Header list of 1cl4.pdb file
Complete list - 3 20 Bytes
HEADER VIRAL PROTEIN 06-MAY-99 1CL4
TITLE NUCLEOCAPSID PROTEIN FROM MASON-PFIZER MONKEY VIRUS (MPMV)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (GAG POLYPROTEIN);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GAG RESIDUES 574-605 (P14 RESIDUES 49-80);
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MASON-PFIZER MONKEY VIRUS;
SOURCE 3 ORGANISM_TAXID: 11855;
SOURCE 4 GENE: NCP14;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET3D;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PT72180.MPMV;
SOURCE 10 EXPRESSION_SYSTEM_GENE: NCP14_2180
KEYWDS NUCLEOCAPSID PROTEIN, RNA BINDING PROTEIN, RETROVIRUS, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 12
AUTHOR Y.GAO,K.KALUARACHCHI,D.P.GIEDROC
REVDAT 3 03-NOV-21 1CL4 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1CL4 1 VERSN
REVDAT 1 11-MAY-99 1CL4 0
JRNL AUTH Y.GAO,K.KALUARACHCHI,D.P.GIEDROC
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF MASON-PFIZER
JRNL TITL 2 MONKEY VIRUS (MPMV) NUCLEOCAPSID PROTEIN.
JRNL REF PROTEIN SCI. V. 7 2265 1998
JRNL REFN ISSN 0961-8368
JRNL PMID 9827993
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1CL4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000001011.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; UNITY INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 12
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-12
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 21
REMARK 465 GLY A 22
REMARK 465 SER A 23
REMARK 465 CYS A 24
REMARK 465 PHE A 25
REMARK 465 LYS A 26
REMARK 465 CYS A 27
REMARK 465 GLY A 28
REMARK 465 LYS A 29
REMARK 465 LYS A 30
REMARK 465 GLY A 31
REMARK 465 HIS A 32
REMARK 465 PHE A 33
REMARK 465 ALA A 34
REMARK 465 LYS A 35
REMARK 465 ASN A 36
REMARK 465 CYS A 37
REMARK 465 HIS A 38
REMARK 465 GLU A 39
REMARK 465 HIS A 40
REMARK 465 ALA A 41
REMARK 465 HIS A 42
REMARK 465 ASN A 43
REMARK 465 ASN A 44
REMARK 465 ALA A 45
REMARK 465 GLU A 46
REMARK 465 PRO A 47
REMARK 465 LYS A 48
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 LEU A 52 94.56 -31.14
REMARK 500 1 CYS A 53 130.53 -22.42
REMARK 500 1 CYS A 56 -145.14 -110.92
REMARK 500 1 LYS A 57 18.85 -161.02
REMARK 500 1 LYS A 60 54.63 -119.29
REMARK 500 1 GLU A 65 62.74 -106.95
REMARK 500 1 ASP A 71 -156.00 -148.25
REMARK 500 1 GLN A 73 -95.17 -133.21
REMARK 500 2 LEU A 52 -68.26 -2.65
REMARK 500 2 CYS A 53 124.44 141.34
REMARK 500 2 CYS A 56 -144.32 -104.18
REMARK 500 2 LYS A 57 25.52 -164.00
REMARK 500 2 LYS A 60 78.95 -161.76
REMARK 500 2 HIS A 61 -173.31 -172.60
REMARK 500 2 ASN A 64 -39.96 -39.76
REMARK 500 2 GLU A 65 59.02 -116.51
REMARK 500 2 SER A 68 63.96 -174.50
REMARK 500 2 LYS A 69 98.68 -66.13
REMARK 500 2 ASP A 71 -88.59 -119.43
REMARK 500 2 GLN A 73 -155.12 -119.11
REMARK 500 2 ILE A 77 77.75 -110.09
REMARK 500 3 LEU A 52 -68.14 -4.90
REMARK 500 3 CYS A 53 122.73 142.37
REMARK 500 3 CYS A 56 -143.11 -107.61
