 500 25 ARG A 2 CZ ARG A 2 NH2 0.094
REMARK 500
REMARK 500 THIS ENTRY HAS 54 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AY3 A 1 5 NOR NOR00279 NOR00279 1 5
SEQADV 1AY3 MFD A 3 NOR NOR00279 1ZN 3 CONFLICT
SEQRES 1 A 5 ACB ARG MFD FGA MDH
HET ACB A 1 15
HET MFD A 3 50
HET FGA A 4 14
HET MDH A 5 14
HETNAM ACB 3-METHYL-BETA-D-ASPARTIC ACID
HETNAM MFD (2S,3S,8S,9S)-3-AMINO-9-METHOXY-2,6,8-TRIMETHYL-10-
HETNAM 2 MFD PHENYLDECA-4,6-DIENOIC ACID
HETNAM FGA GAMMA-D-GLUTAMIC ACID
HETNAM MDH N-METHYLDEHYDROBUTYRINE
HETSYN ACB (3S)-3-METHYL-D-ASPARTIC ACID; D-METHYL ASPARTIC ACID
HETSYN FGA D-GLUTAMIC ACID
FORMUL 1 ACB C5 H9 N O4
FORMUL 1 MFD C20 H29 N O3
FORMUL 1 FGA C5 H9 N O4
FORMUL 1 MDH C5 H9 N O2
LINK C ACB A 1 N ARG A 2 1555 1555 3.86
LINK C ARG A 2 N3 MFD A 3 1555 1555 1.39
LINK C1 MFD A 3 N FGA A 4 1555 1555 1.39
LINK CD FGA A 4 N MDH A 5 1555 1555 1.42
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 - 27 20 Bytes