Header list of 2bai.pdb file
Complete list - 9 20 Bytes
HEADER VIRAL PROTEIN 14-OCT-05 2BAI
TITLE THE ZINC FINGER DOMAIN OF MENGOVIRUS LEADER POLYPEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENOME POLYPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZINC FINGER DOMAIN, RESIDUES 1-32;
COMPND 5 SYNONYM: MENGOVIRUS LEADER POLYPEPTIDE;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MENGO VIRUS;
SOURCE 3 ORGANISM_TAXID: 12107;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ZINC FINGER DOMAIN, VIRUS, VIRUSES, CARDIOVIRUS, MENGOVIRUS,
KEYWDS 2 STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, CENTER FOR
KEYWDS 3 EUKARYOTIC STRUCTURAL GENOMICS, CESG, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.C.CORNILESCU,F.W.PORTER,Z.QIN,M.S.LEE,A.C.PALMENBERG,J.L.MARKLEY,
AUTHOR 2 CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS (CESG)
REVDAT 4 09-MAR-22 2BAI 1 REMARK LINK
REVDAT 3 24-FEB-09 2BAI 1 VERSN
REVDAT 2 04-NOV-08 2BAI 1 JRNL
REVDAT 1 24-JAN-06 2BAI 0
JRNL AUTH C.C.CORNILESCU,F.W.PORTER,K.Q.ZHAO,A.C.PALMENBERG,
JRNL AUTH 2 J.L.MARKLEY
JRNL TITL NMR STRUCTURE OF THE MENGOVIRUS LEADER PROTEIN ZINC-FINGER
JRNL TITL 2 DOMAIN.
JRNL REF FEBS LETT. V. 582 896 2008
JRNL REFN ISSN 0014-5793
JRNL PMID 18291103
JRNL DOI 10.1016/J.FEBSLET.2008.02.023
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, CYANA 2.0
REMARK 3 AUTHORS : FRANK DELAGLIO (NMRPIPE), GUENTERT (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2BAI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034878.
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 : 50MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM NC-LABELED MENGOL, 50MM
REMARK 210 NAPI, 93% H2O, 7% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HCCHTOCSY;
REMARK 210 HNCA; HCCONH
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; DMX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PIPP/STAPP, CYANA 2.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 THR A 3 77.08 39.99
REMARK 500 1 MET A 5 -47.74 -154.59
REMARK 500 1 GLU A 6 91.36 71.40
REMARK 500 1 GLN A 7 40.54 170.39
REMARK 500 1 GLU A 8 86.25 52.33
REMARK 500 1 HIS A 12 -45.88 -130.34
REMARK 500 1 SER A 13 45.90 143.54
REMARK 500 1 GLN A 26 26.08 49.74
REMARK 500 2 GLU A 6 77.72 45.37
REMARK 500 2 GLU A 8 72.37 85.14
REMARK 500 2 SER A 13 43.11 141.82
REMARK 500 2 ALA A 24 63.62 -101.98
REMARK 500 2 GLN A 26 27.42 49.55
REMARK 500 2 PHE A 31 -172.05 -176.95
REMARK 500 3 ALA A 2 112.71 60.75
REMARK 500 3 THR A 3 -87.00 -151.72
REMARK 500 3 GLU A 6 91.34 83.41
REMARK 500 3 GLN A 7 -164.75 -163.28
REMARK 500 3 GLU A 8 79.37 -65.13
REMARK 500 3 SER A 13 44.97 143.12
REMARK 500 3 ALA A 24 49.64 -86.93
REMARK 500 4 THR A 4 -168.58 -59.95
REMARK 500 4 GLN A 7 -51.93 -172.30
REMARK 500 4 GLU A 8 85.06 178.47
REMARK 500 4 SER A 13 42.62 144.97
REMARK 500 4 MET A 14 -159.55 -151.95
REMARK 500 4 ALA A 24 65.32 -103.33
REMARK 500 4 PHE A 31 -86.02 57.12
REMARK 500 5 GLU A 6 76.84 57.72
REMARK 500 5 GLN A 7 -82.30 -132.19
REMARK 500 5 SER A 13 43.47 147.44
REMARK 500 5 MET A 14 -151.73 -152.46
REMARK 500 5 PHE A 31 89.06 -169.10
REMARK 500 6 ALA A 2 -71.09 -151.33
REMARK 500 6 THR A 3 -158.81 40.83
REMARK 500 6 THR A 4 43.77 -147.66
REMARK 500 6 GLN A 7 -50.22 -128.29
REMARK 500 6 GLU A 8 74.35 158.62
REMARK 500 6 HIS A 12 -46.84 -130.63
REMARK 500 6 SER A 13 48.10 144.41
REMARK 500 6 ASN A 29 -73.89 -44.34
REMARK 500 7 ALA A 2 64.52 -170.13
REMARK 500 7 GLN A 7 -159.56 -174.21
REMARK 500 7 GLU A 8 79.02 -64.87
REMARK 500 7 SER A 13 44.58 143.37
REMARK 500 7 MET A 14 -159.57 -153.64
REMARK 500 7 ASN A 29 -84.16 -50.01
REMARK 500 8 ALA A 2 -161.39 76.15
REMARK 500 8 MET A 5 173.58 59.23
REMARK 500 8 GLN A 7 -37.56 -176.37
REMARK 500
REMARK 500 THIS ENTRY HAS 163 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 110 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 10 SG
REMARK 620 2 HIS A 12 NE2 101.6
REMARK 620 3 CYS A 19 SG 80.2 79.6
REMARK 620 4 CYS A 22 SG 127.6 110.0 144.7
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 110
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: GO.79761 RELATED DB: TARGETDB
DBREF 2BAI A 1 32 UNP P32540 POLG_ENMG3 1 32
SEQRES 1 A 32 MET ALA THR THR MET GLU GLN GLU ILE CYS ALA HIS SER
SEQRES 2 A 32 MET THR PHE GLU GLU CYS PRO LYS CYS SER ALA LEU GLN
SEQRES 3 A 32 TYR ARG ASN GLY PHE TYR
HET ZN A 110 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 THR A 15 GLU A 17 5 3
HELIX 2 2 GLU A 18 ALA A 24 1 7
LINK SG CYS A 10 ZN ZN A 110 1555 1555 2.30
LINK NE2 HIS A 12 ZN ZN A 110 1555 1555 2.08
LINK SG CYS A 19 ZN ZN A 110 1555 1555 2.40
LINK SG CYS A 22 ZN ZN A 110 1555 1555 2.39
SITE 1 AC1 4 CYS A 10 HIS A 12 CYS A 19 CYS A 22
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