Header list of 1gh8.pdb file
Complete list - b 23 2 Bytes
HEADER GENE REGULATION 30-NOV-00 1GH8
TITLE SOLUTION STRUCTURE OF THE ARCHAEAL TRANSLATION ELONGATION FACTOR 1BETA
TITLE 2 FROM METHANOBACTERIUM THERMOAUTOTROPHICUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSLATION ELONGATION FACTOR 1BETA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 145262;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA-BETA SANDWICH, GENE REGULATION, STRUCTURAL GENOMICS, PSI,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, NESG
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR G.KOZLOV,I.EKIEL,K.GEHRING,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 2 (NESG)
REVDAT 4 23-FEB-22 1GH8 1 REMARK
REVDAT 3 24-FEB-09 1GH8 1 VERSN
REVDAT 2 25-JAN-05 1GH8 1 JRNL AUTHOR KEYWDS REMARK
REVDAT 1 13-DEC-00 1GH8 0
SPRSDE 13-DEC-00 1GH8 1D5K
JRNL AUTH G.KOZLOV,I.EKIEL,N.BEGLOVA,A.YEE,A.DHARAMSI,A.ENGEL,
JRNL AUTH 2 N.SIDDIQUI,A.NONG,K.GEHRING
JRNL TITL RAPID FOLD AND STRUCTURE DETERMINATION OF THE ARCHAEAL
JRNL TITL 2 TRANSLATION ELONGATION FACTOR 1BETA FROM METHANOBACTERIUM
JRNL TITL 3 THERMOAUTOTROPHICUM.
JRNL REF J.BIOMOL.NMR V. 17 187 2000
JRNL REFN ISSN 0925-2738
JRNL PMID 10959626
JRNL DOI 10.1023/A:1008363304977
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, ARIA 0.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURE IS BASED ON A TOTAL OF 1962 RESTRAINTS, 1854 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 82 DIHEDRAL ANGLE RESTRAINTS, 26 HYDROGEN
REMARK 3 BOND
REMARK 3 CONSTRAINTS.
REMARK 4
REMARK 4 1GH8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-00.
REMARK 100 THE DEPOSITION ID IS D_1000001512.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : 0.15 M NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.0-3.0 MM N15-LABELED PROTEIN;
REMARK 210 2.0-3.0 MM N15,C13-LABELED
REMARK 210 PROTEIN; 2.0-3.0 MM UNLABELED
REMARK 210 PROTEIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GIFA 4.0, XEASY 1.3.13, CNS 0.5,
REMARK 210 ARIA 0.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
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:
REMARK 210 THE STRUCTURE WAS DETERMINED FOR THE PROTEIN WITH N-TERMINAL HIS-
REMARK 210 TAG ATTACHED
REMARK 210 TO IT. THE HIS-TAG SEQUENCE IS MGSSHHHHHHSSGLVPRGSH.
