Header list of 1nee.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSLATION 11-DEC-02 1NEE
TITLE STRUCTURE OF ARCHAEAL TRANSLATION FACTOR AIF2BETA FROM
TITLE 2 METHANOBACTERIUM THERMOAUTROPHICUM
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: METHANOTHERMOBACTER THERMAUTOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 145262;
SOURCE 4 GENE: MTH1769;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET15B
KEYWDS TWO DOMAIN PROTEIN, MIXED ALPHA-BETA STRUCTURE, ZINC FINGER,
KEYWDS 2 TRANSLATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.GUTIERREZ,J.F.TREMPE,N.SIDDIQUI,C.ARROWSMITH,K.GEHRING
REVDAT 3 23-FEB-22 1NEE 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1NEE 1 VERSN
REVDAT 1 09-MAR-04 1NEE 0
JRNL AUTH P.GUTIERREZ,M.J.OSBORNE,N.SIDDIQUI,J.F.TREMPE,C.ARROWSMITH,
JRNL AUTH 2 K.GEHRING
JRNL TITL STRUCTURE OF THE ARCHAEAL TRANSLATION INITIATION FACTOR
JRNL TITL 2 AIF2BETA FROM METHANOBACTERIUM THERMOAUTOTROPHICUM:
JRNL TITL 3 IMPLICATIONS FOR TRANSLATION INITIATION.
JRNL REF PROTEIN SCI. V. 13 659 2004
JRNL REFN ISSN 0961-8368
JRNL PMID 14978306
JRNL DOI 10.1110/PS.03506604
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, CNS 0.9
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NEE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1000017803.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : ~1.0MM AIF2BETA, 50MM TRIS
REMARK 210 BUFFER, 300MM NACL, 50UM ZNCL2,
REMARK 210 1MM DTT, PH 6.0, 90% H2O, 10%
REMARK 210 D2O; ~1.0MM AIF2BETA, 50MM TRIS
REMARK 210 BUFFER, 300MM NACL, 50UM ZNCL2,
REMARK 210 1MM DTT, PH 6.0, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA;
REMARK 210 HNCACB; CBCA(CO)NH; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GIFA 4.31, XEASY 1.3.13, ARIA
REMARK 210 1.1
REMARK 210 METHOD USED : THE STRUCTURES ARE BASED ON 1142
REMARK 210 NOE-DERIVED CONSTRAINTS, 118
REMARK 210 DIHEDRAL ANGLE RESTRAINTS, 39
REMARK 210 HYDROGEN BONDS AND 58 NH
REMARK 210 RESIDUAL DIPOLAR COUPLINGS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
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 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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
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 ASP A 3 -72.81 -74.07
REMARK 500 1 LYS A 6 55.91 -105.28
REMARK 500 1 ASP A 13 -95.66 -157.34
REMARK 500 1 PRO A 17 24.19 -65.55
REMARK 500 1 PRO A 28 168.60 -48.86
REMARK 500 1 LYS A 29 106.39 54.49
REMARK 500 1 ALA A 30 64.61 -157.77
REMARK 500 1 ASN A 37 29.62 -156.42
REMARK 500 1 ASN A 43 46.19 -109.03
REMARK 500 1 ASN A 52 105.04 -177.04
REMARK 500 1 ALA A 69 -62.67 -23.37
REMARK 500 1 ARG A 76 -97.90 -90.07
REMARK 500 1 ALA A 77 71.12 -161.94
REMARK 500 1 PHE A 83 49.63 -88.28
REMARK 500 1 PHE A 86 -76.43 -92.04
REMARK 500 1 ASN A 97 50.03 -111.05
REMARK 500 1 GLU A 104 75.09 44.53
REMARK 500 1 ASN A 106 -93.20 -72.69
REMARK 500 1 ARG A 107 60.24 -106.94
REMARK 500 1 ASP A 109 46.60 -81.70
REMARK 500 1 ARG A 117 69.98 64.28
