Header list of 1mfs.pdb file
Complete list - v 29 2 Bytes
HEADER VIRAL PROTEIN 01-APR-98 1MFS TITLE DYNAMICAL BEHAVIOR OF THE HIV-1 NUCLEOCAPSID PROTEIN; NMR, 30 TITLE 2 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: HIV-1 NUCLEOCAPSID PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: NUCLEOCAPSID, ZINC BINDING DOMAINS; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS; SOURCE 3 ORGANISM_TAXID: 12721; SOURCE 4 STRAIN: NL4-3; SOURCE 5 CELL_LINE: BL21; SOURCE 6 GENE: NC; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSE; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-3A; SOURCE 11 EXPRESSION_SYSTEM_GENE: NC KEYWDS NUCLEOCAPSID PROTEIN, DYNAMICS, ZINC KNUCKLE, HIV-1, ZINC BINDING, KEYWDS 2 VIRAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR M.F.SUMMERS,B.G.TURNER,R.N.DE GUZMAN,B.M.LEE,N.TJANDRA REVDAT 3 29-NOV-17 1MFS 1 REMARK HELIX REVDAT 2 24-FEB-09 1MFS 1 VERSN REVDAT 1 17-JUN-98 1MFS 0 JRNL AUTH B.M.LEE,R.N.DE GUZMAN,B.G.TURNER,N.TJANDRA,M.F.SUMMERS JRNL TITL DYNAMICAL BEHAVIOR OF THE HIV-1 NUCLEOCAPSID PROTEIN. JRNL REF J.MOL.BIOL. V. 279 633 1998 JRNL REFN ISSN 0022-2836 JRNL PMID 9641983 JRNL DOI 10.1006/JMBI.1998.1766 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DIANA 2.8 REMARK 3 AUTHORS : WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: DETAILS OF THE REFINEMENT AND STRATEGY REMARK 3 ARE LOCATED IN THE PUBLICATION REMARK 4 REMARK 4 1MFS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000174993. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; TOCSY; HSQC; HMQC; 3D REMARK 210 NOESY-HSQC; 3D TOCSY-HSQC; 3D REMARK 210 HMQC-NOESY; 4D CNNOE REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : BRUKER DMX; GE OMEGA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; GE REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DIANA REMARK 210 METHOD USED : DISTANCE GEOMETRY REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 30 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 PHE A 6 -45.05 -138.06 REMARK 500 1 ARG A 7 76.06 -100.81 REMARK 500 1 ASN A 8 -84.38 60.42 REMARK 500 1 GLN A 9 -64.35 -178.18 REMARK 500 1 LYS A 11 162.31 86.27 REMARK 500 1 THR A 12 -164.15 46.93 REMARK 500 1 VAL A 13 -174.40 48.25 REMARK 500 1 ARG A 32 165.21 179.57 REMARK 500 1 LYS A 33 -104.31 40.50 REMARK 500 1 LYS A 41 101.11 -56.09 REMARK 500 1 ALA A 54 -62.18 74.32 REMARK 500 2 GLN A 2 -59.20 179.88 REMARK 500 2 LYS A 3 -62.74 -168.41 REMARK 500 2 ASN A 5 113.81 176.28 REMARK 500 2 PHE A 6 -164.36 41.77 REMARK 500 2 ARG A 7 -61.28 71.94 REMARK 500 2 ASN A 8 -52.59 -137.85 REMARK 500 2 GLN A 9 80.29 -69.35 REMARK 500 2 ARG A 10 83.68 -172.19 REMARK 500 2 VAL A 13 160.44 -41.85 REMARK 500 2 ALA A 30 153.63 60.02 REMARK 500 2 ARG A 32 -91.01 -108.20 REMARK 500 2 LYS A 34 -60.16 71.88 REMARK 500 2 LYS A 47 -30.89 -39.79 REMARK 500 2 ASP A 48 45.14 -155.14 REMARK 500 2 ARG A 52 129.22 65.25 REMARK 500 2 GLN A 53 -76.98 