REMARK 500 3 LYS A 57 27.49 -164.11
REMARK 500 3 LYS A 60 77.24 -161.28
REMARK 500 3 HIS A 61 -170.44 -179.50
REMARK 500 3 ALA A 63 -87.13 -37.26
REMARK 500 3 ASN A 64 90.79 -55.62
REMARK 500 3 GLU A 65 31.00 118.44
REMARK 500 3 SER A 68 26.67 -167.43
REMARK 500 3 LYS A 69 95.17 -45.99
REMARK 500 3 ASP A 71 -60.08 -165.58
REMARK 500 3 ASN A 72 -81.67 -94.00
REMARK 500 3 GLN A 73 -95.07 -119.94
REMARK 500 4 LEU A 52 -72.07 5.03
REMARK 500 4 CYS A 53 125.13 141.47
REMARK 500 4 CYS A 56 -144.30 -108.46
REMARK 500 4 LYS A 57 24.36 -163.96
REMARK 500 4 HIS A 61 -176.06 -172.52
REMARK 500 4 SER A 68 72.44 -171.83
REMARK 500 4 LYS A 69 88.89 -63.28
REMARK 500 4 ASP A 71 -75.40 -139.05
REMARK 500 4 GLN A 73 -123.98 -118.83
REMARK 500 5 LEU A 52 -68.93 -12.92
REMARK 500 5 CYS A 53 123.20 147.51
REMARK 500 5 CYS A 56 -143.30 -118.86
REMARK 500 5 LYS A 57 25.83 -163.06
REMARK 500 5 LYS A 60 86.42 -163.04
REMARK 500 5 HIS A 61 -175.64 179.63
REMARK 500
REMARK 500 THIS ENTRY HAS 135 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 55 0.25 SIDE CHAIN
REMARK 500 1 ARG A 58 0.25 SIDE CHAIN
REMARK 500 2 ARG A 55 0.09 SIDE CHAIN
REMARK 500 2 ARG A 58 0.17 SIDE CHAIN
REMARK 500 3 ARG A 55 0.29 SIDE CHAIN
REMARK 500 3 ARG A 58 0.31 SIDE CHAIN
REMARK 500 4 ARG A 55 0.28 SIDE CHAIN
REMARK 500 4 ARG A 58 0.10 SIDE CHAIN
REMARK 500 5 ARG A 55 0.26 SIDE CHAIN
REMARK 500 5 ARG A 58 0.30 SIDE CHAIN
REMARK 500 6 ARG A 55 0.31 SIDE CHAIN
REMARK 500 7 ARG A 55 0.30 SIDE CHAIN
REMARK 500 7 ARG A 58 0.16 SIDE CHAIN
REMARK 500 8 ARG A 55 0.32 SIDE CHAIN
REMARK 500 8 ARG A 58 0.30 SIDE CHAIN
REMARK 500 9 ARG A 55 0.20 SIDE CHAIN
REMARK 500 9 ARG A 58 0.26 SIDE CHAIN
REMARK 500 10 ARG A 55 0.18 SIDE CHAIN
REMARK 500 10 ARG A 58 0.31 SIDE CHAIN
REMARK 500 11 ARG A 55 0.10 SIDE CHAIN
REMARK 500 11 ARG A 58 0.14 SIDE CHAIN
REMARK 500 12 ARG A 55 0.24 SIDE CHAIN
REMARK 500 12 ARG A 58 0.20 SIDE CHAIN
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 81 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 53 SG
REMARK 620 2 CYS A 56 SG 106.7
REMARK 620 3 HIS A 61 NE2 107.7 117.7
REMARK 620 4 CYS A 66 SG 100.0 123.1 99.7
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 A 81
DBREF 1CL4 A 21 80 UNP P07567 GAG_MPMV 546 605
SEQADV 1CL4 SER A 23 UNP P07567 CYS 548 ENGINEERED MUTATION
SEQRES 1 A 60 GLY GLY SER CYS PHE LYS CYS GLY LYS LYS GLY HIS PHE
SEQRES 2 A 60 ALA LYS ASN CYS HIS GLU HIS ALA HIS ASN ASN ALA GLU
SEQRES 3 A 60 PRO LYS VAL PRO GLY LEU CYS PRO ARG CYS LYS ARG GLY
SEQRES 4 A 60 LYS HIS TRP ALA ASN GLU CYS LYS SER LYS THR ASP ASN
SEQRES 5 A 60 GLN GLY ASN PRO ILE PRO PRO HIS
HET ZN A 81 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
LINK SG CYS A 53 ZN ZN A 81 1555 1555 2.29
LINK SG CYS A 56 ZN ZN A 81 1555 1555 2.33
LINK NE2 HIS A 61 ZN ZN A 81 1555 1555 2.01
LINK SG CYS A 66 ZN ZN A 81 1555 1555 2.29
SITE 1 AC1 4 CYS A 53 CYS A 56 HIS A 61 CYS A 66
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 - 3 20 Bytes