Header list of 2bl6.pdb file
Complete list - n 15 2 Bytes
HEADER NUCLEOCAPSID PROTEIN 02-MAR-05 2BL6 TITLE SOLUTION STRUCTURE OF THE ZN COMPLEX OF EIAV NCP11(22-58) PEPTIDE, TITLE 2 INCLUDING TWO CCHC ZN-BINDING MOTIFS. COMPND MOL_ID: 1; COMPND 2 MOLECULE: NUCLEOCAPSID PROTEIN P11; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 381-417; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: FRAGMENT 22-58 OF NCP11 CORRESPONDS TO 381-417 OF THE COMPND 7 WHOLE EIAV GAG PROTEIN CONTAINS TWO ZN IONS IN TWO CCHC ZN-BINDING COMPND 8 DOMAINS SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: EQUINE INFECTIOUS ANEMIA VIRUS; SOURCE 4 ORGANISM_COMMON: EIAV; SOURCE 5 ORGANISM_TAXID: 11665 KEYWDS NUCLEOCAPSID PROTEIN, LENTIVIRUS, POLYPROTEIN, CORE PROTEIN, KEYWDS 2 RETROVIRUS ZINC FINGER-LIKE DOMAINS EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR P.AMODEO,M.A.CASTIGLIONE-MORELLI,A.OSTUNI,A.BAVOSO REVDAT 4 15-JAN-20 2BL6 1 REMARK REVDAT 3 24-FEB-09 2BL6 1 VERSN REVDAT 2 03-MAY-06 2BL6 1 JRNL REVDAT 1 10-APR-06 2BL6 0 JRNL AUTH P.AMODEO,M.A.CASTIGLIONE-MORELLI,A.OSTUNI,G.BATTISTUZZI, JRNL AUTH 2 A.BAVOSO JRNL TITL STRUCTURAL FEATURES IN EIAV NCP11: A LENTIVIRUS NUCLEOCAPSID JRNL TITL 2 PROTEIN WITH A SHORT LINKER JRNL REF BIOCHEMISTRY V. 45 5517 2006 JRNL REFN ISSN 0006-2960 JRNL PMID 16634633 JRNL DOI 10.1021/BI0524924 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AMBER REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM, FERGUSON, REMARK 3 SEIBEL,SINGH,WEINER,KOLLMAN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING FOLLOWED BY ENERGY REMARK 3 MINIMIZATION, BOTH PERFORMED WITH A GBSA IMPLICIT SOLVENT REMARK 3 APPROACH REMARK 4 REMARK 4 2BL6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-MAR-05. REMARK 100 THE DEPOSITION ID IS D_1290022966. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293.0 REMARK 210 PH : 5.8 REMARK 210 IONIC STRENGTH : 210 REMARK 210 PRESSURE : 1.0 ATM REMARK 210 SAMPLE CONTENTS : 10% WATER/90% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : AMBER REMARK 210 METHOD USED : SIMULATED ANNEALING-ENERGY REMARK 210 MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 150 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY, FAVORABLE REMARK 210 ENERGY, THE LEAST RESTRAINT REMARK 210 VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: NONE 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: 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 ASN A 26 -39.62 -139.41 REMARK 500 1 PRO A 30 -168.39 -72.08 REMARK 500 1 SER A 34 -2.74 -58.03 REMARK 500 1 CYS A 43 -154.66 -147.73 REMARK 500 1 PHE A 44 -23.00 -140.52 REMARK 500 1 LYS A 45 -53.68 -155.67 REMARK 500 1 LYS A 47 24.11 44.16 REMARK 500 1 GLN A 55 -54.85 -149.43 REMARK 500 1 ARG A 57 19.33 -152.10 REMARK 500 2 ASN A 26 -46.85 -132.57 REMARK 500 2 LYS A 41 -9.45 -58.13 REMARK 500 2 CYS A 43 -154.74 -148.62 REMARK 500 2 LYS A 45 -51.49 -158.28 REMARK 500 2 LYS A 47 24.83 42.85 REMARK 500 2 GLN A 55 -51.66 -151.02 REMARK 500 3 ASN A 26 -48.86 -137.09 REMARK 500 3 SER A 34 -2.03 -58.15 REMARK 500 3 CYS A 43 -153.32 -150.29 REMARK 500 3 PHE A 44 -18.00 -143.00 REMARK 500 3 