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 ASP A 16 44.88 -90.93
REMARK 500 1 VAL A 17 78.35 -63.80
REMARK 500 1 ASP A 18 95.13 -69.91
REMARK 500 1 GLU A 32 3.01 -59.52
REMARK 500 1 THR A 34 -135.47 -130.61
REMARK 500 1 HIS A 37 -77.51 -130.79
REMARK 500 1 ILE A 44 -83.69 -127.15
REMARK 500 1 ALA A 45 -150.88 -67.34
REMARK 500 1 ALA A 60 -149.22 -67.67
REMARK 500 1 ILE A 74 -163.38 -73.38
REMARK 500 1 GLU A 75 94.20 -51.29
REMARK 500 2 ASP A 16 41.15 -90.43
REMARK 500 2 VAL A 17 77.69 -65.93
REMARK 500 2 ASP A 18 95.04 -69.49
REMARK 500 2 GLU A 32 -4.61 -57.79
REMARK 500 2 THR A 34 -148.66 -130.61
REMARK 500 2 HIS A 37 -74.85 -130.84
REMARK 500 2 ILE A 44 -82.51 -124.64
REMARK 500 2 ALA A 45 -152.01 -67.52
REMARK 500 2 ALA A 60 -146.47 -67.22
REMARK 500 2 ILE A 74 -163.10 -72.68
REMARK 500 2 GLU A 75 98.65 -50.91
REMARK 500 3 ASP A 16 43.52 -90.79
REMARK 500 3 VAL A 17 75.49 -65.52
REMARK 500 3 GLU A 32 2.88 -59.43
REMARK 500 3 THR A 34 -133.56 -130.19
REMARK 500 3 HIS A 37 -77.62 -130.83
REMARK 500 3 ILE A 44 -82.49 -124.76
REMARK 500 3 ALA A 45 -153.97 -67.27
REMARK 500 3 ALA A 60 -139.36 -67.56
REMARK 500 3 ILE A 74 -161.02 -73.21
REMARK 500 3 GLU A 75 90.69 -51.82
REMARK 500 4 ASP A 16 41.98 -91.18
REMARK 500 4 VAL A 17 79.55 -65.80
REMARK 500 4 GLU A 32 2.20 -59.71
REMARK 500 4 THR A 34 -134.74 -130.07
REMARK 500 4 HIS A 37 -77.69 -130.55
REMARK 500 4 ILE A 44 -83.19 -126.63
REMARK 500 4 ALA A 45 -149.91 -67.62
REMARK 500 4 ALA A 60 -139.02 -67.56
REMARK 500 4 ILE A 74 -163.59 -73.10
REMARK 500 4 GLU A 75 96.60 -51.68
REMARK 500 5 ASP A 16 45.74 -92.61
REMARK 500 5 VAL A 17 76.66 -64.96
REMARK 500 5 GLU A 32 -2.58 -58.17
REMARK 500 5 THR A 34 -145.21 -130.51
REMARK 500 5 HIS A 37 -76.95 -130.70
REMARK 500 5 ILE A 44 -83.27 -125.76
REMARK 500 5 ALA A 45 -147.67 -67.42
REMARK 500 5 ALA A 60 -152.40 -67.21
REMARK 500
REMARK 500 THIS ENTRY HAS 307 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TT12 RELATED DB: TARGETDB
DBREF 1GH8 A 1 89 UNP O27734 EF1B_METTH 1 89
SEQRES 1 A 89 MET GLY ASP VAL VAL ALA THR ILE LYS VAL MET PRO GLU
SEQRES 2 A 89 SER PRO ASP VAL ASP LEU GLU ALA LEU LYS LYS GLU ILE
SEQRES 3 A 89 GLN GLU ARG ILE PRO GLU GLY THR GLU LEU HIS LYS ILE
SEQRES 4 A 89 ASP GLU GLU PRO ILE ALA PHE GLY LEU VAL ALA LEU ASN
SEQRES 5 A 89 VAL MET VAL VAL VAL GLY ASP ALA GLU GLY GLY THR GLU
SEQRES 6 A 89 ALA ALA GLU GLU SER LEU SER GLY ILE GLU GLY VAL SER
SEQRES 7 A 89 ASN ILE GLU VAL THR ASP VAL ARG ARG LEU MET
HELIX 1 1 ASP A 18 ILE A 30 1 13
HELIX 2 2 GLU A 61 THR A 64 5 4
HELIX 3 3 GLU A 65 SER A 72 1 8
SHEET 1 A 4 SER A 78 ARG A 87 0
SHEET 2 A 4 VAL A 4 PRO A 12 -1 N VAL A 5 O ARG A 86
SHEET 3 A 4 VAL A 49 VAL A 57 -1 N LEU A 51 O VAL A 10
SHEET 4 A 4 GLU A 35 LEU A 36 -1 N GLU A 35 O VAL A 56
SHEET 1 B 4 SER A 78 ARG A 87 0
SHEET 2 B 4 VAL A 4 PRO A 12 -1 N VAL A 5 O ARG A 86
SHEET 3 B 4 VAL A 49 VAL A 57 -1 N LEU A 51 O VAL A 10
SHEET 4 B 4 GLU A 41 PRO A 43 -1 O GLU A 42 N ALA A 50
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