Header list of 2atg.pdb file
Complete list - 9 20 Bytes
HEADER ANTIVIRAL PROTEIN 24-AUG-05 2ATG
TITLE NMR STRUCTURE OF RETROCYCLIN-2 IN SDS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RETROCYCLIN-2;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE IS AN EXPRESSED PSEUDOGENE IN THE HUMAN
SOURCE 4 GENOME.
KEYWDS BETA-SHEET, CIRCULAR PEPTIDE, LADDERED DISULFIDE CONNECTIVITY,
KEYWDS 2 ANTIVIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.L.DALY,Y.K.CHEN,K.J.ROSENGREN,U.C.MARX,M.L.PHILLIPS,A.J.WARING,
AUTHOR 2 W.WANG,R.I.LEHRER,D.J.CRAIK
REVDAT 3 09-MAR-22 2ATG 1 REMARK LINK
REVDAT 2 27-MAY-08 2ATG 1 JRNL VERSN
REVDAT 1 06-SEP-05 2ATG 0
JRNL AUTH N.L.DALY,Y.K.CHEN,K.J.ROSENGREN,U.C.MARX,M.L.PHILLIPS,
JRNL AUTH 2 A.J.WARING,W.WANG,R.I.LEHRER,D.J.CRAIK
JRNL TITL RETROCYCLIN-2: STRUCTURAL ANALYSIS OF A POTENT ANTI-HIV
JRNL TITL 2 THETA-DEFENSIN
JRNL REF BIOCHEMISTRY V. 46 9920 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17685559
JRNL DOI 10.1021/BI700720E
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ATG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1000034290.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : 1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6MM RETROCYCLIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY; E
REMARK 210 -COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.7, DYANA 1.5, CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 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 ARG A 2 -35.13 -173.47
REMARK 500 1 CYS A 13 120.00 -160.66
REMARK 500 2 ARG A 2 -36.25 -171.91
REMARK 500 2 ARG A 10 49.42 -80.28
REMARK 500 2 CYS A 13 116.45 -161.32
REMARK 500 3 ARG A 2 -45.07 -176.96
REMARK 500 4 ARG A 2 -51.72 -156.10
REMARK 500 4 ARG A 10 49.12 -79.21
REMARK 500 4 CYS A 13 98.78 -162.95
REMARK 500 5 ARG A 2 -30.20 -138.25
REMARK 500 5 ARG A 10 49.65 -92.10
REMARK 500 6 ARG A 2 -45.13 -158.56
REMARK 500 9 ARG A 2 -53.52 -169.83
REMARK 500 9 ARG A 10 49.05 -73.95
REMARK 500 11 ARG A 2 -34.40 -171.70
REMARK 500 11 CYS A 13 106.53 -161.08
REMARK 500 12 ARG A 2 -31.08 -171.79
REMARK 500 13 ARG A 2 -31.12 -179.36
REMARK 500 13 ARG A 10 49.43 -80.18
REMARK 500 13 CYS A 13 87.77 -160.76
REMARK 500 14 ARG A 2 -32.77 -157.60
REMARK 500 16 ARG A 2 -36.90 -173.77
REMARK 500 17 ARG A 2 -32.40 -166.25
REMARK 500 17 CYS A 13 90.66 -161.96
REMARK 500 18 CYS A 4 91.51 -166.84
REMARK 500 18 ARG A 10 49.33 -82.97
REMARK 500 19 ARG A 2 -43.70 -131.92
REMARK 500 19 CYS A 4 87.07 -159.25
REMARK 500 19 ARG A 10 48.72 -82.28
REMARK 500 20 CYS A 13 111.56 -160.07
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2ATG A 1 18 PDB 2ATG 2ATG 1 18
SEQRES 1 A 18 ARG ARG ILE CYS ARG CYS ILE CYS GLY ARG GLY ILE CYS
SEQRES 2 A 18 ARG CYS ILE CYS GLY
SHEET 1 A 2 ILE A 3 CYS A 4 0
SHEET 2 A 2 CYS A 17 GLY A 18 -1 O GLY A 18 N ILE A 3
SHEET 1 B 2 ILE A 7 CYS A 8 0
SHEET 2 B 2 CYS A 13 ARG A 14 -1 O ARG A 14 N ILE A 7
SSBOND 1 CYS A 4 CYS A 17 1555 1555 2.03
SSBOND 2 CYS A 6 CYS A 15 1555 1555 2.03
SSBOND 3 CYS A 8 CYS A 13 1555 1555 2.03
LINK N ARG A 1 C GLY A 18 1555 1555 1.34
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 - 9 20 Bytes