Header list of 1k81.pdb file
Complete list - 23 20 Bytes
HEADER TRANSLATION 22-OCT-01 1K81
TITLE NMR STRUCTURE OF THE ZINC-RIBBON DOMAIN WITHIN TRANSLATION INITIATION
TITLE 2 FACTOR 2 SUBUNIT BETA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE TRANSLATION INITIATION FACTOR 2 BETA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EIF-2-BETA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII;
SOURCE 3 ORGANISM_TAXID: 2190;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS TRANSLATION INITIATION FACTOR, ZINC RIBBON, TRANSLATION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR S.CHO,D.W.HOFFMAN
REVDAT 4 23-FEB-22 1K81 1 REMARK LINK
REVDAT 3 24-FEB-09 1K81 1 VERSN
REVDAT 2 16-OCT-02 1K81 1 JRNL
REVDAT 1 24-APR-02 1K81 0
JRNL AUTH S.CHO,D.W.HOFFMAN
JRNL TITL STRUCTURE OF THE BETA SUBUNIT OF TRANSLATION INITIATION
JRNL TITL 2 FACTOR 2 FROM THE ARCHAEON METHANOCOCCUS JANNASCHII: A
JRNL TITL 3 REPRESENTATIVE OF THE EIF2BETA/EIF5 FAMILY OF PROTEINS
JRNL REF BIOCHEMISTRY V. 41 5730 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11980477
JRNL DOI 10.1021/BI011984N
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K81 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014676.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 50 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM AIF2 BETA U-15N,13C; 10 MM
REMARK 210 PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_ROESY
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 : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 170
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D AND 3D
REMARK 210 HETERONUCLEAR NMR TECHNIQUES.
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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 ILE A 143 C ILE A 143 O -0.137
REMARK 500 1 ILE A 143 C ILE A 143 OXT -0.127
REMARK 500 3 ILE A 143 C ILE A 143 O -0.755
REMARK 500 3 ILE A 143 C ILE A 143 OXT -0.846
REMARK 500 4 ILE A 143 C ILE A 143 O -0.957
REMARK 500 4 ILE A 143 C ILE A 143 OXT -1.047
REMARK 500 5 ILE A 143 C ILE A 143 O -0.330
REMARK 500 5 ILE A 143 C ILE A 143 OXT -0.551
REMARK 500 6 ILE A 143 C ILE A 143 OXT -0.179
REMARK 500 7 ILE A 143 C ILE A 143 OXT -0.232
REMARK 500 8 ILE A 143 C ILE A 143 O -0.242
REMARK 500 8 ILE A 143 C ILE A 143 OXT -0.272
REMARK 500 9 ILE A 143 C ILE A 143 O -0.327
REMARK 500 9 ILE A 143 C ILE A 143 OXT -0.401
REMARK 500 10 ILE A 143 C ILE A 143 OXT -0.126
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 ILE A 143 CA - C - O ANGL. DEV. = -31.0 DEGREES
REMARK 500 3 ILE A 143 CA - C - O ANGL. DEV. = -67.8 DEGREES
REMARK 500 4 ILE A 143 CA - C - O ANGL. DEV. = -30.5 DEGREES
REMARK 500 5 ILE A 143 CA - C - O ANGL. DEV. = 105.4 DEGREES
REMARK 500 6 ILE A 143 CA - C - O ANGL. DEV. = -58.2 DEGREES
REMARK 500 7 ILE A 143 CA - C - O ANGL. DEV. = -43.0 DEGREES
REMARK 500 8 ILE A 143 CA - C - O ANGL. DEV. = -32.4 DEGREES
REMARK 500 9 ILE A 143 CA - C - O ANGL. DEV. = -64.4 DEGREES
REMARK 500 10 ILE A 143 CA - C - O ANGL. DEV. = -57.4 DEGREES
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 GLU A 112 34.41 -96.54