REMARK 500 1 LEU A 121 172.08 178.10
REMARK 500 1 CYS A 123 47.82 -143.12
REMARK 500 1 ALA A 125 -72.97 -74.13
REMARK 500 1 CYS A 126 49.33 -80.27
REMARK 500 1 LEU A 132 -72.22 177.67
REMARK 500 2 ALA A 11 37.78 71.90
REMARK 500 2 ASP A 13 -37.69 72.61
REMARK 500 2 PRO A 17 -72.60 -58.84
REMARK 500 2 GLU A 18 -73.74 66.76
REMARK 500 2 LYS A 29 57.97 -174.99
REMARK 500 2 ALA A 30 -74.01 -136.87
REMARK 500 2 SER A 32 -176.43 -63.60
REMARK 500 2 GLN A 35 97.00 -171.82
REMARK 500 2 ASN A 37 26.69 -161.98
REMARK 500 2 ASN A 43 52.31 -110.53
REMARK 500 2 ASN A 52 96.66 -176.80
REMARK 500 2 ARG A 53 -39.62 -33.27
REMARK 500 2 ARG A 76 -154.89 -91.19
REMARK 500 2 ALA A 77 79.97 -113.87
REMARK 500 2 LYS A 82 30.73 -167.43
REMARK 500 2 PHE A 86 -81.98 -92.14
REMARK 500 2 ASN A 97 51.74 -110.50
REMARK 500 2 GLU A 104 75.88 48.31
REMARK 500 2 CYS A 105 53.22 -68.56
REMARK 500 2 ASN A 106 -88.86 -73.02
REMARK 500 2 ARG A 107 54.63 -107.22
REMARK 500 2 ASP A 109 43.94 -89.88
REMARK 500 2 ILE A 118 66.25 67.09
REMARK 500 2 SER A 119 -31.17 -142.03
REMARK 500
REMARK 500 THIS ENTRY HAS 545 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 136 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 102 SG
REMARK 620 2 CYS A 105 SG 109.7
REMARK 620 3 CYS A 123 SG 109.4 109.3
REMARK 620 4 CYS A 126 SG 109.7 109.4 109.3
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 136
DBREF 1NEE A 1 135 UNP O27797 IF2B_METTH 1 135
SEQADV 1NEE GLY A -2 UNP O27797 EXPRESSION TAG
SEQADV 1NEE SER A -1 UNP O27797 EXPRESSION TAG
SEQADV 1NEE HIS A 0 UNP O27797 EXPRESSION TAG
SEQRES 1 A 138 GLY SER HIS MET ASP ASP TYR GLU LYS LEU LEU GLU ARG
SEQRES 2 A 138 ALA ILE ASP GLN LEU PRO PRO GLU VAL PHE GLU THR LYS
SEQRES 3 A 138 ARG PHE GLU VAL PRO LYS ALA TYR SER VAL ILE GLN GLY
SEQRES 4 A 138 ASN ARG THR PHE ILE GLN ASN PHE ARG GLU VAL ALA ASP
SEQRES 5 A 138 ALA LEU ASN ARG ASP PRO GLN HIS LEU LEU LYS PHE LEU
SEQRES 6 A 138 LEU ARG GLU LEU GLY THR ALA GLY ASN LEU GLU GLY GLY
SEQRES 7 A 138 ARG ALA ILE LEU GLN GLY LYS PHE THR HIS PHE LEU ILE
SEQRES 8 A 138 ASN GLU ARG ILE GLU ASP TYR VAL ASN LYS PHE VAL ILE
SEQRES 9 A 138 CYS HIS GLU CYS ASN ARG PRO ASP THR ARG ILE ILE ARG
SEQRES 10 A 138 GLU GLY ARG ILE SER LEU LEU LYS CYS GLU ALA CYS GLY
SEQRES 11 A 138 ALA LYS ALA PRO LEU LYS ASN VAL
HET ZN A 136 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 ASN A 43 ASN A 52 1 10
HELIX 2 2 ASP A 54 LEU A 66 1 13
HELIX 3 3 PHE A 86 ASN A 97 1 12
HELIX 4 4 ASN A 97 HIS A 103 1 7
SHEET 1 A 3 ILE A 34 GLN A 35 0
SHEET 2 A 3 ARG A 38 ILE A 41 -1 O ARG A 38 N GLN A 35
SHEET 3 A 3 ALA A 77 GLN A 80 -1 O ALA A 77 N ILE A 41
SHEET 1 B 2 ILE A 113 GLU A 115 0
SHEET 2 B 2 LEU A 120 LYS A 122 -1 O LEU A 120 N GLU A 115
LINK SG CYS A 102 ZN ZN A 136 1555 1555 2.33
LINK SG CYS A 105 ZN ZN A 136 1555 1555 2.32
LINK SG CYS A 123 ZN ZN A 136 1555 1555 2.31
LINK SG CYS A 126 ZN ZN A 136 1555 1555 2.32
SITE 1 AC1 4 CYS A 102 CYS A 105 CYS A 123 CYS A 126
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 - b 23 2 Bytes