LYS A 45 -62.65 -156.80 REMARK 500 3 LYS A 47 27.88 42.11 REMARK 500 3 GLN A 55 -46.73 -150.06 REMARK 500 4 ASN A 26 -47.92 -134.54 REMARK 500 4 CYS A 43 -153.70 -149.63 REMARK 500 4 LYS A 45 -59.28 -155.98 REMARK 500 4 LYS A 47 26.65 43.14 REMARK 500 4 GLN A 55 -64.44 -152.09 REMARK 500 4 ARG A 57 15.47 -144.83 REMARK 500 5 ASN A 26 -47.73 -135.55 REMARK 500 5 CYS A 43 -152.77 -150.23 REMARK 500 5 PHE A 44 -20.34 -140.25 REMARK 500 5 LYS A 45 -57.52 -156.96 REMARK 500 5 LYS A 47 27.04 42.43 REMARK 500 5 GLN A 55 -47.46 -149.38 REMARK 500 6 ASN A 26 -48.73 -131.83 REMARK 500 6 CYS A 43 -158.69 -148.92 REMARK 500 6 LYS A 45 -61.68 -157.22 REMARK 500 6 LYS A 47 20.60 44.42 REMARK 500 6 GLN A 55 -51.60 -150.34 REMARK 500 6 ARG A 57 19.37 -152.64 REMARK 500 7 ASN A 26 -47.79 -135.54 REMARK 500 7 CYS A 43 -157.24 -149.44 REMARK 500 7 LYS A 45 -62.21 -158.65 REMARK 500 7 LYS A 47 24.16 44.08 REMARK 500 7 GLN A 55 -57.97 -150.90 REMARK 500 7 ARG A 57 15.72 -143.77 REMARK 500 8 ASN A 26 -48.32 -135.05 REMARK 500 8 CYS A 43 -156.78 -149.35 REMARK 500 8 LYS A 45 -56.60 -156.00 REMARK 500 8 LYS A 47 24.88 43.19 REMARK 500 REMARK 500 THIS ENTRY HAS 196 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A1059 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 24 SG REMARK 620 2 CYS A 27 SG 105.0 REMARK 620 3 HIS A 32 NE2 105.0 113.9 REMARK 620 4 CYS A 37 SG 108.8 117.8 105.7 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A1060 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 46 SG REMARK 620 2 HIS A 51 NE2 101.9 REMARK 620 3 CYS A 56 SG 117.9 105.2 REMARK 620 4 CYS A 43 SG 103.0 103.3 122.7 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1059 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1060 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1EIA RELATED DB: PDB REMARK 900 X-RAY CRYSTAL STRUCTURE OF EQUINE INFECTIOUS ANEMIA VIRUS(EIAV) REMARK 900 CAPSID PROTEIN P26 REMARK 900 RELATED ID: 1HEK RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF EQUINE INFECTIOUS ANAEMIA VIRUS MATRIX ANTIGEN REMARK 900 (EIAV MA) REMARK 900 RELATED ID: 2EIA RELATED DB: PDB REMARK 900 X-RAY CRYSTAL STRUCTURE OF EQUINE INFECTIOUS ANEMIA VIRUS(EIAV) REMARK 900 CAPSID PROTEIN P26 REMARK 900 RELATED ID: 7352 RELATED DB: BMRB DBREF 2BL6 A 22 58 UNP P69732 GAG_EIAVY 381 417 SEQRES 1 A 37 GLN THR CYS TYR ASN CYS GLY LYS PRO GLY HIS LEU SER SEQRES 2 A 37 SER GLN CYS ARG ALA PRO LYS VAL CYS PHE LYS CYS LYS SEQRES 3 A 37 GLN PRO GLY HIS PHE SER LYS GLN CYS ARG SER HET ZN A1059 1 HET ZN A1060 1 HETNAM ZN ZINC ION FORMUL 2 ZN 2(ZN 2+) HELIX 1 1 GLY A 50 GLN A 55 5 6 LINK ZN ZN A1059 SG CYS A 24 1555 1555 2.20 LINK ZN ZN A1059 SG CYS A 27 1555 1555 2.19 LINK ZN ZN A1059 NE2 HIS A 32 1555 1555 2.16 LINK ZN ZN A1059 SG CYS A 37 1555 1555 2.18 LINK ZN ZN A1060 SG CYS A 46 1555 1555 2.18 LINK ZN ZN A1060 NE2 HIS A 51 1555 1555 2.07 LINK ZN ZN A1060 SG CYS A 56 1555 1555 2.17 LINK ZN ZN A1060 SG CYS A 43 1555 1555 2.17 SITE 1 AC1 4 CYS A 24 CYS A 27 HIS A 32 CYS A 37 SITE 1 AC2 5 CYS A 43 CYS A 46 HIS A 51 GLN A 55 SITE 2 AC2 5 CYS A 56 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 - n 15 2 Bytes