REMARK 500 1 PRO A 116 -148.23 -101.15
REMARK 500 1 ARG A 125 35.58 -145.37
REMARK 500 1 ALA A 133 -38.35 133.57
REMARK 500 2 ARG A 111 -95.99 -54.67
REMARK 500 2 GLU A 112 43.39 -105.70
REMARK 500 2 PRO A 116 -151.61 -101.85
REMARK 500 2 ALA A 133 -39.32 131.12
REMARK 500 2 ARG A 141 97.32 62.94
REMARK 500 3 CYS A 110 38.34 -97.33
REMARK 500 3 PRO A 116 -102.07 -80.77
REMARK 500 3 ALA A 133 -38.73 130.34
REMARK 500 3 MET A 142 -175.66 62.43
REMARK 500 4 PRO A 116 -150.55 -103.42
REMARK 500 4 ALA A 133 -42.31 135.37
REMARK 500 4 ARG A 141 67.50 62.46
REMARK 500 5 CYS A 110 142.93 -172.43
REMARK 500 5 GLU A 112 68.61 -154.65
REMARK 500 5 LYS A 115 55.86 -156.77
REMARK 500 5 PRO A 116 -141.81 -97.82
REMARK 500 5 ALA A 133 -39.00 127.48
REMARK 500 5 ARG A 141 43.17 -152.97
REMARK 500 5 MET A 142 108.51 62.20
REMARK 500 6 ILE A 109 -70.22 -55.77
REMARK 500 6 CYS A 113 -53.22 -123.68
REMARK 500 6 LYS A 115 76.28 53.92
REMARK 500 6 PRO A 116 -145.93 -99.77
REMARK 500 6 ARG A 125 34.14 -140.67
REMARK 500 6 ALA A 133 -38.45 135.54
REMARK 500 6 MET A 142 178.67 60.05
REMARK 500 7 ILE A 109 -70.22 -68.11
REMARK 500 7 ARG A 111 83.24 -66.61
REMARK 500 7 GLU A 112 61.96 66.59
REMARK 500 7 CYS A 113 -78.39 -55.00
REMARK 500 7 LYS A 115 -61.76 -169.46
REMARK 500 7 PRO A 116 -99.62 -36.66
REMARK 500 7 ASP A 117 -171.00 171.48
REMARK 500 7 ALA A 133 -42.11 130.49
REMARK 500 7 ARG A 141 65.35 -151.09
REMARK 500 8 CYS A 110 -66.09 77.26
REMARK 500 8 ARG A 111 -64.27 165.06
REMARK 500 8 LYS A 115 -67.60 -177.99
REMARK 500 8 PRO A 116 -104.23 -47.48
REMARK 500 8 ASP A 117 -166.37 168.52
REMARK 500 8 ALA A 133 -38.83 126.34
REMARK 500 8 ARG A 141 113.17 61.21
REMARK 500 8 MET A 142 34.56 -141.26
REMARK 500 9 CYS A 110 -170.00 -172.36
REMARK 500 9 PRO A 116 -150.55 -104.40
REMARK 500 9 ARG A 125 31.94 -140.28
REMARK 500
REMARK 500 THIS ENTRY HAS 57 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 144 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 110 SG
REMARK 620 2 CYS A 113 SG 111.0
REMARK 620 3 CYS A 131 SG 110.7 110.5
REMARK 620 4 CYS A 134 SG 107.2 106.8 110.6
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 144
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K8B RELATED DB: PDB
REMARK 900 NMR STRUCTURE ANALYSIS OF THE N-TERMINAL DOMAIN OF ARCHAEAL
REMARK 900 TRANSLATION INITIATION FACTOR 2 SUBUNIT BETA
DBREF 1K81 A 108 143 UNP Q57562 IF2B_METJA 108 143
SEQRES 1 A 36 VAL ILE CYS ARG GLU CYS GLY LYS PRO ASP THR LYS ILE
SEQRES 2 A 36 ILE LYS GLU GLY ARG VAL HIS LEU LEU LYS CYS MET ALA
SEQRES 3 A 36 CYS GLY ALA ILE ARG PRO ILE ARG MET ILE
HET ZN A 144 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
SHEET 1 A 3 ASP A 117 GLU A 123 0
SHEET 2 A 3 VAL A 126 MET A 132 -1 O LYS A 130 N LYS A 119
SHEET 3 A 3 ALA A 136 ILE A 140 -1 O ILE A 140 N HIS A 127
LINK SG CYS A 110 ZN ZN A 144 1555 1555 2.34
LINK SG CYS A 113 ZN ZN A 144 1555 1555 2.33
LINK SG CYS A 131 ZN ZN A 144 1555 1555 2.34
LINK SG CYS A 134 ZN ZN A 144 1555 1555 2.33
SITE 1 AC1 4 CYS A 110 CYS A 113 CYS A 131 CYS A 134
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 - 23 20 Bytes