63.91 REMARK 500 3 GLN A 2 -59.62 -120.88 REMARK 500 3 LYS A 3 -66.43 74.34 REMARK 500 3 ASN A 5 -50.93 -159.96 REMARK 500 3 GLN A 9 61.18 70.93 REMARK 500 3 ARG A 10 -69.77 -134.16 REMARK 500 3 ARG A 32 94.20 -165.54 REMARK 500 3 LYS A 33 78.30 -104.49 REMARK 500 3 LYS A 34 -76.34 75.24 REMARK 500 3 ASP A 48 40.05 -156.21 REMARK 500 3 CYS A 49 -103.24 -73.55 REMARK 500 3 THR A 50 19.55 51.78 REMARK 500 3 GLU A 51 -152.44 -78.29 REMARK 500 3 ALA A 54 -77.86 64.63 REMARK 500 4 GLN A 2 172.94 179.75 REMARK 500 4 ASN A 5 139.80 170.66 REMARK 500 4 PHE A 6 102.39 55.56 REMARK 500 4 ARG A 7 57.76 -170.03 REMARK 500 4 HIS A 23 -179.94 -175.08 REMARK 500 4 LYS A 33 -73.12 -50.68 REMARK 500 4 LYS A 34 -148.80 76.96 REMARK 500 4 ALA A 54 -62.03 74.54 REMARK 500 5 GLN A 2 -74.31 -90.77 REMARK 500 5 LYS A 3 -63.04 -136.29 REMARK 500 REMARK 500 THIS ENTRY HAS 331 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 A 56 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 15 SG REMARK 620 2 CYS A 18 SG 85.9 REMARK 620 3 HIS A 23 NE2 86.0 93.6 REMARK 620 4 CYS A 28 SG 105.6 131.8 133.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 57 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 36 SG REMARK 620 2 CYS A 39 SG 85.8 REMARK 620 3 HIS A 44 NE2 105.1 82.4 REMARK 620 4 CYS A 49 SG 123.9 139.2 111.2 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: MNG REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: THESE 4 RESIDUES ARE THE ZINC BINDING LIGANDS OF REMARK 800 THE SECOND ZINC FINGER DOMAIN OF P7. REMARK 800 REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 56 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 57 DBREF 1MFS A 1 55 UNP P35963 POL_HV1Y2 377 431 SEQADV 1MFS LYS A 3 UNP P35963 ARG 379 CONFLICT SEQRES 1 A 55 MET GLN LYS GLY ASN PHE ARG ASN GLN ARG LYS THR VAL SEQRES 2 A 55 LYS CYS PHE ASN CYS GLY LYS GLU GLY HIS ILE ALA LYS SEQRES 3 A 55 ASN CYS ARG ALA PRO ARG LYS LYS GLY CYS TRP LYS CYS SEQRES 4 A 55 GLY LYS GLU GLY HIS GLN MET LYS ASP CYS THR GLU ARG SEQRES 5 A 55 GLN ALA ASN HET ZN A 56 1 HET ZN A 57 1 HETNAM ZN ZINC ION FORMUL 2 ZN 2(ZN 2+) HELIX 1 H1 ILE A 24 CYS A 28 1 5 HELIX 2 H2 GLN A 45 CYS A 49 1 5 SHEET 1 S1 2 THR A 12 PHE A 16 0 SHEET 2 S1 2 CYS A 18 GLY A 22 -1 SHEET 1 S2 2 LYS A 34 TRP A 37 0 SHEET 2 S2 2 CYS A 39 GLY A 43 -1 LINK ZN ZN A 56 SG CYS A 15 1555 1555 2.35 LINK ZN ZN A 56 SG CYS A 18 1555 1555 2.35 LINK ZN ZN A 56 NE2 HIS A 23 1555 1555 2.05 LINK ZN ZN A 56 SG CYS A 28 1555 1555 2.30 LINK ZN ZN A 57 SG CYS A 36 1555 1555 2.35 LINK ZN ZN A 57 SG CYS A 39 1555 1555 2.35 LINK ZN ZN A 57 NE2 HIS A 44 1555 1555 2.04 LINK ZN ZN A 57 SG CYS A 49 1555 1555 2.30 SITE 1 MNG 8 CYS A 15 CYS A 18 HIS A 23 CYS A 28 SITE 2 MNG 8 CYS A 36 CYS A 39 HIS A 44 CYS A 49 SITE 1 AC1 4 CYS A 15 CYS A 18 HIS A 23 CYS A 28 SITE 1 AC2 4 CYS A 36 CYS A 39 HIS A 44 CYS A 49 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 - v 29 2 Bytes